PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
7778849-6	1995	Robust 32-kd bands corresponding to heme oxygenase-1 were observed by Western blotting of protein extracts derived from AD temporal cortex and hippocampus after sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	161-183	heme oxygenase 1	Homo sapiens	36-52
7778849-6	1995	Robust 32-kd bands corresponding to heme oxygenase-1 were observed by Western blotting of protein extracts derived from AD temporal cortex and hippocampus after sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	184-198	heme oxygenase 1	Homo sapiens	36-52
8163576-7	1994	Heavy metal ions and thiol reagents were also highly potent inducers of HO-1 in human RPE cells.	Metals	6-11	heme oxygenase 1	Homo sapiens	72-76
7857260-0	1995	Differential control of the metal-mediated activation of the human heme oxygenase-1 and metallothionein IIA genes.	Metals	28-33	heme oxygenase 1	Homo sapiens	67-83
7857260-1	1995	Heme oxygenase-1, an essential enzyme in heme catabolism, and metallothionein IIA, a small metal-binding protein with clusters of cysteins, are remarkably induced in HeLa cells following the treatment with cadmium or zinc.	Cadmium	206-213	heme oxygenase 1	Homo sapiens	0-16
7857260-3	1995	Here we showed by transient expression assays that the cadmium-responsive element (CdRE) of the human heme oxygenase-1 gene is not responsive to zinc, whereas a metal-regulatory element (MRE) of the human metallothionein IIA gene is able to respond to either cadmium or zinc.	Cadmium	55-62	heme oxygenase 1	Homo sapiens	102-118
7857260-3	1995	Here we showed by transient expression assays that the cadmium-responsive element (CdRE) of the human heme oxygenase-1 gene is not responsive to zinc, whereas a metal-regulatory element (MRE) of the human metallothionein IIA gene is able to respond to either cadmium or zinc.	cdre	83-87	heme oxygenase 1	Homo sapiens	102-118
7857260-3	1995	Here we showed by transient expression assays that the cadmium-responsive element (CdRE) of the human heme oxygenase-1 gene is not responsive to zinc, whereas a metal-regulatory element (MRE) of the human metallothionein IIA gene is able to respond to either cadmium or zinc.	Metals	161-166	heme oxygenase 1	Homo sapiens	102-118
7857260-3	1995	Here we showed by transient expression assays that the cadmium-responsive element (CdRE) of the human heme oxygenase-1 gene is not responsive to zinc, whereas a metal-regulatory element (MRE) of the human metallothionein IIA gene is able to respond to either cadmium or zinc.	Cadmium	259-266	heme oxygenase 1	Homo sapiens	102-118
8030754-1	1994	Heme oxygenase-1 is an important enzyme that degrades heme, a pro-oxidant, leading to the formation of antioxidant molecules.	Heme	54-58	heme oxygenase 1	Homo sapiens	0-16
8016102-3	1994	Heme treatment increased both HO activity and HO-1 mRNA in the human erythroleukemic cell line K562.	Heme	0-4	heme oxygenase 1	Homo sapiens	46-50
7703255-3	1995	The purified, truncated hHO-1/heme complex is spectroscopically indistinguishable from that of the rat enzyme and converts heme to biliverdin when reconstituted with rat liver cytochrome P450 reductase.	Heme	30-34	heme oxygenase 1	Homo sapiens	24-29
7703255-3	1995	The purified, truncated hHO-1/heme complex is spectroscopically indistinguishable from that of the rat enzyme and converts heme to biliverdin when reconstituted with rat liver cytochrome P450 reductase.	Heme	123-127	heme oxygenase 1	Homo sapiens	24-29
7703255-3	1995	The purified, truncated hHO-1/heme complex is spectroscopically indistinguishable from that of the rat enzyme and converts heme to biliverdin when reconstituted with rat liver cytochrome P450 reductase.	Biliverdine	131-141	heme oxygenase 1	Homo sapiens	24-29
7525927-0	1994	Induction of heart heme oxygenase-1 (HSP32) by hyperthermia: possible role in stress-mediated elevation of cyclic 3":5"-guanosine monophosphate.	Cyclic GMP	107-143	heme oxygenase 1	Homo sapiens	19-35
7525927-0	1994	Induction of heart heme oxygenase-1 (HSP32) by hyperthermia: possible role in stress-mediated elevation of cyclic 3":5"-guanosine monophosphate.	Cyclic GMP	107-143	heme oxygenase 1	Homo sapiens	37-42
7525927-2	1994	Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin.	Carbon Monoxide	179-194	heme oxygenase 1	Homo sapiens	30-34
7525927-2	1994	Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin.	Carbon Monoxide	179-194	heme oxygenase 1	Homo sapiens	36-41
7525927-2	1994	Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin.	Bilirubin	217-226	heme oxygenase 1	Homo sapiens	30-34
7525927-2	1994	Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin.	Bilirubin	217-226	heme oxygenase 1	Homo sapiens	36-41
8163576-7	1994	Heavy metal ions and thiol reagents were also highly potent inducers of HO-1 in human RPE cells.	Sulfhydryl Compounds	21-26	heme oxygenase 1	Homo sapiens	72-76
8455037-1	1993	In mammalian systems, the heme oxygenase (HO) isozymes HO-1 (HSP32) and HO-2 oxidatively cleave the heme molecule to produce bile pigments and carbon monoxide.	Heme	26-30	heme oxygenase 1	Homo sapiens	61-66
19912946-0	1993	Heme Oxygenase, a Likely Regulator of cGMP Production in the Brain: Induction in Vivo of HO-1 Compensates for Depression in NO Synthase Activity.	Cyclic GMP	38-42	heme oxygenase 1	Homo sapiens	89-93
19912946-2	1993	The sole source of CO in mammalian systems is the alpha-meso carbon bridge of the heme molecule cleaved by heme oxygenase isozymes, HO-1 and HO-2.	Carbon	61-67	heme oxygenase 1	Homo sapiens	132-145
19912946-2	1993	The sole source of CO in mammalian systems is the alpha-meso carbon bridge of the heme molecule cleaved by heme oxygenase isozymes, HO-1 and HO-2.	Heme	82-86	heme oxygenase 1	Homo sapiens	132-145
19912946-10	1993	Increased capability of select cerebellar cell populations to generate CO, as indicated by an increase in their HO-1 protein content, points to the active role of this isozyme in maintenance of cGMP level under stress conditions, when nitric oxide production is compromised.	Carbon Monoxide	71-73	heme oxygenase 1	Homo sapiens	112-116
8146161-1	1994	Oxidative stress of human skin fibroblasts by treatment with ultraviolet A (UVA) radiation has been shown to lead to an increase in levels of the heme catabolizing enzyme heme oxygenase 1 [heme, hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating), EC 1.14.99.3] and the iron storage protein ferritin.	Heme	146-150	heme oxygenase 1	Homo sapiens	171-187
8146161-1	1994	Oxidative stress of human skin fibroblasts by treatment with ultraviolet A (UVA) radiation has been shown to lead to an increase in levels of the heme catabolizing enzyme heme oxygenase 1 [heme, hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating), EC 1.14.99.3] and the iron storage protein ferritin.	Hydrogen	195-203	heme oxygenase 1	Homo sapiens	171-187
8146161-3	1994	Pretreating cells with heme oxygenase 1 antisense oligonucleotide inhibited the irradiation-dependent induction of both the heme oxygenase I enzyme and ferritin and abolished the protective effect of preirradiation.	Oligonucleotides	50-65	heme oxygenase 1	Homo sapiens	23-39
8455037-1	1993	In mammalian systems, the heme oxygenase (HO) isozymes HO-1 (HSP32) and HO-2 oxidatively cleave the heme molecule to produce bile pigments and carbon monoxide.	Carbon Monoxide	143-158	heme oxygenase 1	Homo sapiens	61-66
1754738-2	1991	We observed an increase in mRNA levels of heat-shock protein (hsp) 70, hsp 90, hsp 32 and metallothionein after treatment of GOTO cells with cadmium, although the time courses of the changes of individual mRNA of the heat-shock proteins and metallothionein were somewhat different from each other.	Cadmium	141-148	heme oxygenase 1	Homo sapiens	79-85
33818898-6	2021	Deoxynivalenol (IC50 = 20 muM) activated mitochondrial apoptotic pathway by modulating antioxidant protein expressions (Nrf2, HO-1 and NQO1).	deoxynivalenol	0-14	heme oxygenase 1	Homo sapiens	126-130
33775716-0	2021	The signaling pathway PI3K/Akt/Nrf2/HO-1 plays a role in the mitochondrial protection promoted by astaxanthin in the SH-SY5Y cells exposed to hydrogen peroxide.	astaxanthine	98-109	heme oxygenase 1	Homo sapiens	36-40
33775716-0	2021	The signaling pathway PI3K/Akt/Nrf2/HO-1 plays a role in the mitochondrial protection promoted by astaxanthin in the SH-SY5Y cells exposed to hydrogen peroxide.	Hydrogen Peroxide	142-159	heme oxygenase 1	Homo sapiens	36-40
33775716-9	2021	Inhibition of the PI3K/Akt or of the HO-1 enzyme abolished the AST-induced mitochondrial protection in cells challenged with H2O2.	astaxanthine	63-66	heme oxygenase 1	Homo sapiens	37-41
33775716-9	2021	Inhibition of the PI3K/Akt or of the HO-1 enzyme abolished the AST-induced mitochondrial protection in cells challenged with H2O2.	Hydrogen Peroxide	125-129	heme oxygenase 1	Homo sapiens	37-41
33775716-11	2021	Thus, we suggest that AST promotes mitochondrial protection by a mechanism dependent on the PI3K/Akt/Nrf2/HO-1 signaling pathway in SH-SY5Y cells exposed to H2O2.	Hydrogen Peroxide	157-161	heme oxygenase 1	Homo sapiens	106-110
2052613-1	1991	Catalytic activity of heme oxygenase (heme, hydrogen-donor:oxygen oxidoreductase, EC 1.14.99.3) isozymes, HO-1 and HO-2, permits production of physiologic isomers of bile pigments.	Hydrogen	44-52	heme oxygenase 1	Homo sapiens	106-119
33761605-0	2021	Heme oxygenase-1 inducer hemin does not inhibit SARS-CoV-2 virus infection.	Hemin	25-30	heme oxygenase 1	Homo sapiens	0-16
33761605-3	2021	Given that hemin is a natural inducer of the HO-1 gene, the aim of this study was to develop an in vitro assay to analyze the antiviral potency of hemin against SARS-CoV-2 infection.	Hemin	11-16	heme oxygenase 1	Homo sapiens	45-49
33761605-3	2021	Given that hemin is a natural inducer of the HO-1 gene, the aim of this study was to develop an in vitro assay to analyze the antiviral potency of hemin against SARS-CoV-2 infection.	Hemin	147-152	heme oxygenase 1	Homo sapiens	45-49
33761605-7	2021	Hemin administration to the culture medium induced a high induction in the expression of the HO-1 gene that was stronger in Vero-E6 macaque-derived cells than in the human Calu-3 cell line.	Hemin	0-5	heme oxygenase 1	Homo sapiens	93-97
33761605-9	2021	In conclusion, although exposure to hemin induced strong HO-1 up-regulation, this effect was unable to inhibit or delay the progression of SARS-CoV-2 infection in two epithelial cell lines susceptible to infection.	Hemin	36-41	heme oxygenase 1	Homo sapiens	57-61
33788639-6	2021	ECs pre-treated with different concentrations RA and co-cultured with thapsigargin-induced ER stressed pancreatic beta-cells showed increased levels of Nrf2 and its downstream targets such as heme oxygenase-1 (HO-1) and NADPH-quinone oxidoreductase-1 (NQO-1), and reduction of ER stress evinced by the decreased levels of glucose-regulated protein (GRP) 78 and C/ERB homologous protein (CHOP).	Thapsigargin	70-82	heme oxygenase 1	Homo sapiens	192-208
33818552-9	2021	The protective effect of chrysin on sepsis-induced cardiac dysfunction was blocked by ZnPP, which is a HO-1 blocker.	chrysin	25-32	heme oxygenase 1	Homo sapiens	103-107
33818552-9	2021	The protective effect of chrysin on sepsis-induced cardiac dysfunction was blocked by ZnPP, which is a HO-1 blocker.	zinc protoporphyrin	86-90	heme oxygenase 1	Homo sapiens	103-107
33788639-6	2021	ECs pre-treated with different concentrations RA and co-cultured with thapsigargin-induced ER stressed pancreatic beta-cells showed increased levels of Nrf2 and its downstream targets such as heme oxygenase-1 (HO-1) and NADPH-quinone oxidoreductase-1 (NQO-1), and reduction of ER stress evinced by the decreased levels of glucose-regulated protein (GRP) 78 and C/ERB homologous protein (CHOP).	Thapsigargin	70-82	heme oxygenase 1	Homo sapiens	210-214
33805292-4	2021	We systematically reviewed published evidence on HMOX1 polymorphisms in perinatal diseases and clarified their possible significant contribution to neonatal jaundice development, presumably due to their direct effect of inducing HO enzymatic activity in the bilirubin-producing pathway.	Bilirubin	258-267	heme oxygenase 1	Homo sapiens	49-54
33807391-6	2021	IL-8 mRNA expression was analyzed in saliva-stimulated THP-1 cells treated with CAPE and the heme oxygenase-1 (HO-1) inhibitor tin-protoporphyrin (SnPP).	tin protoporphyrin IX	127-145	heme oxygenase 1	Homo sapiens	93-109
33807391-6	2021	IL-8 mRNA expression was analyzed in saliva-stimulated THP-1 cells treated with CAPE and the heme oxygenase-1 (HO-1) inhibitor tin-protoporphyrin (SnPP).	tin protoporphyrin IX	127-145	heme oxygenase 1	Homo sapiens	111-115
33807391-11	2021	CAPE induced HO-1 expression and inhibited IKK2, IkappaBalpha, and NF-kappaB phosphorylation.	caffeic acid phenethyl ester	0-4	heme oxygenase 1	Homo sapiens	13-17
33807391-12	2021	Blocking HO-1 decreased the anti-inflammatory activity of CAPE.	caffeic acid phenethyl ester	58-62	heme oxygenase 1	Homo sapiens	9-13
33808635-7	2021	SiRNA-mediated knockdown of HO-1 significantly increased the oxidative stress induced by palmitate, whereas pre-treatment with SnCl2, a well-known HO-1 inducer, significantly decreased it.	Palmitates	89-98	heme oxygenase 1	Homo sapiens	28-32
33774859-5	2021	HO-1, Trx-1 and Nrf-2 expression levels significantly increased on pre-treatment with SS-31 compared with the H2 O2 group.	arginyl-2,'6'-dimethyltyrosyl-lysyl-phenylalaninamide	86-91	heme oxygenase 1	Homo sapiens	0-4
33770188-11	2021	We demonstrated that PSF enhanced Nrf2 activation and heme oxygenase-1 (HO-1) expression via extracellular signal-regulated kinase (ERK) and Akt signaling in HRMECs, which subsequently resulted in intracellular ROS scavenging.	Reactive Oxygen Species	211-214	heme oxygenase 1	Homo sapiens	72-76
33815094-0	2021	Elevated Heme Oxygenase-1 Correlates With Increased Brain Iron Deposition Measured by Quantitative Susceptibility Mapping and Decreased Hemoglobin in Patients With Parkinson"s Disease.	Iron	58-62	heme oxygenase 1	Homo sapiens	9-25
33815094-3	2021	Objective: To explore the association of the level of HO-1 with brain iron deposition and low level of HGB in PD.	Iron	70-74	heme oxygenase 1	Homo sapiens	54-58
33808635-8	2021	Moreover, SB203580, a selective p38 inhibitor, reduced HO-1 mRNA expression and increased palmitate-induced oxidative stress in HepG2 cells.	SB 203580	10-18	heme oxygenase 1	Homo sapiens	55-59
33815094-11	2021	There was a significantly positive correlation between the serum HO-1 concentration and iron deposition within SN, an inverse correlation between the serum HO-1 concentration and HGB level in PD patients.	Iron	88-92	heme oxygenase 1	Homo sapiens	65-69
33808635-9	2021	These results suggest that the HO-1-mediated anti-oxidative stress compensatory reaction plays an essential role against saturated fatty acid-induced lipotoxicity in the liver.	Fatty Acids	121-141	heme oxygenase 1	Homo sapiens	31-35
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Heme	64-68	heme oxygenase 1	Homo sapiens	0-16
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Heme	64-68	heme oxygenase 1	Homo sapiens	18-22
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Biliverdine	101-111	heme oxygenase 1	Homo sapiens	0-16
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Biliverdine	101-111	heme oxygenase 1	Homo sapiens	18-22
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	0-16
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	18-22
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Iron	139-143	heme oxygenase 1	Homo sapiens	0-16
33804125-1	2021	Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron.	Iron	139-143	heme oxygenase 1	Homo sapiens	18-22
33803317-5	2021	Heme oxygenase-1 (HO-1) is an iron-dependent cytoprotective enzyme that functions as the inducible form of HO.	Iron	30-34	heme oxygenase 1	Homo sapiens	0-16
33803317-5	2021	Heme oxygenase-1 (HO-1) is an iron-dependent cytoprotective enzyme that functions as the inducible form of HO.	Iron	30-34	heme oxygenase 1	Homo sapiens	18-22
33803289-7	2021	The DMF treatment was associated with no changes in virus replication; higher expressions of the antioxidant enzymes NQO1, GPX1, and HO-1 in the brain and PRDX1 and HO-2 in the spleen; lower levels of 8-OHdG and 3NT; a lower optical redox ratio.	Dimethyl Fumarate	4-7	heme oxygenase 1	Homo sapiens	133-137
33803317-6	2021	HO-1 and its metabolites carbon monoxide and biliverdin contribute towards the maintenance of redox homeostasis.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-4
33803317-6	2021	HO-1 and its metabolites carbon monoxide and biliverdin contribute towards the maintenance of redox homeostasis.	Biliverdine	45-55	heme oxygenase 1	Homo sapiens	0-4
33801315-8	2021	Moreover, we showed that onopordopicrin promoted the expression of the nuclear factor-erythroid-2-related factor 2 (Nrf2) downstream target protein heme oxygenase-1 (HO-1) in muscle cells.	onopordopicrin	25-39	heme oxygenase 1	Homo sapiens	148-164
33801315-8	2021	Moreover, we showed that onopordopicrin promoted the expression of the nuclear factor-erythroid-2-related factor 2 (Nrf2) downstream target protein heme oxygenase-1 (HO-1) in muscle cells.	onopordopicrin	25-39	heme oxygenase 1	Homo sapiens	166-170
33801315-9	2021	By using siRNA, we demonstrated that the inhibition of the expression of Nrf2 reduced the protective effect of onopordopicrin, indicating that the activation of the Nrf2/HO-1 signaling pathway mediates the antioxidant effect of onopordopicrin in primary human muscle cells.	onopordopicrin	111-125	heme oxygenase 1	Homo sapiens	170-174
33801315-9	2021	By using siRNA, we demonstrated that the inhibition of the expression of Nrf2 reduced the protective effect of onopordopicrin, indicating that the activation of the Nrf2/HO-1 signaling pathway mediates the antioxidant effect of onopordopicrin in primary human muscle cells.	onopordopicrin	228-242	heme oxygenase 1	Homo sapiens	170-174
33801351-4	2021	In this study, we found that 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2), one of the final products of COX-2, induced upregulation of vascular endothelial growth factor (VEGF) and capillary formation and migration through nuclear factor erythroid 2-related factor 2 (NRF2)-dependent heme oxygenase-1 (HO-1) induction in MCF-7 cells.	14-prostaglandin j2	46-65	heme oxygenase 1	Homo sapiens	287-303
33801351-4	2021	In this study, we found that 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2), one of the final products of COX-2, induced upregulation of vascular endothelial growth factor (VEGF) and capillary formation and migration through nuclear factor erythroid 2-related factor 2 (NRF2)-dependent heme oxygenase-1 (HO-1) induction in MCF-7 cells.	14-prostaglandin j2	46-65	heme oxygenase 1	Homo sapiens	305-309
33801351-4	2021	In this study, we found that 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2), one of the final products of COX-2, induced upregulation of vascular endothelial growth factor (VEGF) and capillary formation and migration through nuclear factor erythroid 2-related factor 2 (NRF2)-dependent heme oxygenase-1 (HO-1) induction in MCF-7 cells.	15-deoxy-delta(12,14)-prostaglandin J2	67-75	heme oxygenase 1	Homo sapiens	287-303
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Heme	79-83	heme oxygenase 1	Homo sapiens	0-16
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Heme	79-83	heme oxygenase 1	Homo sapiens	18-22
33801351-4	2021	In this study, we found that 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2), one of the final products of COX-2, induced upregulation of vascular endothelial growth factor (VEGF) and capillary formation and migration through nuclear factor erythroid 2-related factor 2 (NRF2)-dependent heme oxygenase-1 (HO-1) induction in MCF-7 cells.	15-deoxy-delta(12,14)-prostaglandin J2	67-75	heme oxygenase 1	Homo sapiens	305-309
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Heme	79-83	heme oxygenase 1	Homo sapiens	35-40
33801351-7	2021	In conclusion, the elevated levels of 15d-PGJ2 during inflammatory response activate VEGF expression through NRF2-driven induction of HO-1 in human breast cancer cells, proposing a novel mechanism underlying the oncogenic function of 15d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	38-46	heme oxygenase 1	Homo sapiens	134-138
33801351-7	2021	In conclusion, the elevated levels of 15d-PGJ2 during inflammatory response activate VEGF expression through NRF2-driven induction of HO-1 in human breast cancer cells, proposing a novel mechanism underlying the oncogenic function of 15d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	234-242	heme oxygenase 1	Homo sapiens	134-138
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	0-16
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Carbon Monoxide	135-150	heme oxygenase 1	Homo sapiens	15-31
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	18-22
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	35-40
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	ammonium ferrous sulfate	93-97	heme oxygenase 1	Homo sapiens	0-16
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	ammonium ferrous sulfate	93-97	heme oxygenase 1	Homo sapiens	18-22
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	ammonium ferrous sulfate	93-97	heme oxygenase 1	Homo sapiens	35-40
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Biliverdine	103-113	heme oxygenase 1	Homo sapiens	0-16
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Biliverdine	103-113	heme oxygenase 1	Homo sapiens	18-22
33804563-1	2021	Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin.	Biliverdine	103-113	heme oxygenase 1	Homo sapiens	35-40
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Heme	15-19	heme oxygenase 1	Homo sapiens	33-37
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Carbon Monoxide	135-150	heme oxygenase 1	Homo sapiens	33-37
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Biliverdine	152-162	heme oxygenase 1	Homo sapiens	15-31
33589574-5	2021	Our results showed that high expression of HO-1 and CD163 were detected in TAMs for 57.9% (73/126) and 61.9% (78/126) of the studied patients, and both of them were significantly associated with worse survival.	tams	75-79	heme oxygenase 1	Homo sapiens	43-47
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Biliverdine	152-162	heme oxygenase 1	Homo sapiens	33-37
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Bilirubin	163-172	heme oxygenase 1	Homo sapiens	15-31
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Bilirubin	163-172	heme oxygenase 1	Homo sapiens	33-37
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Iron	183-187	heme oxygenase 1	Homo sapiens	15-31
33587911-4	2021	In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli.	Iron	183-187	heme oxygenase 1	Homo sapiens	33-37
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	Heme	77-81	heme oxygenase 1	Homo sapiens	0-22
33232417-6	2020	Moreover, IOT also enhanced the expression of the GCLC, GCLM, HO-1, NQO1 and Trx-1 proteins, which mostly depends on the nuclear translation of Nrf2 and reduced expression of the Keap1 protein.	homoorientin	10-13	heme oxygenase 1	Homo sapiens	62-66
29662820-7	2018	Interestingly, the increased heme oxygenase 1 expression under hypoxic conditions was decreased by selenium treatment, whereas superoxide dismutase expression was increased in trophoblast cells by selenium treatment for 72 hours, regardless of hypoxia.	Selenium	99-107	heme oxygenase 1	Homo sapiens	29-45
33763175-7	2021	Furthermore, farrerol markedly activated Nrf2, thereby increasing the levels of antioxidant enzymes downstream of Nrf2, such as HO-1, NQO1, and GCLM.	farrerol	13-21	heme oxygenase 1	Homo sapiens	128-132
33763175-8	2021	Knockdown of Nrf2 with a specific siRNA successfully suppressed farrerol-mediated HO-1 transcription and partially abolished the cytoprotective effect on ARPE-19 cells.	farrerol	64-72	heme oxygenase 1	Homo sapiens	82-86
31624724-14	2019	We observed that genes encoding C/EBP delta, FOS-like antigen 1, c-Jun, and heme oxygenase-1 (HO-1) were most highly induced in the HCT116 cells following 15d-PGJ2 treatment.	15-deoxy-delta(12,14)-prostaglandin J2	155-163	heme oxygenase 1	Homo sapiens	76-92
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	Heme	77-81	heme oxygenase 1	Homo sapiens	35-40
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	Carbon Monoxide	87-102	heme oxygenase 1	Homo sapiens	0-22
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	Carbon Monoxide	87-102	heme oxygenase 1	Homo sapiens	35-40
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	ammonium ferrous sulfate	123-127	heme oxygenase 1	Homo sapiens	0-22
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	ammonium ferrous sulfate	123-127	heme oxygenase 1	Homo sapiens	35-40
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	Biliverdine	133-143	heme oxygenase 1	Homo sapiens	0-22
29628790-1	2018	Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties.	Biliverdine	133-143	heme oxygenase 1	Homo sapiens	35-40
29628790-6	2018	Metalloporphyrins are widely used in in vitro studies, however, they are unselective and may exert serious side effects including an increase in HMOX1 mRNA level.	Metalloporphyrins	0-17	heme oxygenase 1	Homo sapiens	145-150
25303561-5	2015	The "braking system" includes the protective pathways of haem oxygenase 1 (also referred as Hmox1 or HO-1) and cystathionine-gamma-lyase (also known as CSE or Cth), which generate carbon monoxide (CO) and hydrogen sulphide (H2S) respectively.	Carbon Monoxide	180-195	heme oxygenase 1	Homo sapiens	92-97
26331632-6	2015	Moreover, hydrogenation of the double bond of the functional alpha,beta-unsaturated carbonyl group of AVAs eliminated their effects on HO-1 expression, suggesting that this group is crucial for the antioxidant activity of AVAs.	avenanthramide-2C	102-106	heme oxygenase 1	Homo sapiens	135-139
26331632-6	2015	Moreover, hydrogenation of the double bond of the functional alpha,beta-unsaturated carbonyl group of AVAs eliminated their effects on HO-1 expression, suggesting that this group is crucial for the antioxidant activity of AVAs.	avenanthramide-2C	222-226	heme oxygenase 1	Homo sapiens	135-139
26629073-9	2015	Moreover, when HO-1 was interfered with siRNA, the effects of RLM on the levels of ROS and MMP were diminished, indicating that HO-1 induction was necessary for the function of RLM.	Reactive Oxygen Species	83-86	heme oxygenase 1	Homo sapiens	15-19
26629073-9	2015	Moreover, when HO-1 was interfered with siRNA, the effects of RLM on the levels of ROS and MMP were diminished, indicating that HO-1 induction was necessary for the function of RLM.	Reactive Oxygen Species	83-86	heme oxygenase 1	Homo sapiens	128-132
26629073-12	2015	RLM inhibits ROS production and elevates MMP, through the induction of HO-1 expression, in LECs under high glucose condition.	Glucose	107-114	heme oxygenase 1	Homo sapiens	71-75
25493608-10	2015	This could reflect decreases in cellular heme caused by the massive induction by arsenite of heme oxygenase mRNA (HMOX1; 68-fold increase), the rate-limiting enzyme in heme catabolism.	Heme	41-45	heme oxygenase 1	Homo sapiens	114-119
25493608-10	2015	This could reflect decreases in cellular heme caused by the massive induction by arsenite of heme oxygenase mRNA (HMOX1; 68-fold increase), the rate-limiting enzyme in heme catabolism.	arsenite	81-89	heme oxygenase 1	Homo sapiens	114-119
26331632-0	2015	Oat avenanthramides induce heme oxygenase-1 expression via Nrf2-mediated signaling in HK-2 cells.	avenanthramide-2C	4-19	heme oxygenase 1	Homo sapiens	27-43
26331632-2	2015	Here, we investigated whether AVAs affect heme oxygenase-1 (HO-1) expression through the activation of Nrf2 translocation.	avenanthramide-2C	30-34	heme oxygenase 1	Homo sapiens	42-58
26331632-2	2015	Here, we investigated whether AVAs affect heme oxygenase-1 (HO-1) expression through the activation of Nrf2 translocation.	avenanthramide-2C	30-34	heme oxygenase 1	Homo sapiens	60-64
26331632-4	2015	Furthermore, we found that AVA-induced HO-1 expression is mediated by Nrf2 translocation.	avenanthramide-2C	27-30	heme oxygenase 1	Homo sapiens	39-43
26331632-5	2015	The addition of N-acetylcysteine (NAC), but not specific inhibitors of p38 (SB202190), PI3K (LY294002), and MEK1 (PD098059) attenuated AVA-induced HO-1 expression, demonstrating an important role for reactive oxygen species, but not PI3K or MAPK activation, in activating the HO-1 pathway.	Acetylcysteine	16-32	heme oxygenase 1	Homo sapiens	147-151
26331632-5	2015	The addition of N-acetylcysteine (NAC), but not specific inhibitors of p38 (SB202190), PI3K (LY294002), and MEK1 (PD098059) attenuated AVA-induced HO-1 expression, demonstrating an important role for reactive oxygen species, but not PI3K or MAPK activation, in activating the HO-1 pathway.	Acetylcysteine	16-32	heme oxygenase 1	Homo sapiens	276-280
25303561-5	2015	The "braking system" includes the protective pathways of haem oxygenase 1 (also referred as Hmox1 or HO-1) and cystathionine-gamma-lyase (also known as CSE or Cth), which generate carbon monoxide (CO) and hydrogen sulphide (H2S) respectively.	Carbon Monoxide	197-199	heme oxygenase 1	Homo sapiens	92-97
25303561-5	2015	The "braking system" includes the protective pathways of haem oxygenase 1 (also referred as Hmox1 or HO-1) and cystathionine-gamma-lyase (also known as CSE or Cth), which generate carbon monoxide (CO) and hydrogen sulphide (H2S) respectively.	Hydrogen Sulfide	205-222	heme oxygenase 1	Homo sapiens	92-97
25303561-5	2015	The "braking system" includes the protective pathways of haem oxygenase 1 (also referred as Hmox1 or HO-1) and cystathionine-gamma-lyase (also known as CSE or Cth), which generate carbon monoxide (CO) and hydrogen sulphide (H2S) respectively.	Hydrogen Sulfide	224-227	heme oxygenase 1	Homo sapiens	92-97
19161347-1	2009	HO-1 (haem oxygenase 1) is an essential antioxidant enzyme in the cell that exerts its effects through removal of pro-oxidant haem groups and the formation of antioxidant molecules and carbon monoxide.	Carbon Monoxide	185-200	heme oxygenase 1	Homo sapiens	0-22
19161347-2	2009	The electrophilic cyclopentenone 15d-PGJ2 (15-deoxy-Delta(12,14)-prostaglandin J2) induces the expression of HO-1 protein through the covalent modification of protein thiols.	cyclopentenone 15d-pgj2	18-41	heme oxygenase 1	Homo sapiens	109-113
19161347-7	2009	IBTP had no effect on basal HO-1 levels, but effectively blocked HO-1 induction by a variety of reagents including haemin, iodoacetamide and 15d-PGJ2.	Iodoacetamide	123-136	heme oxygenase 1	Homo sapiens	65-69
19161347-7	2009	IBTP had no effect on basal HO-1 levels, but effectively blocked HO-1 induction by a variety of reagents including haemin, iodoacetamide and 15d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	141-149	heme oxygenase 1	Homo sapiens	65-69
19161347-2	2009	The electrophilic cyclopentenone 15d-PGJ2 (15-deoxy-Delta(12,14)-prostaglandin J2) induces the expression of HO-1 protein through the covalent modification of protein thiols.	15-deoxy-delta(12,14)-prostaglandin J2	43-81	heme oxygenase 1	Homo sapiens	109-113
19161347-9	2009	However, IBTP prevented the 15d-PGJ2-dependent increases in HO-1 mRNA and protein.	ibtp	9-13	heme oxygenase 1	Homo sapiens	60-64
19161347-12	2009	In addition, IBTP significantly enhanced the toxicity of high concentrations of 15d-PGJ2, suggesting that loss of mitochondrial control of HO-1 leads to increased susceptibility to electrophilic stress in endothelial cells.	ibtp	13-17	heme oxygenase 1	Homo sapiens	139-143
19161347-2	2009	The electrophilic cyclopentenone 15d-PGJ2 (15-deoxy-Delta(12,14)-prostaglandin J2) induces the expression of HO-1 protein through the covalent modification of protein thiols.	Sulfhydryl Compounds	167-173	heme oxygenase 1	Homo sapiens	109-113
19161347-12	2009	In addition, IBTP significantly enhanced the toxicity of high concentrations of 15d-PGJ2, suggesting that loss of mitochondrial control of HO-1 leads to increased susceptibility to electrophilic stress in endothelial cells.	15-deoxy-delta(12,14)-prostaglandin J2	80-88	heme oxygenase 1	Homo sapiens	139-143
19161347-3	2009	It has been shown that specific thiol residues of the redox-sensor Keap1 (Kelch-like ECH-associated protein 1) are modified by 15d-PGJ2, leading to activation of the transcription factor Nrf-2 (nuclear factor-erythroid 2 p45 subunit-related factor 2) and up-regulation of genes under control of the electrophile-response element, including HO-1.	Sulfhydryl Compounds	32-37	heme oxygenase 1	Homo sapiens	340-344
19161347-6	2009	In order to determine the role of mitochondrial protein thiol modification in HO-1 induction, we used the mitochondrial-targeted thiol-reactive compound IBTP [(4-iodobutyl)triphenylphosphonium].	ibtp	153-157	heme oxygenase 1	Homo sapiens	78-82
19161347-7	2009	IBTP had no effect on basal HO-1 levels, but effectively blocked HO-1 induction by a variety of reagents including haemin, iodoacetamide and 15d-PGJ2.	ibtp	0-4	heme oxygenase 1	Homo sapiens	65-69
19161347-7	2009	IBTP had no effect on basal HO-1 levels, but effectively blocked HO-1 induction by a variety of reagents including haemin, iodoacetamide and 15d-PGJ2.	Hemin	115-121	heme oxygenase 1	Homo sapiens	65-69
34919942-0	2022	Catalpol alleviates myocardial ischemia reperfusion injury by activating the Nrf2/HO-1 signaling pathway.	catalpol	0-8	heme oxygenase 1	Homo sapiens	82-86
12709575-4	2003	The research was developed, switching off inducible nitric oxide synthase (iNOS) expression through antisense oligonucleotide transfection by studying the possible coregulation in the expression of HSP32 (also named HO-1), HSP70, and iNOS and their involvement in the induction of DNA damage.	Oligonucleotides	110-125	heme oxygenase 1	Homo sapiens	198-203
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	tin protoporphyrin IX	10-17	heme oxygenase 1	Homo sapiens	106-122
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	tin protoporphyrin IX	10-17	heme oxygenase 1	Homo sapiens	124-128
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	cdt	80-83	heme oxygenase 1	Homo sapiens	106-122
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	cdt	80-83	heme oxygenase 1	Homo sapiens	124-128
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	Heme	139-143	heme oxygenase 1	Homo sapiens	106-122
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	Heme	139-143	heme oxygenase 1	Homo sapiens	124-128
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	Bilirubin	174-183	heme oxygenase 1	Homo sapiens	106-122
34863556-7	2022	Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin.	Bilirubin	174-183	heme oxygenase 1	Homo sapiens	124-128
19497345-8	2009	Interestingly, palmatine increased heme oxygenase (HO)-1 induction in human aortic endothelial cells.	palmatine	15-24	heme oxygenase 1	Homo sapiens	35-56
34920080-10	2022	Quercetin, an HO-1 inducer, reduced syncytia formation and spike protein expression.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	14-18
34919942-11	2022	CONCLUSION: In summary, the findings suggest that Catalpol exerted significant cardioprotective effects following myocardial ischemia, possibly through the activation of the Nrf2/HO-1 signaling pathway.	catalpol	50-58	heme oxygenase 1	Homo sapiens	179-183
34953799-0	2022	Overexpressed mitogen-and stress-activated protein kinase 1 promotes the resistance of cytarabine in acute myeloid leukemia through brahma related gene 1-mediated upregulation of heme oxygenase-1.	Cytarabine	87-97	heme oxygenase 1	Homo sapiens	179-195
34614244-8	2022	Suppression of high glucose-induced cell proliferation by lutein was not associated with apoptosis induction, but it was linked with inhibition of hyperglycemia-mediated elevated ROS and upregulated expression of high glucose-mediated repressed heme oxygenase 1 (HO1).	Glucose	218-225	heme oxygenase 1	Homo sapiens	245-261
34953799-10	2022	However, the increased cell sensitivity induced by MSK1 downregulation was reversed by the induction of HO-1 inducer Hemin.	Hemin	117-122	heme oxygenase 1	Homo sapiens	104-108
34614244-8	2022	Suppression of high glucose-induced cell proliferation by lutein was not associated with apoptosis induction, but it was linked with inhibition of hyperglycemia-mediated elevated ROS and upregulated expression of high glucose-mediated repressed heme oxygenase 1 (HO1).	Glucose	218-225	heme oxygenase 1	Homo sapiens	263-266
34614244-8	2022	Suppression of high glucose-induced cell proliferation by lutein was not associated with apoptosis induction, but it was linked with inhibition of hyperglycemia-mediated elevated ROS and upregulated expression of high glucose-mediated repressed heme oxygenase 1 (HO1).	Glucose	20-27	heme oxygenase 1	Homo sapiens	245-261
34614244-8	2022	Suppression of high glucose-induced cell proliferation by lutein was not associated with apoptosis induction, but it was linked with inhibition of hyperglycemia-mediated elevated ROS and upregulated expression of high glucose-mediated repressed heme oxygenase 1 (HO1).	Glucose	20-27	heme oxygenase 1	Homo sapiens	263-266
34129218-0	2022	Astaxanthin Relieves Busulfan-Induced Oxidative Apoptosis in Cultured Human Spermatogonial Stem Cells by Activating the Nrf-2/HO-1 pathway.	astaxanthine	0-11	heme oxygenase 1	Homo sapiens	126-130
34613549-7	2022	The results showed that oleuropein significantly decreased levels of the inflammatory mediator cyclooxygenase-2 and increased anti-inflammatory protein HO-1 expression.	oleuropein	24-34	heme oxygenase 1	Homo sapiens	152-156
34565648-0	2022	Corrigendum to "Neuroprotective effect of phosphocreatine on oxidative stress and mitochondrial dysfunction induced apoptosis in vitro and in vivo: Involvement of dual PI3K/Akt and Nrf2/HO-1 pathways" (Free Radic.	Phosphocreatine	42-57	heme oxygenase 1	Homo sapiens	186-190
34664771-0	2022	Bisphenol A induced apoptosis via oxidative stress generation involved Nrf2/HO-1 pathway and mitochondrial dependent pathways in human retinal pigment epithelium (ARPE-19) cells.	bis(4-hydroxyphenyl)sulfone	0-9	heme oxygenase 1	Homo sapiens	76-80
34742568-12	2022	Mechanistically, mitoquinone was found to enhance the activity of Nrf2 and heme oxygenase-1 and to induce nuclear translocation of Nrf2 in human peritoneal mesothelial cells.	mitoquinone	17-28	heme oxygenase 1	Homo sapiens	75-91
34813774-5	2022	Interestingly, salidroside partly reversed DHT mediated effects, via stimulation of nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway and the downstream antioxidant proteins heme oxygenase-1(HO-1) and quinine oxidoreductase 1(NQO1).	rhodioloside	15-26	heme oxygenase 1	Homo sapiens	210-214
34813774-5	2022	Interestingly, salidroside partly reversed DHT mediated effects, via stimulation of nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway and the downstream antioxidant proteins heme oxygenase-1(HO-1) and quinine oxidoreductase 1(NQO1).	Dihydrotestosterone	43-46	heme oxygenase 1	Homo sapiens	210-214
34813774-7	2022	Mechanistically, AMP-activated protein kinase (AMPK) was identified to be the upstream signaling involved in salidroside-induced Nrf2 activation, as silencing of AMPK partly prevented the upregulation of Nrf2 and the downstream proteins HO-1 and NQO1.	rhodioloside	109-120	heme oxygenase 1	Homo sapiens	237-241
34664771-9	2022	Our results showed that expression of HO-1 and Nrf2 suppressed by BPA.	bisphenol A	66-69	heme oxygenase 1	Homo sapiens	38-42
34664771-13	2022	Taken together, these results suggest that BPA induced ARPE-19 cells via oxidative stress, which was associated with down regulated Nrf2/HO-1 pathway, and the mitochondria dependent apoptotic signaling pathway.	bisphenol A	43-46	heme oxygenase 1	Homo sapiens	137-141
34848368-12	2022	Probenecid, a well-known UA-lowering drug, significantly suppressed the activation of TXNIP and Nrf2/HO-1 signaling.	Probenecid	0-10	heme oxygenase 1	Homo sapiens	101-105
34716926-0	2022	Surfactin reduces particulate matter-induced VCAM-1-dependent monocyte adhesion in human gingival fibroblasts by increasing Nrf2-dependent HO-1 expression.	surfactin peptide	0-9	heme oxygenase 1	Homo sapiens	139-143
34716926-3	2022	As surfactin has potential to induce Nrf2 activation and HO-1 expression, this study aimed to investigate the anti-inflammatory effects of surfactin on PM-exposed human gingival fibroblasts (HGFs) and signaling pathways engaged by surfactin.	surfactin peptide	3-12	heme oxygenase 1	Homo sapiens	57-61
34716926-3	2022	As surfactin has potential to induce Nrf2 activation and HO-1 expression, this study aimed to investigate the anti-inflammatory effects of surfactin on PM-exposed human gingival fibroblasts (HGFs) and signaling pathways engaged by surfactin.	surfactin peptide	139-148	heme oxygenase 1	Homo sapiens	57-61
34716926-3	2022	As surfactin has potential to induce Nrf2 activation and HO-1 expression, this study aimed to investigate the anti-inflammatory effects of surfactin on PM-exposed human gingival fibroblasts (HGFs) and signaling pathways engaged by surfactin.	surfactin peptide	231-240	heme oxygenase 1	Homo sapiens	57-61
34906793-7	2022	Our study revealed that m-beta-CoV upregulated Park7, RelA, Nrf2, and Hmox1 transcripts involved in ROS production and antioxidant pathways, describing the possible nexus between oxidative pathways, MMPs, and TIMP in m-beta-CoV-induced neuroinflammation.	ros	100-103	heme oxygenase 1	Homo sapiens	70-75
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Heme	76-80	heme oxygenase 1	Homo sapiens	0-16
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Heme	76-80	heme oxygenase 1	Homo sapiens	18-22
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Iron	91-95	heme oxygenase 1	Homo sapiens	0-16
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Iron	91-95	heme oxygenase 1	Homo sapiens	18-22
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Carbon Monoxide	97-112	heme oxygenase 1	Homo sapiens	0-16
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Carbon Monoxide	97-112	heme oxygenase 1	Homo sapiens	18-22
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Biliverdine	117-127	heme oxygenase 1	Homo sapiens	0-16
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Biliverdine	117-127	heme oxygenase 1	Homo sapiens	18-22
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Bilirubin	166-175	heme oxygenase 1	Homo sapiens	0-16
34841438-1	2022	Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin.	Bilirubin	166-175	heme oxygenase 1	Homo sapiens	18-22
34841438-4	2022	In the 5"-non-coding region of the HO-1 gene, there are two polymorphic sites, namely the (GT)n dinucleotide and T(-413)A single nucleotide polymorphism sites, which regulate the transcriptional activity of HO-1.	gt)n dinucleotide	91-108	heme oxygenase 1	Homo sapiens	35-39
34841438-4	2022	In the 5"-non-coding region of the HO-1 gene, there are two polymorphic sites, namely the (GT)n dinucleotide and T(-413)A single nucleotide polymorphism sites, which regulate the transcriptional activity of HO-1.	gt)n dinucleotide	91-108	heme oxygenase 1	Homo sapiens	207-211
34964128-0	2021	Cyanidin-3-glucoside protects against high glucose-induced injury in human nucleus pulposus cells by regulating the Nrf2/HO-1 signaling.	cyanidin-3-o-glucoside	0-20	heme oxygenase 1	Homo sapiens	121-125
34927515-8	2022	Furthermore, 5-ALA is a metabolic precursor of heme, which is a potent inducer of the enzyme heme oxygenase-1, the levels of which are decreased in patients with severe COVID-19.	5-amino levulinic acid	13-18	heme oxygenase 1	Homo sapiens	93-109
34927515-8	2022	Furthermore, 5-ALA is a metabolic precursor of heme, which is a potent inducer of the enzyme heme oxygenase-1, the levels of which are decreased in patients with severe COVID-19.	Heme	47-51	heme oxygenase 1	Homo sapiens	93-109
34927515-9	2022	Oral administration of 5-ALA/SFC induced heme oxygenase-1 in the peripheral blood of uninfected healthy individuals.	5-amino levulinic acid	23-28	heme oxygenase 1	Homo sapiens	41-57
34927515-9	2022	Oral administration of 5-ALA/SFC induced heme oxygenase-1 in the peripheral blood of uninfected healthy individuals.	SFC	29-32	heme oxygenase 1	Homo sapiens	41-57
34964128-15	2021	Summarily, C3G exerted a protective effect on ROS-mediated cellular damage in HNPCs under HG condition, which was attributed to the induction of the Nrf2/HO-1 signaling pathway.	ros	46-49	heme oxygenase 1	Homo sapiens	154-158
34973332-2	2022	Humans express two isoforms of HO: the inducible HO-1, which is up-regulated in response to various stressors, including excess heme, and the constitutive HO-2.	Heme	128-132	heme oxygenase 1	Homo sapiens	49-53
34973332-8	2022	When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation.	Heme	5-9	heme oxygenase 1	Homo sapiens	24-28
34973332-8	2022	When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation.	Heme	5-9	heme oxygenase 1	Homo sapiens	58-62
34973332-8	2022	When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation.	Heme	91-95	heme oxygenase 1	Homo sapiens	58-62
34959690-0	2021	From Far West to East: Joining the Molecular Architecture of Imidazole-like Ligands in HO-1 Complexes.	imidazole	61-70	heme oxygenase 1	Homo sapiens	87-91
34874275-0	2021	HIF1A-induced heme oxygenase 1 promotes the survival of decidual stromal cells against excess heme-mediated oxidative stress.	Heme	94-98	heme oxygenase 1	Homo sapiens	14-30
34874275-1	2021	Heme oxygenase 1 (HO-1, encoded by the HMOX1 gene), is the rate-limiting enzyme that catalyzes heme degradation, and it has been reported to exert antioxidative effects.	Heme	95-99	heme oxygenase 1	Homo sapiens	0-16
34874275-1	2021	Heme oxygenase 1 (HO-1, encoded by the HMOX1 gene), is the rate-limiting enzyme that catalyzes heme degradation, and it has been reported to exert antioxidative effects.	Heme	95-99	heme oxygenase 1	Homo sapiens	18-22
34874275-1	2021	Heme oxygenase 1 (HO-1, encoded by the HMOX1 gene), is the rate-limiting enzyme that catalyzes heme degradation, and it has been reported to exert antioxidative effects.	Heme	95-99	heme oxygenase 1	Homo sapiens	39-44
34874275-6	2021	However, addition of the competitive HO-1 inhibitor ZnPP resulted in an increase in HIF1A expression.	zinc protoporphyrin	52-56	heme oxygenase 1	Homo sapiens	37-41
34874275-8	2021	As an HO-1 inducer, cobalt protoporphyrin IX (CoPP) decreased ROS production and significantly reversed the inhibitory effect of H2O2 on cell viability.	cobaltiprotoporphyrin	20-44	heme oxygenase 1	Homo sapiens	6-10
34874275-8	2021	As an HO-1 inducer, cobalt protoporphyrin IX (CoPP) decreased ROS production and significantly reversed the inhibitory effect of H2O2 on cell viability.	cobaltiprotoporphyrin	46-50	heme oxygenase 1	Homo sapiens	6-10
34874275-8	2021	As an HO-1 inducer, cobalt protoporphyrin IX (CoPP) decreased ROS production and significantly reversed the inhibitory effect of H2O2 on cell viability.	Reactive Oxygen Species	62-65	heme oxygenase 1	Homo sapiens	6-10
34874275-8	2021	As an HO-1 inducer, cobalt protoporphyrin IX (CoPP) decreased ROS production and significantly reversed the inhibitory effect of H2O2 on cell viability.	Hydrogen Peroxide	129-133	heme oxygenase 1	Homo sapiens	6-10
34874275-10	2021	This study suggests that the upregulation of HO-1 expression via HIF1A protects DSCs against excessive heme-mediated oxidative stress.	Heme	103-107	heme oxygenase 1	Homo sapiens	45-49
34496009-6	2021	HO-1 inhibition by tin porphyrin eliminated ex vivo HIV-1 restriction.	tin porphyrin	19-32	heme oxygenase 1	Homo sapiens	0-4
34954677-7	2021	In addition, BPA increased the levels of intracellular reactive oxygen species (ROS) and malondialdehyde (MDA) and decreased antioxidant enzymes nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) levels, resulting in oxidative stress.	bisphenol A	13-16	heme oxygenase 1	Homo sapiens	191-207
34954677-7	2021	In addition, BPA increased the levels of intracellular reactive oxygen species (ROS) and malondialdehyde (MDA) and decreased antioxidant enzymes nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) levels, resulting in oxidative stress.	bisphenol A	13-16	heme oxygenase 1	Homo sapiens	209-213
34928467-3	2021	This study aimed to investigate the predictive value of the total bilirubin level, a marker of heme oxygenase-1 enzyme activity, in determining myocarditis in patients with COVID-19.	Bilirubin	66-75	heme oxygenase 1	Homo sapiens	95-111
34946766-0	2021	Nanogold Particles Suppresses 5-Flurouracil-Induced Renal Injury: An Insight into the Modulation of Nrf-2 and Its Downstream Targets, HO-1 and gamma-GCS.	5-flurouracil	30-43	heme oxygenase 1	Homo sapiens	134-138
34912465-0	2021	Shikonin Alleviates Endothelial Cell Injury Induced by ox-LDL via AMPK/Nrf2/HO-1 Signaling Pathway.	shikonin	0-8	heme oxygenase 1	Homo sapiens	76-80
34912465-7	2021	Compared to the ox-LDL group, SKN treatment improves cell viability, alleviates cell apoptosis and oxidative stress injury, and upregulates the protein levels of p-AMPK, Nrf2, and HO-1.	shikonin	30-33	heme oxygenase 1	Homo sapiens	180-184
34943041-2	2021	The parasite regulates the host immune system by inducing a strong Th2 and regulatory T (Treg) cell immune response through mechanisms that might involve the expression or activity of heme-oxygenase-1 (HO-1), the rate-limiting enzyme in the catabolism of free heme that also has immunoregulatory and antioxidant properties.	th2	67-70	heme oxygenase 1	Homo sapiens	202-206
34912465-8	2021	Compound C, si-Nrf2, and si-HO-1 administration inhibits the AMPK/Nrf2/HO-1 signaling pathway, increases ROS generation, and inhibits the antagonistic effect of SKN on ox-LDL-induced HUVECs damage.	Silicon	12-14	heme oxygenase 1	Homo sapiens	71-75
34912465-8	2021	Compound C, si-Nrf2, and si-HO-1 administration inhibits the AMPK/Nrf2/HO-1 signaling pathway, increases ROS generation, and inhibits the antagonistic effect of SKN on ox-LDL-induced HUVECs damage.	Reactive Oxygen Species	105-108	heme oxygenase 1	Homo sapiens	28-32
34912465-8	2021	Compound C, si-Nrf2, and si-HO-1 administration inhibits the AMPK/Nrf2/HO-1 signaling pathway, increases ROS generation, and inhibits the antagonistic effect of SKN on ox-LDL-induced HUVECs damage.	shikonin	161-164	heme oxygenase 1	Homo sapiens	28-32
34866353-14	2022	Heme was the most abundant metabolite in degenerated regions, whereas Heme oxygenase-1 (HO-1), which catabolizes heme, was found in intact regions.	Heme	113-117	heme oxygenase 1	Homo sapiens	70-86
34866353-14	2022	Heme was the most abundant metabolite in degenerated regions, whereas Heme oxygenase-1 (HO-1), which catabolizes heme, was found in intact regions.	Heme	113-117	heme oxygenase 1	Homo sapiens	88-92
34866353-15	2022	Higher HO-1 levels correlated with lower heme accumulation.	Heme	41-45	heme oxygenase 1	Homo sapiens	7-11
34943041-2	2021	The parasite regulates the host immune system by inducing a strong Th2 and regulatory T (Treg) cell immune response through mechanisms that might involve the expression or activity of heme-oxygenase-1 (HO-1), the rate-limiting enzyme in the catabolism of free heme that also has immunoregulatory and antioxidant properties.	Heme	260-264	heme oxygenase 1	Homo sapiens	202-206
34634993-1	2021	BACKGROUND: Heme oxygenase (HO)-1 is a rate-limiting enzyme for degrading heme into carbon monoxide.	Heme	74-78	heme oxygenase 1	Homo sapiens	12-33
34940692-7	2021	EEB decreased UVB-induced reactive oxygen species (ROS) generation by upregulating glutathione peroxidase 1 (GPx1) and heme oxygenase-1 (HO-1) expression via nuclear factor erythroid-2-related factor 2 (Nrf2) activation in Hs68 cells.	Reactive Oxygen Species	26-49	heme oxygenase 1	Homo sapiens	119-135
34940692-7	2021	EEB decreased UVB-induced reactive oxygen species (ROS) generation by upregulating glutathione peroxidase 1 (GPx1) and heme oxygenase-1 (HO-1) expression via nuclear factor erythroid-2-related factor 2 (Nrf2) activation in Hs68 cells.	Reactive Oxygen Species	26-49	heme oxygenase 1	Homo sapiens	137-141
34940692-7	2021	EEB decreased UVB-induced reactive oxygen species (ROS) generation by upregulating glutathione peroxidase 1 (GPx1) and heme oxygenase-1 (HO-1) expression via nuclear factor erythroid-2-related factor 2 (Nrf2) activation in Hs68 cells.	Reactive Oxygen Species	51-54	heme oxygenase 1	Homo sapiens	119-135
34940692-7	2021	EEB decreased UVB-induced reactive oxygen species (ROS) generation by upregulating glutathione peroxidase 1 (GPx1) and heme oxygenase-1 (HO-1) expression via nuclear factor erythroid-2-related factor 2 (Nrf2) activation in Hs68 cells.	Reactive Oxygen Species	51-54	heme oxygenase 1	Homo sapiens	137-141
34634993-1	2021	BACKGROUND: Heme oxygenase (HO)-1 is a rate-limiting enzyme for degrading heme into carbon monoxide.	Carbon Monoxide	84-99	heme oxygenase 1	Homo sapiens	12-33
34520103-0	2021	Fenofibrate inhibits hypoxia-inducible factor-1 alpha and carbonic anhydrase expression through activation of AMP-activated protein kinase/HO-1/Sirt1 pathway in glioblastoma cells.	Fenofibrate	0-11	heme oxygenase 1	Homo sapiens	139-143
34710668-0	2021	Growing the molecular architecture of imidazole-like ligands in HO-1 complexes.	imidazole	38-47	heme oxygenase 1	Homo sapiens	64-68
34520103-7	2021	Moreover, fenofibrate-inhibited HIF-1alpha expression is mediated by HO-1 activation in GBM cells through the AMP-activated protein kinase (AMPK) pathway.	Fenofibrate	10-21	heme oxygenase 1	Homo sapiens	69-73
34520103-8	2021	In addition, fenofibrate-enhanced HO-1 upregulation activates SIRT1 and leads to subsequent accumulation of SIRT1 in the nucleus, which further promotes HIF-1alpha deacetylation and inhibits CA9 expression.	Fenofibrate	13-24	heme oxygenase 1	Homo sapiens	34-38
34342160-0	2021	Pterostilbene suppresses oxidative stress and allergic airway inflammation through AMPK/Sirt1 and Nrf2/HO-1 pathways.	pterostilbene	0-13	heme oxygenase 1	Homo sapiens	103-107
34342160-4	2021	Herein, we aim to explore the pharmacological effects of Pts on oxidative stress and allergic inflammatory response as well as the mechanism involving AMPK/Sirt1 and Nrf2/HO-1 pathways.	pterostilbene	57-60	heme oxygenase 1	Homo sapiens	171-175
34633051-0	2021	(Corrigendum) Synergistic cardioprotective effects of Danshensu and hydroxysafflor yellow A against myocardial ischemia-reperfusion injury are mediated through the Akt/Nrf2/HO-1 pathway.	danshensu and hydroxysafflor yellow a	54-91	heme oxygenase 1	Homo sapiens	173-177
34167427-0	2021	Novel mutual prodrug of 5-fluorouracil and heme oxygenase-1 inhibitor (5-FU/HO-1 hybrid): design and preliminary in vitro evaluation.	Fluorouracil	24-38	heme oxygenase 1	Homo sapiens	43-59
34943103-2	2021	The aim of our study was to assess the role of bilirubin, and the heme oxygenase 1 (HMOX1) and bilirubin UDP-glucuronosyl transferase (UGT1A1) promoter gene variants, which are involved in bilirubin homeostasis, in the NAFLD development in adult patients.	Bilirubin	189-198	heme oxygenase 1	Homo sapiens	66-82
34943103-2	2021	The aim of our study was to assess the role of bilirubin, and the heme oxygenase 1 (HMOX1) and bilirubin UDP-glucuronosyl transferase (UGT1A1) promoter gene variants, which are involved in bilirubin homeostasis, in the NAFLD development in adult patients.	Bilirubin	189-198	heme oxygenase 1	Homo sapiens	84-89
34943103-5	2021	The (GT)n/(TA)n dinucleotide variations in HMOX1/UGT1A1 gene promoters, respectively, were analyzed by fragment analysis.	Nitrogen	8-9	heme oxygenase 1	Homo sapiens	43-48
34943103-5	2021	The (GT)n/(TA)n dinucleotide variations in HMOX1/UGT1A1 gene promoters, respectively, were analyzed by fragment analysis.	(ta)n dinucleotide	10-28	heme oxygenase 1	Homo sapiens	43-48
34943105-10	2021	CONCLUSION: In patients with CCS, higher plasma HO-1 levels are associated with lower cholesterol and a more diffuse but mainly non-obstructive coronary atherosclerosis, confirming a potential role for the Nrf2/HO-1 pathway as a protective feedback.	Cholesterol	86-97	heme oxygenase 1	Homo sapiens	48-52
34167427-0	2021	Novel mutual prodrug of 5-fluorouracil and heme oxygenase-1 inhibitor (5-FU/HO-1 hybrid): design and preliminary in vitro evaluation.	Fluorouracil	24-38	heme oxygenase 1	Homo sapiens	76-80
34167427-0	2021	Novel mutual prodrug of 5-fluorouracil and heme oxygenase-1 inhibitor (5-FU/HO-1 hybrid): design and preliminary in vitro evaluation.	Fluorouracil	71-75	heme oxygenase 1	Homo sapiens	43-59
34167427-0	2021	Novel mutual prodrug of 5-fluorouracil and heme oxygenase-1 inhibitor (5-FU/HO-1 hybrid): design and preliminary in vitro evaluation.	Fluorouracil	71-75	heme oxygenase 1	Homo sapiens	76-80
34167427-1	2021	In this work, the first mutual prodrug of 5-fluorouracil and heme oxygenase1 inhibitor (5-FU/HO-1 hybrid) has been designed, synthesised, and evaluated for its in vitro chemical and enzymatic hydrolysis stability.	Fluorouracil	42-56	heme oxygenase 1	Homo sapiens	61-76
34167427-1	2021	In this work, the first mutual prodrug of 5-fluorouracil and heme oxygenase1 inhibitor (5-FU/HO-1 hybrid) has been designed, synthesised, and evaluated for its in vitro chemical and enzymatic hydrolysis stability.	Fluorouracil	42-56	heme oxygenase 1	Homo sapiens	93-97
34167427-1	2021	In this work, the first mutual prodrug of 5-fluorouracil and heme oxygenase1 inhibitor (5-FU/HO-1 hybrid) has been designed, synthesised, and evaluated for its in vitro chemical and enzymatic hydrolysis stability.	Fluorouracil	88-92	heme oxygenase 1	Homo sapiens	61-76
34167427-1	2021	In this work, the first mutual prodrug of 5-fluorouracil and heme oxygenase1 inhibitor (5-FU/HO-1 hybrid) has been designed, synthesised, and evaluated for its in vitro chemical and enzymatic hydrolysis stability.	Fluorouracil	88-92	heme oxygenase 1	Homo sapiens	93-97
34167427-6	2021	Altogether our results served as an initial proof-of-concept to develop 5-FU/HO-1 mutual prodrugs as potential novel anticancer agents.	Fluorouracil	72-76	heme oxygenase 1	Homo sapiens	77-81
34338973-0	2021	Pinocembrin pretreatment counteracts the chlorpyrifos-induced HO-1 downregulation, mitochondrial dysfunction, and inflammation in the SH-SY5Y cells.	pinocembrin	0-11	heme oxygenase 1	Homo sapiens	62-66
34663512-3	2021	In this study, the effects of PGG on Nrf2/HO-1 and JAK2/STAT3 signaling were explored in AGE-stimulated mesangial cells.	pentagalloylglucose	30-33	heme oxygenase 1	Homo sapiens	42-46
34663512-5	2021	Our results showed that PGG significantly inhibited AGE-induced ROS generation and activated AGE-inhibited Nrf2/HO-1 signaling.	pentagalloylglucose	24-27	heme oxygenase 1	Homo sapiens	112-116
34663512-7	2021	Furthermore, ML385 suppressed Nrf2/HO-1 signaling, elevated ROS and cytokine production, and activated JAK2/STAT3 cascade were reversed by PGG.	ML385	13-18	heme oxygenase 1	Homo sapiens	35-39
34663512-7	2021	Furthermore, ML385 suppressed Nrf2/HO-1 signaling, elevated ROS and cytokine production, and activated JAK2/STAT3 cascade were reversed by PGG.	pentagalloylglucose	139-142	heme oxygenase 1	Homo sapiens	35-39
34663512-8	2021	These findings indicate that PGG inhibits the JAK2/STAT3 cascade by activating Nrf2/HO-1 signaling.	pentagalloylglucose	29-32	heme oxygenase 1	Homo sapiens	84-88
34338973-0	2021	Pinocembrin pretreatment counteracts the chlorpyrifos-induced HO-1 downregulation, mitochondrial dysfunction, and inflammation in the SH-SY5Y cells.	Chlorpyrifos	41-53	heme oxygenase 1	Homo sapiens	62-66
34338973-8	2021	Silencing of Nrf2 or inhibition of HO-1 suppressed the PB-induced effects in the CPF-challenged cells.	pinocembrin	55-57	heme oxygenase 1	Homo sapiens	35-39
34338973-9	2021	Thus, PB promoted beneficial effects by a mechanism dependent on the Nrf2/HO-1/CO + BR axis in the CPF-treated cells.	pinocembrin	6-8	heme oxygenase 1	Homo sapiens	74-78
34917622-3	2021	Studies have demonstrated that heme oxygenase 1 (HO-1), an inducible enzyme catalyzing heme degradation, exhibits anti-inflammatory, anti-oxidative stress and anti-apoptosis properties.	Heme	87-91	heme oxygenase 1	Homo sapiens	31-47
34547407-0	2021	Heme Oxygenase-1 (HMOX-1) and inhibitor of differentiation proteins (ID1, ID3) are key response mechanisms against iron-overload in pancreatic beta-cells.	Iron	115-119	heme oxygenase 1	Homo sapiens	0-16
34547407-0	2021	Heme Oxygenase-1 (HMOX-1) and inhibitor of differentiation proteins (ID1, ID3) are key response mechanisms against iron-overload in pancreatic beta-cells.	Iron	115-119	heme oxygenase 1	Homo sapiens	18-24
34547407-12	2021	Our findings suggest that HMOX1, ID1 and ID3 define the response mechanism against iron-overload-induced stress in beta-cells.	Iron	83-87	heme oxygenase 1	Homo sapiens	26-31
34622385-8	2021	The mRNA and protein expression levels of nuclear Nrf2, heme oxygenase 1 (HO-1), and NAD(P)H: quinone oxidoreductase 1 (NQO1) were significantly increased upon COS treatment.	carbonyl sulfide	160-163	heme oxygenase 1	Homo sapiens	56-72
34622385-8	2021	The mRNA and protein expression levels of nuclear Nrf2, heme oxygenase 1 (HO-1), and NAD(P)H: quinone oxidoreductase 1 (NQO1) were significantly increased upon COS treatment.	carbonyl sulfide	160-163	heme oxygenase 1	Homo sapiens	74-78
34622385-9	2021	Moreover, Nrf2-siRNA evidently reversed the promotive effect of COS on expression levels of HO-1 and NQO1, and ARE-driven transcriptional activity as determined by double-luciferase reporter gene assay.	carbonyl sulfide	64-67	heme oxygenase 1	Homo sapiens	92-96
34933382-3	2021	HO-1 production can also be stimulated by potassium iodide (KI).	Potassium Iodide	42-58	heme oxygenase 1	Homo sapiens	0-4
34933382-3	2021	HO-1 production can also be stimulated by potassium iodide (KI).	KS I	60-62	heme oxygenase 1	Homo sapiens	0-4
34933382-8	2021	CONCLUSION:  Our findings suggest that KI alleviates oxidative stress leading to decreased HO-1 expression; plasma from preeclamptic women did not induce the enzyme"s expression in HUVECs, and we hypothesize that this is possibly due to inhibitory post-transcriptional mechanisms in response to overexpression of this enzyme during early pregnancy.	KS I	39-41	heme oxygenase 1	Homo sapiens	91-95
34600339-12	2021	miR-194 mimic attenuated the effect of OGD/R on cell viability and protein levels of Nrf2, HO-1 and Bach1, whereas Bach1 overexpression reversed the effect of miR-194 mimics.	mir-194	0-7	heme oxygenase 1	Homo sapiens	91-95
34876806-0	2021	Methylcobalamin Protects Melanocytes from H2O2-Induced Oxidative Stress by Activating the Nrf2/HO-1 Pathway.	mecobalamin	0-15	heme oxygenase 1	Homo sapiens	95-99
34876806-11	2021	Results: We found that MeCbl treatment enhanced cell viability, increased melanin content, reduced intracellular reactive oxygen species (ROS) accumulation, increased the activities of antioxidant enzyme superoxide dismutase (SOD) and catalase (CAT), reduced melanocyte apoptosis, and up-regulated the expression of the Nrf2/HO-1 pathway.	mecobalamin	23-28	heme oxygenase 1	Homo sapiens	325-329
34876806-12	2021	Moreover, the protective effects of MeCbl were significantly weakened after inhibiting the Nrf2/HO-1 pathway.	mecobalamin	36-41	heme oxygenase 1	Homo sapiens	96-100
34876806-13	2021	Conclusion: Our results indicate that MeCbl attenuated the H2O2-induced oxidative stress in melanocytes by activating the Nrf2/HO-1 pathway, this suggests that MeCbl may be an effective treatment against vitiligo.	mecobalamin	38-43	heme oxygenase 1	Homo sapiens	127-131
34876806-13	2021	Conclusion: Our results indicate that MeCbl attenuated the H2O2-induced oxidative stress in melanocytes by activating the Nrf2/HO-1 pathway, this suggests that MeCbl may be an effective treatment against vitiligo.	Hydrogen Peroxide	59-63	heme oxygenase 1	Homo sapiens	127-131
34917622-3	2021	Studies have demonstrated that heme oxygenase 1 (HO-1), an inducible enzyme catalyzing heme degradation, exhibits anti-inflammatory, anti-oxidative stress and anti-apoptosis properties.	Heme	87-91	heme oxygenase 1	Homo sapiens	49-53
34836523-0	2021	Arctiin suppresses H9N2 avian influenza virus-mediated inflammation via activation of Nrf2/HO-1 signaling.	arctiin	0-7	heme oxygenase 1	Homo sapiens	91-95
34836523-11	2021	Interestingly, arctiin treatment obviously reversed H9N2 virus-induced reduction of Nrf2, increased the nuclear translocation of Nrf2, and upregulated Nrf2 signaling target genes (HO-1 and SOD2).	arctiin	15-22	heme oxygenase 1	Homo sapiens	180-184
34836523-12	2021	Zinc protoporphyrin (Znpp)-an HO-1 inhibitor-weakened the inhibitory effect of arctiin on H9N2 virus-induced RIG-I/JNK MAPK and proinflammatory mediators.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	30-34
34836523-12	2021	Zinc protoporphyrin (Znpp)-an HO-1 inhibitor-weakened the inhibitory effect of arctiin on H9N2 virus-induced RIG-I/JNK MAPK and proinflammatory mediators.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	30-34
34836523-12	2021	Zinc protoporphyrin (Znpp)-an HO-1 inhibitor-weakened the inhibitory effect of arctiin on H9N2 virus-induced RIG-I/JNK MAPK and proinflammatory mediators.	arctiin	79-86	heme oxygenase 1	Homo sapiens	30-34
34836523-13	2021	CONCLUSION: Taken together, these results suggested that the anti-inflammatory effects of arctiin on H9N2 virus infection may be due to the activation of Nrf2/HO-1 and blocked RIG-I/JNK MAPK signaling; thus, arctiin may be a promising agent for prevention and treatment of H9N2 virus infections.	arctiin	90-97	heme oxygenase 1	Homo sapiens	159-163
34836523-13	2021	CONCLUSION: Taken together, these results suggested that the anti-inflammatory effects of arctiin on H9N2 virus infection may be due to the activation of Nrf2/HO-1 and blocked RIG-I/JNK MAPK signaling; thus, arctiin may be a promising agent for prevention and treatment of H9N2 virus infections.	arctiin	208-215	heme oxygenase 1	Homo sapiens	159-163
34610361-7	2021	Mechanically, our findings revealed that Cd-induced ferroptosis depended upon the excessive activation of Heme oxygenase 1 (HMOX1) and the release of free iron from heme.	Cadmium	41-43	heme oxygenase 1	Homo sapiens	106-122
34901124-6	2021	Furthermore, we demonstrated that CS-EVs can alter the gene expression of several genes involved in inflammation (i.e., ICAM1 and HMOX-1) and tight junctions (i.e., OCLN, CLDN1, and MLCK), contributing to limit inflammatory stimuli and restore a functional barrier by increasing the tight junction OCLN protein.	CEV regimen	34-40	heme oxygenase 1	Homo sapiens	130-136
34956624-6	2021	Exposure to HCP and ATCP increased both hmox1 and srxn1 gene expression, and was associated with accumulation of Nrf2 protein in cells.	hcp	12-15	heme oxygenase 1	Homo sapiens	40-45
34800278-2	2022	HO-1 catalyzes heme breakdown, reducing the levels of this important oxidant molecule and generating antioxidant, anti-inflammatory, and anti-apoptotic byproducts.	Heme	15-19	heme oxygenase 1	Homo sapiens	0-4
34610361-7	2021	Mechanically, our findings revealed that Cd-induced ferroptosis depended upon the excessive activation of Heme oxygenase 1 (HMOX1) and the release of free iron from heme.	Cadmium	41-43	heme oxygenase 1	Homo sapiens	124-129
34610361-9	2021	Collectively, Cd induced ferroptosis by iron homeostasis dysregulation, mediated by excessive activation of HMOX-1.	Cadmium	14-16	heme oxygenase 1	Homo sapiens	108-114
34562468-0	2021	Astragalus polysaccharide prevents ferroptosis in a murine model of experimental colitis and human Caco-2 cells via inhibiting NRF2/HO-1 pathway.	Polysaccharides	11-25	heme oxygenase 1	Homo sapiens	132-136
34840667-10	2021	Moreover, inhibition of HO-1 by ZnPP weakened the cytoprotective effect of NAR.	zinc protoporphyrin	32-36	heme oxygenase 1	Homo sapiens	24-28
34840667-10	2021	Moreover, inhibition of HO-1 by ZnPP weakened the cytoprotective effect of NAR.	naringenin	75-78	heme oxygenase 1	Homo sapiens	24-28
34867473-11	2021	Moreover, melatonin can repair the endothelial damage from preeclampsia at the placenta level, increasing PIGF, Nrf-2, HO-1 production and reducing critical markers of vascular injury during the pregnancy.	Melatonin	10-19	heme oxygenase 1	Homo sapiens	119-123
34787456-0	2022	The Antimalaria Drug Artesunate Inhibits Porcine Reproductive and Respiratory Syndrome Virus Replication via Activating AMPK and Nrf2/HO-1 Signaling Pathways.	Artesunate	21-31	heme oxygenase 1	Homo sapiens	134-138
34582846-5	2021	In particular, this biomolecule reduces the generation of reactive oxygen species (ROS) by blocking the activation of inflammatory transcription factors, especially nuclear factor-kappaB (NF-kappaB), and accelerating the synthesis of antioxidant compounds such as heme oxygenase 1 (HO-1) and superoxide dismutase (SOD).	Reactive Oxygen Species	83-86	heme oxygenase 1	Homo sapiens	264-280
34582846-5	2021	In particular, this biomolecule reduces the generation of reactive oxygen species (ROS) by blocking the activation of inflammatory transcription factors, especially nuclear factor-kappaB (NF-kappaB), and accelerating the synthesis of antioxidant compounds such as heme oxygenase 1 (HO-1) and superoxide dismutase (SOD).	Reactive Oxygen Species	83-86	heme oxygenase 1	Homo sapiens	282-286
34582846-5	2021	In particular, this biomolecule reduces the generation of reactive oxygen species (ROS) by blocking the activation of inflammatory transcription factors, especially nuclear factor-kappaB (NF-kappaB), and accelerating the synthesis of antioxidant compounds such as heme oxygenase 1 (HO-1) and superoxide dismutase (SOD).	Reactive Oxygen Species	58-81	heme oxygenase 1	Homo sapiens	264-280
34582846-5	2021	In particular, this biomolecule reduces the generation of reactive oxygen species (ROS) by blocking the activation of inflammatory transcription factors, especially nuclear factor-kappaB (NF-kappaB), and accelerating the synthesis of antioxidant compounds such as heme oxygenase 1 (HO-1) and superoxide dismutase (SOD).	Reactive Oxygen Species	58-81	heme oxygenase 1	Homo sapiens	282-286
34858164-4	2021	It is showed that some natural compounds such as flavonoids, phenols, glycosides and coumarins have a protective role in melanocytes and thereby arrest the depigmentation, and, additionally, Nrf2/HO-1, MAPK, JAK/STAT, cAMP/PKA, and Wnt/beta-catenin signaling pathways were reported to be implicated in these protective effects.	Phenols	61-68	heme oxygenase 1	Homo sapiens	196-200
34782602-0	2021	Iron overload in endometriosis peritoneal fluid induces early embryo ferroptosis mediated by HMOX1.	Iron	0-4	heme oxygenase 1	Homo sapiens	93-98
34858164-4	2021	It is showed that some natural compounds such as flavonoids, phenols, glycosides and coumarins have a protective role in melanocytes and thereby arrest the depigmentation, and, additionally, Nrf2/HO-1, MAPK, JAK/STAT, cAMP/PKA, and Wnt/beta-catenin signaling pathways were reported to be implicated in these protective effects.	Glycosides	70-80	heme oxygenase 1	Homo sapiens	196-200
34858164-4	2021	It is showed that some natural compounds such as flavonoids, phenols, glycosides and coumarins have a protective role in melanocytes and thereby arrest the depigmentation, and, additionally, Nrf2/HO-1, MAPK, JAK/STAT, cAMP/PKA, and Wnt/beta-catenin signaling pathways were reported to be implicated in these protective effects.	Flavonoids	49-59	heme oxygenase 1	Homo sapiens	196-200
34858164-4	2021	It is showed that some natural compounds such as flavonoids, phenols, glycosides and coumarins have a protective role in melanocytes and thereby arrest the depigmentation, and, additionally, Nrf2/HO-1, MAPK, JAK/STAT, cAMP/PKA, and Wnt/beta-catenin signaling pathways were reported to be implicated in these protective effects.	Coumarins	85-94	heme oxygenase 1	Homo sapiens	196-200
34803685-0	2021	Paeoniflorin Suppresses TBHP-Induced Oxidative Stress and Apoptosis in Human Umbilical Vein Endothelial Cells via the Nrf2/HO-1 Signaling Pathway and Improves Skin Flap Survival.	peoniflorin	0-12	heme oxygenase 1	Homo sapiens	123-127
34803685-11	2021	However, the PF-mediated protection was partially lost after co-treatment with ML385, a selective Nrf2 inhibitor, suggesting that PF is a crucial modulator regulating the Nrf2/HO-1 signaling pathway.	ML385	79-84	heme oxygenase 1	Homo sapiens	176-180
34478827-7	2021	More so, treatment with ZnPP under hypoxic conditions down-regulated HO-1 expression, stimulated proliferation, and resisted apoptosis in yak PASMCs.	zinc protoporphyrin	24-28	heme oxygenase 1	Homo sapiens	69-73
34728736-0	2021	Hemin as a novel candidate for treating COVID-19 via heme oxygenase-1 induction.	Hemin	0-5	heme oxygenase 1	Homo sapiens	53-69
34728736-5	2021	To confirm whether HO-1 suppresses SARS-CoV-2 infection, we assessed the antiviral activity of hemin, an effective and safe HO-1 inducer, in SARS-CoV-2 infection.	Hemin	95-100	heme oxygenase 1	Homo sapiens	124-128
34728736-8	2021	Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection.	Iron	5-9	heme oxygenase 1	Homo sapiens	78-82
34728736-8	2021	Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection.	Biliverdine	14-24	heme oxygenase 1	Homo sapiens	78-82
34728736-8	2021	Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection.	Heme	60-64	heme oxygenase 1	Homo sapiens	78-82
34728736-10	2021	Overall, the findings suggested that HO-1, induced by hemin, effectively suppressed SARS-CoV-2 in vitro.	Hemin	54-59	heme oxygenase 1	Homo sapiens	37-41
34796171-0	2021	Butyric Acid Protects Against Renal Ischemia-Reperfusion Injury by Adjusting the Treg/Th17 Balance via HO-1/p-STAT3 Signaling.	Butyric Acid	0-12	heme oxygenase 1	Homo sapiens	103-107
34796171-0	2021	Butyric Acid Protects Against Renal Ischemia-Reperfusion Injury by Adjusting the Treg/Th17 Balance via HO-1/p-STAT3 Signaling.	treg	81-85	heme oxygenase 1	Homo sapiens	103-107
34796171-5	2021	Mechanism studies have shown that heme oxygenase 1 (HO-1)/STAT3 signaling pathway was involved in the inhibitory effect of BA on Th17 cell differentiation.	Butyric Acid	123-125	heme oxygenase 1	Homo sapiens	34-50
34796171-5	2021	Mechanism studies have shown that heme oxygenase 1 (HO-1)/STAT3 signaling pathway was involved in the inhibitory effect of BA on Th17 cell differentiation.	Butyric Acid	123-125	heme oxygenase 1	Homo sapiens	52-56
34796171-6	2021	HO-1 inhibitors can significantly rescue the BA-mediated inhibition of Th17 cell differentiation.	Butyric Acid	45-47	heme oxygenase 1	Homo sapiens	0-4
34510844-0	2021	Echinatin mitigates H2O2-induced oxidative damage and apoptosis in lens epithelial cells via the Nrf2/HO-1 pathway.	echinatin	0-9	heme oxygenase 1	Homo sapiens	102-106
34510844-10	2021	Moreover, H2O2 significantly reduced Nrf2 nuclear localization, as well as HO-1 and NQO1 expression, which could be reversed by Ech.	Hydrogen Peroxide	10-14	heme oxygenase 1	Homo sapiens	75-79
34510844-12	2021	CONCLUSIONS: Echinatin mitigates H2O2-induced oxidative damage and apoptosis in HLECs via the Nrf2/HO-1 pathway, suggesting that Ech may be a potential drug for the treatment of cataracts.	echinatin	13-22	heme oxygenase 1	Homo sapiens	99-103
34298225-0	2021	Paeoniflorin ameliorates oxidase stress in Glutamate-stimulated SY5Y and prenatally stressed female offspring through Nrf2/HO-1 signaling pathway.	peoniflorin	0-12	heme oxygenase 1	Homo sapiens	123-127
34146326-10	2021	Interestingly, melatonin not only markedly decreased the protein levels of TRPV1 and CGRP, but also enhanced the expression of Nrf2, quinone oxidoreductase-1 (NQO-1), and heme oxygenase-1 (HO-1).	Melatonin	15-24	heme oxygenase 1	Homo sapiens	171-187
34146326-10	2021	Interestingly, melatonin not only markedly decreased the protein levels of TRPV1 and CGRP, but also enhanced the expression of Nrf2, quinone oxidoreductase-1 (NQO-1), and heme oxygenase-1 (HO-1).	Melatonin	15-24	heme oxygenase 1	Homo sapiens	189-193
34582963-3	2021	Western blot analysis indicated that C3G and PCA minimized PhIP-induced cell damage by reversing the abnormal expression of Bax/Bcl-2, Cytochrome c, cleaved Caspase-3, XIAP, Nrf2, HO-1, LC3 and p62 involved in intrinsic apoptotic and Nrf2/p62 pathways.	2-amino-1-methyl-6-phenylimidazo(4,5-b)pyridine	59-63	heme oxygenase 1	Homo sapiens	180-184
34769290-9	2021	Data from the Human Apoptosis Array revealed that FLLL32 increases the expression of cleaved caspase-3 and heme oxygenase-1 (HO-1).	FLLL 32	50-56	heme oxygenase 1	Homo sapiens	107-123
34769290-9	2021	Data from the Human Apoptosis Array revealed that FLLL32 increases the expression of cleaved caspase-3 and heme oxygenase-1 (HO-1).	FLLL 32	50-56	heme oxygenase 1	Homo sapiens	125-129
34769290-12	2021	In conclusion, our findings suggest that FLLL32 is a potential therapeutic agent for oral cancer by inducing caspase-dependent apoptosis and HO-1 activation through the p38 pathway.	FLLL 32	41-47	heme oxygenase 1	Homo sapiens	141-145
34822480-5	2021	The cytoprotective mechanism of these peptides involves an improvement in the cellular antioxidant defense system, as indicated by the suppression of the intracellular ROS generation through upregulation of the cytoprotective enzyme heme oxygenase-1.	ros	168-171	heme oxygenase 1	Homo sapiens	233-249
34769290-13	2021	We believe that the activation of HO-1 and the p38 pathway by FLLL32 represent potential targets for further research in oral cancer.	FLLL 32	62-68	heme oxygenase 1	Homo sapiens	34-38
34508760-9	2021	More importantly, HMOX1 knockdown attenuated Fe2+ overload, reduced iron content and ROS, and alleviated lipid peroxidation, which led to a reduction in ferroptosis in diabetic human endothelial cells.	ammonium ferrous sulfate	45-49	heme oxygenase 1	Homo sapiens	18-23
34508760-9	2021	More importantly, HMOX1 knockdown attenuated Fe2+ overload, reduced iron content and ROS, and alleviated lipid peroxidation, which led to a reduction in ferroptosis in diabetic human endothelial cells.	Iron	68-72	heme oxygenase 1	Homo sapiens	18-23
34508760-9	2021	More importantly, HMOX1 knockdown attenuated Fe2+ overload, reduced iron content and ROS, and alleviated lipid peroxidation, which led to a reduction in ferroptosis in diabetic human endothelial cells.	ros	85-88	heme oxygenase 1	Homo sapiens	18-23
34558653-0	2021	Ginsenoside Rk1 protects human melanocytes from H2O2-induced oxidative injury via regulation of the PI3K/AKT/Nrf2/HO-1 pathway.	ginsenoside Rk1	0-15	heme oxygenase 1	Homo sapiens	114-118
34558653-11	2021	In addition, RK1 treatment notably induced Nrf2 nuclear translocation, increased the protein expression levels of Nrf2 and HO-1, and the ratio of phosphorylated-AKT to AKT in the PIG1 cells exposed to H2O2.	Hydrogen Peroxide	201-205	heme oxygenase 1	Homo sapiens	123-127
34754326-11	2021	Conclusion: Our data suggested that treatment with DMF mitigated LPS-induced oxidative stress, inflammation, and ER stress-associated apoptosis in NPCs via the Nrf2/HO-1 signaling pathway, thus reliving LPS-induced dysfunction of NPCs, which offered a novel potential pharmacological treatment strategy for IVDD.	Dimethyl Fumarate	51-54	heme oxygenase 1	Homo sapiens	165-169
34737578-6	2021	Hydrogen sulfide (H2S) likewise opposes mast cell activation; H2S can boost AMPK activity, up-regulate cGMP production, and trigger Nrf2-mediated induction of Phase 2 enzymes - including heme oxygenase-1, whose generation of bilirubin suppresses NADPH oxidase activity.	Deuterium	18-21	heme oxygenase 1	Homo sapiens	187-203
34737578-6	2021	Hydrogen sulfide (H2S) likewise opposes mast cell activation; H2S can boost AMPK activity, up-regulate cGMP production, and trigger Nrf2-mediated induction of Phase 2 enzymes - including heme oxygenase-1, whose generation of bilirubin suppresses NADPH oxidase activity.	Deuterium	62-65	heme oxygenase 1	Homo sapiens	187-203
34737578-6	2021	Hydrogen sulfide (H2S) likewise opposes mast cell activation; H2S can boost AMPK activity, up-regulate cGMP production, and trigger Nrf2-mediated induction of Phase 2 enzymes - including heme oxygenase-1, whose generation of bilirubin suppresses NADPH oxidase activity.	Bilirubin	225-234	heme oxygenase 1	Homo sapiens	187-203
34509368-6	2021	In summary, WEKPPVSH might protect against oxidative stress and inflammation in LPS-stimulated BV-2 microglia by enhancing the Nrf2/HO-1 signaling pathway and blocking the nuclear factor-kappaB/p38 mitogen - activated protein kinase (NF-kappaB/p38 MAPK) signaling pathway.	wekppvsh	12-20	heme oxygenase 1	Homo sapiens	132-136
34609010-7	2021	Our results showed that berberine-LCNs significantly reduced the expression of CCl-20, CXCL-8 and HO-1 at dose of 5microM.	Berberine	24-33	heme oxygenase 1	Homo sapiens	98-102
34609010-7	2021	Our results showed that berberine-LCNs significantly reduced the expression of CCl-20, CXCL-8 and HO-1 at dose of 5microM.	lcns	34-38	heme oxygenase 1	Homo sapiens	98-102
34609010-8	2021	Collectively, our findings suggest that berberine-LCNs have inhibitory effect on inflammation/oxidative stress related cytokines i.e. CCL20, CXCL-8, and HO-1 which could be a novel therapeutic target for the management of lung cancer.	Berberine	40-49	heme oxygenase 1	Homo sapiens	153-157
34609010-11	2021	Our study showed that Berberine LCNs significantly downregulate the expression of CXCL-8, CCL-20 and HO-1 which suggests that Berberine loaded nanoparticles could be a promising therapeutic alternative for the management of lung cancer.	berberine lcns	22-36	heme oxygenase 1	Homo sapiens	101-105
34609010-11	2021	Our study showed that Berberine LCNs significantly downregulate the expression of CXCL-8, CCL-20 and HO-1 which suggests that Berberine loaded nanoparticles could be a promising therapeutic alternative for the management of lung cancer.	Berberine	126-135	heme oxygenase 1	Homo sapiens	101-105
34453944-1	2021	AIM: Biliverdin reductase-A (BVR-A) other than its canonical role in the degradation pathway of heme as partner of heme oxygenase-1 (HO1), has recently drawn attention as a protein with pleiotropic functions involved in insulin-glucose homeostasis.	Heme	96-100	heme oxygenase 1	Homo sapiens	115-131
34453944-1	2021	AIM: Biliverdin reductase-A (BVR-A) other than its canonical role in the degradation pathway of heme as partner of heme oxygenase-1 (HO1), has recently drawn attention as a protein with pleiotropic functions involved in insulin-glucose homeostasis.	Heme	96-100	heme oxygenase 1	Homo sapiens	133-136
34476501-4	2021	The expression levels of apoptosis-related proteins, activation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway induced by H2O2 and the effect of treatment with ANP on vertebral EPCs were detected by western blotting.	Hydrogen Peroxide	175-179	heme oxygenase 1	Homo sapiens	122-138
34476501-4	2021	The expression levels of apoptosis-related proteins, activation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway induced by H2O2 and the effect of treatment with ANP on vertebral EPCs were detected by western blotting.	Hydrogen Peroxide	175-179	heme oxygenase 1	Homo sapiens	140-144
34476501-8	2021	Finally, ANP blocked H2O2-induced oxidative stress through activating the Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	21-25	heme oxygenase 1	Homo sapiens	79-83
34476501-9	2021	These findings suggested that ANP may effectively protect EPCs through inhibition of H2O2-induced oxidant injury and cell death by activating the Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	85-89	heme oxygenase 1	Homo sapiens	151-155
34688156-2	2021	With the continuous deepening of research, in addition to directly regulating redox by catalyzing the degradation of heme, HO-1 protein also participates in the gene expression level in a great diversity of methods, thereby initiating cell defense.	Heme	117-121	heme oxygenase 1	Homo sapiens	123-127
34688156-5	2021	Especially for malignant diseases, there may be new advances in the treatment of HO-1 by regulating abnormal ROS and metabolic signaling.	ros	109-112	heme oxygenase 1	Homo sapiens	81-85
34754326-0	2021	Dimethyl Fumarate Ameliorates Nucleus Pulposus Cell Dysfunction through Activating the Nrf2/HO-1 Pathway in Intervertebral Disc Degeneration.	Dimethyl Fumarate	0-17	heme oxygenase 1	Homo sapiens	92-96
34737578-6	2021	Hydrogen sulfide (H2S) likewise opposes mast cell activation; H2S can boost AMPK activity, up-regulate cGMP production, and trigger Nrf2-mediated induction of Phase 2 enzymes - including heme oxygenase-1, whose generation of bilirubin suppresses NADPH oxidase activity.	Hydrogen Sulfide	0-16	heme oxygenase 1	Homo sapiens	187-203
34269613-5	2021	Internalization of ferrylHb is accompanied by up-regulation of heme oxygenase-1 and H-ferritin and accumulation of iron within lysosomes as a result of heme/iron uptake.	Heme	152-156	heme oxygenase 1	Homo sapiens	63-79
34828827-0	2021	Selenium-Enriched Soy Protein Has Antioxidant Potential via Modulation of the NRF2-HO1 Signaling Pathway.	Selenium	0-8	heme oxygenase 1	Homo sapiens	83-86
34768836-0	2021	5-Aminolevulinic Acid Attenuates Glucose-Regulated Protein 78 Expression and Hepatocyte Lipoapoptosis via Heme Oxygenase-1 Induction.	5-amino levulinic acid	0-21	heme oxygenase 1	Homo sapiens	106-122
34768836-12	2021	5-ALA significantly induced HO-1 and decreased GRP78 expression.	5-amino levulinic acid	0-5	heme oxygenase 1	Homo sapiens	28-32
34768836-16	2021	5-ALA has a therapeutic potential on hepatic steatosis by suppressing ER stress and lipoapoptosis by attenuating GRP78 via HO-1 induction.	5-amino levulinic acid	0-5	heme oxygenase 1	Homo sapiens	123-127
34269613-5	2021	Internalization of ferrylHb is accompanied by up-regulation of heme oxygenase-1 and H-ferritin and accumulation of iron within lysosomes as a result of heme/iron uptake.	Iron	157-161	heme oxygenase 1	Homo sapiens	63-79
34622673-10	2021	In eAAA, HO-1 expression was negatively correlated with aortic collagen content and oxidative stress parameters H2O2 release, oxidized proteins, and thiobarbituric acid reactive substances.	Hydrogen Peroxide	112-116	heme oxygenase 1	Homo sapiens	9-13
34622673-10	2021	In eAAA, HO-1 expression was negatively correlated with aortic collagen content and oxidative stress parameters H2O2 release, oxidized proteins, and thiobarbituric acid reactive substances.	thiobarbituric acid	149-168	heme oxygenase 1	Homo sapiens	9-13
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	Bexarotene	111-121	heme oxygenase 1	Homo sapiens	169-174
34679025-0	2021	The Protective Effect of Heme Oxygenase-1 on Liver Injury Caused by DON-Induced Oxidative Stress and Cytotoxicity.	deoxynivalenol	68-71	heme oxygenase 1	Homo sapiens	25-41
34679025-10	2021	Significantly, AAV-mediated liver-specific overexpression of HO-1 reduced DON-induced liver damage and indirectly protected the abilities of antioxidant enzyme/DNA damage repair system, while AAV-mediated silence of HO-1 produced the opposite effect.	deoxynivalenol	74-77	heme oxygenase 1	Homo sapiens	61-65
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	Bexarotene	111-121	heme oxygenase 1	Homo sapiens	314-319
34679025-11	2021	In addition, we found that overexpression of HO-1 could enhance autophagy and combined it with an antioxidant enzyme/DNA damage repair system to inhibit DON-induced hepatocyte damage.	deoxynivalenol	153-156	heme oxygenase 1	Homo sapiens	45-49
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	desloratadine	127-140	heme oxygenase 1	Homo sapiens	169-174
34679025-12	2021	Altogether, these data suggest that HO-1 reduces the oxidative stress and DNA damage caused by DON sub-chronic exposure through maintaining DNA repair, antioxidant activity, as well as autophagy.	deoxynivalenol	95-98	heme oxygenase 1	Homo sapiens	36-40
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	desloratadine	127-140	heme oxygenase 1	Homo sapiens	314-319
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	conivaptan	99-109	heme oxygenase 1	Homo sapiens	169-174
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	1-(adamantan-1-yl)-2-(1h-imidazol-1-yl)ethenone	226-273	heme oxygenase 1	Homo sapiens	169-174
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	conivaptan	99-109	heme oxygenase 1	Homo sapiens	314-319
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	1-(adamantan-1-yl)-2-(1h-imidazol-1-yl)ethenone	226-273	heme oxygenase 1	Homo sapiens	314-319
34681275-6	2021	Using virtual drug screening and molecular docking analyses, we identified FDA-approved compounds (conivaptan, bexarotene, and desloratadine) that were interacting with HMOX1 and PRKCA at even stronger binding affinities than 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethenone and ellagic acid as known inhibitors of HMOX1 and PRKCA, respectively.	Ellagic Acid	278-290	heme oxygenase 1	Homo sapiens	314-319
34681275-7	2021	Conivaptan treatment increased doxorubicin sensitivity of both HMOX1- and PRKCA-transfected cell lines.	conivaptan	0-10	heme oxygenase 1	Homo sapiens	63-68
34119834-7	2021	In an LPS-induced peritoneal macrophage cell model, this compound could cause a significant increase in the nuclear Nrf2 protein, decrease in the cytosolic Nrf2 protein, and further elevate the downstream protective enzymes HO-1 and NQO-1, which were better than the lead compound NXPZ-2 and sulforaphane.	nxpz-2	281-287	heme oxygenase 1	Homo sapiens	224-228
34681275-8	2021	Bexarotene treatment had a comparable doxorubicin-sensitizing effect in HMOX1-transfected cells and desloratadine in PRKCA-transfected cells.	Bexarotene	0-10	heme oxygenase 1	Homo sapiens	72-77
34119834-7	2021	In an LPS-induced peritoneal macrophage cell model, this compound could cause a significant increase in the nuclear Nrf2 protein, decrease in the cytosolic Nrf2 protein, and further elevate the downstream protective enzymes HO-1 and NQO-1, which were better than the lead compound NXPZ-2 and sulforaphane.	sulforaphane	292-304	heme oxygenase 1	Homo sapiens	224-228
34190424-3	2021	To enhance the efficacy of PDT for tumor treatment, a versatile nanoparticle (NP)-based drug is developed, which the authors call PZB NP, containing the glutathione inhibitor l-buthionine sulfoximine (BSO) and the heme oxygenase 1 (HO-1) inhibitor protoporphyrin zinc(II) (ZnPP) to suppress the innate antioxidant defense system of cancer cells in a two-pronged manner.	protoporphyrin zinc(ii)	248-271	heme oxygenase 1	Homo sapiens	214-230
34681608-0	2021	Bisphenol a Induces Autophagy Defects and AIF-Dependent Apoptosis via HO-1 and AMPK to Degenerate N2a Neurons.	bis(4-hydroxyphenyl)sulfone	0-9	heme oxygenase 1	Homo sapiens	70-74
34680118-0	2021	Protocatechuic Acid, a Simple Plant Secondary Metabolite, Induced Apoptosis by Promoting Oxidative Stress through HO-1 Downregulation and p21 Upregulation in Colon Cancer Cells.	protocatechuic acid	0-19	heme oxygenase 1	Homo sapiens	114-118
34265290-8	2021	Inhibition of the enzyme heme oxygenase-1 (HO-1) or silencing of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) suppressed the AST-promoted cellular and mitochondrial protection.	astaxanthine	156-159	heme oxygenase 1	Homo sapiens	25-41
34265290-8	2021	Inhibition of the enzyme heme oxygenase-1 (HO-1) or silencing of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) suppressed the AST-promoted cellular and mitochondrial protection.	astaxanthine	156-159	heme oxygenase 1	Homo sapiens	43-47
34681608-8	2021	Both heme oxygenase (HO)-1 and AMP-activated protein kinase (AMPK) up-regulated/activated by BPA mediated the molecular signalings involved in apoptosis and autophagy.	bisphenol A	93-96	heme oxygenase 1	Homo sapiens	5-26
34681608-9	2021	HO-1 inhibition or AIF silencing effectively reduced BPA-induced neuronal death.	bisphenol A	53-56	heme oxygenase 1	Homo sapiens	0-4
34681608-11	2021	These results suggest that BPA induces N2a neurotoxicity characterized by AIF-dependent apoptosis and p62-related autophagy defects via HO-1 up-regulation and AMPK activation, thereby resulting in neuronal degeneration.	bisphenol A	27-30	heme oxygenase 1	Homo sapiens	136-140
34680118-7	2021	The phenolic acid induced modifications in levels of HO-1, non-proteic thiol groups, gamma-glutamylcysteine synthetase, reactive oxygen species, and p21.	phenolic acid	4-17	heme oxygenase 1	Homo sapiens	53-57
34265290-10	2021	Overall, our data demonstrate that AST prevented mitochondrial dysfunction by a mechanism related to the Nrf2/HO-1 axis in GLU-challenged cells.	Glutamic Acid	123-126	heme oxygenase 1	Homo sapiens	110-114
34190424-3	2021	To enhance the efficacy of PDT for tumor treatment, a versatile nanoparticle (NP)-based drug is developed, which the authors call PZB NP, containing the glutathione inhibitor l-buthionine sulfoximine (BSO) and the heme oxygenase 1 (HO-1) inhibitor protoporphyrin zinc(II) (ZnPP) to suppress the innate antioxidant defense system of cancer cells in a two-pronged manner.	protoporphyrin zinc(ii)	248-271	heme oxygenase 1	Homo sapiens	232-236
34190424-3	2021	To enhance the efficacy of PDT for tumor treatment, a versatile nanoparticle (NP)-based drug is developed, which the authors call PZB NP, containing the glutathione inhibitor l-buthionine sulfoximine (BSO) and the heme oxygenase 1 (HO-1) inhibitor protoporphyrin zinc(II) (ZnPP) to suppress the innate antioxidant defense system of cancer cells in a two-pronged manner.	zinc protoporphyrin	273-277	heme oxygenase 1	Homo sapiens	214-230
34190424-3	2021	To enhance the efficacy of PDT for tumor treatment, a versatile nanoparticle (NP)-based drug is developed, which the authors call PZB NP, containing the glutathione inhibitor l-buthionine sulfoximine (BSO) and the heme oxygenase 1 (HO-1) inhibitor protoporphyrin zinc(II) (ZnPP) to suppress the innate antioxidant defense system of cancer cells in a two-pronged manner.	zinc protoporphyrin	273-277	heme oxygenase 1	Homo sapiens	232-236
34190424-4	2021	BSO reduces intracellular glutathione levels to minimize ROS elimination and protein protection during PDT, and ZnPP inhibits the ROS-stimulated upregulation of the antioxidant HO-1, thus preventing ROS removal by cells after PDT.	zinc protoporphyrin	112-116	heme oxygenase 1	Homo sapiens	177-181
34190424-4	2021	BSO reduces intracellular glutathione levels to minimize ROS elimination and protein protection during PDT, and ZnPP inhibits the ROS-stimulated upregulation of the antioxidant HO-1, thus preventing ROS removal by cells after PDT.	ros	130-133	heme oxygenase 1	Homo sapiens	177-181
34190424-4	2021	BSO reduces intracellular glutathione levels to minimize ROS elimination and protein protection during PDT, and ZnPP inhibits the ROS-stimulated upregulation of the antioxidant HO-1, thus preventing ROS removal by cells after PDT.	ros	199-202	heme oxygenase 1	Homo sapiens	177-181
34480604-5	2021	Bardoxolone-methyl (CDDO-Me) induced oxidative stress caused similarly increased expression of both the wild-type and eGFP-tagged HMOX1 at the mRNA and protein level.	bardoxolone methyl	0-18	heme oxygenase 1	Homo sapiens	130-135
34293961-10	2021	Meanwhile, administration of antioxidants or heme oxygenase-1 induction to elevate the hepatocellular levels of the endogenous scavenger bilirubin are promising alternatives that need to be re-evaluated and implemented.	Bilirubin	137-146	heme oxygenase 1	Homo sapiens	45-61
34480604-5	2021	Bardoxolone-methyl (CDDO-Me) induced oxidative stress caused similarly increased expression of both the wild-type and eGFP-tagged HMOX1 at the mRNA and protein level.	bardoxolone methyl	20-27	heme oxygenase 1	Homo sapiens	130-135
34189835-5	2021	Pb nanoparticles also induced the gene expression of heme oxygenase-1 in dTHP-1 cells but not in A549 cells.	Lead	0-2	heme oxygenase 1	Homo sapiens	53-69
34346143-0	2021	Arbutin attenuates ethanol-induced acute hepatic injury by the modulation of oxidative stress and Nrf-2/HO-1 signaling pathway.	Ethanol	19-26	heme oxygenase 1	Homo sapiens	104-108
34380011-5	2021	The QUE was also found to counteract STE-induced ROS generation and decrease STE-induced up-regulation of the expression of the stress-inducible enzymes HO-1 and NOS-2.	Sterigmatocystin	77-80	heme oxygenase 1	Homo sapiens	153-157
34346143-12	2021	Arbutin triggered Nrf-2/HO-1 signaling cascade liver tissues of ethanol-provoked animals.	Arbutin	0-7	heme oxygenase 1	Homo sapiens	24-28
34346143-0	2021	Arbutin attenuates ethanol-induced acute hepatic injury by the modulation of oxidative stress and Nrf-2/HO-1 signaling pathway.	Arbutin	0-7	heme oxygenase 1	Homo sapiens	104-108
34346143-12	2021	Arbutin triggered Nrf-2/HO-1 signaling cascade liver tissues of ethanol-provoked animals.	Ethanol	64-71	heme oxygenase 1	Homo sapiens	24-28
34487292-9	2021	The intracellular antioxidant enzymes HO-1 and SOD-2 were upregulated by neoxanthin pretreatment.	neoxanthin	73-83	heme oxygenase 1	Homo sapiens	38-42
34241977-0	2021	Computational Designing and Prediction of ADMET Properties of Four Novel Imidazole-Based Drug Candidates Inhibiting Heme Oxygenase-1 Causing Cancers.	imidazole	73-82	heme oxygenase 1	Homo sapiens	116-132
34241977-2	2021	The inhibition of HO-1 through imidazole-based drugs, which is non-competitive with heme, is a focus of anticancer drug research.	imidazole	31-40	heme oxygenase 1	Homo sapiens	18-22
34241977-2	2021	The inhibition of HO-1 through imidazole-based drugs, which is non-competitive with heme, is a focus of anticancer drug research.	Heme	84-88	heme oxygenase 1	Homo sapiens	18-22
34530349-4	2021	In the present study, we found that iron overload promoted ferroptosis in hepatocytes by excessively inducing HO-1 expression, which contributed to the progression of liver injury and fibrosis, accompanied by the upregulation of the FGF21 protein level in vitro and in vivo.	Iron	36-40	heme oxygenase 1	Homo sapiens	110-114
34470469-0	2021	The protective benefit of heme oxygenase-1 gene modified human placenta-derived Mesenchymal stem cell in N-nitro-L-arginine methyl ester -induced preeclampsia-like rat model: Possible implications for placental angiogenesis.	n-nitro-l-arginine methyl ester	105-136	heme oxygenase 1	Homo sapiens	26-42
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	cu-hemin-peg-la	38-53	heme oxygenase 1	Homo sapiens	210-226
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	cu-hemin-peg-la	38-53	heme oxygenase 1	Homo sapiens	228-233
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	weak acid	81-90	heme oxygenase 1	Homo sapiens	210-226
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	weak acid	81-90	heme oxygenase 1	Homo sapiens	228-233
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	cu(ii)	103-109	heme oxygenase 1	Homo sapiens	210-226
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	cu(ii)	103-109	heme oxygenase 1	Homo sapiens	228-233
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	Hemin	114-119	heme oxygenase 1	Homo sapiens	210-226
34448349-4	2021	After highly ingested by HepG2 cells, Cu-Hemin-PEG-LA nanosheets are degraded by weak acid and release Cu(II) and hemin, which consuming intracellular glutathione (GSH) content and increasing the expression of heme oxygenase 1 (HMOX1) protein, respectively.	Hemin	114-119	heme oxygenase 1	Homo sapiens	228-233
34448349-6	2021	The intracellular Fe2+ content is overloaded by the significant up-regulation of HMOX1 expression, which is denoted as nonclassical mode.	ammonium ferrous sulfate	18-22	heme oxygenase 1	Homo sapiens	81-86
34583348-3	2021	Erythrocyte destruction results in increased release of cytotoxic free heme that is scavenged by haptoglobin (Hp), hemopexin (Hx) and heme oxygenase-1 (HO-1).	Heme	71-75	heme oxygenase 1	Homo sapiens	134-150
34089821-1	2021	The intracellular enzyme heme oxygenase-1 (HO-1) is responsible for the degradation of cell-free (cf) heme.	Heme	102-106	heme oxygenase 1	Homo sapiens	25-41
34089821-1	2021	The intracellular enzyme heme oxygenase-1 (HO-1) is responsible for the degradation of cell-free (cf) heme.	Heme	102-106	heme oxygenase 1	Homo sapiens	43-47
34583348-3	2021	Erythrocyte destruction results in increased release of cytotoxic free heme that is scavenged by haptoglobin (Hp), hemopexin (Hx) and heme oxygenase-1 (HO-1).	Heme	71-75	heme oxygenase 1	Homo sapiens	152-156
34583348-7	2021	A cross-sectional study was conducted to determine the association between plasma levels of free heme, HO-1, Hp, Hx, and malaria status in pregnant women who received routine iron supplementation and their birth outcomes.	Iron	175-179	heme oxygenase 1	Homo sapiens	103-107
34472337-0	2021	Discovery of Novel Acetamide-Based Heme Oxygenase-1 Inhibitors with Potent In Vitro Antiproliferative Activity.	acetamide	19-28	heme oxygenase 1	Homo sapiens	35-51
34472337-1	2021	Heme oxygenase-1 (HO-1) promotes heme catabolism exercising cytoprotective roles in normal and cancer cells.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-16
34472337-1	2021	Heme oxygenase-1 (HO-1) promotes heme catabolism exercising cytoprotective roles in normal and cancer cells.	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
34638586-13	2021	The upregulation of NEDD4-1 attenuated PTEN expression and promoted the AKT/NRF2/HO-1 oxidative stress signaling axis, which in turn conferred amplified defense against reactive oxygen species (ROS) and eventually higher resistance against TMZ treatment.	Reactive Oxygen Species	169-192	heme oxygenase 1	Homo sapiens	81-85
34630071-7	2021	Mechanistically, the expression of NADPH oxidase 1 (Nox1) was found to be suppressed and antioxidant enzymes including catalase, superoxide dismutase 2 (SOD-2), and heme oxygenase-1(HO-1) were enhanced following RH treatment, suggesting RH exhibited antioxidant activity by reducing the generation of reactive oxygen species (ROS) as well as enhancing the depletion of ROS.	rhapontin	212-214	heme oxygenase 1	Homo sapiens	165-181
34630071-7	2021	Mechanistically, the expression of NADPH oxidase 1 (Nox1) was found to be suppressed and antioxidant enzymes including catalase, superoxide dismutase 2 (SOD-2), and heme oxygenase-1(HO-1) were enhanced following RH treatment, suggesting RH exhibited antioxidant activity by reducing the generation of reactive oxygen species (ROS) as well as enhancing the depletion of ROS.	rhapontin	212-214	heme oxygenase 1	Homo sapiens	182-186
34638586-13	2021	The upregulation of NEDD4-1 attenuated PTEN expression and promoted the AKT/NRF2/HO-1 oxidative stress signaling axis, which in turn conferred amplified defense against reactive oxygen species (ROS) and eventually higher resistance against TMZ treatment.	Reactive Oxygen Species	194-197	heme oxygenase 1	Homo sapiens	81-85
34638586-13	2021	The upregulation of NEDD4-1 attenuated PTEN expression and promoted the AKT/NRF2/HO-1 oxidative stress signaling axis, which in turn conferred amplified defense against reactive oxygen species (ROS) and eventually higher resistance against TMZ treatment.	Temozolomide	240-243	heme oxygenase 1	Homo sapiens	81-85
34638586-15	2021	CONCLUSIONS: These findings demonstrate the critical role of NEDD4-1 in regulating the redox imbalance in TMZ-resistant GBM cells via the degradation of PTEN and the upregulation of the AKT/NRF2/HO-1 signaling pathway.	Temozolomide	106-109	heme oxygenase 1	Homo sapiens	195-199
34214916-5	2021	Low doses of DMEP upregulated nuclear factor E2-related factor 2 (Nrf2) and downstream protein haeme oxygenase-1 (HO-1) levels and high doses down-regulated their levels.	dimethoxyethyl phthalate	13-17	heme oxygenase 1	Homo sapiens	95-112
34680412-5	2021	The human apoptosis array and Western blot assay showed that magnolol increased the expression of cleaved caspase-3 proteins and heme oxygenase-1 (HO-1).	magnolol	61-69	heme oxygenase 1	Homo sapiens	129-145
34680412-5	2021	The human apoptosis array and Western blot assay showed that magnolol increased the expression of cleaved caspase-3 proteins and heme oxygenase-1 (HO-1).	magnolol	61-69	heme oxygenase 1	Homo sapiens	147-151
34214916-5	2021	Low doses of DMEP upregulated nuclear factor E2-related factor 2 (Nrf2) and downstream protein haeme oxygenase-1 (HO-1) levels and high doses down-regulated their levels.	dimethoxyethyl phthalate	13-17	heme oxygenase 1	Homo sapiens	114-118
34455781-5	2021	Besides, the EPS-b by its scavenging potential also maintained the oxidative balance in the Caco-2 cells under oxidative stress and preserved the cellular antioxidative defense system (CAT, GPx, SOD, HO1, and GCLC) at the basal level.	N-ethyl-3-piperidyl benzilate	13-18	heme oxygenase 1	Homo sapiens	200-203
34573098-8	2021	Treatment with RTA402 results in antiapoptotic, antioxidative stress, anti-inflammatory, and myelin-preserving effects on retinal ganglion cell (RGC) survival and visual function via regulation of NQO1 and HO-1, reduced IL-6 and Iba1 expression in macrophages, and promoted microglial expression of TGF-beta and Ym1 + 2 in the retina and optic nerve.	bardoxolone methyl	15-21	heme oxygenase 1	Homo sapiens	206-210
34573068-6	2021	Moreover, BTDE could inhibit the expression of Kelch-like epichlorohydrin-associated protein 1 (Keap1) and increase the expression of both nuclear factor erythroid 2-related factor 2 (Nrf2) and its downstream proteins TrXR1, HO-1, and NQO1.	btde	10-14	heme oxygenase 1	Homo sapiens	225-229
34566656-7	2021	In addition, JSH-23 attenuated H2O2-induced apoptosis and mineralization reduction in osteoblasts by reducing ROS production and enhancing Nrf2/HO-1 expression.	Hydrogen Peroxide	31-35	heme oxygenase 1	Homo sapiens	144-148
34646329-12	2021	Molecular docking revealed a good binding affinity of active components (quercetin, bisdemethoxycurcumin, and kaempferol) with the corresponding targets (CYP3A4, CYP1A1, HMOX1, DRD2, DPP4, ADRA2A, ADRA2C, NR1I2, and LGALS4).	Quercetin	73-82	heme oxygenase 1	Homo sapiens	170-175
34646329-12	2021	Molecular docking revealed a good binding affinity of active components (quercetin, bisdemethoxycurcumin, and kaempferol) with the corresponding targets (CYP3A4, CYP1A1, HMOX1, DRD2, DPP4, ADRA2A, ADRA2C, NR1I2, and LGALS4).	bisdemethoxycurcumin	84-104	heme oxygenase 1	Homo sapiens	170-175
34646329-12	2021	Molecular docking revealed a good binding affinity of active components (quercetin, bisdemethoxycurcumin, and kaempferol) with the corresponding targets (CYP3A4, CYP1A1, HMOX1, DRD2, DPP4, ADRA2A, ADRA2C, NR1I2, and LGALS4).	kaempferol	110-120	heme oxygenase 1	Homo sapiens	170-175
34575836-11	2021	The effects of compound 1 were partly reversed by co-treatment with a HO-1 inhibitor, tin protoporphyrin IX.	tin protoporphyrin IX	86-107	heme oxygenase 1	Homo sapiens	70-74
34572050-3	2021	Subcellular traffics of HO-1 to different organelles constitute a network of interactions compromising a variety of effectors such as pro-oxidants, ROS, mitochondrial enzymes, and nucleic transcription factors.	ros	148-151	heme oxygenase 1	Homo sapiens	24-28
34499923-5	2022	Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs).	Bilirubin	74-83	heme oxygenase 1	Homo sapiens	29-33
34499923-5	2022	Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs).	epoxyeicosatrienoic acid	153-177	heme oxygenase 1	Homo sapiens	29-33
34499923-5	2022	Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs).	EET	179-182	heme oxygenase 1	Homo sapiens	29-33
34081904-8	2021	Therefore, this review summarizes the biological characteristics of HO-1, and the relationship between inflammatory response and reactive oxygen species production regulated by HO-1 and osteoporosis.	Reactive Oxygen Species	129-152	heme oxygenase 1	Homo sapiens	68-72
34081904-8	2021	Therefore, this review summarizes the biological characteristics of HO-1, and the relationship between inflammatory response and reactive oxygen species production regulated by HO-1 and osteoporosis.	Reactive Oxygen Species	129-152	heme oxygenase 1	Homo sapiens	177-181
34499923-5	2022	Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs).	omega-3	185-192	heme oxygenase 1	Homo sapiens	29-33
34118221-10	2021	This study suggests that ALA priming may improve the therapeutic potential of ADSCs against chronic liver problems by activating the nuclear factor erythroid 2-related factor 2 (Nrf2) and its downstream antioxidant factors heme oxygenase 1 (HO-1) and quinone acceptor oxidoreductase-1 (NQO1).	Thioctic Acid	25-28	heme oxygenase 1	Homo sapiens	223-239
34118221-10	2021	This study suggests that ALA priming may improve the therapeutic potential of ADSCs against chronic liver problems by activating the nuclear factor erythroid 2-related factor 2 (Nrf2) and its downstream antioxidant factors heme oxygenase 1 (HO-1) and quinone acceptor oxidoreductase-1 (NQO1).	Thioctic Acid	25-28	heme oxygenase 1	Homo sapiens	241-245
34499923-5	2022	Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs).	Fatty Acids, Unsaturated	203-230	heme oxygenase 1	Homo sapiens	29-33
34499923-5	2022	Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs).	Fatty Acids, Unsaturated	232-237	heme oxygenase 1	Homo sapiens	29-33
34518768-8	2021	Further experiments showed that CR 8 : 2 exhibited significantly greater effects in increasing Nrf2 translocation and expressions of Nrf2 and HO-1 proteins, as well as SOD activity and total cellular NAD production, than that of C or R alone.	Chromium	32-34	heme oxygenase 1	Homo sapiens	142-146
34365685-0	2021	Melatonin induces Nrf2-HO-1 reprogramming and corrections in hepatic core clock oscillations in Non-alcoholic fatty liver disease.	Melatonin	0-9	heme oxygenase 1	Homo sapiens	23-27
34153850-6	2021	In addition, curcumin pretreatment significantly increased the expression of nuclear Nrf2, and the productions of superoxide dismutase 1 and heme oxygenase-1, which were the target anti-oxidative enzymes of the Keap1/Nrf2/ARE pathway.	Curcumin	13-21	heme oxygenase 1	Homo sapiens	141-157
34306210-9	2021	In addition, salinomycin significantly downregulated the expression of nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase-1, NAD(P)H quinone dehydrogenase 1 and glutamate-cysteine ligase catalytic subunit and decreased the activity of the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase in PC-3 and DU145 cells.	salinomycin	13-24	heme oxygenase 1	Homo sapiens	123-139
34314818-6	2021	EAA treatment increased nuclear Nrf2 translocation via the p38, PKC, and ROS pathways leading to HO-1, gamma-GCLC, and NQO-1 antioxidant expression in HaCaT cells.	3-O-ethylascorbic acid	0-3	heme oxygenase 1	Homo sapiens	97-101
34426902-10	2021	Moreover, the expression of HO-1 and NQO-1 was upregulated in hASCs pretreated with DMF which confirms the activation of the Nrf2 pathway.	Dimethyl Fumarate	84-87	heme oxygenase 1	Homo sapiens	28-32
34296312-0	2021	Dimethyl itaconate inhibits LPS-induced microglia inflammation and inflammasome-mediated pyroptosis via inducing autophagy and regulating the Nrf-2/HO-1 signaling pathway.	dimethyl itaconate	0-18	heme oxygenase 1	Homo sapiens	148-152
34296312-9	2021	In addition, DI effectively reduced reactive oxygen species production through the Nrf-2/HO-1 pathway.	dimethyl itaconate	13-15	heme oxygenase 1	Homo sapiens	89-93
34296312-9	2021	In addition, DI effectively reduced reactive oxygen species production through the Nrf-2/HO-1 pathway.	Reactive Oxygen Species	36-59	heme oxygenase 1	Homo sapiens	89-93
34197898-7	2021	We demonstrated that the drug exerted its cytoprotective effects by activating nuclear factor erythroid 2-related factor 2 (Nrf2)/heme-oxygenase (HO)-1 pathway, which in turn, is dependent on AKT activation by metformin.	Metformin	210-219	heme oxygenase 1	Homo sapiens	130-151
34106394-11	2021	NaB also suppressed the BAX nuclear translocation and modulated Nrf-2, HO-1 and MnSOD expression in neuroblastoma cells.	nab	0-3	heme oxygenase 1	Homo sapiens	71-75
34573035-0	2021	Bilirubin Links HO-1 and UGT1A1*28 Gene Polymorphisms to Predict Cardiovascular Outcome in Patients Receiving Maintenance Hemodialysis.	Bilirubin	0-9	heme oxygenase 1	Homo sapiens	16-20
34425169-7	2021	While the progression of gene changes was different for each subject, a common pattern was observed in arsenic treated cells over time, with early upregulation of oxidative stress responses (HMOX1, NQ01, TXN, TXNRD1) and down-regulation of immune/inflammatory responses (IKKalpha).	Arsenic	103-110	heme oxygenase 1	Homo sapiens	191-196
34216683-10	2021	The increase in nuclear Nrf2, HO-1 and NQO1 expression induced by isoflurane was amplified by treatment with BCA.	Isoflurane	66-76	heme oxygenase 1	Homo sapiens	30-34
34573035-1	2021	Serum bilirubin levels, which are determined by a complex interplay of various enzymes, including heme oxygenase-1 (HO-1) and uridine diphosphate-glucuronosyl transferase (UGT1A1), may be protective against progression of cardiovascular disease (CVD) in hemodialysis patients.	Bilirubin	6-15	heme oxygenase 1	Homo sapiens	98-114
34427071-12	2021	Our results also showed that temozolomide-induced ferroptosis is associated with regulation of the Nrf2/HO-1 pathway.	Temozolomide	29-41	heme oxygenase 1	Homo sapiens	104-108
34573035-1	2021	Serum bilirubin levels, which are determined by a complex interplay of various enzymes, including heme oxygenase-1 (HO-1) and uridine diphosphate-glucuronosyl transferase (UGT1A1), may be protective against progression of cardiovascular disease (CVD) in hemodialysis patients.	Bilirubin	6-15	heme oxygenase 1	Homo sapiens	116-120
34573035-3	2021	This retrospective study enrolled 1080 prevalent hemodialysis patients and the combined genetic polymorphisms of HO-1 and UGT1A1 on serum bilirubin were analyzed.	Bilirubin	138-147	heme oxygenase 1	Homo sapiens	113-117
34573035-5	2021	Mean serum bilirubin was highest in patients with S/S + S/L of the HO-1 promoter and UGT1A1 7/7 genotypes (Group 1), intermediate in those with S/S + S/L of the HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 2), and lowest in the carriers with the L/L HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 3) (p < 0.001).	Bilirubin	11-20	heme oxygenase 1	Homo sapiens	67-71
34573035-5	2021	Mean serum bilirubin was highest in patients with S/S + S/L of the HO-1 promoter and UGT1A1 7/7 genotypes (Group 1), intermediate in those with S/S + S/L of the HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 2), and lowest in the carriers with the L/L HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 3) (p < 0.001).	Bilirubin	11-20	heme oxygenase 1	Homo sapiens	161-165
34504854-4	2021	Heme oxygenase-1 (HO-1), an enzyme involved in the process of heme degradation, has attracted widespread attention in recent years due to its cytoprotective properties.	Heme	62-66	heme oxygenase 1	Homo sapiens	0-16
34503136-0	2021	Chrysosplenol D Triggers Apoptosis through Heme Oxygenase-1 and Mitogen-Activated Protein Kinase Signaling in Oral Squamous Cell Carcinoma.	chrysosplenol D	0-15	heme oxygenase 1	Homo sapiens	43-59
34503136-7	2021	Moreover, the upregulation of heme oxygenase-1 (HO-1) was found to be critical for chrysosplenol D-induced apoptotic cell death.	Chrysosplenol C	83-96	heme oxygenase 1	Homo sapiens	30-46
34503136-7	2021	Moreover, the upregulation of heme oxygenase-1 (HO-1) was found to be critical for chrysosplenol D-induced apoptotic cell death.	Chrysosplenol C	83-96	heme oxygenase 1	Homo sapiens	48-52
34503136-9	2021	The findings of the present study indicated that chrysosplenol D exerts anticancer effects on OSCC by suppressing the MAPK pathway and activating HO-1 expression.	chrysosplenol D	49-64	heme oxygenase 1	Homo sapiens	146-150
34217685-5	2021	Furthermore, it was demonstrated that luteolin promoted Nrf2 nuclear translocation, thereby increasing the expression of HO-1 that reduces ROS production, while the anti-pyroptotic effect of luteolin was reversed by a specific Nrf2 inhibitor.	ros	139-142	heme oxygenase 1	Homo sapiens	121-125
34504854-4	2021	Heme oxygenase-1 (HO-1), an enzyme involved in the process of heme degradation, has attracted widespread attention in recent years due to its cytoprotective properties.	Heme	62-66	heme oxygenase 1	Homo sapiens	18-22
34504854-7	2021	Many strategies, such as the administration of HO-1-overexpressing macrophages, use of phytochemicals, and carbon monoxide-based therapies, have been developed to target HO-1 in a variety of nephropathological animal models, indicating that HO-1 is a promising protein for the treatment of kidney diseases.	Carbon Monoxide	107-122	heme oxygenase 1	Homo sapiens	170-174
34483918-0	2021	Nicardipine Inhibits Breast Cancer Migration via Nrf2/HO-1 Axis and Matrix Metalloproteinase-9 Regulation.	Nicardipine	0-11	heme oxygenase 1	Homo sapiens	54-58
34557667-12	2021	Notably, the administration of dimethyl itaconate to compensate for the deficiency of immunoresponsive gene 1/itaconate axis led to enhanced microglial heme oxygenase-1 expression, alleviated ischaemic brain injury, improved motor function and decreased mortality in IRG1-/- stroke animals.	dimethyl itaconate	31-49	heme oxygenase 1	Homo sapiens	152-168
34557667-12	2021	Notably, the administration of dimethyl itaconate to compensate for the deficiency of immunoresponsive gene 1/itaconate axis led to enhanced microglial heme oxygenase-1 expression, alleviated ischaemic brain injury, improved motor function and decreased mortality in IRG1-/- stroke animals.	itaconic acid	110-119	heme oxygenase 1	Homo sapiens	152-168
34485154-8	2021	5-FU promoted the expression of Keap1 and increased the binding to NF-E2-related factor 2 (Nrf2) to reduce the nuclear translocation of Nrf2, thereby weakening the transcriptional activity of Nrf2 to inhibit the expression of HO-1; reducing the activity of GSH, SOD, and CAT to increase ROS content; and aggravating DNA damage (indicated by the increase in 8-OHdG).	Fluorouracil	0-4	heme oxygenase 1	Homo sapiens	226-230
34602929-8	2021	In addition, the effects of TMF on Abeta25-35 toxicity were related to the upregulation of phase II antioxidant and nuclear factor erythroid 2-related factor-2 (Nrf2) signaling, including superoxide dismutase (SOD), heme oxygenase (HO)-1, and nuclear translocation of Nrf2.	5,6,7,4'-tetramethoxyflavanone	28-31	heme oxygenase 1	Homo sapiens	216-237
34445549-7	2021	In addition, western blot analysis also demonstrated that kaempferol and kaempferide reduced expression of heme oxygenase-1 (HO-1) and nuclear transcription factor-erythroid 2-related factor 2 (Nrf2).	kaempferol	58-68	heme oxygenase 1	Homo sapiens	107-123
34445549-7	2021	In addition, western blot analysis also demonstrated that kaempferol and kaempferide reduced expression of heme oxygenase-1 (HO-1) and nuclear transcription factor-erythroid 2-related factor 2 (Nrf2).	kaempferol	58-68	heme oxygenase 1	Homo sapiens	125-129
34445549-7	2021	In addition, western blot analysis also demonstrated that kaempferol and kaempferide reduced expression of heme oxygenase-1 (HO-1) and nuclear transcription factor-erythroid 2-related factor 2 (Nrf2).	kaempferide	73-84	heme oxygenase 1	Homo sapiens	107-123
34445549-7	2021	In addition, western blot analysis also demonstrated that kaempferol and kaempferide reduced expression of heme oxygenase-1 (HO-1) and nuclear transcription factor-erythroid 2-related factor 2 (Nrf2).	kaempferide	73-84	heme oxygenase 1	Homo sapiens	125-129
34087331-13	2021	RT-PCR confirmed the HMOX1 upregulation and ATG12 downregulation protected the PC-3rst23 cells from SRJ23 cytotoxicity.	srj23	100-105	heme oxygenase 1	Homo sapiens	21-26
34483918-10	2021	The inhibition of HO-1 abrogates nicardipine-reduced matrix metalloproteinase-9 expression.	Nicardipine	33-44	heme oxygenase 1	Homo sapiens	18-22
34483918-11	2021	Moreover, the end products of HO-1, namely, CO, Fe2+, and biliverdin (will converted to bilirubin), also decreases the expression of matrix metalloproteinase-9.	Carbon Monoxide	44-46	heme oxygenase 1	Homo sapiens	30-34
34483918-11	2021	Moreover, the end products of HO-1, namely, CO, Fe2+, and biliverdin (will converted to bilirubin), also decreases the expression of matrix metalloproteinase-9.	ammonium ferrous sulfate	48-52	heme oxygenase 1	Homo sapiens	30-34
34483918-11	2021	Moreover, the end products of HO-1, namely, CO, Fe2+, and biliverdin (will converted to bilirubin), also decreases the expression of matrix metalloproteinase-9.	Biliverdine	58-68	heme oxygenase 1	Homo sapiens	30-34
34483918-11	2021	Moreover, the end products of HO-1, namely, CO, Fe2+, and biliverdin (will converted to bilirubin), also decreases the expression of matrix metalloproteinase-9.	Bilirubin	88-97	heme oxygenase 1	Homo sapiens	30-34
34483918-12	2021	Conclusion: These findings suggest that nicardipine-mediated matrix metalloproteinase-9 reduction is regulated by Nrf2/HO-1 axis and its catalytic end products.	Nicardipine	40-51	heme oxygenase 1	Homo sapiens	119-123
34483918-9	2021	In addition, we also revealed that nicardipine increases the Nrf2 and HO-1 expression.	Nicardipine	35-46	heme oxygenase 1	Homo sapiens	70-74
34369898-0	2022	Effect of Ginsenoside Rh1 on proliferation, apoptosis, and oxidative stress in vascular endothelial cells via regulation of the Nrf2/HO-1 signaling pathway.	ginsenoside Rh1	10-25	heme oxygenase 1	Homo sapiens	133-137
34456904-8	2021	ME markedly increased the expression of Nrf2, thus resulting in a higher level of HO-1.	methionylglutamic acid	0-2	heme oxygenase 1	Homo sapiens	82-86
34452191-5	2021	Hemin (HO-1 inducer) induced HO-1 mRNA and protein expression, as expected, and below 50 mM, dose-dependently reduced the viral RNA and proteins in the HAV-infected cells without cytotoxicity.	Hemin	0-5	heme oxygenase 1	Homo sapiens	7-11
34452191-5	2021	Hemin (HO-1 inducer) induced HO-1 mRNA and protein expression, as expected, and below 50 mM, dose-dependently reduced the viral RNA and proteins in the HAV-infected cells without cytotoxicity.	Hemin	0-5	heme oxygenase 1	Homo sapiens	29-33
34452191-7	2021	Although ZnPP-9, an HO-1 inhibitor, did not affect HAV replication, it significantly inhibited hemin-induced antiviral activity in HAV-infected cells.	zinc protoporphyrin	9-15	heme oxygenase 1	Homo sapiens	20-24
34452191-8	2021	Additionally, FeCl3, CORM-3, biliverdin, and the HO-1 inducers andrographolide and CoPP inhibited HAV replication in the HAV-infected cells; andrographolide and CoPP exhibited a dose-dependent effect.	andrographolide	63-78	heme oxygenase 1	Homo sapiens	49-53
34452191-8	2021	Additionally, FeCl3, CORM-3, biliverdin, and the HO-1 inducers andrographolide and CoPP inhibited HAV replication in the HAV-infected cells; andrographolide and CoPP exhibited a dose-dependent effect.	COPP protocol	83-87	heme oxygenase 1	Homo sapiens	49-53
34369898-7	2022	Moreover, ginsenoside Rh1 also relieved oxidative stress in ox-LDL-treated VECs by activating the Nef2/HO-1 signaling pathway.	ginsenoside Rh1	10-25	heme oxygenase 1	Homo sapiens	103-107
34369898-8	2022	Thus, ginsenoside Rh1 affects the proliferation, apoptosis, and oxidative stress in ox-LDL-treated VECs by activating the Nef2/HO-1 signaling pathway.	ginsenoside Rh1	6-21	heme oxygenase 1	Homo sapiens	127-131
34313971-12	2021	Moreover, A-EVs significantly upregulated the mRNA expression of Nrf2, HO-1, CAT, and SOD genes in H2O2-treated HaCaT cells.	a-evs	10-15	heme oxygenase 1	Homo sapiens	71-75
34361114-8	2021	The results of the present study demonstrate that pDCs can respond to LPS and that quercetin exposure modulates soluble factors release through the same molecular pathway used by mDCs (Slpi, Hmox1, and AP-1).	Quercetin	83-92	heme oxygenase 1	Homo sapiens	191-196
34338265-6	2021	Further study showed that the protective effect of kaempferol was associated with an enhanced mRNA level of genes related to cell cycle progression (cyclin D1, CDK4, and E2F1) and genes implicated in the anti-oxidant system (GSR, GSTA4, and HO-1), up-regulated abundance of tight junctions (ZO-1, ZO-2, occludin, and claudin-4), as well as enhanced Nrf2, an anti-oxidant transcription factor.	kaempferol	51-61	heme oxygenase 1	Homo sapiens	241-245
34382871-2	2021	In this study, the effects of CYJ-27 on the regulation of inducible nitric oxide synthase (iNOS), heme oxygenase (HO)-1, and cyclooxygenase (COX-)2 were characterized in lipopolysaccharide (LPS)-treated human umbilical vein endothelial cells (HUVECs).	cyj-27	30-36	heme oxygenase 1	Homo sapiens	98-139
34175589-6	2021	RESULTS: Obesity-associated AHR is ameliorated by administration of BCP by inhibition of the macrophage polarization by activation of AMPKalpha, Nrf2/HO-1 and AdipoR1 and AdipoR2 signaling pathway, up-regulation of adiponectin, GLP-1, IFN-gamma, SOD, catalase and down-regulation of NF-kappaB, leptin, IL-4, TNF, and IL-1beta.	caryophyllene	68-71	heme oxygenase 1	Homo sapiens	150-154
34313971-12	2021	Moreover, A-EVs significantly upregulated the mRNA expression of Nrf2, HO-1, CAT, and SOD genes in H2O2-treated HaCaT cells.	Hydrogen Peroxide	99-103	heme oxygenase 1	Homo sapiens	71-75
34360702-5	2021	Overexpression of Nrf2 or its target gene heme oxygenase 1 (HO1) significantly blocked the ROS accumulation in MCF-7 cells under T-2 toxin treatment.	Reactive Oxygen Species	91-94	heme oxygenase 1	Homo sapiens	42-58
34361019-6	2021	Here, we examined whether pharmacological induction of HO-1 by cobalt protoporphyrin (CoPP) ameliorates cholestatic liver injury.	cobaltiprotoporphyrin	63-84	heme oxygenase 1	Homo sapiens	55-59
34361019-6	2021	Here, we examined whether pharmacological induction of HO-1 by cobalt protoporphyrin (CoPP) ameliorates cholestatic liver injury.	cobaltiprotoporphyrin	86-90	heme oxygenase 1	Homo sapiens	55-59
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Heme	114-118	heme oxygenase 1	Homo sapiens	0-16
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Heme	114-118	heme oxygenase 1	Homo sapiens	18-22
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Carbon Monoxide	145-160	heme oxygenase 1	Homo sapiens	0-16
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Carbon Monoxide	145-160	heme oxygenase 1	Homo sapiens	18-22
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Iron	162-166	heme oxygenase 1	Homo sapiens	0-16
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Iron	162-166	heme oxygenase 1	Homo sapiens	18-22
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Biliverdine	172-182	heme oxygenase 1	Homo sapiens	0-16
34360940-3	2021	Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin.	Biliverdine	172-182	heme oxygenase 1	Homo sapiens	18-22
34321570-2	2021	Quantifying circadian disruption by analyzing expression of the circadian gene period circadian regulator 2 (PER2) and heme oxygenase 1 (HO1), which determines heme turnover, may prove to be potential diagnostic tools.	Heme	160-164	heme oxygenase 1	Homo sapiens	119-135
34321570-2	2021	Quantifying circadian disruption by analyzing expression of the circadian gene period circadian regulator 2 (PER2) and heme oxygenase 1 (HO1), which determines heme turnover, may prove to be potential diagnostic tools.	Heme	160-164	heme oxygenase 1	Homo sapiens	137-140
34312792-12	2022	Associations of early low HO-1 expression with vasospasm and late elevated HO-1 expression with DCI may point to detrimental effects of late HO-1 induction, warranting the need for further investigation in a larger study population.	dci	96-99	heme oxygenase 1	Homo sapiens	75-79
34360702-5	2021	Overexpression of Nrf2 or its target gene heme oxygenase 1 (HO1) significantly blocked the ROS accumulation in MCF-7 cells under T-2 toxin treatment.	Reactive Oxygen Species	91-94	heme oxygenase 1	Homo sapiens	60-63
34290541-3	2021	In 2018, we reported that heme oxygenase-1 (HO-1), an inducible stress response protein important for heme catabolism and implicated in PD pathology, was higher in PD saliva relative to healthy controls, suggesting that salivary HO-1 may serve as a potential biomarker of PD.	Heme	102-106	heme oxygenase 1	Homo sapiens	44-48
34305600-6	2021	At the same time, the GN combination could also inhibit the H2O2-induced inflammatory response and apoptosis of human umbilical vein endothelial cells (HUVECs), which is mainly related to the activation of the AMPK/mTOR pathway by GN combination, which in turn induces the activation of Nrf2/HO-1 signal.	Hydrogen Peroxide	60-64	heme oxygenase 1	Homo sapiens	292-296
34439417-7	2021	The cellular components mediating the downregulation of ROS included extracellular signal-regulated kinase 1/2 (ERK1/2), nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1), and uncoupling protein 2 (UCP2).	Reactive Oxygen Species	56-59	heme oxygenase 1	Homo sapiens	173-189
34439417-7	2021	The cellular components mediating the downregulation of ROS included extracellular signal-regulated kinase 1/2 (ERK1/2), nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1), and uncoupling protein 2 (UCP2).	Reactive Oxygen Species	56-59	heme oxygenase 1	Homo sapiens	191-195
34264023-10	2022	Carcinoma cells with high HO-1 levels were significantly associated with pathological resistance to NACRT.	nacrt	100-105	heme oxygenase 1	Homo sapiens	26-30
34264023-13	2022	HO-1 levels in lymph node metastases could be used to predict the eventual clinical outcome of patients with esophageal cancer receiving NACRT.	nacrt	137-142	heme oxygenase 1	Homo sapiens	0-4
34290541-3	2021	In 2018, we reported that heme oxygenase-1 (HO-1), an inducible stress response protein important for heme catabolism and implicated in PD pathology, was higher in PD saliva relative to healthy controls, suggesting that salivary HO-1 may serve as a potential biomarker of PD.	Heme	102-106	heme oxygenase 1	Homo sapiens	26-42
34228907-10	2021	Additionally, Isoeucommin A protected H2 O2 -stimulated renal tubular epithelial cells (RTECs) from oxidative stress and activated Nrf2/HO-1 signaling pathway in high glucose-stimulated human renal mesangial cells (HRMCs).	Isoeucommin A	14-27	heme oxygenase 1	Homo sapiens	136-140
34228907-10	2021	Additionally, Isoeucommin A protected H2 O2 -stimulated renal tubular epithelial cells (RTECs) from oxidative stress and activated Nrf2/HO-1 signaling pathway in high glucose-stimulated human renal mesangial cells (HRMCs).	Hydrogen Peroxide	38-43	heme oxygenase 1	Homo sapiens	136-140
34228907-11	2021	In conclusion, Isoeucommin A could alleviate inflammation and oxidative stress in in vitro and in vivo DN models and thus attenuate kidney injury by activating the Nrf2/HO-1 signaling pathway.	Isoeucommin A	15-28	heme oxygenase 1	Homo sapiens	169-173
34209690-6	2021	Treatment with Hidrox  was able to improve CYP-induced inflammation and oxidative stress via the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	hidrox	15-21	heme oxygenase 1	Homo sapiens	148-164
34075731-2	2021	Herein, PEGylated CuMoOx -coated and zinc protoporphyrin IX (ZP)-loaded Cu (CCMZ) NPs are designed to afford rapid degradation ability and augmented CDT efficacy through inhibiting HO-1 activity and depleting GSH.	cumoox	18-24	heme oxygenase 1	Homo sapiens	181-185
34075731-2	2021	Herein, PEGylated CuMoOx -coated and zinc protoporphyrin IX (ZP)-loaded Cu (CCMZ) NPs are designed to afford rapid degradation ability and augmented CDT efficacy through inhibiting HO-1 activity and depleting GSH.	zinc protoporphyrin	37-59	heme oxygenase 1	Homo sapiens	181-185
34075731-2	2021	Herein, PEGylated CuMoOx -coated and zinc protoporphyrin IX (ZP)-loaded Cu (CCMZ) NPs are designed to afford rapid degradation ability and augmented CDT efficacy through inhibiting HO-1 activity and depleting GSH.	zinc protoporphyrin	61-63	heme oxygenase 1	Homo sapiens	181-185
34075731-2	2021	Herein, PEGylated CuMoOx -coated and zinc protoporphyrin IX (ZP)-loaded Cu (CCMZ) NPs are designed to afford rapid degradation ability and augmented CDT efficacy through inhibiting HO-1 activity and depleting GSH.	Copper	72-74	heme oxygenase 1	Homo sapiens	181-185
34075731-2	2021	Herein, PEGylated CuMoOx -coated and zinc protoporphyrin IX (ZP)-loaded Cu (CCMZ) NPs are designed to afford rapid degradation ability and augmented CDT efficacy through inhibiting HO-1 activity and depleting GSH.	ccmz	76-80	heme oxygenase 1	Homo sapiens	181-185
34075731-2	2021	Herein, PEGylated CuMoOx -coated and zinc protoporphyrin IX (ZP)-loaded Cu (CCMZ) NPs are designed to afford rapid degradation ability and augmented CDT efficacy through inhibiting HO-1 activity and depleting GSH.	cdt	149-152	heme oxygenase 1	Homo sapiens	181-185
34075731-5	2021	Furthermore, the release of ZP from CCMZ NPs can inhibit HO-1 activity and provide a favorable microenvironment for CDT, and the release of Cu and Mo ions can convert hydrogen peroxide into hydroxyl radical to eliminate tumor cells more efficiently.	ccmz	36-40	heme oxygenase 1	Homo sapiens	57-61
34082940-6	2021	Compared with free BA, Exo-BA significantly reduced the generation of reactive oxygen species (ROS) and activated the Nrf2/HO-1 pathway in neurons, thus significantly alleviating cerebral ischemic injury in a stroke model.	exo-ba	23-29	heme oxygenase 1	Homo sapiens	123-127
34209690-6	2021	Treatment with Hidrox  was able to improve CYP-induced inflammation and oxidative stress via the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	hidrox	15-21	heme oxygenase 1	Homo sapiens	166-170
34345202-0	2021	Tagitinin C induces ferroptosis through PERK-Nrf2-HO-1 signaling pathway in colorectal cancer cells.	tagitinin	0-11	heme oxygenase 1	Homo sapiens	50-54
34345202-11	2021	As a downstream gene (effector) of Nrf2, heme oxygenase-1 (HO-1) expression increased significantly with the treatment of tagitinin C. Upregulated HO-1 led to the increase in the labile iron pool, which promoted lipid peroxidation, meanwhile tagitinin C showed synergistic anti-tumor effect together with erastin.	Iron	186-190	heme oxygenase 1	Homo sapiens	147-151
34345202-13	2021	Mechanistically, tagitinin C induces ferroptosis through ER stress-mediated activation of PERK-Nrf2-HO-1 signaling pathway.	tagitinin	17-28	heme oxygenase 1	Homo sapiens	100-104
34208670-5	2021	After HO-1 pharmacological induction with hemin, PC3 and C4-2B cells exhibited a significantly impaired cellular metabolic rate, reflected by glucose uptake, ATP production, lactate dehydrogenase (LDH) activity and extracellular lactate levels.	Hemin	42-47	heme oxygenase 1	Homo sapiens	6-10
34202670-0	2021	Cytoprotection against Oxidative Stress by Methylnissolin-3-O-beta-d-glucopyranoside from Astragalus membranaceus Mainly via the Activation of the Nrf2/HO-1 Pathway.	methylnissolin-3-o-beta-d-glucopyranoside	43-84	heme oxygenase 1	Homo sapiens	152-156
34202670-5	2021	MNG induced the expression of Nrf2, HO-1 and NQO1, accelerated the translocation of Nrf2 into nuclei, and enhanced the phosphorylation of AKT.	1-Methyl-3-nitro-1-nitrosoguanidine	0-3	heme oxygenase 1	Homo sapiens	36-40
34202670-6	2021	The MNG-induced expression of Nrf2, HO-1, and NQO1 were abolished by Nrf2 siRNA, while the MNG-induced expression of Nrf2 and HO-1 was abated and the AKT phosphorylation was blocked by LY294002 (a PI3K inhibitor).	1-Methyl-3-nitro-1-nitrosoguanidine	4-7	heme oxygenase 1	Homo sapiens	36-40
34202670-6	2021	The MNG-induced expression of Nrf2, HO-1, and NQO1 were abolished by Nrf2 siRNA, while the MNG-induced expression of Nrf2 and HO-1 was abated and the AKT phosphorylation was blocked by LY294002 (a PI3K inhibitor).	1-Methyl-3-nitro-1-nitrosoguanidine	4-7	heme oxygenase 1	Homo sapiens	126-130
34202670-6	2021	The MNG-induced expression of Nrf2, HO-1, and NQO1 were abolished by Nrf2 siRNA, while the MNG-induced expression of Nrf2 and HO-1 was abated and the AKT phosphorylation was blocked by LY294002 (a PI3K inhibitor).	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	185-193	heme oxygenase 1	Homo sapiens	36-40
34202670-6	2021	The MNG-induced expression of Nrf2, HO-1, and NQO1 were abolished by Nrf2 siRNA, while the MNG-induced expression of Nrf2 and HO-1 was abated and the AKT phosphorylation was blocked by LY294002 (a PI3K inhibitor).	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	185-193	heme oxygenase 1	Homo sapiens	126-130
34202670-9	2021	The enhancement of Nrf2 and HO-1 by MNG upon H2O2 injury was reduced by LY294002.	1-Methyl-3-nitro-1-nitrosoguanidine	36-39	heme oxygenase 1	Homo sapiens	28-32
34202670-9	2021	The enhancement of Nrf2 and HO-1 by MNG upon H2O2 injury was reduced by LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	72-80	heme oxygenase 1	Homo sapiens	28-32
34202670-10	2021	These data showed that MNG protected EA.hy926 cells against oxidative damage through the Nrf2/HO-1 and at least partially the PI3K/Akt pathways.	1-Methyl-3-nitro-1-nitrosoguanidine	23-26	heme oxygenase 1	Homo sapiens	94-98
34135317-9	2021	Functionally, overexpression of HO-1 counteracted the promotional effects of SIRT4 on ROS accumulation and apoptosis.	Reactive Oxygen Species	86-89	heme oxygenase 1	Homo sapiens	32-36
34135317-11	2021	By contrast, downregulation of p38-MAPK by SB203580 decreased intracellular ROS level and enhanced the expression of HO-1.	SB 203580	43-51	heme oxygenase 1	Homo sapiens	117-121
34208670-5	2021	After HO-1 pharmacological induction with hemin, PC3 and C4-2B cells exhibited a significantly impaired cellular metabolic rate, reflected by glucose uptake, ATP production, lactate dehydrogenase (LDH) activity and extracellular lactate levels.	Glucose	142-149	heme oxygenase 1	Homo sapiens	6-10
34208670-5	2021	After HO-1 pharmacological induction with hemin, PC3 and C4-2B cells exhibited a significantly impaired cellular metabolic rate, reflected by glucose uptake, ATP production, lactate dehydrogenase (LDH) activity and extracellular lactate levels.	Adenosine Triphosphate	158-161	heme oxygenase 1	Homo sapiens	6-10
34208670-5	2021	After HO-1 pharmacological induction with hemin, PC3 and C4-2B cells exhibited a significantly impaired cellular metabolic rate, reflected by glucose uptake, ATP production, lactate dehydrogenase (LDH) activity and extracellular lactate levels.	Lactic Acid	229-236	heme oxygenase 1	Homo sapiens	6-10
34306342-8	2021	UTI blocked ferroptosis-induced lipid peroxide accumulation by promoting nuclear translocation of NRF2 to activate its downstream targets (HO-1).	Lipid Peroxides	32-46	heme oxygenase 1	Homo sapiens	139-143
34646076-14	2021	Conclusions: We concluded that d-Leu protects oocytes from psychological stress through the induction of HO-1 and SOD2 expression then by reducing oxidative stress.	D-LEUCINE	31-36	heme oxygenase 1	Homo sapiens	105-109
34127699-5	2021	Furthermore, selumetinib reduced acrolein-induced increases in heme oxygenase-1 (a redox-regulated chaperone protein) and its transcriptional factor, Nrf-2 as well as FDP-lysine (acrolein-lysine adducts) and alpha-synuclein aggregation (a pathological biomarker of neurodegeneration).	AZD 6244	13-24	heme oxygenase 1	Homo sapiens	63-79
34127699-8	2021	In conclusion, our study showed that selumetinib inhibited acrolein-activated Nrf-2-HO-1 pathway, acrolein-induced protein conjugation and aggregation as well as damage in neurite outgrowth and cell death, suggesting that selumetinib, a MEK-ERK inhibitor, may be a potential neuroprotective agent against acrolein-induced neurotoxicity in the CNS neurodegenerative diseases.	AZD 6244	37-48	heme oxygenase 1	Homo sapiens	84-88
34127699-5	2021	Furthermore, selumetinib reduced acrolein-induced increases in heme oxygenase-1 (a redox-regulated chaperone protein) and its transcriptional factor, Nrf-2 as well as FDP-lysine (acrolein-lysine adducts) and alpha-synuclein aggregation (a pathological biomarker of neurodegeneration).	Acrolein	33-41	heme oxygenase 1	Homo sapiens	63-79
34127699-8	2021	In conclusion, our study showed that selumetinib inhibited acrolein-activated Nrf-2-HO-1 pathway, acrolein-induced protein conjugation and aggregation as well as damage in neurite outgrowth and cell death, suggesting that selumetinib, a MEK-ERK inhibitor, may be a potential neuroprotective agent against acrolein-induced neurotoxicity in the CNS neurodegenerative diseases.	Acrolein	59-67	heme oxygenase 1	Homo sapiens	84-88
34212035-3	2021	When treated with Carvacrol or tert-butylhydroquinone (TBHQ) that activates Nrf2, the expression of Keap1/Nrf2/HO-1, epithelial-mesenchymal transition- (EMT-) related proteins, and NALP3 was examined in OSCC cells.	carvacrol	18-27	heme oxygenase 1	Homo sapiens	111-115
34208202-9	2021	Antioxidant properties of santamarine were also shown to arise from stimulating Nrf2-dependent expression of antioxidant enzymes SOD-1 and HO-1 in UVA-irradiated HDFs.	santamarine	26-37	heme oxygenase 1	Homo sapiens	139-143
34212035-8	2021	Carvacrol significantly suppressed Keap1/Nrf2/HO-1 activation.	carvacrol	0-9	heme oxygenase 1	Homo sapiens	46-50
34212035-9	2021	Carvacrol or silencing Nrf2 markedly inhibited the expression of Keap1/Nrf2/HO-1, EMT-related proteins, and NALP3 inflammasome in OSCC cells.	carvacrol	0-9	heme oxygenase 1	Homo sapiens	76-80
34198827-7	2021	In addition, carnosic acid increased the translation of heme oxygenase-1 (HO-1), gamma-glutamylcysteine synthetase (gamma-GCSc), and glutathione S-transferase (GST) and both the translation and nuclear translocation of nuclear factor erythroid 2-related factor 2 (Nrf2).	salvin	13-26	heme oxygenase 1	Homo sapiens	56-72
34198827-7	2021	In addition, carnosic acid increased the translation of heme oxygenase-1 (HO-1), gamma-glutamylcysteine synthetase (gamma-GCSc), and glutathione S-transferase (GST) and both the translation and nuclear translocation of nuclear factor erythroid 2-related factor 2 (Nrf2).	salvin	13-26	heme oxygenase 1	Homo sapiens	74-78
34198827-8	2021	Taken together, these results indicate that carnosic acid could down-regulate ROS level in an early stage of MPI-induced adipocyte differentiation by attenuating ROS generation through suppression of NF-kappaB-mediated translation of Nox4 enzyme and increasing ROS neutralization through induction of Nrf2-mediated translation of phase II antioxidant enzymes such as HO-1, gamma-GCS, and GST, leading to its anti-adipogenetic effect.	salvin	44-57	heme oxygenase 1	Homo sapiens	367-371
34198827-8	2021	Taken together, these results indicate that carnosic acid could down-regulate ROS level in an early stage of MPI-induced adipocyte differentiation by attenuating ROS generation through suppression of NF-kappaB-mediated translation of Nox4 enzyme and increasing ROS neutralization through induction of Nrf2-mediated translation of phase II antioxidant enzymes such as HO-1, gamma-GCS, and GST, leading to its anti-adipogenetic effect.	Reactive Oxygen Species	78-81	heme oxygenase 1	Homo sapiens	367-371
34077680-7	2021	In addition, ZMO treatment markedly upregulated the expression of Nrf2 as well as its target genes, HO-1 and NAD(P)H:quinone oxidoreductase 1 in HepG2 cells.	S-[2-({n-[(2s)-2-Hydroxy-3,3-Dimethyl-4-(Phosphonooxy)butanoyl]-Beta-Alanyl}amino)ethyl] (9z)-Hexadec-9-Enethioate	13-16	heme oxygenase 1	Homo sapiens	100-104
34199777-3	2021	Using an in vitro model, we demonstrated that HO-1 overexpression regulates stemness and resistance to 5-FU treatment, regardless of p53.	Fluorouracil	103-107	heme oxygenase 1	Homo sapiens	46-50
34199777-5	2021	Carbon monoxide (CO) activated the ECE-1/endothelin-1 (ET-1) pathway, which could account for the protumoral effects of HO-1 in p53 wild-type cells, as demonstrated after treatment with bosentan (an antagonist of both ETRA and ETRB endothelin-1 receptors).	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	120-124
34199777-5	2021	Carbon monoxide (CO) activated the ECE-1/endothelin-1 (ET-1) pathway, which could account for the protumoral effects of HO-1 in p53 wild-type cells, as demonstrated after treatment with bosentan (an antagonist of both ETRA and ETRB endothelin-1 receptors).	Bosentan	186-194	heme oxygenase 1	Homo sapiens	120-124
34199777-7	2021	In these cells, HO-1 could activate or inactivate certain unknown routes that could induce these contrary responses after treatment with bosentan in our cell model.	Bosentan	137-145	heme oxygenase 1	Homo sapiens	16-20
35561750-9	2022	CoCl2-induced oxidative stress results in activation of the NRF2/HO-1-mediated cell survival pathway and inhibition of DNA repair, both of which were prevented by MSM.	cobaltous chloride	0-5	heme oxygenase 1	Homo sapiens	65-69
34073678-7	2021	Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms.	Heme	0-4	heme oxygenase 1	Homo sapiens	20-36
34073678-7	2021	Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms.	Heme	0-4	heme oxygenase 1	Homo sapiens	38-42
34073678-7	2021	Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms.	Heme	76-80	heme oxygenase 1	Homo sapiens	20-36
34073678-7	2021	Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms.	Heme	76-80	heme oxygenase 1	Homo sapiens	38-42
34073678-8	2021	Therapeutic strategies targeting the heme/HO-1 pathway, including therapeutic modulation of heme levels, elevation (or inhibition) of HO-1 protein and activity, and application of CO donor compounds or gas show potential in inflammatory conditions including sepsis and pulmonary diseases.	Heme	37-41	heme oxygenase 1	Homo sapiens	42-46
34065300-2	2021	In recent years, 5-ALA has been shown to possess anti-inflammatory and immunoregulatory properties through upregulation of heme oxygenase-1 via enhancement of porphyrin, indicating that it may be beneficial for the treatment of inflammatory conditions.	5-amino levulinic acid	17-22	heme oxygenase 1	Homo sapiens	123-139
34065584-7	2021	Form a molecular point of view, hydroxytyrosol is able to preserve the cellular redox balance and protein homeostasis by activating the Nrf2 pathway and increasing the expression of phase II detoxifying enzymes such as HO-1, SOD, Catalase, and GSH, thus counteracting the neurodegenerative damage.	3,4-dihydroxyphenylethanol	32-46	heme oxygenase 1	Homo sapiens	219-223
34104310-8	2021	In particular, the methanol extract was the most effective in protecting neuron-like SH-SY5Y cells against H2O2-induced oxidative stress by upregulating endogenous antioxidant enzymes such as thioredoxin reductase, heme oxygenase 1, NADPH quinone oxidoreductase, and glutathione reductase.	Methanol	19-27	heme oxygenase 1	Homo sapiens	215-231
34104310-8	2021	In particular, the methanol extract was the most effective in protecting neuron-like SH-SY5Y cells against H2O2-induced oxidative stress by upregulating endogenous antioxidant enzymes such as thioredoxin reductase, heme oxygenase 1, NADPH quinone oxidoreductase, and glutathione reductase.	Hydrogen Peroxide	107-111	heme oxygenase 1	Homo sapiens	215-231
34066673-6	2021	The expression of genes coding for antioxidant molecules, namely, heme oxygenase-1, alpha glutathione s-transferase, NF-kB, and liver fatty acid binding protein, were decreased due to benomyl.	Benomyl	184-191	heme oxygenase 1	Homo sapiens	66-82
34277866-12	2021	Results: Photobiomodulation at 1, 2, and 3 J/cm2 combined with metformin significantly promoted diabetic cell lines of HPDLSCs viability (in MTT assay and ELISA reader of ROS, TNF-alpha, IL-10 results) and gene expression of Nrf2, Keap1, PIK3, and HO-1 levels (p< 0.05).	Metformin	63-72	heme oxygenase 1	Homo sapiens	248-252
34121971-0	2021	Vinpocetine-based therapy is an attractive strategy against oxidative stress-induced hepatotoxicity in vitro by targeting Nrf2/HO-1 pathway.	vinpocetine	0-11	heme oxygenase 1	Homo sapiens	127-131
34113558-12	2021	HMOX1 (up-regulated) and NME1-NME2 (down-regulated) were the main nodes in a PPI network consisting of 16 DEGs that were modulated by sporamin in the presence of TG.	Thapsigargin	162-164	heme oxygenase 1	Homo sapiens	0-5
34069696-3	2021	In H2O2-induced Jukat T cells, haplopine (25 and 50 muM) suppressed the productions of proinflammatory cytokines (IL-4, IL-13, and COX-2) and increased the mRNA and protein expressions of oxidative stress defense enzymes (SOD, CAT, and HO-1) in a concentration-dependent manner.	4,8-dimethoxy-7-hydroxyfuro(2,3-b)quinoline	31-40	heme oxygenase 1	Homo sapiens	236-240
34064340-6	2021	The results showed that DHMBA protected mitochondrial function mainly during cold preservation, and suppressed cell death after rewarming, as shown by the MTT, ATP, mitochondrial membrane potential, LDH, and lipid peroxidation assays, together with enhanced survival signals (PI3K, Akt, p70S6K) and induction of antioxidant proteins (HO-1, NQO-1, TRX-1).	3,5-dihydroxy-4-methoxybenzyl alcohol	24-29	heme oxygenase 1	Homo sapiens	334-338
34277866-0	2021	Efficacy of Photobiomodulation and Metformin on Diabetic Cell Line of Human Periodontal Ligament Stem Cells through Keap1/Nrf2/Ho-1 Pathway.	Metformin	35-44	heme oxygenase 1	Homo sapiens	127-131
34560924-9	2021	Our observations are the first to show that cardiac arrest followed by successful cardiopulmonary resuscitation results in significant alteration in cerebral concentrations of HO-1 and HO-2 levels indicating a prominent role of CO in brain pathology and methylene blue during CPR followed by induced hypothermia leading to superior neuroprotection after return of spontaneous circulation (ROSC), not reported earlier.	Methylene Blue	254-268	heme oxygenase 1	Homo sapiens	176-180
35247778-14	2022	Further mechanistic study demonstrated that 7-d-GDN induced heme oxygenase-1 (HO-1), NAD(P)H dehydrogenase quinone 1(NQO1), which all participated in suppressing of oxidative stress.	7-d-gdn	44-51	heme oxygenase 1	Homo sapiens	60-76
35609387-17	2022	In addition, AU appears to reduce oxidative stress by upregulating NRF2/HO-1.	aucubin	13-15	heme oxygenase 1	Homo sapiens	72-76
35618033-11	2022	Nevertheless, unlike HCQ, CQ is more likely to exaggerate intracellular prooxidant processes in activated starved microglia, which are inefficiently buffered by Nrf2/HO-1 signaling pathway activation.	Chloroquine	26-28	heme oxygenase 1	Homo sapiens	166-170
35460631-1	2022	Carbon monoxide (CO), a member of the multifunctional gasotransmitters family produced by heme oxygenases (i.e., HO-1 and HO-2), has received significant attention because of its involvement in carbohydrate metabolism.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	113-117
35460631-1	2022	Carbon monoxide (CO), a member of the multifunctional gasotransmitters family produced by heme oxygenases (i.e., HO-1 and HO-2), has received significant attention because of its involvement in carbohydrate metabolism.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	113-117
35460631-1	2022	Carbon monoxide (CO), a member of the multifunctional gasotransmitters family produced by heme oxygenases (i.e., HO-1 and HO-2), has received significant attention because of its involvement in carbohydrate metabolism.	Carbohydrates	194-206	heme oxygenase 1	Homo sapiens	113-117
35489465-7	2022	Our results showed that ZEA reduced the antioxidant capacity of the ST cells, induced the cell apoptosis and inhibited the gene and protein expression of Nrf2 and its downstream genes (ho-1,nqo1), while PC improved the cell antioxidant capacity, reduced the degree of ZEA-induced cell apoptosis and promoted the gene and protein expression of Nrf2 and its downstream genes.	Zearalenone	24-27	heme oxygenase 1	Homo sapiens	185-189
35354089-0	2022	Cucurbitacin E glucoside alleviates concanavalin A-induced hepatitis through enhancing SIRT1/Nrf2/HO-1 and inhibiting NF-kB/NLRP3 signaling pathways.	cucurbitacin E	0-14	heme oxygenase 1	Homo sapiens	98-102
35354089-0	2022	Cucurbitacin E glucoside alleviates concanavalin A-induced hepatitis through enhancing SIRT1/Nrf2/HO-1 and inhibiting NF-kB/NLRP3 signaling pathways.	Glucosides	15-24	heme oxygenase 1	Homo sapiens	98-102
35452771-2	2022	Increasing lines of evidence show that T-2 toxin can reduce the levels of tight junction proteins, and nuclear factor erythroid 2-related factor 2 (Nrf2) by disrupting cellular barriers and the cyclic adenosine monophosphate (cAMP)-protein kinase A (PKA) and Nrf2/heme oxygenase (HO)-1 pathways.	Adenosine	201-210	heme oxygenase 1	Homo sapiens	259-285
35452771-2	2022	Increasing lines of evidence show that T-2 toxin can reduce the levels of tight junction proteins, and nuclear factor erythroid 2-related factor 2 (Nrf2) by disrupting cellular barriers and the cyclic adenosine monophosphate (cAMP)-protein kinase A (PKA) and Nrf2/heme oxygenase (HO)-1 pathways.	Cyclic AMP	226-230	heme oxygenase 1	Homo sapiens	259-285
35500767-6	2022	Fucoidan targets multiple signaling systems, including Nrf2/HO-1, NF-kappaB, ERK and p38 MAPK, TGF-beta1, SIRT1, and GLP-1R signaling that are known to be associated with CKD pathobiology.	fucoidan	0-8	heme oxygenase 1	Homo sapiens	60-64
35247778-14	2022	Further mechanistic study demonstrated that 7-d-GDN induced heme oxygenase-1 (HO-1), NAD(P)H dehydrogenase quinone 1(NQO1), which all participated in suppressing of oxidative stress.	7-d-gdn	44-51	heme oxygenase 1	Homo sapiens	78-82
35609009-3	2022	CGA antioxidant effects mediated through the Nrf2-heme oxygenase-1 signaling pathway were shown to enhance the levels of antioxidant enzymes such as superoxide dismutase, catalase, glutathione-S-transferases, glutathione peroxidase, and glutathione reductase as well as glutathione content.	Superoxides	149-159	heme oxygenase 1	Homo sapiens	50-66
35475506-0	2022	3,4-Dihydroxyacetophenone attenuates oxidative stress-induced damage to HUVECs via regulation of the Nrf2/HO-1 pathway.	3,4-dihydroxyacetophenone	0-25	heme oxygenase 1	Homo sapiens	106-110
35475506-12	2022	In addition, high glucose upregulated Nrf2 and HO-1 protein and mRNA expression levels.	Glucose	18-25	heme oxygenase 1	Homo sapiens	47-51
35475506-17	2022	3,4-DHAP markedly decreased the production of ROS, increased Nrf2 and HO-1 protein and mRNA expression levels, and promoted nuclear translocation of Nrf2 in HUVECs.	3,4-dihydroxyacetophenone	0-8	heme oxygenase 1	Homo sapiens	70-74
35475506-19	2022	Moreover, it was determined that compared to the 3,4-DHAP group, treatment with 3,4-DHAP and ML385 enhanced cell viability, and decreased ROS production, Nrf2 and HO-1 protein and mRNA expression levels, nuclear translocation of Nrf2, and LC3-II/LC3-I and PARP-1 protein expression levels.	3,4-dihydroxyacetophenone	49-57	heme oxygenase 1	Homo sapiens	163-167
35475506-19	2022	Moreover, it was determined that compared to the 3,4-DHAP group, treatment with 3,4-DHAP and ML385 enhanced cell viability, and decreased ROS production, Nrf2 and HO-1 protein and mRNA expression levels, nuclear translocation of Nrf2, and LC3-II/LC3-I and PARP-1 protein expression levels.	3,4-dihydroxyacetophenone	80-88	heme oxygenase 1	Homo sapiens	163-167
35475506-19	2022	Moreover, it was determined that compared to the 3,4-DHAP group, treatment with 3,4-DHAP and ML385 enhanced cell viability, and decreased ROS production, Nrf2 and HO-1 protein and mRNA expression levels, nuclear translocation of Nrf2, and LC3-II/LC3-I and PARP-1 protein expression levels.	ML385	93-98	heme oxygenase 1	Homo sapiens	163-167
35475506-20	2022	Collectively, the results of the present study showed that 3,4-DHAP protected HUVECs against oxidative stress via regulation of the Nrf2/HO-1 pathway, by increasing autophagy and promoting DNA damage repair.	3,4-dihydroxyacetophenone	59-67	heme oxygenase 1	Homo sapiens	137-141
35635297-4	2022	In addition, LT significantly affected mitochondrial biogenesis and function and antioxidative related genes expression, and increased the protein expression of p-adenosine monophosphate (AMP)-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-gamma coactivator-1alpha (PGC-1alpha), nuclear factor E2-related factor 2 (Nrf2), NADPH quinone oxidoreductase-1 (NQO1) and heme oxygenase-1 (HO-1) and decreased the Keap1 protein levels.	Adenosine	163-172	heme oxygenase 1	Homo sapiens	396-412
35635297-4	2022	In addition, LT significantly affected mitochondrial biogenesis and function and antioxidative related genes expression, and increased the protein expression of p-adenosine monophosphate (AMP)-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-gamma coactivator-1alpha (PGC-1alpha), nuclear factor E2-related factor 2 (Nrf2), NADPH quinone oxidoreductase-1 (NQO1) and heme oxygenase-1 (HO-1) and decreased the Keap1 protein levels.	Adenosine	163-172	heme oxygenase 1	Homo sapiens	414-418
35609009-3	2022	CGA antioxidant effects mediated through the Nrf2-heme oxygenase-1 signaling pathway were shown to enhance the levels of antioxidant enzymes such as superoxide dismutase, catalase, glutathione-S-transferases, glutathione peroxidase, and glutathione reductase as well as glutathione content.	Glutathione	181-192	heme oxygenase 1	Homo sapiens	50-66
35609009-3	2022	CGA antioxidant effects mediated through the Nrf2-heme oxygenase-1 signaling pathway were shown to enhance the levels of antioxidant enzymes such as superoxide dismutase, catalase, glutathione-S-transferases, glutathione peroxidase, and glutathione reductase as well as glutathione content.	Glutathione	209-220	heme oxygenase 1	Homo sapiens	50-66
35537139-11	2022	Meanwhile, the increased expression of SIRT1/PPAR-alpha and Nrf2/HO-1 pathways under the pretreatment of CPs in LO2 cells indicated that CPs could markedly relieve high fat-induced fatty liver injury, regulate insulin sensitivity, and reduce production of ROS.	cps	105-108	heme oxygenase 1	Homo sapiens	65-69
35537139-11	2022	Meanwhile, the increased expression of SIRT1/PPAR-alpha and Nrf2/HO-1 pathways under the pretreatment of CPs in LO2 cells indicated that CPs could markedly relieve high fat-induced fatty liver injury, regulate insulin sensitivity, and reduce production of ROS.	cps	137-140	heme oxygenase 1	Homo sapiens	65-69
35537139-11	2022	Meanwhile, the increased expression of SIRT1/PPAR-alpha and Nrf2/HO-1 pathways under the pretreatment of CPs in LO2 cells indicated that CPs could markedly relieve high fat-induced fatty liver injury, regulate insulin sensitivity, and reduce production of ROS.	Reactive Oxygen Species	256-259	heme oxygenase 1	Homo sapiens	65-69
35598199-4	2022	METHODS AND RESULTS: Proteomic analyses found that ATO can affect the signaling pathway associated with ferroptosis, including the upregulation of iron absorption (FTL, FTH1, HO-1), ferritinophagy (LC3, P62, ATG7, NCOA4) and modifier of glutathione synthesis (GCLM); downregulation of glutamine synthetase (GS) and GPX4, which was the critical inhibitor of ferroptosis.	Iron	147-151	heme oxygenase 1	Homo sapiens	175-179
35598290-0	2022	Hemin mitigates contrast-induced nephropathy by inhibiting ferroptosis via HO-1/Nrf2/GPX4 pathway.	Hemin	0-5	heme oxygenase 1	Homo sapiens	75-79
35598290-9	2022	Furthermore, hemin"s induction of GPX4 involved HO-1 and nuclear factor Nrf2.	Hemin	13-18	heme oxygenase 1	Homo sapiens	48-52
35598290-10	2022	Either HO-1 or Nrf2 inhibitor prevented hemin"s effect on GPX4 to a comparable extent, and over-expression of Nrf2 increased GPX4 expression.	Hemin	40-45	heme oxygenase 1	Homo sapiens	7-11
35603834-7	2022	Fe-R-H regulators such as lactoferrin (LF), hemoxygenase-1 (HO-1), erythropoietin (EPO) and hepcidin modulators are innate bio-replenishments that sequester iron, neutralize iron-mediated free radicals, reduce oxidative stress, and improve host defense by optimizing iron metabolism.	Iron	157-161	heme oxygenase 1	Homo sapiens	60-64
35603834-7	2022	Fe-R-H regulators such as lactoferrin (LF), hemoxygenase-1 (HO-1), erythropoietin (EPO) and hepcidin modulators are innate bio-replenishments that sequester iron, neutralize iron-mediated free radicals, reduce oxidative stress, and improve host defense by optimizing iron metabolism.	Iron	174-178	heme oxygenase 1	Homo sapiens	60-64
35603834-7	2022	Fe-R-H regulators such as lactoferrin (LF), hemoxygenase-1 (HO-1), erythropoietin (EPO) and hepcidin modulators are innate bio-replenishments that sequester iron, neutralize iron-mediated free radicals, reduce oxidative stress, and improve host defense by optimizing iron metabolism.	Iron	267-271	heme oxygenase 1	Homo sapiens	60-64
35603834-9	2022	Ferroptosis inhibitors such as ferrostatin-1, liproxstatin-1, quercetin, and melatonin could prevent mitochondrial lipid peroxidation, up-regulate antioxidant/GSH levels and abrogate iron overload-induced apoptosis through activation of Nrf2 and HO-1 signaling pathways.	Quercetin	62-71	heme oxygenase 1	Homo sapiens	246-250
35598290-12	2022	Thus, we showed hemin mitigated CIN, inhibiting oxidative stress and ferroptosis, by upregulation of GPX4 via activation of HO-1/Nrf2.	Hemin	16-21	heme oxygenase 1	Homo sapiens	124-128
35603834-9	2022	Ferroptosis inhibitors such as ferrostatin-1, liproxstatin-1, quercetin, and melatonin could prevent mitochondrial lipid peroxidation, up-regulate antioxidant/GSH levels and abrogate iron overload-induced apoptosis through activation of Nrf2 and HO-1 signaling pathways.	Melatonin	77-86	heme oxygenase 1	Homo sapiens	246-250
35472411-3	2022	There is a significant body of research investigating the effects of oxidative stress/ROS on ASM behaviour, falling into the following categories; cigarette smoke and associated compounds, air pollutants, aero-allergens, asthma and COPD relevant mediators, and the anti-oxidant Nrf2/HO-1 signalling pathway.	ros	86-89	heme oxygenase 1	Homo sapiens	283-287
35584686-7	2022	RESULTS: mRNA expression of HO-1, GCLC, HSPB1, VEGFA, PDGFA and PDGFB were significantly increased in ARPE-19 cells treated with H2O2 + hUCESC-CM compared to cells treated with H2O2 only.	Hydrogen Peroxide	129-133	heme oxygenase 1	Homo sapiens	28-32
35605918-12	2022	The mechanism underlying the effect of DPH5 in alleviating IR was related to the PI3K/AKT- and Nrf2/HO-1-mediated regulation of the GSK3beta signaling pathway, and the results were further confirmed using the specific inhibitors LY294002 and ML385.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	229-237	heme oxygenase 1	Homo sapiens	100-104
35605918-12	2022	The mechanism underlying the effect of DPH5 in alleviating IR was related to the PI3K/AKT- and Nrf2/HO-1-mediated regulation of the GSK3beta signaling pathway, and the results were further confirmed using the specific inhibitors LY294002 and ML385.	ML385	242-247	heme oxygenase 1	Homo sapiens	100-104
35620405-0	2022	11,12-Diacetyl-carnosol Protects SH-SY5Y Cells from Hydrogen Peroxide Damage through the Nrf2/HO-1 Pathway.	Hydrogen Peroxide	52-69	heme oxygenase 1	Homo sapiens	94-98
35583593-0	2022	A Pretreatment with Isoorientin Attenuates Redox Disruption, Mitochondrial Impairment, and Inflammation Caused by Chlorpyrifos in a Dopaminergic Cell Line: Involvement of the Nrf2/HO-1 Axis.	homoorientin	20-31	heme oxygenase 1	Homo sapiens	180-184
35583593-0	2022	A Pretreatment with Isoorientin Attenuates Redox Disruption, Mitochondrial Impairment, and Inflammation Caused by Chlorpyrifos in a Dopaminergic Cell Line: Involvement of the Nrf2/HO-1 Axis.	Chlorpyrifos	114-126	heme oxygenase 1	Homo sapiens	180-184
35583593-8	2022	On the other hand, ISO upregulated HO-1 activity in SH-SY5Y cells.	homoorientin	19-22	heme oxygenase 1	Homo sapiens	35-39
35583593-9	2022	Inhibition of HO-1 by zinc protoporphyrin-IX (ZnPP-IX) suppressed the cytoprotection induced by ISO in the CPF-treated cells.	zinc protoporphyrin	22-44	heme oxygenase 1	Homo sapiens	14-18
35583593-9	2022	Inhibition of HO-1 by zinc protoporphyrin-IX (ZnPP-IX) suppressed the cytoprotection induced by ISO in the CPF-treated cells.	zinc protoporphyrin	46-53	heme oxygenase 1	Homo sapiens	14-18
35583593-10	2022	Besides, silencing of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) abolished the ISO-induced HO-1 upregulation and mitochondrial benefits induced by this flavone on the CPF-challenged cells.	homoorientin	112-115	heme oxygenase 1	Homo sapiens	124-128
35583593-10	2022	Besides, silencing of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) abolished the ISO-induced HO-1 upregulation and mitochondrial benefits induced by this flavone on the CPF-challenged cells.	flavone	185-192	heme oxygenase 1	Homo sapiens	124-128
35583593-11	2022	Thus, ISO protected mitochondria of the CPF-treated cells by an Nrf2/HO-1-dependent fashion in the SH-SY5Y cells.	homoorientin	6-9	heme oxygenase 1	Homo sapiens	69-73
35620405-0	2022	11,12-Diacetyl-carnosol Protects SH-SY5Y Cells from Hydrogen Peroxide Damage through the Nrf2/HO-1 Pathway.	11,12-diacetyl-carnosol	0-23	heme oxygenase 1	Homo sapiens	94-98
35630697-2	2022	The newly designed and synthesized compounds are structurally related to nilotinib (NIL), a second-generation oral TKI, and to a series of imatinib (IM)-based TKIs, previously reported by our research group, these latter characterized by a hybrid structure between TKIs and heme oxygenase-1 (HO-1) inhibitors.	nilotinib	73-82	heme oxygenase 1	Homo sapiens	274-290
35630697-2	2022	The newly designed and synthesized compounds are structurally related to nilotinib (NIL), a second-generation oral TKI, and to a series of imatinib (IM)-based TKIs, previously reported by our research group, these latter characterized by a hybrid structure between TKIs and heme oxygenase-1 (HO-1) inhibitors.	nilotinib	73-82	heme oxygenase 1	Homo sapiens	292-296
35630697-2	2022	The newly designed and synthesized compounds are structurally related to nilotinib (NIL), a second-generation oral TKI, and to a series of imatinib (IM)-based TKIs, previously reported by our research group, these latter characterized by a hybrid structure between TKIs and heme oxygenase-1 (HO-1) inhibitors.	Imatinib Mesylate	139-147	heme oxygenase 1	Homo sapiens	274-290
35630697-2	2022	The newly designed and synthesized compounds are structurally related to nilotinib (NIL), a second-generation oral TKI, and to a series of imatinib (IM)-based TKIs, previously reported by our research group, these latter characterized by a hybrid structure between TKIs and heme oxygenase-1 (HO-1) inhibitors.	Imatinib Mesylate	139-147	heme oxygenase 1	Homo sapiens	292-296
35620405-9	2022	Conclusion: These results demonstrate that NO.20 protects SH-SY5Y cells from H2O2-induced neurotoxicity by activating the Nrf2/HO-1 pathway.	Hydrogen Peroxide	77-81	heme oxygenase 1	Homo sapiens	127-131
35569637-0	2022	Synthesis and biological evaluation of scutellarein derivatives as neuroprotective agents via activating Nrf2/HO-1 pathway.	scutellarein	39-51	heme oxygenase 1	Homo sapiens	110-114
35580917-9	2022	In addition, treatment with vinpocetine suppressed protein expression of Nrf2 and inhibited messenger RNA levels of heme oxygenase 1 and NAD(P)H dehydrogenase quinone 1 induced by cisplatin.	vinpocetine	28-39	heme oxygenase 1	Homo sapiens	116-132
35580917-9	2022	In addition, treatment with vinpocetine suppressed protein expression of Nrf2 and inhibited messenger RNA levels of heme oxygenase 1 and NAD(P)H dehydrogenase quinone 1 induced by cisplatin.	Cisplatin	180-189	heme oxygenase 1	Homo sapiens	116-132
35292342-0	2022	Preliminary studies of an imidazole-based alcohol derivative for imaging of Heme oxygenase 1.	imidazole	26-35	heme oxygenase 1	Homo sapiens	76-92
35292342-0	2022	Preliminary studies of an imidazole-based alcohol derivative for imaging of Heme oxygenase 1.	Alcohols	42-49	heme oxygenase 1	Homo sapiens	76-92
35292342-4	2022	We report herein the synthesis and characterization of a 11C-labeled imidazole-based alcohol derivative ((11C)QC-33) for imaging of HO-1 in the brain.	Carbon-11	57-60	heme oxygenase 1	Homo sapiens	132-136
35292342-4	2022	We report herein the synthesis and characterization of a 11C-labeled imidazole-based alcohol derivative ((11C)QC-33) for imaging of HO-1 in the brain.	imidazole	69-78	heme oxygenase 1	Homo sapiens	132-136
35292342-4	2022	We report herein the synthesis and characterization of a 11C-labeled imidazole-based alcohol derivative ((11C)QC-33) for imaging of HO-1 in the brain.	Alcohols	85-92	heme oxygenase 1	Homo sapiens	132-136
35292342-4	2022	We report herein the synthesis and characterization of a 11C-labeled imidazole-based alcohol derivative ((11C)QC-33) for imaging of HO-1 in the brain.	Carbon-11	106-109	heme oxygenase 1	Homo sapiens	132-136
35292342-7	2022	In vitro autoradiography studies indicated specific binding of (11C)QC-33 in the HO-1 rich regions, showing 75%, 75%, and 69% radioactivity binding reductions in cerebellum, brain stem, and midbrain, respectively.	Carbon-11	64-67	heme oxygenase 1	Homo sapiens	81-85
35476430-3	2022	We found that the herbicidal-active imazethapyr enantiomer ((R)-IM) stimulated heme oxygenase-1 activity, triggered the release of the catalytic product Fe2+, increased reactive oxygen species production, decreased the DIMBOA content, and increased the DIMBOA-Fe content.	imazethapyr enantiomer	36-58	heme oxygenase 1	Homo sapiens	79-95
35551540-1	2022	INTRODUCTION: Heme-oxygenase 1 (HMOX1) is a critical stress response gene that catalyzes the multistep oxidation of heme.	Heme	116-120	heme oxygenase 1	Homo sapiens	14-30
35551540-1	2022	INTRODUCTION: Heme-oxygenase 1 (HMOX1) is a critical stress response gene that catalyzes the multistep oxidation of heme.	Heme	116-120	heme oxygenase 1	Homo sapiens	32-37
35629355-7	2022	ROS interrupted the cellular oxidative balance by activating NOX and inhibiting HIF-1alpha and HO-1 expression.	Reactive Oxygen Species	0-3	heme oxygenase 1	Homo sapiens	95-99
35601897-6	2022	The in vivo study showed that in situ injection of HT/HGA hydrogel significantly reduced malondialdehyde (MDA) production and increased glutathione (GSH) expression in lesion area after treatment for 3 or 21 days, which might be associated with the activation of Nrf2/HO-1 pathway.	Glutathione	136-147	heme oxygenase 1	Homo sapiens	268-272
35592532-0	2022	Ferulic Acid Protects Human Lens Epithelial Cells against Ionizing Radiation-Induced Oxidative Damage by Activating Nrf2/HO-1 Signal Pathway.	ferulic acid	0-12	heme oxygenase 1	Homo sapiens	121-125
35629355-8	2022	Pretreatment with N-acetylcysteine (NAC) reduced Apl-1-induced mitochondria-dependent apoptosis and preserved the expression of NOX, HO-1, and HIF-1a.	Acetylcysteine	18-34	heme oxygenase 1	Homo sapiens	133-137
35629355-8	2022	Pretreatment with N-acetylcysteine (NAC) reduced Apl-1-induced mitochondria-dependent apoptosis and preserved the expression of NOX, HO-1, and HIF-1a.	Acetylcysteine	36-39	heme oxygenase 1	Homo sapiens	133-137
35395341-7	2022	We established that dithianon (0.01-1 mumol.L-1) and captan (0.1, 1 mumol.L-1) induced mRNA expression of NQO1 and HMOX1 antioxidant enzymes.	dithianone	20-29	heme oxygenase 1	Homo sapiens	115-120
35427872-10	2022	In contrast, honey"s anti-inflammatory actions and flavonoids induce anti-inflammatory and antioxidant pathways by inducing NRF2 target genes, including HO-1 and PRDX1.	Flavonoids	51-61	heme oxygenase 1	Homo sapiens	153-157
35565605-8	2022	Additionally, dietary EA improved the antioxidant enzyme activity and mRNA levels of Nrf2/HO-1 in the ileum of heat-stressed broilers.	Ellagic Acid	22-24	heme oxygenase 1	Homo sapiens	90-94
35305818-8	2022	As a potential mechanism, the expression of intracellular reactive oxygen species (ROS) and its related proteins, including p-ERK, NRF2, p-p38, HO-1, and gammaH2AX, was affected in EOC cells.	Reactive Oxygen Species	58-81	heme oxygenase 1	Homo sapiens	144-148
35015114-3	2022	RESULTS: In experimental models, curcumin showed its pleiotropic effects in retinal diseases like diabetic retinopathy by increasing anti-oxidant enzymes, upregulating HO-1, nrf2 and reducing or inhibiting inflammatory mediators, growth factors and by inhibiting proliferation and migration of retinal endothelial cells in a dose-dependent manner in HRPC, HREC and ARPE-19 cells.	Curcumin	33-41	heme oxygenase 1	Homo sapiens	168-172
35015114-4	2022	In age-related macular degeneration, curcumin acts by reducing ROS and inhibiting apoptosis inducing proteins and cellular inflammatory genes and upregulating HO-1, thioredoxin and NQO1.	Curcumin	37-45	heme oxygenase 1	Homo sapiens	159-163
35305818-8	2022	As a potential mechanism, the expression of intracellular reactive oxygen species (ROS) and its related proteins, including p-ERK, NRF2, p-p38, HO-1, and gammaH2AX, was affected in EOC cells.	Reactive Oxygen Species	83-86	heme oxygenase 1	Homo sapiens	144-148
35428017-2	2022	The aim of this study was to investigate the role of heme in HO-1 and HO-2 induced colorectal carcinogenesis and the clinicopathological significance of their expressions in patients with colorectal carcinoma (CRC).	Heme	53-57	heme oxygenase 1	Homo sapiens	61-65
35399331-0	2022	Carboxymethylated pachyman induces ferroptosis in ovarian cancer by suppressing NRF1/HO-1 signaling.	pachyman	18-26	heme oxygenase 1	Homo sapiens	85-89
35428017-7	2022	HO-1 expression in SW480 was increased with all hemin concentrations and HO-2 expression was downregulated at the highest hemin concentration.	Hemin	122-127	heme oxygenase 1	Homo sapiens	0-4
35428017-3	2022	METHODS: HO-1 and HO-2 expression alterations in normal colonic epithelial (FHC) and colon cancer cells (SW480) were explored following treatment with 0 microM, 25 microM, 100 microM and 250 microM concentrations of hemin, using qPCR.	Hemin	216-221	heme oxygenase 1	Homo sapiens	9-13
35428017-12	2022	CONCLUSION: HO-1 and HO-2 expression is respectively induced and repressed by exogenous hemin in normal colon and colon cancer cells.	Hemin	88-93	heme oxygenase 1	Homo sapiens	12-16
35428017-6	2022	RESULTS: Low concentrations of hemin caused upregulation and high concentration caused downregulation of HO-1 expression, whereas HO-2 expression was significantly downregulated with all hemin concentrations in FHC.	Hemin	31-36	heme oxygenase 1	Homo sapiens	105-109
35428017-7	2022	HO-1 expression in SW480 was increased with all hemin concentrations and HO-2 expression was downregulated at the highest hemin concentration.	Hemin	48-53	heme oxygenase 1	Homo sapiens	0-4
35306372-3	2022	Photochemical oxidation of isoprene leads to the formation of hydroperoxides, environmental oxidants that lead to inflammatory (IL-8) and adaptive (HMOX1) gene expression in human airway epithelial cells (HAEC).	isoprene	27-35	heme oxygenase 1	Homo sapiens	148-153
35306372-3	2022	Photochemical oxidation of isoprene leads to the formation of hydroperoxides, environmental oxidants that lead to inflammatory (IL-8) and adaptive (HMOX1) gene expression in human airway epithelial cells (HAEC).	Hydrogen Peroxide	62-76	heme oxygenase 1	Homo sapiens	148-153
35565370-3	2022	We quantified the heme-degrading enzyme, heme oxygenase-1 (HO-1, encoded by Hmox1) in normal peritoneum, endometriotic lesions and endometriosis-associated ovarian cancer (EAOC) of clear cell type (OCCC).	Heme	18-22	heme oxygenase 1	Homo sapiens	41-57
35565370-3	2022	We quantified the heme-degrading enzyme, heme oxygenase-1 (HO-1, encoded by Hmox1) in normal peritoneum, endometriotic lesions and endometriosis-associated ovarian cancer (EAOC) of clear cell type (OCCC).	Heme	18-22	heme oxygenase 1	Homo sapiens	59-63
35565370-3	2022	We quantified the heme-degrading enzyme, heme oxygenase-1 (HO-1, encoded by Hmox1) in normal peritoneum, endometriotic lesions and endometriosis-associated ovarian cancer (EAOC) of clear cell type (OCCC).	Heme	18-22	heme oxygenase 1	Homo sapiens	76-81
35572500-10	2022	Further analysis showed that the Nrf2 inhibitor ML385 weakened TIPE2-induced activation of the Nrf2/HO-1 pathway, as well as TIPE2-induced suppression in M1 polarization of macrophage and inflammatory cytokines secretion.	ML385	48-53	heme oxygenase 1	Homo sapiens	100-104
35490795-0	2022	Induction of ferroptosis by carnosic acid-mediated inactivation of Nrf2/HO-1 potentiates cisplatin responsiveness in OSCC cells.	salvin	28-41	heme oxygenase 1	Homo sapiens	72-76
35490795-0	2022	Induction of ferroptosis by carnosic acid-mediated inactivation of Nrf2/HO-1 potentiates cisplatin responsiveness in OSCC cells.	Cisplatin	89-98	heme oxygenase 1	Homo sapiens	72-76
35490795-9	2022	Furthermore, compared with parental cells, stronger activation of the Nrf2/HO-1/xCT signaling was observed in cisplatin-resistant cells, which was inhibited by carnosic acid.	Cisplatin	110-119	heme oxygenase 1	Homo sapiens	75-79
35490795-9	2022	Furthermore, compared with parental cells, stronger activation of the Nrf2/HO-1/xCT signaling was observed in cisplatin-resistant cells, which was inhibited by carnosic acid.	salvin	160-173	heme oxygenase 1	Homo sapiens	75-79
35490795-11	2022	Together, the current findings highlight that carnosic acid may re-sensitize cisplatin-resistant cells to cisplatin by inducing ferroptosis, which involves the inactivation of Nrf2/HO-1/xCT pathway.	salvin	46-59	heme oxygenase 1	Homo sapiens	181-185
35490795-11	2022	Together, the current findings highlight that carnosic acid may re-sensitize cisplatin-resistant cells to cisplatin by inducing ferroptosis, which involves the inactivation of Nrf2/HO-1/xCT pathway.	Cisplatin	77-86	heme oxygenase 1	Homo sapiens	181-185
35490795-11	2022	Together, the current findings highlight that carnosic acid may re-sensitize cisplatin-resistant cells to cisplatin by inducing ferroptosis, which involves the inactivation of Nrf2/HO-1/xCT pathway.	Cisplatin	106-115	heme oxygenase 1	Homo sapiens	181-185
35426252-8	2022	Mechanically, EGCG upregulated nuclear factor erythroid 2-related factor 2 (Nrf2), oxygenase-1 (HO-1), and NADPH quinone oxidoreductase1 (NQO1).	epigallocatechin gallate	14-18	heme oxygenase 1	Homo sapiens	96-100
35420033-8	2022	Sesamin significantly increased TNF-alpha/IL-4-induced superoxide dismutase (SOD), catalase (CAT), heme oxygenase 1 (HO-1), and nuclear factor erythroid 2 related factor 2 (Nrf2), and decreased malondialdehyde.	sesamin	0-7	heme oxygenase 1	Homo sapiens	99-115
35420033-8	2022	Sesamin significantly increased TNF-alpha/IL-4-induced superoxide dismutase (SOD), catalase (CAT), heme oxygenase 1 (HO-1), and nuclear factor erythroid 2 related factor 2 (Nrf2), and decreased malondialdehyde.	sesamin	0-7	heme oxygenase 1	Homo sapiens	117-121
35624663-7	2022	Furthermore, empagliflozin significantly upregulated the expressions of antioxidant enzymes superoxide dismutase (SOD) and HO-1.	empagliflozin	13-26	heme oxygenase 1	Homo sapiens	123-127
35631320-0	2022	Activation of Nrf2/HO-1 Antioxidant Pathway by Heme Attenuates Calcification of Human Lens Epithelial Cells.	Heme	47-51	heme oxygenase 1	Homo sapiens	19-23
35631320-8	2022	We used heme to activate Nrf2, which strongly upregulated the expression of Nrf2 and heme oxygenase-1 (HO-1).	Heme	8-12	heme oxygenase 1	Homo sapiens	85-101
35631320-8	2022	We used heme to activate Nrf2, which strongly upregulated the expression of Nrf2 and heme oxygenase-1 (HO-1).	Heme	8-12	heme oxygenase 1	Homo sapiens	103-107
35631320-11	2022	Anti-calcification effect of heme was lost when the transcriptional activity of Nrf2 or the enzyme activity of HO-1 was blocked with pharmacological inhibitors.	Heme	29-33	heme oxygenase 1	Homo sapiens	111-115
35631320-12	2022	Among products of HO-1 catalyzed heme degradation iron mimicked the anti-calcification effect of heme.	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
35631320-12	2022	Among products of HO-1 catalyzed heme degradation iron mimicked the anti-calcification effect of heme.	Iron	50-54	heme oxygenase 1	Homo sapiens	18-22
35631320-12	2022	Among products of HO-1 catalyzed heme degradation iron mimicked the anti-calcification effect of heme.	Heme	97-101	heme oxygenase 1	Homo sapiens	18-22
35631320-13	2022	We concluded that heme-induced upregulation of the Nrf2/HO-1 system inhibits HuLECs calcification through the liberation of heme iron.	Heme	18-22	heme oxygenase 1	Homo sapiens	56-60
35631320-13	2022	We concluded that heme-induced upregulation of the Nrf2/HO-1 system inhibits HuLECs calcification through the liberation of heme iron.	Heme	124-128	heme oxygenase 1	Homo sapiens	56-60
35631320-13	2022	We concluded that heme-induced upregulation of the Nrf2/HO-1 system inhibits HuLECs calcification through the liberation of heme iron.	Iron	129-133	heme oxygenase 1	Homo sapiens	56-60
35422193-9	2022	Exo improved MI induced by SAP through activating Akt/Nrf2/HO-1 signaling pathway.	BENSULIDE	27-30	heme oxygenase 1	Homo sapiens	59-63
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Heme	71-75	heme oxygenase 1	Homo sapiens	0-16
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Heme	71-75	heme oxygenase 1	Homo sapiens	18-22
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Carbon Monoxide	108-123	heme oxygenase 1	Homo sapiens	0-16
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Carbon Monoxide	108-123	heme oxygenase 1	Homo sapiens	18-22
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Carbon Monoxide	125-127	heme oxygenase 1	Homo sapiens	0-16
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Carbon Monoxide	125-127	heme oxygenase 1	Homo sapiens	18-22
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Biliverdine	130-140	heme oxygenase 1	Homo sapiens	0-16
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Biliverdine	130-140	heme oxygenase 1	Homo sapiens	18-22
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Biliverdine	142-144	heme oxygenase 1	Homo sapiens	0-16
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Biliverdine	142-144	heme oxygenase 1	Homo sapiens	18-22
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Iron	151-155	heme oxygenase 1	Homo sapiens	0-16
35624725-1	2022	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron.	Iron	151-155	heme oxygenase 1	Homo sapiens	18-22
35624725-3	2022	However, iron constitutes an important product of HO-1 activity involved in the regulation of several cellular biological processes.	Iron	9-13	heme oxygenase 1	Homo sapiens	50-54
35480872-0	2022	Biliverdin/Bilirubin Redox Pair Protects Lens Epithelial Cells against Oxidative Stress in Age-Related Cataract by Regulating NF-kappaB/iNOS and Nrf2/HO-1 Pathways.	Biliverdine	0-10	heme oxygenase 1	Homo sapiens	150-154
35457199-6	2022	First, we observed an increase of HO-1 expression in Caco-2 cells treated with K-8-K and S-10-S, following the activation of the Keap1/Nrf2 pathway.	k-8-k	79-84	heme oxygenase 1	Homo sapiens	34-38
35457199-6	2022	First, we observed an increase of HO-1 expression in Caco-2 cells treated with K-8-K and S-10-S, following the activation of the Keap1/Nrf2 pathway.	S 10	89-95	heme oxygenase 1	Homo sapiens	34-38
35453467-0	2022	HO-1 Upregulation by Kaempferol via ROS-Dependent Nrf2-ARE Cascade Attenuates Lipopolysaccharide-Mediated Intercellular Cell Adhesion Molecule-1 Expression in Human Pulmonary Alveolar Epithelial Cells.	kaempferol	21-31	heme oxygenase 1	Homo sapiens	0-4
35453467-0	2022	HO-1 Upregulation by Kaempferol via ROS-Dependent Nrf2-ARE Cascade Attenuates Lipopolysaccharide-Mediated Intercellular Cell Adhesion Molecule-1 Expression in Human Pulmonary Alveolar Epithelial Cells.	Reactive Oxygen Species	36-39	heme oxygenase 1	Homo sapiens	0-4
35453467-2	2022	Heme oxygenase-1 (HO-1) is a key antioxidant enzyme that could be induced by kaempferol (KPR) and exerts anti-inflammatory effects.	kaempferol	77-87	heme oxygenase 1	Homo sapiens	0-16
35453467-2	2022	Heme oxygenase-1 (HO-1) is a key antioxidant enzyme that could be induced by kaempferol (KPR) and exerts anti-inflammatory effects.	kaempferol	77-87	heme oxygenase 1	Homo sapiens	18-22
35453467-2	2022	Heme oxygenase-1 (HO-1) is a key antioxidant enzyme that could be induced by kaempferol (KPR) and exerts anti-inflammatory effects.	kaempferol	89-92	heme oxygenase 1	Homo sapiens	0-16
35453467-2	2022	Heme oxygenase-1 (HO-1) is a key antioxidant enzyme that could be induced by kaempferol (KPR) and exerts anti-inflammatory effects.	kaempferol	89-92	heme oxygenase 1	Homo sapiens	18-22
35496911-0	2022	Heme Oxygenase-1 Protects Hair Cells From Gentamicin-Induced Death.	Gentamicins	42-52	heme oxygenase 1	Homo sapiens	0-16
35496911-4	2022	We found that during gentamicin-induced death in HCs, Heme oxygenase-1 (HO-1) had a high fold change in the HCs of the cochlea.	Gentamicins	21-31	heme oxygenase 1	Homo sapiens	54-70
35496911-4	2022	We found that during gentamicin-induced death in HCs, Heme oxygenase-1 (HO-1) had a high fold change in the HCs of the cochlea.	Gentamicins	21-31	heme oxygenase 1	Homo sapiens	72-76
35496911-5	2022	Moreover, the use of CoPPIX to induce HO-1 inhibited gentamicin-induced HC death, while HO-1 inhibitors ZnPPIX after CoPPIX reversed this process.	Gentamicins	53-63	heme oxygenase 1	Homo sapiens	38-42
35496911-5	2022	Moreover, the use of CoPPIX to induce HO-1 inhibited gentamicin-induced HC death, while HO-1 inhibitors ZnPPIX after CoPPIX reversed this process.	zinc protoporphyrin	104-110	heme oxygenase 1	Homo sapiens	38-42
35496911-5	2022	Moreover, the use of CoPPIX to induce HO-1 inhibited gentamicin-induced HC death, while HO-1 inhibitors ZnPPIX after CoPPIX reversed this process.	zinc protoporphyrin	104-110	heme oxygenase 1	Homo sapiens	88-92
35496911-6	2022	Furthermore, the inhibitors of NF-E2-related factor-2 (Nrf2) reduced the expression of HO-1 and inhibited the protective effect of HO-1 after gentamicin, thus suggesting that the Nrf2/HO-1 axis might regulate gentamicin-associated ototoxicity.	Gentamicins	142-152	heme oxygenase 1	Homo sapiens	87-91
35496911-6	2022	Furthermore, the inhibitors of NF-E2-related factor-2 (Nrf2) reduced the expression of HO-1 and inhibited the protective effect of HO-1 after gentamicin, thus suggesting that the Nrf2/HO-1 axis might regulate gentamicin-associated ototoxicity.	Gentamicins	142-152	heme oxygenase 1	Homo sapiens	131-135
35496911-6	2022	Furthermore, the inhibitors of NF-E2-related factor-2 (Nrf2) reduced the expression of HO-1 and inhibited the protective effect of HO-1 after gentamicin, thus suggesting that the Nrf2/HO-1 axis might regulate gentamicin-associated ototoxicity.	Gentamicins	142-152	heme oxygenase 1	Homo sapiens	184-188
35496911-6	2022	Furthermore, the inhibitors of NF-E2-related factor-2 (Nrf2) reduced the expression of HO-1 and inhibited the protective effect of HO-1 after gentamicin, thus suggesting that the Nrf2/HO-1 axis might regulate gentamicin-associated ototoxicity.	Gentamicins	209-219	heme oxygenase 1	Homo sapiens	87-91
35496911-6	2022	Furthermore, the inhibitors of NF-E2-related factor-2 (Nrf2) reduced the expression of HO-1 and inhibited the protective effect of HO-1 after gentamicin, thus suggesting that the Nrf2/HO-1 axis might regulate gentamicin-associated ototoxicity.	Gentamicins	209-219	heme oxygenase 1	Homo sapiens	131-135
35496911-6	2022	Furthermore, the inhibitors of NF-E2-related factor-2 (Nrf2) reduced the expression of HO-1 and inhibited the protective effect of HO-1 after gentamicin, thus suggesting that the Nrf2/HO-1 axis might regulate gentamicin-associated ototoxicity.	Gentamicins	209-219	heme oxygenase 1	Homo sapiens	184-188
35496911-8	2022	In summary, these findings indicated that HO-1 protects HCs from gentamicin by up-regulating its expression in HCs and interacting with Nrf2 to inhibit reactive oxygen species (ROS).	Gentamicins	65-75	heme oxygenase 1	Homo sapiens	42-46
35496911-8	2022	In summary, these findings indicated that HO-1 protects HCs from gentamicin by up-regulating its expression in HCs and interacting with Nrf2 to inhibit reactive oxygen species (ROS).	Reactive Oxygen Species	152-175	heme oxygenase 1	Homo sapiens	42-46
35496911-8	2022	In summary, these findings indicated that HO-1 protects HCs from gentamicin by up-regulating its expression in HCs and interacting with Nrf2 to inhibit reactive oxygen species (ROS).	Reactive Oxygen Species	177-180	heme oxygenase 1	Homo sapiens	42-46
35453452-0	2022	TLR4 Signaling and Heme Oxygenase-1/Carbon Monoxide Pathway Crosstalk Induces Resiliency of Myeloma Plasma Cells to Bortezomib Treatment.	Bortezomib	116-126	heme oxygenase 1	Homo sapiens	19-35
35453452-2	2022	Since our group previously demonstrated that heme oxygenase-1 (HO-1) and Toll-like receptor 4 (TLR4) are two signaling pathways protecting MM cells from the proteasome inhibitor bortezomib (BTZ), we here evaluated their cross-regulation by a pharmacological approach.	Bortezomib	178-188	heme oxygenase 1	Homo sapiens	45-61
35453452-2	2022	Since our group previously demonstrated that heme oxygenase-1 (HO-1) and Toll-like receptor 4 (TLR4) are two signaling pathways protecting MM cells from the proteasome inhibitor bortezomib (BTZ), we here evaluated their cross-regulation by a pharmacological approach.	Bortezomib	178-188	heme oxygenase 1	Homo sapiens	63-67
35453452-2	2022	Since our group previously demonstrated that heme oxygenase-1 (HO-1) and Toll-like receptor 4 (TLR4) are two signaling pathways protecting MM cells from the proteasome inhibitor bortezomib (BTZ), we here evaluated their cross-regulation by a pharmacological approach.	Bortezomib	190-193	heme oxygenase 1	Homo sapiens	45-61
35453452-2	2022	Since our group previously demonstrated that heme oxygenase-1 (HO-1) and Toll-like receptor 4 (TLR4) are two signaling pathways protecting MM cells from the proteasome inhibitor bortezomib (BTZ), we here evaluated their cross-regulation by a pharmacological approach.	Bortezomib	190-193	heme oxygenase 1	Homo sapiens	63-67
35453452-3	2022	We found that cell toxicity and mitochondrial depolarization by BTZ were increased upon inhibition of HO-1 and TLR4 by using tin protoporphyrin IX (SnPP) and TAK-242, respectively.	Bortezomib	64-67	heme oxygenase 1	Homo sapiens	102-106
35453452-3	2022	We found that cell toxicity and mitochondrial depolarization by BTZ were increased upon inhibition of HO-1 and TLR4 by using tin protoporphyrin IX (SnPP) and TAK-242, respectively.	tin protoporphyrin IX	125-146	heme oxygenase 1	Homo sapiens	102-106
35453452-3	2022	We found that cell toxicity and mitochondrial depolarization by BTZ were increased upon inhibition of HO-1 and TLR4 by using tin protoporphyrin IX (SnPP) and TAK-242, respectively.	S-Nitroso-N-propionyl-D,L-penicillamine	148-152	heme oxygenase 1	Homo sapiens	102-106
35453452-3	2022	We found that cell toxicity and mitochondrial depolarization by BTZ were increased upon inhibition of HO-1 and TLR4 by using tin protoporphyrin IX (SnPP) and TAK-242, respectively.	ethyl 6-(N-(2-chloro-4-fluorophenyl)sulfamoyl)cyclohex-1-ene-1-carboxylate	158-165	heme oxygenase 1	Homo sapiens	102-106
35453452-4	2022	Furthermore, the combination of TAK-242 and BTZ activated mitophagy and decreased the unfolded protein response (UPR) survival pathway in association with a downregulation in HO-1 expression.	ethyl 6-(N-(2-chloro-4-fluorophenyl)sulfamoyl)cyclohex-1-ene-1-carboxylate	32-39	heme oxygenase 1	Homo sapiens	175-179
35453452-4	2022	Furthermore, the combination of TAK-242 and BTZ activated mitophagy and decreased the unfolded protein response (UPR) survival pathway in association with a downregulation in HO-1 expression.	Bortezomib	44-47	heme oxygenase 1	Homo sapiens	175-179
35453452-6	2022	Interestingly, treatment of cells with either hemin, an HO-1 inducer, or supplementation with carbon monoxide (CO), a by-product of HO-1 enzymatic activity, increased TLR4 expression.	Hemin	46-51	heme oxygenase 1	Homo sapiens	56-60
35453452-6	2022	Interestingly, treatment of cells with either hemin, an HO-1 inducer, or supplementation with carbon monoxide (CO), a by-product of HO-1 enzymatic activity, increased TLR4 expression.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	132-136
35453452-6	2022	Interestingly, treatment of cells with either hemin, an HO-1 inducer, or supplementation with carbon monoxide (CO), a by-product of HO-1 enzymatic activity, increased TLR4 expression.	Carbon Monoxide	111-113	heme oxygenase 1	Homo sapiens	132-136
35453452-7	2022	In conclusion, we showed that treatment of MM cells with BTZ triggers the TLR4/HO-1/CO axis, serving as a stress-responsive signal that leads to increased cell survival while protecting mitochondria against BTZ and ultimately promoting drug resistance.	Bortezomib	57-60	heme oxygenase 1	Homo sapiens	79-83
35480872-0	2022	Biliverdin/Bilirubin Redox Pair Protects Lens Epithelial Cells against Oxidative Stress in Age-Related Cataract by Regulating NF-kappaB/iNOS and Nrf2/HO-1 Pathways.	Bilirubin	11-20	heme oxygenase 1	Homo sapiens	150-154
35453452-7	2022	In conclusion, we showed that treatment of MM cells with BTZ triggers the TLR4/HO-1/CO axis, serving as a stress-responsive signal that leads to increased cell survival while protecting mitochondria against BTZ and ultimately promoting drug resistance.	Bortezomib	207-210	heme oxygenase 1	Homo sapiens	79-83
35480872-12	2022	These findings implicated that BV/BR redox pair protects LECs against H2O2-induced apoptosis by regulating NF-kappaB/iNOS and Nrf2/HO-1 pathways.	Hydrogen Peroxide	70-74	heme oxygenase 1	Homo sapiens	131-135
35396773-6	2022	We screened for a novel chlorambucil-polyamide conjugate (Chb) to target PRCC-TFE3 dependent transcription, and identified Chb16 as a PRCC-TFE3-dependent transcriptional inhibitor of HMOX1 expression.	Chlorambucil	24-36	heme oxygenase 1	Homo sapiens	183-188
35396773-6	2022	We screened for a novel chlorambucil-polyamide conjugate (Chb) to target PRCC-TFE3 dependent transcription, and identified Chb16 as a PRCC-TFE3-dependent transcriptional inhibitor of HMOX1 expression.	Nylons	37-46	heme oxygenase 1	Homo sapiens	183-188
35393708-0	2022	Heme oxygenase-1 induction by gallic acid-g-chitosan is an important event in modulating adipocyte differentiation.	Gallic Acid	30-41	heme oxygenase 1	Homo sapiens	0-16
35393708-4	2022	This study focused on investigating the probable anti-adipogenic effects of gallic acid-g-chitosan (GAC) and plain chitosan (PC) through regulating the heme oxygenase-1 (HO-1)/Nrf2 pathway on mesenchymal stem cells.	Gallic Acid	76-87	heme oxygenase 1	Homo sapiens	152-168
35393708-4	2022	This study focused on investigating the probable anti-adipogenic effects of gallic acid-g-chitosan (GAC) and plain chitosan (PC) through regulating the heme oxygenase-1 (HO-1)/Nrf2 pathway on mesenchymal stem cells.	Gallic Acid	76-87	heme oxygenase 1	Homo sapiens	170-174
35393708-4	2022	This study focused on investigating the probable anti-adipogenic effects of gallic acid-g-chitosan (GAC) and plain chitosan (PC) through regulating the heme oxygenase-1 (HO-1)/Nrf2 pathway on mesenchymal stem cells.	g-chitosan	88-98	heme oxygenase 1	Homo sapiens	152-168
35393708-4	2022	This study focused on investigating the probable anti-adipogenic effects of gallic acid-g-chitosan (GAC) and plain chitosan (PC) through regulating the heme oxygenase-1 (HO-1)/Nrf2 pathway on mesenchymal stem cells.	g-chitosan	88-98	heme oxygenase 1	Homo sapiens	170-174
35393708-4	2022	This study focused on investigating the probable anti-adipogenic effects of gallic acid-g-chitosan (GAC) and plain chitosan (PC) through regulating the heme oxygenase-1 (HO-1)/Nrf2 pathway on mesenchymal stem cells.	gallic acid-g-chitosan	100-103	heme oxygenase 1	Homo sapiens	152-168
35393708-4	2022	This study focused on investigating the probable anti-adipogenic effects of gallic acid-g-chitosan (GAC) and plain chitosan (PC) through regulating the heme oxygenase-1 (HO-1)/Nrf2 pathway on mesenchymal stem cells.	gallic acid-g-chitosan	100-103	heme oxygenase 1	Homo sapiens	170-174
35393708-7	2022	On the contrary, zinc protoporphyrin IX (ZnPP), a HO-1 inhibitor reversed these effects of GAC on adipogenesis.	zinc protoporphyrin	17-39	heme oxygenase 1	Homo sapiens	50-54
35393708-7	2022	On the contrary, zinc protoporphyrin IX (ZnPP), a HO-1 inhibitor reversed these effects of GAC on adipogenesis.	zinc protoporphyrin	41-45	heme oxygenase 1	Homo sapiens	50-54
35393708-8	2022	Taken all together, this study revealed that grafting GA onto the chitosan improved potential anti-adipogenic activity by induction of the HO-1/Nrf2 pathway on mesenchymal stem cells (MSCs).	Gallium	54-56	heme oxygenase 1	Homo sapiens	139-143
35464033-4	2022	Additionally, EBCs and NEBCs from G. rubra displayed anti-inflammatory functions via inhibiting the production of nitric oxide (NO), reactive oxygen species (ROS), and proinflammatory cytokines in activated macrophages and regulating the expression levels of cyclooxygenase-2 (COX-2), inducible nitric oxide synthase (iNOS), NADPH-quinone oxidoreductase-1 (NQO-1), and heme oxygenase 1 (HO-1).	ebcs	14-18	heme oxygenase 1	Homo sapiens	369-385
35432723-10	2022	sip62 interference results showed that GDN cause the less expression of HO-1 and Keap1 and also fail to inhibit cytokines after sip62 interference.	sip62	0-5	heme oxygenase 1	Homo sapiens	72-76
35464033-4	2022	Additionally, EBCs and NEBCs from G. rubra displayed anti-inflammatory functions via inhibiting the production of nitric oxide (NO), reactive oxygen species (ROS), and proinflammatory cytokines in activated macrophages and regulating the expression levels of cyclooxygenase-2 (COX-2), inducible nitric oxide synthase (iNOS), NADPH-quinone oxidoreductase-1 (NQO-1), and heme oxygenase 1 (HO-1).	ebcs	14-18	heme oxygenase 1	Homo sapiens	387-391
35453402-6	2022	Transient knockdown or inhibitor-based suppression of HO-1 enhances vulnerability to the TKI, quizartinib, in both TKI-resistant and sensitive primary AML and cell line models.	quizartinib	94-105	heme oxygenase 1	Homo sapiens	54-58
35453402-7	2022	NRF2 suppression (genetically or pharmacologically using brusatol) results in decreased HO-1, suggesting that TKI-resistance is dependent on an active NRF2-driven pathway.	brusatol	57-65	heme oxygenase 1	Homo sapiens	88-92
35422894-0	2022	Choline Protects the Heart from Doxorubicin-Induced Cardiotoxicity through Vagal Activation and Nrf2/HO-1 Pathway.	Choline	0-7	heme oxygenase 1	Homo sapiens	101-105
35422894-0	2022	Choline Protects the Heart from Doxorubicin-Induced Cardiotoxicity through Vagal Activation and Nrf2/HO-1 Pathway.	Doxorubicin	32-43	heme oxygenase 1	Homo sapiens	101-105
35422894-5	2022	Levels of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme-oxygenase-1 (HO-1), which are antioxidant markers, were lowered by DOX and upregulated by choline.	Doxorubicin	137-140	heme oxygenase 1	Homo sapiens	65-81
35422894-5	2022	Levels of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme-oxygenase-1 (HO-1), which are antioxidant markers, were lowered by DOX and upregulated by choline.	Doxorubicin	137-140	heme oxygenase 1	Homo sapiens	83-87
35422894-5	2022	Levels of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme-oxygenase-1 (HO-1), which are antioxidant markers, were lowered by DOX and upregulated by choline.	Choline	160-167	heme oxygenase 1	Homo sapiens	65-81
35422894-5	2022	Levels of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme-oxygenase-1 (HO-1), which are antioxidant markers, were lowered by DOX and upregulated by choline.	Choline	160-167	heme oxygenase 1	Homo sapiens	83-87
35218740-10	2022	Taken together, the present study indicates that CORM-2-induced Nrf2/HO-1 alleviates IL-6/Jak2/Stat3-mediated inflammatory responses to Ang II by inhibiting NADPH oxidase- and mitochondria-derived ROS, suggesting that CORM-2 is a promising pharmacologic candidate to reverse the pathological changes involved in the inflammation of vessel wall for the prevention and treatment of AAA.	ros	197-200	heme oxygenase 1	Homo sapiens	69-73
35408731-6	2022	It could reduce UV-induced intracellular ROS generation and initiate the antioxidant defense system by activating the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway in human skin fibroblasts.	Reactive Oxygen Species	41-44	heme oxygenase 1	Homo sapiens	169-185
35408731-6	2022	It could reduce UV-induced intracellular ROS generation and initiate the antioxidant defense system by activating the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway in human skin fibroblasts.	Reactive Oxygen Species	41-44	heme oxygenase 1	Homo sapiens	187-191
35366876-11	2022	PRM verified that the apoptosis-related proteins HMOX1 and GCLM were up-regulated and IL1B was down-regulated in BCPAP cells treated with parthenolide.	parthenolide	138-150	heme oxygenase 1	Homo sapiens	49-54
35379891-5	2022	The network analyses led to the construction of the respiratory system-related biological network associated with formaldehyde exposure, and six upregulated hub genes (AREG, CXCL2, HMOX1, PLAUR, PTGS2, and TIMP1) were identified.	Formaldehyde	114-126	heme oxygenase 1	Homo sapiens	181-186
35092472-0	2022	Astragaloside IV suppresses migration and invasion of TGF-beta1-induced human hepatoma HuH-7 cells by regulating Nrf2/HO-1 and TGF-beta1/Smad3 pathways.	astragaloside	0-13	heme oxygenase 1	Homo sapiens	118-122
35350102-10	2022	Furthermore, spermine enhanced Nrf2 nuclear translocation, thereby increasing heme oxygenase-1 and NADPH quinone oxidoreductase-1 expression, which subsequently reduced ROS production.	Spermine	13-21	heme oxygenase 1	Homo sapiens	78-94
35361044-0	2022	Curcumin analog, GO-Y078, induces HO-1 transactivation-mediated apoptotic cell death of oral cancer cells by triggering MAPK pathways and AP-1 DNA-binding activity.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	34-38
35361044-0	2022	Curcumin analog, GO-Y078, induces HO-1 transactivation-mediated apoptotic cell death of oral cancer cells by triggering MAPK pathways and AP-1 DNA-binding activity.	GO-Y078	17-24	heme oxygenase 1	Homo sapiens	34-38
35361044-5	2022	GO-Y078 transcriptionally induced upregulation of the HO-1 gene by increasing the AP-1 DNA-binding activity, which was initiated by activation of the p38 /JNK1/2 pathways.	GO-Y078	0-7	heme oxygenase 1	Homo sapiens	54-58
35531734-12	2022	FLFs showed a protective effect against H_2O_2-induced oxidative damage in L02 cells, and the underlying mechanism is associated with the enhancement of cell capability in clearing oxygen free radicals and the inhibition of apoptosis by the activation of the MAPKs/Nrf2/HO-1 signaling pathway.	h_2o	40-44	heme oxygenase 1	Homo sapiens	270-274
35396005-3	2022	Heme oxygenase 1 (HO 1) is a key rate limiting enzyme in the process of heme metabolism, which has the functions of anti inflammation, anti oxidation, anti apoptosis, anti aging, reducing cell damage and promoting angiogenesis.	Heme	72-76	heme oxygenase 1	Homo sapiens	0-16
35396005-3	2022	Heme oxygenase 1 (HO 1) is a key rate limiting enzyme in the process of heme metabolism, which has the functions of anti inflammation, anti oxidation, anti apoptosis, anti aging, reducing cell damage and promoting angiogenesis.	Heme	72-76	heme oxygenase 1	Homo sapiens	18-22
35192145-8	2022	TG caused the increases in intracellular reactive oxygen species (ROS) and in the protein levels of pSer40-Nrf2 and hemoglobin oxygenase 1 (HO-1).	Thapsigargin	0-2	heme oxygenase 1	Homo sapiens	116-138
35192145-8	2022	TG caused the increases in intracellular reactive oxygen species (ROS) and in the protein levels of pSer40-Nrf2 and hemoglobin oxygenase 1 (HO-1).	Thapsigargin	0-2	heme oxygenase 1	Homo sapiens	140-144
35085765-9	2022	Additionally, photo-activated DMA upregulated the oxidative stress marker gene, hemeoxygenase-1 and apoptotic marker genes (cytochrome-C, caspase-3, caspase-9).	N-myristoyl-alaninol	30-33	heme oxygenase 1	Homo sapiens	80-95
35419025-8	2022	Finally, Hemin, the agonist of HO-1, was applied in rescue assays, thereby verifying the mechanism of KLF7 modulating osteoclast differentiation by HO-1.	Hemin	9-14	heme oxygenase 1	Homo sapiens	31-35
35453348-4	2022	Increased levels of Reactive Oxygen Species (ROS) activate NRF2 signalling, inducing the expression of antioxidant enzymes, such as haem oxygenase (HO-1), catalase (CAT), glutathione peroxidase (GPx) and superoxide dismutase (SOD), that protect cells against oxidative stress.	Reactive Oxygen Species	20-43	heme oxygenase 1	Homo sapiens	148-152
35453348-4	2022	Increased levels of Reactive Oxygen Species (ROS) activate NRF2 signalling, inducing the expression of antioxidant enzymes, such as haem oxygenase (HO-1), catalase (CAT), glutathione peroxidase (GPx) and superoxide dismutase (SOD), that protect cells against oxidative stress.	Reactive Oxygen Species	45-48	heme oxygenase 1	Homo sapiens	148-152
35419301-2	2022	HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron.	Heme	15-19	heme oxygenase 1	Homo sapiens	0-4
35419301-2	2022	HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	0-4
35419301-2	2022	HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron.	Carbon Monoxide	87-89	heme oxygenase 1	Homo sapiens	0-4
35419301-2	2022	HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron.	Biliverdine	92-102	heme oxygenase 1	Homo sapiens	0-4
35419301-2	2022	HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron.	Iron	108-112	heme oxygenase 1	Homo sapiens	0-4
35419301-3	2022	The upregulation of HO-1 under pathological conditions associated with cellular stress represents an important cytoprotective defense mechanism by virtue of the anti-oxidant properties of the bilirubin and the anti-inflammatory effect of the CO produced.	Bilirubin	192-201	heme oxygenase 1	Homo sapiens	20-24
35453313-0	2022	Reduced Levels of H2S in Diabetes-Associated Osteoarthritis Are Linked to Hyperglycaemia, Nrf-2/HO-1 Signalling Downregulation and Chondrocyte Dysfunction.	Deuterium	18-21	heme oxygenase 1	Homo sapiens	96-100
35388300-9	2022	Codonopsis pilosula could upregulate HMOX1 via luteolin, capsaicin, and sulforaphane.	Capsaicin	57-66	heme oxygenase 1	Homo sapiens	37-42
35388300-9	2022	Codonopsis pilosula could upregulate HMOX1 via luteolin, capsaicin, and sulforaphane.	sulforaphane	72-84	heme oxygenase 1	Homo sapiens	37-42
35453313-6	2022	In addition, our results indicate that H2S is an inductor of the Nrf-2/HO-1 signalling pathway in cartilage, but is also a downstream target of Nrf-2 transcriptional activity.	Deuterium	39-42	heme oxygenase 1	Homo sapiens	71-75
35259284-8	2022	Furthermore, the NCHDH and NTHDH treatment significantly enhanced the antioxidants signaling proteins such as nuclear factor erythroid 2-related factor 2 (Nrf2) and Heme oxygenase 1 (HO-1).	nchdh	17-22	heme oxygenase 1	Homo sapiens	165-181
35332611-4	2022	The expression level of nuclear factor erythroid 2-related factor 2 and heme oxygenase-1 markedly increased after BE treatment will intimidate A549 cells proliferation by the ROS-independent pathway via the antioxidant pathway.	baicalein	114-116	heme oxygenase 1	Homo sapiens	72-88
35332611-4	2022	The expression level of nuclear factor erythroid 2-related factor 2 and heme oxygenase-1 markedly increased after BE treatment will intimidate A549 cells proliferation by the ROS-independent pathway via the antioxidant pathway.	Reactive Oxygen Species	175-178	heme oxygenase 1	Homo sapiens	72-88
35401165-5	2022	The in vitro results showed that: 1) Fr increased the expression of antioxidant enzymes including SOD1 and HO-1 to inhibit high glucose (HG)-induced fibronectin (FN) and inflammatory cell adhesion molecule (ICAM-1) overexpression; 2) Fr exerted antioxidant effect through activating the Nrf2/ARE pathway; 3) Fr significantly up-regulated the expression of Cx43 in HG-induced glomerular mesangial cells (GMCs), while the knock down of Cx43 largely impaired the activation of Nrf2/ARE pathway induced by Fr; 4) Fr promoted the activation of Nrf2/ARE pathway via regulating the interaction between Cx43 and AKT.	Glucose	128-135	heme oxygenase 1	Homo sapiens	107-111
35387349-0	2022	Metformin Promotes Differentiation and Attenuates H2O2-Induced Oxidative Damage of Osteoblasts via the PI3K/AKT/Nrf2/HO-1 Pathway.	Metformin	0-9	heme oxygenase 1	Homo sapiens	117-121
35387349-0	2022	Metformin Promotes Differentiation and Attenuates H2O2-Induced Oxidative Damage of Osteoblasts via the PI3K/AKT/Nrf2/HO-1 Pathway.	Hydrogen Peroxide	50-54	heme oxygenase 1	Homo sapiens	117-121
35387349-9	2022	Antioxidative Nrf2/HO-1 pathway, regarded as the downstream of PI3K/AKT pathway, was modulated by metformin in the protective process.	Metformin	98-107	heme oxygenase 1	Homo sapiens	19-23
35387349-11	2022	In conclusion, our study revealed that metformin promoted osteogenic differentiation and H2O2-induced oxidative damage of osteoblasts via the PI3K/AKT/Nrf2/HO-1 pathway.	Metformin	39-48	heme oxygenase 1	Homo sapiens	156-160
35387349-11	2022	In conclusion, our study revealed that metformin promoted osteogenic differentiation and H2O2-induced oxidative damage of osteoblasts via the PI3K/AKT/Nrf2/HO-1 pathway.	Hydrogen Peroxide	89-93	heme oxygenase 1	Homo sapiens	156-160
35286219-6	2022	Mechanistically, raloxifene suppressed NLRP3 inflammasomes activation by lowering the cellular levels of ROS through the modulation of redox signaling mediated via aryl hydrocarbon receptor (AhR)-Nrf2-HO-1 axis or the impaired generation of mitochondrial ROS in a mitophagy-dependent manner.	Raloxifene Hydrochloride	17-27	heme oxygenase 1	Homo sapiens	201-205
35286219-6	2022	Mechanistically, raloxifene suppressed NLRP3 inflammasomes activation by lowering the cellular levels of ROS through the modulation of redox signaling mediated via aryl hydrocarbon receptor (AhR)-Nrf2-HO-1 axis or the impaired generation of mitochondrial ROS in a mitophagy-dependent manner.	ros	105-108	heme oxygenase 1	Homo sapiens	201-205
35286219-6	2022	Mechanistically, raloxifene suppressed NLRP3 inflammasomes activation by lowering the cellular levels of ROS through the modulation of redox signaling mediated via aryl hydrocarbon receptor (AhR)-Nrf2-HO-1 axis or the impaired generation of mitochondrial ROS in a mitophagy-dependent manner.	ros	255-258	heme oxygenase 1	Homo sapiens	201-205
35453311-6	2022	These results indicated that luteolin treatment retarded oxaliplatin-induced tumor growth by facilitating apoptotic cell death and inhibiting HO-1-mediated cytoprotection.	Oxaliplatin	57-68	heme oxygenase 1	Homo sapiens	142-146
35300705-13	2022	Moreover, the encapsulation of glial cell-derived neurotrophic factor (GNDF)-containing DHAH-NLCs (DHAH-NLC-GNDF) activated the Nrf2/HO-1 pathway, suggesting the triggering of the endogenous anti-oxidative system present in microglia.	dhah	88-92	heme oxygenase 1	Homo sapiens	133-137
35300705-13	2022	Moreover, the encapsulation of glial cell-derived neurotrophic factor (GNDF)-containing DHAH-NLCs (DHAH-NLC-GNDF) activated the Nrf2/HO-1 pathway, suggesting the triggering of the endogenous anti-oxidative system present in microglia.	dhah	99-103	heme oxygenase 1	Homo sapiens	133-137
35260560-7	2022	Further findings revealed that HO-1 was essential for osteocyte ferroptosis in DOP and that its promoter activity was controlled by the interaction between the upstream NRF2 and c-JUN transcription factors.	Diethylhexyl Phthalate	79-82	heme oxygenase 1	Homo sapiens	31-35
35260560-8	2022	Targeting ferroptosis or HO-1 efficiently rescued osteocyte death in DOP by disrupting the vicious cycle between lipid peroxidation and HO-1 activation, eventually ameliorating trabecular deterioration.	Diethylhexyl Phthalate	69-72	heme oxygenase 1	Homo sapiens	25-29
35260560-8	2022	Targeting ferroptosis or HO-1 efficiently rescued osteocyte death in DOP by disrupting the vicious cycle between lipid peroxidation and HO-1 activation, eventually ameliorating trabecular deterioration.	Diethylhexyl Phthalate	69-72	heme oxygenase 1	Homo sapiens	136-140
35350242-9	2022	Furthermore, knockdown of GSK3beta significantly reduced nobiletin-induced ferroptosis and upregulated the Keap1/Nrf2/HO-1 signalling pathway, while the opposite was observed in cells overexpressing GSK3beta.	nobiletin	57-66	heme oxygenase 1	Homo sapiens	118-122
35259284-8	2022	Furthermore, the NCHDH and NTHDH treatment significantly enhanced the antioxidants signaling proteins such as nuclear factor erythroid 2-related factor 2 (Nrf2) and Heme oxygenase 1 (HO-1).	nchdh	17-22	heme oxygenase 1	Homo sapiens	183-187
35300173-0	2022	Local Treatment of Hydrogen-Rich Saline Promotes Wound Healing In Vivo by Inhibiting Oxidative Stress via Nrf-2/HO-1 Pathway.	Hydrogen	19-27	heme oxygenase 1	Homo sapiens	112-116
35259284-8	2022	Furthermore, the NCHDH and NTHDH treatment significantly enhanced the antioxidants signaling proteins such as nuclear factor erythroid 2-related factor 2 (Nrf2) and Heme oxygenase 1 (HO-1).	nthdh	27-32	heme oxygenase 1	Homo sapiens	165-181
35300173-0	2022	Local Treatment of Hydrogen-Rich Saline Promotes Wound Healing In Vivo by Inhibiting Oxidative Stress via Nrf-2/HO-1 Pathway.	Sodium Chloride	33-39	heme oxygenase 1	Homo sapiens	112-116
35300173-11	2022	Besides, hydrogen-rich medium relieved the oxidative stress via the activation of the Nrf-2/heme oxygenase-1 (HO-1) pathway.	Hydrogen	9-17	heme oxygenase 1	Homo sapiens	92-108
35300173-11	2022	Besides, hydrogen-rich medium relieved the oxidative stress via the activation of the Nrf-2/heme oxygenase-1 (HO-1) pathway.	Hydrogen	9-17	heme oxygenase 1	Homo sapiens	110-114
35259284-8	2022	Furthermore, the NCHDH and NTHDH treatment significantly enhanced the antioxidants signaling proteins such as nuclear factor erythroid 2-related factor 2 (Nrf2) and Heme oxygenase 1 (HO-1).	nthdh	27-32	heme oxygenase 1	Homo sapiens	183-187
35300173-13	2022	Hydrogen relieves the oxidative stress in the wound microenvironment via Nrf-2/HO-1 signaling pathway.	Hydrogen	0-8	heme oxygenase 1	Homo sapiens	79-83
35281466-1	2022	Recently, we found that 5,8-dihydroxy-4",7-dimethoxyflavone (DDF) upregulated the expression of heme oxygenase (HO)-1 via p38 mitogen-activated protein kinase/nuclear factor-erythroid factor 2-related factor 2 (MAPK/Nrf2) pathway in human cardiac fibroblasts (HCFs).	5,8-dihydroxy-4",7-dimethoxyflavone	24-59	heme oxygenase 1	Homo sapiens	96-117
35179529-5	2022	Under hypoxia, the expression of Nrf2 and heme oxygenase-1 was up-regulated by SFN treatment.	sulforaphane	79-82	heme oxygenase 1	Homo sapiens	42-58
35281466-1	2022	Recently, we found that 5,8-dihydroxy-4",7-dimethoxyflavone (DDF) upregulated the expression of heme oxygenase (HO)-1 via p38 mitogen-activated protein kinase/nuclear factor-erythroid factor 2-related factor 2 (MAPK/Nrf2) pathway in human cardiac fibroblasts (HCFs).	ddf	61-64	heme oxygenase 1	Homo sapiens	96-117
35281466-11	2022	Chromatin immunoprecipitation assays revealed the interaction between Sp1 and the binding site of proximal ARE on the HO-1 promoter, which was abolished by glutathione, AG1478, Go6976, LY294002, or mithramycin A.	Glutathione	156-167	heme oxygenase 1	Homo sapiens	118-122
35281466-11	2022	Chromatin immunoprecipitation assays revealed the interaction between Sp1 and the binding site of proximal ARE on the HO-1 promoter, which was abolished by glutathione, AG1478, Go6976, LY294002, or mithramycin A.	RTKI cpd	169-175	heme oxygenase 1	Homo sapiens	118-122
35281466-11	2022	Chromatin immunoprecipitation assays revealed the interaction between Sp1 and the binding site of proximal ARE on the HO-1 promoter, which was abolished by glutathione, AG1478, Go6976, LY294002, or mithramycin A.	Go 6976	177-183	heme oxygenase 1	Homo sapiens	118-122
35281466-11	2022	Chromatin immunoprecipitation assays revealed the interaction between Sp1 and the binding site of proximal ARE on the HO-1 promoter, which was abolished by glutathione, AG1478, Go6976, LY294002, or mithramycin A.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	185-193	heme oxygenase 1	Homo sapiens	118-122
35281466-11	2022	Chromatin immunoprecipitation assays revealed the interaction between Sp1 and the binding site of proximal ARE on the HO-1 promoter, which was abolished by glutathione, AG1478, Go6976, LY294002, or mithramycin A.	mithramycin A	198-211	heme oxygenase 1	Homo sapiens	118-122
35281466-13	2022	Pretreatment with an inhibitor of HO-1: zinc protoporphyrin IX reversed these inhibitory effects of HO-1.	zinc protoporphyrin	40-62	heme oxygenase 1	Homo sapiens	34-38
35309045-8	2022	We concluded that glutathione/oxidized glutathione (GSH/GSSG) conversion involved the PI3K/Akt-Nrf2/HO-1 signaling pathway and that the antioxidant enzyme-mediated mitochondrial apoptosis pathway of osteoblasts was necessary for the development of postmenopausal osteoporosis.	Glutathione	18-29	heme oxygenase 1	Homo sapiens	100-104
35309045-8	2022	We concluded that glutathione/oxidized glutathione (GSH/GSSG) conversion involved the PI3K/Akt-Nrf2/HO-1 signaling pathway and that the antioxidant enzyme-mediated mitochondrial apoptosis pathway of osteoblasts was necessary for the development of postmenopausal osteoporosis.	Glutathione	39-50	heme oxygenase 1	Homo sapiens	100-104
35309045-8	2022	We concluded that glutathione/oxidized glutathione (GSH/GSSG) conversion involved the PI3K/Akt-Nrf2/HO-1 signaling pathway and that the antioxidant enzyme-mediated mitochondrial apoptosis pathway of osteoblasts was necessary for the development of postmenopausal osteoporosis.	Glutathione	52-55	heme oxygenase 1	Homo sapiens	100-104
35309045-8	2022	We concluded that glutathione/oxidized glutathione (GSH/GSSG) conversion involved the PI3K/Akt-Nrf2/HO-1 signaling pathway and that the antioxidant enzyme-mediated mitochondrial apoptosis pathway of osteoblasts was necessary for the development of postmenopausal osteoporosis.	Glutathione Disulfide	56-60	heme oxygenase 1	Homo sapiens	100-104
35281466-13	2022	Pretreatment with an inhibitor of HO-1: zinc protoporphyrin IX reversed these inhibitory effects of HO-1.	zinc protoporphyrin	40-62	heme oxygenase 1	Homo sapiens	100-104
35024467-5	2022	Meanwhile, PEITC treatment ameliorated DON-induced an increase of the inducible nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) mRNA levels and intracellular reactive oxygen species (ROS) level, and a decrease of glutathione peroxidase 1 (GPx1), superoxide dismutase 2 (SOD2), catalase (CAT) and heme oxygenase 1 (HO-1) mRNA levels.	phenethyl isothiocyanate	11-16	heme oxygenase 1	Homo sapiens	306-322
35510228-7	2022	High dose of quercetin significantly decreased the gene expressions of NF-kappaB and TNFalpha, whereas the alternations of Nrf2 and HO-1 gene expressions were not significant in quercetin groups in compared with DEHP group.	Quercetin	13-22	heme oxygenase 1	Homo sapiens	132-136
35024467-5	2022	Meanwhile, PEITC treatment ameliorated DON-induced an increase of the inducible nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) mRNA levels and intracellular reactive oxygen species (ROS) level, and a decrease of glutathione peroxidase 1 (GPx1), superoxide dismutase 2 (SOD2), catalase (CAT) and heme oxygenase 1 (HO-1) mRNA levels.	phenethyl isothiocyanate	11-16	heme oxygenase 1	Homo sapiens	324-328
35024467-5	2022	Meanwhile, PEITC treatment ameliorated DON-induced an increase of the inducible nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) mRNA levels and intracellular reactive oxygen species (ROS) level, and a decrease of glutathione peroxidase 1 (GPx1), superoxide dismutase 2 (SOD2), catalase (CAT) and heme oxygenase 1 (HO-1) mRNA levels.	deoxynivalenol	39-42	heme oxygenase 1	Homo sapiens	306-322
35024467-5	2022	Meanwhile, PEITC treatment ameliorated DON-induced an increase of the inducible nitric oxide synthase (iNOS) and cyclooxygenase 2 (COX-2) mRNA levels and intracellular reactive oxygen species (ROS) level, and a decrease of glutathione peroxidase 1 (GPx1), superoxide dismutase 2 (SOD2), catalase (CAT) and heme oxygenase 1 (HO-1) mRNA levels.	deoxynivalenol	39-42	heme oxygenase 1	Homo sapiens	324-328
35045368-7	2022	Collectively, our studies demonstrated that compound D-6 protected against oxLDL-induced endothelial injury by activating Nrf2/HO-1 anti-oxidation pathway.	oxynide	53-56	heme oxygenase 1	Homo sapiens	127-131
34999313-5	2022	In non-transfected cells, we also observed TNF-alpha-induced VCAM1 overexpression as well as heme-induced overexpression of HMOX1 in both cell models.	Heme	93-97	heme oxygenase 1	Homo sapiens	124-129
35488673-0	2022	Raspberry ketone promotes FNDC5 protein expression via HO-1 upregulation in 3T3-L1 adipocytes.	raspberry ketone	0-16	heme oxygenase 1	Homo sapiens	55-59
35085532-5	2022	Berberine had an antagonistic effect for the majority of genes mutual for AD and toxic metal mixture: ACHE, APP, BAX, BCL2, CASP3, HMOX1, IL1B, MAPT, SOD2, TNF.	Berberine	0-9	heme oxygenase 1	Homo sapiens	131-136
35203060-0	2022	Metformin alleviates chronic obstructive pulmonary disease and cigarette smoke extract-induced glucocorticoid resistance by activating the nuclear factor E2-related factor 2/heme oxygenase-1 signaling pathway.	Metformin	0-9	heme oxygenase 1	Homo sapiens	174-190
34973124-11	2022	The antioxidant enzymes, HO1, NQO1, GPX1, and CAT were upregulated by CDDO-Me treatment.	bardoxolone methyl	70-77	heme oxygenase 1	Homo sapiens	25-28
35218032-6	2022	Furthermore, preincubation with Orz reduced H2 O2 -mediated the proapoptotic protein of Bak expression and the phosphorylation of ASK1, p38, JNK, and ERK, and increased the anti-apoptotic protein of Bcl-xl expression and anti-oxidative stress proteins of Nrf2 and HO-1 expression.	gamma-oryzanol	32-35	heme oxygenase 1	Homo sapiens	264-268
35123232-0	2022	Nicotinamide mononucleotide increases cell viability and restores tight junctions in high-glucose-treated human corneal epithelial cells via the SIRT1/Nrf2/HO-1 pathway.	Nicotinamide Mononucleotide	0-27	heme oxygenase 1	Homo sapiens	156-160
35123232-0	2022	Nicotinamide mononucleotide increases cell viability and restores tight junctions in high-glucose-treated human corneal epithelial cells via the SIRT1/Nrf2/HO-1 pathway.	Glucose	90-97	heme oxygenase 1	Homo sapiens	156-160
35268019-2	2022	ROS and inflammatory responses are regulated by the activation of nuclear factor erythroid-2-related factor 2 (Nrf2) and the expression of Nrf2 target genes, superoxide dismutase (SOD) and heme oxygenase-1 (HO-1).	Reactive Oxygen Species	0-3	heme oxygenase 1	Homo sapiens	189-205
35268019-2	2022	ROS and inflammatory responses are regulated by the activation of nuclear factor erythroid-2-related factor 2 (Nrf2) and the expression of Nrf2 target genes, superoxide dismutase (SOD) and heme oxygenase-1 (HO-1).	Reactive Oxygen Species	0-3	heme oxygenase 1	Homo sapiens	207-211
35268019-4	2022	We determined whether RGE suppresses the expression of IL-8 via Nrf2 activation and the expression of SOD and HO-1 in H. pylori-infected gastric epithelial AGS cells.	(2s)-2-Amino-5-(2-(Methylsulfinyl)acetimidamido)pentanoic Acid	22-25	heme oxygenase 1	Homo sapiens	110-114
35268019-5	2022	H. pylori-infected cells were treated with RGE with or without ML385, an Nrf2 inhibitor, or zinc protoporphyrin (ZnPP), a HO-1 inhibitor.	zinc protoporphyrin	92-111	heme oxygenase 1	Homo sapiens	122-126
35268019-5	2022	H. pylori-infected cells were treated with RGE with or without ML385, an Nrf2 inhibitor, or zinc protoporphyrin (ZnPP), a HO-1 inhibitor.	zinc protoporphyrin	113-117	heme oxygenase 1	Homo sapiens	122-126
35268019-8	2022	H. pylori infection decreased the protein levels of SOD-1 and HO-1, as well as SOD activity, which was reversed by RGE treatment.	(2s)-2-Amino-5-(2-(Methylsulfinyl)acetimidamido)pentanoic Acid	115-118	heme oxygenase 1	Homo sapiens	62-66
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Heme	110-114	heme oxygenase 1	Homo sapiens	18-22
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	ferrous iron	120-132	heme oxygenase 1	Homo sapiens	18-22
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Carbon Monoxide	134-149	heme oxygenase 1	Homo sapiens	18-22
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Carbon Monoxide	151-153	heme oxygenase 1	Homo sapiens	18-22
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Biliverdine	160-170	heme oxygenase 1	Homo sapiens	18-22
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Biliverdine	172-174	heme oxygenase 1	Homo sapiens	18-22
35048917-0	2022	Glucopyranose from Pleurotus geesteranus prevent alcoholic liver diseases by regulating Nrf2/HO-1-TLR4/NF-kappaB signalling pathways and gut microbiota.	Glucose	0-13	heme oxygenase 1	Homo sapiens	93-97
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Bilirubin	176-185	heme oxygenase 1	Homo sapiens	18-22
35281042-2	2022	Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation.	Bilirubin	187-189	heme oxygenase 1	Homo sapiens	18-22
35281042-7	2022	Being a highly infectious pathogenic bacterium, Mycobacterium tuberculosis (MTB) infection causes acute oxidative stress, and increases the expression of HO-1, which may in turn facilitate MTB survival and growth due to increased iron availability.	Iron	230-234	heme oxygenase 1	Homo sapiens	154-158
35281042-8	2022	Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe2+) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis.	Reactive Oxygen Species	54-77	heme oxygenase 1	Homo sapiens	127-131
35281042-8	2022	Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe2+) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis.	Reactive Oxygen Species	79-82	heme oxygenase 1	Homo sapiens	127-131
35281042-8	2022	Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe2+) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis.	Iron	93-97	heme oxygenase 1	Homo sapiens	127-131
35281042-8	2022	Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe2+) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis.	ammonium ferrous sulfate	99-103	heme oxygenase 1	Homo sapiens	127-131
35218032-6	2022	Furthermore, preincubation with Orz reduced H2 O2 -mediated the proapoptotic protein of Bak expression and the phosphorylation of ASK1, p38, JNK, and ERK, and increased the anti-apoptotic protein of Bcl-xl expression and anti-oxidative stress proteins of Nrf2 and HO-1 expression.	Hydrogen Peroxide	44-49	heme oxygenase 1	Homo sapiens	264-268
35204307-7	2022	We further found that 3,5,7-trimethoxyflavone suppressed the excessive increase in ROS, mitogen-activated protein kinases (MAPKs), Akt, and cyclooxygenase-2 (COX-2)and increased heme oxygenase (HO)-1 expression.	3,5,7-Trimethoxyflavone	22-45	heme oxygenase 1	Homo sapiens	178-199
35199318-8	2022	Both H2O2 and methemoglobin upregulated the expression of the HO-1 protein in the dTHP-1 monoculture; moreover, co-culture with endometriotic cells further enhanced HO-1 production.	Hydrogen Peroxide	5-9	heme oxygenase 1	Homo sapiens	62-66
35199318-8	2022	Both H2O2 and methemoglobin upregulated the expression of the HO-1 protein in the dTHP-1 monoculture; moreover, co-culture with endometriotic cells further enhanced HO-1 production.	Hydrogen Peroxide	5-9	heme oxygenase 1	Homo sapiens	165-169
35237380-0	2022	Ferritinophagy-Mediated Ferroptosis and Activation of Keap1/Nrf2/HO-1 Pathway Were Conducive to EMT Inhibition of Gastric Cancer Cells in Action of 2,2"-Di-pyridineketone Hydrazone Dithiocarbamate Butyric Acid Ester.	2,2"-di-pyridineketone hydrazone dithiocarbamate	148-196	heme oxygenase 1	Homo sapiens	65-69
35237380-0	2022	Ferritinophagy-Mediated Ferroptosis and Activation of Keap1/Nrf2/HO-1 Pathway Were Conducive to EMT Inhibition of Gastric Cancer Cells in Action of 2,2"-Di-pyridineketone Hydrazone Dithiocarbamate Butyric Acid Ester.	butyric acid ester	197-215	heme oxygenase 1	Homo sapiens	65-69
35222803-8	2022	Silencing nuclear factor erythroid 2-related factor 2 (Nrf2) by targeted-siRNA and inhibiting heme oxygenase-1 (HO-1) through zinc protoporphyrin IX (ZnPP) significantly decreased cytoprotection of KGF-2.	zinc protoporphyrin	126-148	heme oxygenase 1	Homo sapiens	94-110
35195252-5	2022	Specifically, FoxOs regulate mitochondrial biogenesis by dampening NRF1-Tfam and c-Myc-Tfam cascades directly, and inhibiting NAD-Sirt1-Pgc1alpha cascade indirectly by inducing Hmox1 or repressing Fxn and Urod.	NAD	126-129	heme oxygenase 1	Homo sapiens	177-182
35222803-8	2022	Silencing nuclear factor erythroid 2-related factor 2 (Nrf2) by targeted-siRNA and inhibiting heme oxygenase-1 (HO-1) through zinc protoporphyrin IX (ZnPP) significantly decreased cytoprotection of KGF-2.	zinc protoporphyrin	126-148	heme oxygenase 1	Homo sapiens	112-116
35222803-8	2022	Silencing nuclear factor erythroid 2-related factor 2 (Nrf2) by targeted-siRNA and inhibiting heme oxygenase-1 (HO-1) through zinc protoporphyrin IX (ZnPP) significantly decreased cytoprotection of KGF-2.	zinc protoporphyrin	150-154	heme oxygenase 1	Homo sapiens	94-110
35222803-8	2022	Silencing nuclear factor erythroid 2-related factor 2 (Nrf2) by targeted-siRNA and inhibiting heme oxygenase-1 (HO-1) through zinc protoporphyrin IX (ZnPP) significantly decreased cytoprotection of KGF-2.	zinc protoporphyrin	150-154	heme oxygenase 1	Homo sapiens	112-116
35222803-10	2022	As demonstrated by these data, KGF-2 resisted H2O2-mediated apoptosis and oxidative stress in HLECs through Nrf2/HO-1 and PI3K/Akt pathways, suggesting a potential protective effect against the formation of cataracts.	Hydrogen Peroxide	46-50	heme oxygenase 1	Homo sapiens	113-117
35189631-10	2022	Furthermore, curcumin positively regulated the expression of Nrf2, HO-1, and SOD1 mRNAs in cells treated with 0.1 and 0.5 muM doxazosin.	Curcumin	13-21	heme oxygenase 1	Homo sapiens	67-71
35209068-3	2022	In this study, we evaluated the ability of a topical liquid formula of polydeoxyribonucleotide (PDRN), vitamin C, and niacinamide (PVN) delivered via a microneedling therapy system (MTS) to attenuate photoaging and pigmentation by increasing nuclear factor erythroid 2-like 2 (NRF2)/heme oxygenase-1 (HO-1) and decreasing MMP expression in a UV-B-radiated animal model.	pvn	131-134	heme oxygenase 1	Homo sapiens	283-299
35209068-3	2022	In this study, we evaluated the ability of a topical liquid formula of polydeoxyribonucleotide (PDRN), vitamin C, and niacinamide (PVN) delivered via a microneedling therapy system (MTS) to attenuate photoaging and pigmentation by increasing nuclear factor erythroid 2-like 2 (NRF2)/heme oxygenase-1 (HO-1) and decreasing MMP expression in a UV-B-radiated animal model.	pvn	131-134	heme oxygenase 1	Homo sapiens	301-305
35189631-10	2022	Furthermore, curcumin positively regulated the expression of Nrf2, HO-1, and SOD1 mRNAs in cells treated with 0.1 and 0.5 muM doxazosin.	Doxazosin	126-135	heme oxygenase 1	Homo sapiens	67-71
35197970-10	2022	Zinc sulfate significantly increased the levels of P-mTOR Ser2448, P-p70S6K Thr389, and P-tau Ser356 and decreased the levels of nuclear factor erythroid 2-related factor-2 (Nrf2) and heme oxygenase-1 (HO-1) in SH-SY5Y cells and in zinc-treated rats compared with the control groups.	Zinc Sulfate	0-12	heme oxygenase 1	Homo sapiens	184-200
35144642-8	2022	Activated ROS-metabolism was identified in METTL7B-overexpressed LUAD cells, accompanied with upregulated protein level of GPX4, HMOX1 and SOD1 and their enzymatic activities.	ros	10-13	heme oxygenase 1	Homo sapiens	129-134
35197970-10	2022	Zinc sulfate significantly increased the levels of P-mTOR Ser2448, P-p70S6K Thr389, and P-tau Ser356 and decreased the levels of nuclear factor erythroid 2-related factor-2 (Nrf2) and heme oxygenase-1 (HO-1) in SH-SY5Y cells and in zinc-treated rats compared with the control groups.	Zinc Sulfate	0-12	heme oxygenase 1	Homo sapiens	202-206
34981336-10	2022	CONCLUSIONS: These findings suggest that WDR26 mediates H2O2-induced oxidative stress and cell injury, possibly by reducing the intrinsic apoptotic pathway and activating Nrf2 and HO-1 in astrocytes.	Hydrogen Peroxide	56-60	heme oxygenase 1	Homo sapiens	180-184
35204177-9	2022	In addition, GBH restored the expression of ferroptosis marker proteins, such as GPX4, HO-1 and COX-2, which were altered by RSL3.	gbh	13-16	heme oxygenase 1	Homo sapiens	87-91
34994954-8	2022	These phenomena, appeared to correlate with the recovered cellular antioxidant enzyme activities and inducted HO-1 (heme oxygenase-1) expression accompanying the nuclear translocation of Nrf2 conduct by saikosaponin-D preconditioning which had been altered by glutamate, were correlated with its neuroprotective.	Glutamic Acid	260-269	heme oxygenase 1	Homo sapiens	110-114
34994954-8	2022	These phenomena, appeared to correlate with the recovered cellular antioxidant enzyme activities and inducted HO-1 (heme oxygenase-1) expression accompanying the nuclear translocation of Nrf2 conduct by saikosaponin-D preconditioning which had been altered by glutamate, were correlated with its neuroprotective.	Glutamic Acid	260-269	heme oxygenase 1	Homo sapiens	116-132
34994954-11	2022	Taken together, our results indicated that saikosaponin-D enhanced cellular antioxidant capacity through not only intrinsic free radical-scavenging activity but also induction of endogenous antioxidant enzyme activities and HO-1 expression mediated, at least in part, by activating PI3K and subsequently Nrf2 nuclear translocation, thereby protecting the SH-SY5Y cells from glutamate-induced oxidative cytotoxicity.	saikosaponin D	43-57	heme oxygenase 1	Homo sapiens	224-228
35204104-7	2022	Furthermore, the treatment of cells with HC-EA and its active compounds abolished intracellular ROS and increased levels of heme oxygenase-1 and superoxide dismutase.	hc-ea	41-46	heme oxygenase 1	Homo sapiens	124-140
35204159-1	2022	Heme oxygenase 1 (HO-1), the rate-limiting enzyme in heme degradation, is involved in the maintenance of cellular homeostasis, exerting a cytoprotective role by its antioxidative and anti-inflammatory functions.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
35204159-1	2022	Heme oxygenase 1 (HO-1), the rate-limiting enzyme in heme degradation, is involved in the maintenance of cellular homeostasis, exerting a cytoprotective role by its antioxidative and anti-inflammatory functions.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
35204159-2	2022	HO-1 and its end products, biliverdin, carbon monoxide and free iron (Fe2+), confer cytoprotection against inflammatory and oxidative injury.	Biliverdine	27-37	heme oxygenase 1	Homo sapiens	0-4
35204159-2	2022	HO-1 and its end products, biliverdin, carbon monoxide and free iron (Fe2+), confer cytoprotection against inflammatory and oxidative injury.	Carbon Monoxide	39-54	heme oxygenase 1	Homo sapiens	0-4
35204159-2	2022	HO-1 and its end products, biliverdin, carbon monoxide and free iron (Fe2+), confer cytoprotection against inflammatory and oxidative injury.	Iron	64-68	heme oxygenase 1	Homo sapiens	0-4
35204159-2	2022	HO-1 and its end products, biliverdin, carbon monoxide and free iron (Fe2+), confer cytoprotection against inflammatory and oxidative injury.	ammonium ferrous sulfate	70-74	heme oxygenase 1	Homo sapiens	0-4
35043283-9	2022	Transcriptomic RNA-seq showed that FX abrogated TPA-induced differentially expressed genes (DEGs) of Nfe2l2-related genes Nqo1, Ho1, and Keap1.	Tetradecanoylphorbol Acetate	48-51	heme oxygenase 1	Homo sapiens	128-131
35204062-3	2022	Exercise elevates heme oxygenase-1 (HO-1) and biliverdin reductase A (BVRA) expression as built-in protective mechanisms, which produce the most potent antioxidant, bilirubin.	Bilirubin	165-174	heme oxygenase 1	Homo sapiens	18-34
35237424-8	2022	A 6 h pretreatment of 3-MA increased PM2.5-induced oxidative damage and cellular inflammation as indicated by increasing protein levels of HO-1, TXNIP, Bnip3L/NIX and IL-8 gene expression.	3-methyladenine	22-26	heme oxygenase 1	Homo sapiens	139-143
35204062-3	2022	Exercise elevates heme oxygenase-1 (HO-1) and biliverdin reductase A (BVRA) expression as built-in protective mechanisms, which produce the most potent antioxidant, bilirubin.	Bilirubin	165-174	heme oxygenase 1	Homo sapiens	36-40
35204062-7	2022	The main objective of this review is to describe the function of bilirubin as an antioxidant and metabolic hormone and how the HO-1-BVRA-bilirubin-PPARalpha axis influences inflammation, metabolic function and interacts with exercise to improve outcomes of weight management.	Bilirubin	137-146	heme oxygenase 1	Homo sapiens	127-131
35013107-9	2022	MET pretreatment also significantly suppressed MGO-stimulated ROS production, increased signaling through the ROS-mediated PI3K/Akt and Nrf2/HO-1 pathways, and markedly elevated the levels of its downstream antioxidants.	Reactive Oxygen Species	110-113	heme oxygenase 1	Homo sapiens	141-145
35013107-12	2022	In addition, a PI3K inhibitor (LY-294002) and a Nrf2 inhibitor (ML385) observably attenuated the protective effects of MET on MGO-induced apoptosis and ROS generation by inhibiting the Nrf2/HO-1 pathways, while a ROS scavenger (NAC) and a permeability transition pores inhibitor (CsA) completely reversed these effects.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	31-40	heme oxygenase 1	Homo sapiens	190-194
35013107-12	2022	In addition, a PI3K inhibitor (LY-294002) and a Nrf2 inhibitor (ML385) observably attenuated the protective effects of MET on MGO-induced apoptosis and ROS generation by inhibiting the Nrf2/HO-1 pathways, while a ROS scavenger (NAC) and a permeability transition pores inhibitor (CsA) completely reversed these effects.	ML385	64-69	heme oxygenase 1	Homo sapiens	190-194
35013107-12	2022	In addition, a PI3K inhibitor (LY-294002) and a Nrf2 inhibitor (ML385) observably attenuated the protective effects of MET on MGO-induced apoptosis and ROS generation by inhibiting the Nrf2/HO-1 pathways, while a ROS scavenger (NAC) and a permeability transition pores inhibitor (CsA) completely reversed these effects.	Pyruvaldehyde	126-129	heme oxygenase 1	Homo sapiens	190-194
35047060-4	2022	Methods: An HO-1 inducer Hemin or an HO-1 inhibitor ZnPP-IX was used to treat the activated HSC-T6, respectively.	Hemin	25-30	heme oxygenase 1	Homo sapiens	12-16
35047060-4	2022	Methods: An HO-1 inducer Hemin or an HO-1 inhibitor ZnPP-IX was used to treat the activated HSC-T6, respectively.	zinc protoporphyrin	52-59	heme oxygenase 1	Homo sapiens	37-41
35056649-3	2022	In this work, we focused on determining the effect of kaempferol and its glycoside derivatives on the expression level of genes related to the reduction of oxidative stress-NFE2L2, NQO1, SOD1, SOD2, and HO-1; the enzymatic activity of superoxide dismutases; and the level of glutathione.	kaempferol	54-64	heme oxygenase 1	Homo sapiens	203-207
35047556-0	2021	miR-3587 Inhibitor Attenuates Ferroptosis Following Renal Ischemia-Reperfusion Through HO-1.	mir-3587	0-8	heme oxygenase 1	Homo sapiens	87-91
35047556-5	2021	When a miR-3587 inhibitor was applied in a hypoxia-reoxygenation (HR) model system using renal tubular epithelial cells, HO-1 protein (encoded by HMOX1) expression was significantly increased relative to that observed in the HR group, with concomitant increases in GPX4 protein levels, enhanced cell viability, a reduction in malondialdehyde content, decreased Fe2+ level, and the restoration of normal mitochondrial membrane potential.	mir-3587	7-15	heme oxygenase 1	Homo sapiens	121-125
35047556-5	2021	When a miR-3587 inhibitor was applied in a hypoxia-reoxygenation (HR) model system using renal tubular epithelial cells, HO-1 protein (encoded by HMOX1) expression was significantly increased relative to that observed in the HR group, with concomitant increases in GPX4 protein levels, enhanced cell viability, a reduction in malondialdehyde content, decreased Fe2+ level, and the restoration of normal mitochondrial membrane potential.	mir-3587	7-15	heme oxygenase 1	Homo sapiens	146-151
35047556-5	2021	When a miR-3587 inhibitor was applied in a hypoxia-reoxygenation (HR) model system using renal tubular epithelial cells, HO-1 protein (encoded by HMOX1) expression was significantly increased relative to that observed in the HR group, with concomitant increases in GPX4 protein levels, enhanced cell viability, a reduction in malondialdehyde content, decreased Fe2+ level, and the restoration of normal mitochondrial membrane potential.	Malondialdehyde	326-341	heme oxygenase 1	Homo sapiens	121-125
35047556-5	2021	When a miR-3587 inhibitor was applied in a hypoxia-reoxygenation (HR) model system using renal tubular epithelial cells, HO-1 protein (encoded by HMOX1) expression was significantly increased relative to that observed in the HR group, with concomitant increases in GPX4 protein levels, enhanced cell viability, a reduction in malondialdehyde content, decreased Fe2+ level, and the restoration of normal mitochondrial membrane potential.	ammonium ferrous sulfate	361-365	heme oxygenase 1	Homo sapiens	121-125
35047556-7	2021	Targeting of HMOX1 by miR-3587 was confirmed by luciferase reporter gene assay.	mir-3587	22-30	heme oxygenase 1	Homo sapiens	13-18
35047556-8	2021	In conclusion, these preliminary results indicate that inhibition of miR-3587 promotes HO-1 upregulation, thereby protecting renal tissues from IR-induced ferroptosis.	mir-3587	69-77	heme oxygenase 1	Homo sapiens	87-91
34986734-0	2022	Ramelteon protects against human pulmonary microvascular endothelial cell injury induced by lipopolysaccharide (LPS) via activating nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway.	ramelteon	0-9	heme oxygenase 1	Homo sapiens	183-199
34918393-5	2022	Our data indicate that overexpression of HO-1 or its metabolite biliverdin can maintain endothelial integrity upon DENV infection in vitro and in vivo.	Biliverdine	64-74	heme oxygenase 1	Homo sapiens	41-45
34918393-7	2022	Subsequently, we confirmed that two medicinal plant-derived compounds, andrographolide, and celastrol, widely used as a nutritional or medicinal supplement are useful to attenuate DENV-induced plasma leakage through induction of the HO-1 expression in DENV-infected AG129 mice.	andrographolide	71-86	heme oxygenase 1	Homo sapiens	233-237
34918393-7	2022	Subsequently, we confirmed that two medicinal plant-derived compounds, andrographolide, and celastrol, widely used as a nutritional or medicinal supplement are useful to attenuate DENV-induced plasma leakage through induction of the HO-1 expression in DENV-infected AG129 mice.	celastrol	92-101	heme oxygenase 1	Homo sapiens	233-237
34986734-0	2022	Ramelteon protects against human pulmonary microvascular endothelial cell injury induced by lipopolysaccharide (LPS) via activating nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway.	ramelteon	0-9	heme oxygenase 1	Homo sapiens	201-205
34986734-12	2022	Ramelteon treatment also activated the Nrf2/HO-1 signaling pathway in LPS-induced HPMECs.	ramelteon	0-9	heme oxygenase 1	Homo sapiens	44-48
34986734-14	2022	Collectively, the results suggested that ramelteon alleviated LPS-induced HPMEC damage by activating the Nrf2/HO-1 signaling pathway, making it an effective treatment for ALI.	ramelteon	41-50	heme oxygenase 1	Homo sapiens	110-114
33982762-5	2021	Furthermore, THCA upregulated the expression levels of heme oxygenase-1 and NAD(P)H:quinone oxidoreductase 1, and the activation of nuclear factor erythroid 2-related factor 2 in HaCaT cells.	thca	13-17	heme oxygenase 1	Homo sapiens	55-71
3290025-1	1988	In biological systems oxidation of heme is carried out by two isozymes of the microsomal heme oxygenase, HO-1 and HO-2.	Heme	35-39	heme oxygenase 1	Homo sapiens	105-118
3290025-7	1988	Most likely, HO-1 gene is regulated in the same manner as metallothione in the gene.	metallothione	58-71	heme oxygenase 1	Homo sapiens	13-17
3290025-9	1988	In vivo induction of HO-1 activity in the liver is accompanied by decreases in the total P-450 levels and, in a reconstituted system, cytochrome P-450b heme can be quantitatively converted to biliverdin by HO-1 and HO-2.	Heme	152-156	heme oxygenase 1	Homo sapiens	21-25
3290025-9	1988	In vivo induction of HO-1 activity in the liver is accompanied by decreases in the total P-450 levels and, in a reconstituted system, cytochrome P-450b heme can be quantitatively converted to biliverdin by HO-1 and HO-2.	Biliverdine	192-202	heme oxygenase 1	Homo sapiens	21-25
33862517-7	2021	The mechanism studies indicated that 13f exhibited cytoprotective effect by activating the Keap1-Nrf2-ARE pathway and stimulating downstream anti-oxidant protein including HO-1, NQO1, TrxR1, GCLC, and GCLM.	13F	37-40	heme oxygenase 1	Homo sapiens	172-176
479159-7	1979	The data indicate that there are regions of the hydrophobic disulfide knot, Ho1-DSK, which are surface-oriented.	Disulfides	60-69	heme oxygenase 1	Homo sapiens	76-79
479159-8	1979	The distribution of iodine as mono- and diiodotyrosine in N-DSK and Ho1-DSK reflected the percentage (83 and 17, respectively) found in iodinated fibrinogen from which these fragments were prepared.	Iodine	20-26	heme oxygenase 1	Homo sapiens	68-71
34025790-6	2021	Furthermore, it was demonstrated that the expression levels of the ferroptosis-associated genes heme oxygenase-1, glutamate-cysteine ligase catalytic and glutamate-cysteine ligase modifier were significantly upregulated after Andrographis treatment in both GC cell lines in reverse transcription-quantitative PCR experiments (P<0.05); this finding was further confirmed by immunoblotting assays (P<0.05).	Glutamic Acid	114-123	heme oxygenase 1	Homo sapiens	96-112
34025790-6	2021	Furthermore, it was demonstrated that the expression levels of the ferroptosis-associated genes heme oxygenase-1, glutamate-cysteine ligase catalytic and glutamate-cysteine ligase modifier were significantly upregulated after Andrographis treatment in both GC cell lines in reverse transcription-quantitative PCR experiments (P<0.05); this finding was further confirmed by immunoblotting assays (P<0.05).	Glutamic Acid	154-163	heme oxygenase 1	Homo sapiens	96-112
34025790-6	2021	Furthermore, it was demonstrated that the expression levels of the ferroptosis-associated genes heme oxygenase-1, glutamate-cysteine ligase catalytic and glutamate-cysteine ligase modifier were significantly upregulated after Andrographis treatment in both GC cell lines in reverse transcription-quantitative PCR experiments (P<0.05); this finding was further confirmed by immunoblotting assays (P<0.05).	Cysteine	164-172	heme oxygenase 1	Homo sapiens	96-112
32712770-6	2021	In contrast, at 10 mumol.L-1 ziram and zinc associated-disulfiram induced expression of several antioxidants genes HMOX1, SOD2, and catalase, which could suggest the induction of oxidative stress.	Ziram	29-34	heme oxygenase 1	Homo sapiens	115-120
32712770-6	2021	In contrast, at 10 mumol.L-1 ziram and zinc associated-disulfiram induced expression of several antioxidants genes HMOX1, SOD2, and catalase, which could suggest the induction of oxidative stress.	Disulfiram	55-65	heme oxygenase 1	Homo sapiens	115-120
33905708-6	2021	RESULTS: Heme supports carcinogenesis via modulation of immune cell function, promoting inflammation and gut dysbiosis, impeding tumour suppressive potential of P53 gene, promoting cellular cytotoxicity and reactive oxygen species generation and modulating Nfr2 /HO-1 axis.	Heme	9-13	heme oxygenase 1	Homo sapiens	263-267
33850557-0	2021	miR-125b/NRF2/HO-1 axis is involved in protection against oxidative stress of cystic fibrosis: A pilot study.	mir-125b	0-8	heme oxygenase 1	Homo sapiens	14-18
34048148-0	2021	Lipoxin A4 protects primary spinal cord neurons from Erastin-induced ferroptosis by activating the Akt/Nrf2/HO-1 signaling pathway.	lipoxin A4	0-10	heme oxygenase 1	Homo sapiens	108-112
33484436-14	2021	CONCLUSION: The precise mechanism accountable for the anti-inflammatory features of HO-1 is not completely understood; nevertheless, the CO signaling function associated with the antioxidant property shown by bilirubin possibly will play an act in the improvement of inflammation.	Bilirubin	209-218	heme oxygenase 1	Homo sapiens	84-88
34048148-0	2021	Lipoxin A4 protects primary spinal cord neurons from Erastin-induced ferroptosis by activating the Akt/Nrf2/HO-1 signaling pathway.	erastin	53-60	heme oxygenase 1	Homo sapiens	108-112
34048148-11	2021	In conclusion, this work demonstrated that LXA4 exerted a neuroprotective effect in Erastin-induced ferroptosis of primary spinal cord neurons by activating Akt/Nrf2/HO-1 signaling pathway.	lipoxin A4	43-47	heme oxygenase 1	Homo sapiens	166-170
34048148-11	2021	In conclusion, this work demonstrated that LXA4 exerted a neuroprotective effect in Erastin-induced ferroptosis of primary spinal cord neurons by activating Akt/Nrf2/HO-1 signaling pathway.	erastin	84-91	heme oxygenase 1	Homo sapiens	166-170
34049949-10	2021	Treatment of L2 and H441 cells with siRNAs against Nrf2 or HO-1 abrogated the protective effects of AICAR.	AICA ribonucleotide	100-105	heme oxygenase 1	Homo sapiens	59-63
34012878-1	2021	AIM: To investigate the protective effect of heme oxygenase-1 (HO-1) against H2O2-induced apoptosis in human ARPE-19 cells.	Hydrogen Peroxide	77-81	heme oxygenase 1	Homo sapiens	45-61
34049949-11	2021	CONCLUSIONS: Our data indicate that the primary mechanism for the protective action of AICAR in toxic gas injury is by upregulating lung HO-1 levels.	AICA ribonucleotide	87-92	heme oxygenase 1	Homo sapiens	137-141
34039348-9	2021	Increased HO-1 further maintained reactive oxygen species (ROS) within a minimal tumor-promoting level and enhanced cytoprotective autophagy.	Reactive Oxygen Species	34-57	heme oxygenase 1	Homo sapiens	10-14
34039348-9	2021	Increased HO-1 further maintained reactive oxygen species (ROS) within a minimal tumor-promoting level and enhanced cytoprotective autophagy.	Reactive Oxygen Species	59-62	heme oxygenase 1	Homo sapiens	10-14
34012878-1	2021	AIM: To investigate the protective effect of heme oxygenase-1 (HO-1) against H2O2-induced apoptosis in human ARPE-19 cells.	Hydrogen Peroxide	77-81	heme oxygenase 1	Homo sapiens	63-67
34012878-2	2021	METHODS: The lentiviral vector expressing HO-1 was prepared and transfected into apoptotic ARPE-19 cells induced by H2O2.	Hydrogen Peroxide	116-120	heme oxygenase 1	Homo sapiens	42-46
34012878-5	2021	It was found that exogenous HO-1 significantly ameliorated H2O2-induced loss of cell viability, apoptosis and intracellular levels of reactive oxygen species (ROS) in ARPE-19 cells.	Hydrogen Peroxide	59-63	heme oxygenase 1	Homo sapiens	28-32
34012878-5	2021	It was found that exogenous HO-1 significantly ameliorated H2O2-induced loss of cell viability, apoptosis and intracellular levels of reactive oxygen species (ROS) in ARPE-19 cells.	Reactive Oxygen Species	134-157	heme oxygenase 1	Homo sapiens	28-32
34012878-5	2021	It was found that exogenous HO-1 significantly ameliorated H2O2-induced loss of cell viability, apoptosis and intracellular levels of reactive oxygen species (ROS) in ARPE-19 cells.	Reactive Oxygen Species	159-162	heme oxygenase 1	Homo sapiens	28-32
34012878-7	2021	Furthermore, HO-1 upregulation further inhibited H2O2-induced release of cysteinyl aspartate specific proteinase-3 (caspase-3).	Hydrogen Peroxide	49-53	heme oxygenase 1	Homo sapiens	13-17
34012878-7	2021	Furthermore, HO-1 upregulation further inhibited H2O2-induced release of cysteinyl aspartate specific proteinase-3 (caspase-3).	cysteinyl-aspartate	73-92	heme oxygenase 1	Homo sapiens	13-17
34012878-8	2021	CONCLUSION: Exogenous HO-1 protect ARPE-19 cells against H2O2-induced oxidative stress by regulating the expressions of Nrf2, HO-1, Bcl-2, and caspase-3.	Hydrogen Peroxide	57-61	heme oxygenase 1	Homo sapiens	22-26
33999357-10	2021	Taken together, our findings suggest that activation of Nrf2/ARE/HO-1 signaling cascades contributes to PME-induced anti-oxidative and neuroprotective actions, which are at least partially mediated by AKT and ERK pathways.	pinostrobin	104-107	heme oxygenase 1	Homo sapiens	65-69
33990765-3	2022	Preincubation with BELNs decreased the level of reactive oxygen species (ROS), increased the mitochondrial membrane potential, and prevented cell apoptosis by inducing the expression of Bcl-2 and heme oxygenase-1 (HO-1) and decreasing the content of Bax in rotenone-treated HepG2 cells.	belns	19-24	heme oxygenase 1	Homo sapiens	196-212
34011367-0	2021	Esomeprazole attenuates inflammatory and fibrotic response in lung cells through the MAPK/Nrf2/HO1 pathway.	Esomeprazole	0-12	heme oxygenase 1	Homo sapiens	95-98
34011367-6	2021	RESULTS: Our study shows that esomeprazole controls pro-inflammatory and profibrotic molecules through nuclear translocation of the transcription factor nuclear factor-like 2 (Nrf2) and induction of the cytoprotective molecule heme oxygenase 1 (HO1).	Esomeprazole	30-42	heme oxygenase 1	Homo sapiens	227-243
34011367-6	2021	RESULTS: Our study shows that esomeprazole controls pro-inflammatory and profibrotic molecules through nuclear translocation of the transcription factor nuclear factor-like 2 (Nrf2) and induction of the cytoprotective molecule heme oxygenase 1 (HO1).	Esomeprazole	30-42	heme oxygenase 1	Homo sapiens	245-248
34011367-7	2021	Genetic deletion of Nrf2 or pharmacological inhibition of HO1 impaired esomeprazole-mediated regulation of proinflammatory and profibrotic molecules.	Esomeprazole	71-83	heme oxygenase 1	Homo sapiens	58-61
33990765-3	2022	Preincubation with BELNs decreased the level of reactive oxygen species (ROS), increased the mitochondrial membrane potential, and prevented cell apoptosis by inducing the expression of Bcl-2 and heme oxygenase-1 (HO-1) and decreasing the content of Bax in rotenone-treated HepG2 cells.	belns	19-24	heme oxygenase 1	Homo sapiens	214-218
33903766-2	2021	Here we show that a distinct subset of TAMs (F4/80hiCD115hiC3aRhiCD88hi), endowed with high rates of heme catabolism by the stress-responsive enzyme heme oxygenase-1 (HO-1), plays a critical role in shaping a prometastatic tumor microenvironment favoring immunosuppression, angiogenesis and epithelial-to-mesenchymal transition.	Heme	101-105	heme oxygenase 1	Homo sapiens	149-165
34025070-16	2021	Moreover, SB203580 significantly reduced the pulmonary P-p38, NFkappaB, P-signal transducer and activator of transcription-3 and Myd88 levels but increased the IkappaB and HO-1 levels.	SB 203580	10-18	heme oxygenase 1	Homo sapiens	172-176
33845576-0	2021	A Coumarin-Porphyrin FRET Break-Apart Probe for Heme Oxygenase-1.	coumarin	2-10	heme oxygenase 1	Homo sapiens	48-64
33845576-1	2021	Heme oxygenase-1 (HO-1) is a vital enzyme in humans that primarily regulates free heme concentrations.	Heme	82-86	heme oxygenase 1	Homo sapiens	0-16
33845576-1	2021	Heme oxygenase-1 (HO-1) is a vital enzyme in humans that primarily regulates free heme concentrations.	Heme	82-86	heme oxygenase 1	Homo sapiens	18-22
33845576-4	2021	Reported here are the design, synthesis, and photophysical and biological characterization of a coumarin-porphyrin FRET break-apart probe to detect HO-1 activity, Fe-L1.	coumarin	96-104	heme oxygenase 1	Homo sapiens	148-152
33845576-5	2021	We designed Fe-L1 to "break-apart" upon HO-1-catalyzed porphyrin degradation, perturbing the efficient FRET mechanism from a coumarin donor to a porphyrin acceptor fluorophore.	Porphyrins	55-64	heme oxygenase 1	Homo sapiens	40-44
33845576-5	2021	We designed Fe-L1 to "break-apart" upon HO-1-catalyzed porphyrin degradation, perturbing the efficient FRET mechanism from a coumarin donor to a porphyrin acceptor fluorophore.	coumarin	125-133	heme oxygenase 1	Homo sapiens	40-44
33845576-5	2021	We designed Fe-L1 to "break-apart" upon HO-1-catalyzed porphyrin degradation, perturbing the efficient FRET mechanism from a coumarin donor to a porphyrin acceptor fluorophore.	Porphyrins	145-154	heme oxygenase 1	Homo sapiens	40-44
33845576-6	2021	Analysis of HO-1 activity using Escherichia coli lysates overexpressing hHO-1 found that a 6-fold increase in emission intensity at 383 nm was observed following incubation with NADPH.	NADP	178-183	heme oxygenase 1	Homo sapiens	12-16
33845576-6	2021	Analysis of HO-1 activity using Escherichia coli lysates overexpressing hHO-1 found that a 6-fold increase in emission intensity at 383 nm was observed following incubation with NADPH.	NADP	178-183	heme oxygenase 1	Homo sapiens	72-77
33845576-8	2021	Finally, through the analysis of Fe-L2, we have shown that close structural analogues of heme are required to maintain HO-1 activity.	Heme	89-93	heme oxygenase 1	Homo sapiens	119-123
34017261-0	2021	Xanthohumol Attenuated Inflammation and ECM Degradation by Mediating HO-1/C/EBPbeta Pathway in Osteoarthritis Chondrocytes.	xanthohumol	0-11	heme oxygenase 1	Homo sapiens	69-73
34017261-10	2021	HO-1 knockdown could abrogate the protective effects of XH in IL-1beta-treated chondrocytes.	xanthohumol	56-58	heme oxygenase 1	Homo sapiens	0-4
33388910-1	2021	Heme oxygenase (HO)-1 is a rate-limiting enzyme for degrading heme into carbon monoxide.	Heme	62-66	heme oxygenase 1	Homo sapiens	0-21
33388910-1	2021	Heme oxygenase (HO)-1 is a rate-limiting enzyme for degrading heme into carbon monoxide.	Carbon Monoxide	72-87	heme oxygenase 1	Homo sapiens	0-21
33617922-0	2021	Dihydroactinidiolide regulates Nrf2/HO-1 expression and inhibits caspase-3/Bax pathway to protect SH-SY5Y human neuroblastoma cells from oxidative stress induced neuronal apoptosis.	dihydroactinidiolide	0-20	heme oxygenase 1	Homo sapiens	36-40
33617922-6	2021	Western blotting and RT-PCR revealed that DHAc significantly increased anti-apoptotic Bcl-2 expression and mRNA levels of Nrf2 and HO-1.	dihydroactinidiolide	42-46	heme oxygenase 1	Homo sapiens	131-135
33980059-0	2021	Curcumin Can Activate the Nrf2/HO-1 Signaling Pathway and Scavenge Free Radicals in Spinal Cord Injury Treatment.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	31-35
33980059-6	2021	In this review, we analyze the role of curcumin in activating Nrf2/HO-1 and scavenging free radicals to repair SCI.	Curcumin	39-47	heme oxygenase 1	Homo sapiens	67-71
33977953-6	2021	In oleic acid (OA)-induced HepG2 cells, hesperetin upregulated antioxidant levels (SOD/GPx/GR/GCLC/HO-1) by triggering the PI3 K/AKT-Nrf2 pathway, alleviating OA-induced reactive oxygen species (ROS) overproduction and hepatotoxicity.	hesperetin	40-50	heme oxygenase 1	Homo sapiens	99-103
33955073-4	2021	These recent studies have demonstrated that carotenoids also provide photoprotection against UVA-induced pigmentation and inhibit molecular markers of oxidative stress such as intercellular adhesion molecule-1, heme-oxygenase-1, matrix metalloproteinase-1, 9, and others.	Carotenoids	44-55	heme oxygenase 1	Homo sapiens	211-227
34055200-0	2021	Corrigendum to "Myricetin Possesses Potential Protective Effects on Diabetic Cardiomyopathy through Inhibiting IkappaBalpha/NFkappaB and Enhancing Nrf2/HO-1".	myricetin	16-25	heme oxygenase 1	Homo sapiens	152-156
32893669-0	2021	Cpt1a promoted ROS-induced oxidative stress and inflammation in liver injury via the Nrf2/HO-1 and NLRP3 inflammasome signaling pathway.	Reactive Oxygen Species	15-18	heme oxygenase 1	Homo sapiens	90-94
33903766-2	2021	Here we show that a distinct subset of TAMs (F4/80hiCD115hiC3aRhiCD88hi), endowed with high rates of heme catabolism by the stress-responsive enzyme heme oxygenase-1 (HO-1), plays a critical role in shaping a prometastatic tumor microenvironment favoring immunosuppression, angiogenesis and epithelial-to-mesenchymal transition.	Heme	101-105	heme oxygenase 1	Homo sapiens	167-171
33744612-12	2021	Baicalin relieved the above changes caused by DHAV-1 and activated the gene and protein expressions of Nrf2, which activated ARE-dependent genes including heme oxygenase-1 (HO-1), nicotinamide adenine dinucleotide phosphate quinone oxidoreductase 1 (NQO1), SOD-1, and GPX-1.	baicalin	0-8	heme oxygenase 1	Homo sapiens	155-171
33744612-12	2021	Baicalin relieved the above changes caused by DHAV-1 and activated the gene and protein expressions of Nrf2, which activated ARE-dependent genes including heme oxygenase-1 (HO-1), nicotinamide adenine dinucleotide phosphate quinone oxidoreductase 1 (NQO1), SOD-1, and GPX-1.	baicalin	0-8	heme oxygenase 1	Homo sapiens	173-177
33986683-8	2021	Furthermore, the inhibitor of the enzyme heme oxygenase-1 but not that of nitric oxide synthase reduced GUO-induced neurite outgrowth.	Guanosine	104-107	heme oxygenase 1	Homo sapiens	41-57
33975215-0	2021	Associations between blood heavy metal(loid)s and serum heme oxygenase-1 in pregnant women: Do their distribution patterns matter?	Metals	33-38	heme oxygenase 1	Homo sapiens	56-72
33981228-7	2021	Meanwhile, galangin increased ROS accumulation, and reduced Nrf2 and NQO-1, but elevated HO-1 in MGC 803 cells.	galangin	11-19	heme oxygenase 1	Homo sapiens	89-93
33902245-7	2021	Additionally, the concentration of PAHs was negatively correlated with the level of HO-1 (r=-0.358, P=0.017).	Polycyclic Aromatic Hydrocarbons	35-39	heme oxygenase 1	Homo sapiens	84-88
33902245-8	2021	Linear regression analysis showed that the concentration of HO-1 decreased by 1.737 mug/L when the concentration of PAHs increased by 1 mg/L (P=0.035).	Polycyclic Aromatic Hydrocarbons	116-120	heme oxygenase 1	Homo sapiens	60-64
33922144-5	2021	Here, we investigated the protective effects of THF on neurotoxicity induced by METH exposure by enhancing the Nrf2/HO-1 and PI3K/Akt/mTOR signaling pathways in SH-SY5y cells.	Methamphetamine	80-84	heme oxygenase 1	Homo sapiens	116-120
33922144-7	2021	Moreover, we found THF induced Nrf2 nuclear translocation and HO-1 expression.	tetrahydrofuran	19-22	heme oxygenase 1	Homo sapiens	62-66
33922144-5	2021	Here, we investigated the protective effects of THF on neurotoxicity induced by METH exposure by enhancing the Nrf2/HO-1 and PI3K/Akt/mTOR signaling pathways in SH-SY5y cells.	tetrahydrofuran	48-51	heme oxygenase 1	Homo sapiens	116-120
33922144-8	2021	An inhibitor assay confirmed that the induction of HO-1 by THF attenuates METH-induced neurotoxicity.	tetrahydrofuran	59-62	heme oxygenase 1	Homo sapiens	51-55
33922144-8	2021	An inhibitor assay confirmed that the induction of HO-1 by THF attenuates METH-induced neurotoxicity.	Methamphetamine	74-78	heme oxygenase 1	Homo sapiens	51-55
33922144-9	2021	Therefore, we suggest that THF preserves neuronal cells from METH-induced neurotoxicity by upregulating HO-1 expression through the Nrf2 and PI3K/Akt/mTOR signaling pathways.	tetrahydrofuran	27-30	heme oxygenase 1	Homo sapiens	104-108
33919311-4	2021	The results of voxel-based multiple regression analysis showed that blood levels of CypA, HO-1, and IRE1 were correlated with GMV on brain magnetic resonance imaging (MRI) in the entire population (p = 0.0005).	Guanosine-5'-Phosphovanadate	126-129	heme oxygenase 1	Homo sapiens	90-94
33919311-7	2021	HO-1 values increased with increasing GMV at the uncus (r = 0.307, p = 0.0008), lateral globus pallidus and putamen (r = 0.287, p = 0.002), and hippocampus (r = 0.197, p = 0.034).	Guanosine-5'-Phosphovanadate	38-41	heme oxygenase 1	Homo sapiens	0-4
33924157-0	2021	(E)-Guggulsterone Inhibits Dengue Virus Replication by Upregulating Antiviral Interferon Responses through the Induction of Heme Oxygenase-1 Expression.	pregna-4,17-diene-3,16-dione	0-17	heme oxygenase 1	Homo sapiens	124-140
33923922-8	2021	These were effectively antagonized with MGN (20 muM), which led to HUVECs being protected against DOX-induced apoptosis, partly through the PI3K/AKT-mediated NRF2/HO-1 signaling pathway, which could theoretically protect the vessels from severe DOX toxicity.	Doxorubicin	98-101	heme oxygenase 1	Homo sapiens	163-167
33924157-9	2021	The mechanistic studied revealed that (E)-guggulsterone stimulates Nrf2-mediated heme oxygenase-1 (HO-1) expression, which increases the antiviral interferon responses and downstream antiviral gene expression by blocking DENV NS2B/3B protease activity.	pregna-4,17-diene-3,16-dione	38-55	heme oxygenase 1	Homo sapiens	81-97
33924157-9	2021	The mechanistic studied revealed that (E)-guggulsterone stimulates Nrf2-mediated heme oxygenase-1 (HO-1) expression, which increases the antiviral interferon responses and downstream antiviral gene expression by blocking DENV NS2B/3B protease activity.	pregna-4,17-diene-3,16-dione	38-55	heme oxygenase 1	Homo sapiens	99-103
33994055-9	2021	CONCLUSION: These results indicate that AU can reduce inflammation and oxidative stress through the NF-kappaB, Nrf2/HO-1, and MAPK pathways.	aucubin	40-42	heme oxygenase 1	Homo sapiens	116-120
33875681-3	2021	Here, we observed that curcumin induced the expression of genes downstream of Nrf2 such as HO-1, NQO1, and GST-mu1 in neuronal cells, and increased the level of Nrf2 protein.	Curcumin	23-31	heme oxygenase 1	Homo sapiens	91-95
33854358-0	2021	Natural Dietary Supplement, Carvacrol, Alleviates LPS-Induced Oxidative Stress, Neurodegeneration, and Depressive-Like Behaviors via the Nrf2/HO-1 Pathway.	carvacrol	28-37	heme oxygenase 1	Homo sapiens	142-146
33923585-0	2021	Preventive Effects against Retinal Degeneration by Centella asiatica Extract (CA-HE50) and Asiaticoside through Apoptosis Suppression by the Nrf2/HO-1 Signaling Pathway.	ca-he50	78-85	heme oxygenase 1	Homo sapiens	146-150
33923585-0	2021	Preventive Effects against Retinal Degeneration by Centella asiatica Extract (CA-HE50) and Asiaticoside through Apoptosis Suppression by the Nrf2/HO-1 Signaling Pathway.	asiaticoside	91-103	heme oxygenase 1	Homo sapiens	146-150
33920891-0	2021	Heme-Mediated Activation of the Nrf2/HO-1 Axis Attenuates Calcification of Valve Interstitial Cells.	Heme	0-4	heme oxygenase 1	Homo sapiens	37-41
33920891-7	2021	Heme induced Nrf2 and HO-1 expression in VICs.	Heme	0-4	heme oxygenase 1	Homo sapiens	22-26
33920891-8	2021	Heme lost its anti-calcification potential when we blocked transcriptional activity Nrf2 or enzyme activity of HO-1.	Heme	0-4	heme oxygenase 1	Homo sapiens	111-115
33920891-10	2021	This study suggests that heme-mediated activation of the Nrf2/HO-1 pathway inhibits the calcification of VICs.	Heme	25-29	heme oxygenase 1	Homo sapiens	62-66
33678013-14	2022	The GI safety of ATB-352 could be due to the involvement of heme oxygenase-1 and SOCS3 pathways activation.	atb-352	17-24	heme oxygenase 1	Homo sapiens	60-76
33927798-7	2021	Additionally, in clinical patients who received laparoscopic gynecological surgery, pretreatment with hydromorphone resulted in lower serum levels of club cell secretory protein-16 (CC-16) and intercellular adhesion molecule-1 (ICAM-1), a lower prooxidant-antioxidant balance (PAB), and higher heme oxygenase-1 (HO-1) activity than morphine pretreatment.	Hydromorphone	102-115	heme oxygenase 1	Homo sapiens	294-310
33927798-7	2021	Additionally, in clinical patients who received laparoscopic gynecological surgery, pretreatment with hydromorphone resulted in lower serum levels of club cell secretory protein-16 (CC-16) and intercellular adhesion molecule-1 (ICAM-1), a lower prooxidant-antioxidant balance (PAB), and higher heme oxygenase-1 (HO-1) activity than morphine pretreatment.	Hydromorphone	102-115	heme oxygenase 1	Homo sapiens	312-316
33927798-8	2021	Collectively, our results suggest that hydromorphone protects against CO2 pneumoperitoneum-induced lung injury via HO-1-regulated mitochondrial dynamics and may be a promising strategy to treat CO2 pneumoperitoneum-induced lung injury.	Hydromorphone	39-52	heme oxygenase 1	Homo sapiens	115-119
33927798-8	2021	Collectively, our results suggest that hydromorphone protects against CO2 pneumoperitoneum-induced lung injury via HO-1-regulated mitochondrial dynamics and may be a promising strategy to treat CO2 pneumoperitoneum-induced lung injury.	Carbon Dioxide	194-197	heme oxygenase 1	Homo sapiens	115-119
33923744-3	2021	The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body"s antioxidant response to oxidative stress.	Heme	325-329	heme oxygenase 1	Homo sapiens	20-24
33923744-3	2021	The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body"s antioxidant response to oxidative stress.	Carbon Monoxide	371-386	heme oxygenase 1	Homo sapiens	20-24
33923744-3	2021	The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body"s antioxidant response to oxidative stress.	Carbon Monoxide	388-390	heme oxygenase 1	Homo sapiens	20-24
33923744-3	2021	The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body"s antioxidant response to oxidative stress.	Glutathione	433-436	heme oxygenase 1	Homo sapiens	20-24
33860917-7	2021	Furthermore, activation of Nrf-2/HO-1 signaling and upregulation of HSP-70 governs the protection elicited by daphnetin against oxidative stress-induced neuronal apoptosis.	daphnetin	110-119	heme oxygenase 1	Homo sapiens	33-37
33863580-8	2021	In endometriosis, total iron showed a positive correlation with HO-1 (r, 0.518, p = 0.001), but there were no antioxidants that correlated with iron in non-endometriosis.	Iron	24-28	heme oxygenase 1	Homo sapiens	64-68
33863580-10	2021	CONCLUSIONS: HO-1 may regulate the delicate balance of iron-induced oxidative stress in endometriotic cyst fluid.	Iron	55-59	heme oxygenase 1	Homo sapiens	13-17
33854363-8	2021	In further analysis, we found that hub bridge genes HLA-A, HMOX1, and JUN related to endocytosis, cell adhesion, and phagosomes may exert their effects through the dopamine (DA) system and the serotonergic pathway post-ICH depression.	Dopamine	164-172	heme oxygenase 1	Homo sapiens	59-64
33917842-12	2021	EGCG increased antioxidant levels (HO-1) at week-4 (p < 0.01) plus elastin at week-8 (p < 0.01).	epigallocatechin gallate	0-4	heme oxygenase 1	Homo sapiens	35-39
33854363-8	2021	In further analysis, we found that hub bridge genes HLA-A, HMOX1, and JUN related to endocytosis, cell adhesion, and phagosomes may exert their effects through the dopamine (DA) system and the serotonergic pathway post-ICH depression.	Dopamine	174-176	heme oxygenase 1	Homo sapiens	59-64
33754715-1	2021	Human heme oxygenase (hHO-1) is a physiologically important enzyme responsible for free heme catabolism.	Heme	6-10	heme oxygenase 1	Homo sapiens	22-27
33754715-9	2021	These studies suggest that the FeCN fragment in hHO-1 is tilted more strongly toward the porphyrin macrocycle compared to other histidine-ligated proteins, reflecting the propensity of the exogenous hHO-l ligands to position toward the alpha-meso-carbon, which is crucial for the HO reactivity and essential for regioselectivity.	Histidine	128-137	heme oxygenase 1	Homo sapiens	48-53
33754715-9	2021	These studies suggest that the FeCN fragment in hHO-1 is tilted more strongly toward the porphyrin macrocycle compared to other histidine-ligated proteins, reflecting the propensity of the exogenous hHO-l ligands to position toward the alpha-meso-carbon, which is crucial for the HO reactivity and essential for regioselectivity.	alpha-meso-carbon	236-253	heme oxygenase 1	Homo sapiens	48-53
33831425-0	2021	Cephalosporin antibiotics specifically and selectively target nasopharyngeal carcinoma through HMOX1-induced ferroptosis.	Cephalosporins	0-13	heme oxygenase 1	Homo sapiens	95-100
33831425-8	2021	Mechanistic assessment of HMOX1 in cefotaxime-mediated ferroptosis was tested with Protoporphyrin IX zinc.	Cefotaxime	35-45	heme oxygenase 1	Homo sapiens	26-31
33831425-8	2021	Mechanistic assessment of HMOX1 in cefotaxime-mediated ferroptosis was tested with Protoporphyrin IX zinc.	protoporphyrin IX	83-100	heme oxygenase 1	Homo sapiens	26-31
33831425-13	2021	Inhibition of HMOX1 significantly reduced the anticancer efficacy of cefotaxime in CNE2 cells.	Cefotaxime	69-79	heme oxygenase 1	Homo sapiens	14-19
33831425-15	2021	We mechanistically show that induction of ferroptosis through HMOX1 induction mediates cefotaxime anticancer activity.	Cefotaxime	87-97	heme oxygenase 1	Homo sapiens	62-67
33393728-5	2021	In addition, mangiferin attenuated the enhancement of p-JNK, reductions of Nrf2 and HO-1, and increased level of the mitochondrial fission proteins Drp1 caused by fluoride.	mangiferin	13-23	heme oxygenase 1	Homo sapiens	84-88
33898397-8	2021	The mechanism experiments showed that the antitumor activity of ORI-NPs against breast cancer might be through ROS related Nrf2/HO-1 signaling pathway.	ros	111-114	heme oxygenase 1	Homo sapiens	128-132
33898501-1	2021	Fubaiju Hot-Water Extracts Against ARPE-19 Cell Oxidative Damage by Activating PI3K/Akt-Mediated Nrf2/HO-1 Signaling Pathway.	fubaiju	0-7	heme oxygenase 1	Homo sapiens	102-106
33898501-1	2021	Fubaiju Hot-Water Extracts Against ARPE-19 Cell Oxidative Damage by Activating PI3K/Akt-Mediated Nrf2/HO-1 Signaling Pathway.	Water	12-17	heme oxygenase 1	Homo sapiens	102-106
33898501-8	2021	Meanwhile, CM treatment upregulated Akt phosphorylation, nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation, and the expression level of antioxidant gene heme oxygenase-1 (HO-1) in a dose-dependent manner under oxidative stress.	Curium	11-13	heme oxygenase 1	Homo sapiens	194-198
33453607-14	2021	HMOX1 knockdown attenuated EF24-induced cytotoxicity and attenuated EF24-induced inhibition of Glutathione Peroxidase 4 (GPX4) expression.	EF24	27-31	heme oxygenase 1	Homo sapiens	0-5
33453607-14	2021	HMOX1 knockdown attenuated EF24-induced cytotoxicity and attenuated EF24-induced inhibition of Glutathione Peroxidase 4 (GPX4) expression.	EF24	68-72	heme oxygenase 1	Homo sapiens	0-5
33453607-15	2021	CONCLUSION: Our results showed that EF24 upregulated HMOX1 to suppress GPX4 expression to induce ferroptosis by increasing MDA level, ROS level and intracellular ferric ion level.	Reactive Oxygen Species	134-137	heme oxygenase 1	Homo sapiens	53-58
33453607-16	2021	Thus, EF24 might serve as a potential agent for the treatment of HMOX1-positive osteosarcoma patients.	EF24	6-10	heme oxygenase 1	Homo sapiens	65-70
33270331-9	2021	Notably, the expression of antioxidant genes, such as HO-1, and the nuclear translocation of Nrf2 were further enhanced by F-FEJS in UVB/H2 O2 -treated cells.	Hydrogen Peroxide	137-142	heme oxygenase 1	Homo sapiens	54-58
33898501-10	2021	Correspondingly, the protective effect of CM was dramatically blocked after interference with phosphatidylinositol 3-kinase (PI3K)/Akt inhibitor LY294002, indicating that the protective effect of CM on cell oxidative damage was attributed to PI3K/Akt-mediated Nrf2/HO-1 signaling pathway.	Curium	42-44	heme oxygenase 1	Homo sapiens	265-269
33898501-10	2021	Correspondingly, the protective effect of CM was dramatically blocked after interference with phosphatidylinositol 3-kinase (PI3K)/Akt inhibitor LY294002, indicating that the protective effect of CM on cell oxidative damage was attributed to PI3K/Akt-mediated Nrf2/HO-1 signaling pathway.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	145-153	heme oxygenase 1	Homo sapiens	265-269
33898501-10	2021	Correspondingly, the protective effect of CM was dramatically blocked after interference with phosphatidylinositol 3-kinase (PI3K)/Akt inhibitor LY294002, indicating that the protective effect of CM on cell oxidative damage was attributed to PI3K/Akt-mediated Nrf2/HO-1 signaling pathway.	Curium	196-198	heme oxygenase 1	Homo sapiens	265-269
33987332-9	2021	Conclusions: Our work suggests that the Nrf2/HO-1 molecular pathway may play a crucial role in treating ICH patients with PGE1 and may represent novel molecular targets, resulting in discovering new drugs for ICH treatment.	Alprostadil	122-126	heme oxygenase 1	Homo sapiens	45-49
33636332-7	2021	Taken all together, we demonstrate that plasma treated water-derived oxidants sensitize pancreatic cancer cells to ferroptotic cell death by targeting a NRF2-HMOX1-GPX4 specific kinase signaling network.	Water	55-60	heme oxygenase 1	Homo sapiens	158-163
33393728-7	2021	In conclusion, protection by mangiferin against fluoride-induced neurotoxicity involves normalizing the impaired mitochondrial apoptotic pathway and dynamics and reducing oxidative stress via inactivation of the JNK and activation of the Nrf2/HO-1 pathways.	mangiferin	29-39	heme oxygenase 1	Homo sapiens	243-247
33393728-7	2021	In conclusion, protection by mangiferin against fluoride-induced neurotoxicity involves normalizing the impaired mitochondrial apoptotic pathway and dynamics and reducing oxidative stress via inactivation of the JNK and activation of the Nrf2/HO-1 pathways.	Fluorides	48-56	heme oxygenase 1	Homo sapiens	243-247
33537805-2	2021	HO-1 can be induced by a variety of stimuli, including heavy metals, heat shock, inflammatory stimuli, heme and its derivatives, stress, hypoxia, and biological hormones.	Heme	103-107	heme oxygenase 1	Homo sapiens	0-4
33448057-8	2021	CsA-induced oxidative stress, HO-1, TGF-beta1, and type II EMT were also rescued by antioxidants treatment.	Cyclosporine	0-3	heme oxygenase 1	Homo sapiens	30-34
33537805-3	2021	HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron.	Heme	36-40	heme oxygenase 1	Homo sapiens	0-4
33537805-3	2021	HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron.	Heme	66-70	heme oxygenase 1	Homo sapiens	0-4
33537805-3	2021	HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron.	Biliverdine	76-86	heme oxygenase 1	Homo sapiens	0-4
33537805-3	2021	HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	0-4
33537805-3	2021	HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron.	Carbon Monoxide	105-107	heme oxygenase 1	Homo sapiens	0-4
33537805-3	2021	HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron.	Iron	113-117	heme oxygenase 1	Homo sapiens	0-4
33537805-7	2021	In particular, this review focuses on the role of carbon monoxide (CO), one of the primary metabolites of HO-1, in flap survival and discusses the feasibility and existing challenges of HO-1 in flap surgery.	Carbon Monoxide	50-65	heme oxygenase 1	Homo sapiens	106-110
33537805-7	2021	In particular, this review focuses on the role of carbon monoxide (CO), one of the primary metabolites of HO-1, in flap survival and discusses the feasibility and existing challenges of HO-1 in flap surgery.	Carbon Monoxide	67-69	heme oxygenase 1	Homo sapiens	106-110
33513620-4	2021	To understand the underlying mechanism, we investigated the effect of low-dose TSA on HO-1, SOD and CAT induction and activating Akt together with its downstream Nrf2 signaling pathway.	trichostatin A	79-82	heme oxygenase 1	Homo sapiens	86-90
32930996-10	2021	Inhibition of heme oxygenase-1 (HO-1) also blocked the EM-induced mitochondrial protection.	Emodin	55-57	heme oxygenase 1	Homo sapiens	14-30
32930996-10	2021	Inhibition of heme oxygenase-1 (HO-1) also blocked the EM-induced mitochondrial protection.	Emodin	55-57	heme oxygenase 1	Homo sapiens	32-36
32930996-11	2021	Therefore, EM protected the mitochondria by a mechanism dependent on the AMPK/Nrf2/HO-1 signaling pathway in MG-challenged SH-SY5Y cells.	Pyruvaldehyde	109-111	heme oxygenase 1	Homo sapiens	83-87
33915898-8	2021	Intriguingly, MiR-100 antagomir treatment exerted a cytoprotective effect against the H2O2-induced oxidative cell death through attenuating the oxidation-induced AMPK hyperphosphorylation, restoring cellular mTOR and p62/SQSTM1 levels and upregulating heme oxygenase-1 expression.	Hydrogen Peroxide	86-90	heme oxygenase 1	Homo sapiens	252-268
33646477-0	2021	East to West not North-West: Structure-Based Mechanistic Resolution of 8-Hydroxyl Replacement and Resulting Effects on the Activities of Imidazole-Based Heme Oxygenase-1 Inhibitors.	imidazole	137-146	heme oxygenase 1	Homo sapiens	153-169
33646477-3	2021	In a recent study, two selective azole-based HO-1 inhibitors (Cpd1 and Cpd2) were synthesized, which exhibited differential inhibitory potencies of ~200mum.	Azoles	33-38	heme oxygenase 1	Homo sapiens	45-49
33646477-6	2021	Findings revealed favorable binding for the bromobenzene and imidazole substituents of Cpd1 at the western and eastern regions of the HO-1 active domain.	bromobenzene	44-56	heme oxygenase 1	Homo sapiens	134-138
33646477-6	2021	Findings revealed favorable binding for the bromobenzene and imidazole substituents of Cpd1 at the western and eastern regions of the HO-1 active domain.	imidazole	61-70	heme oxygenase 1	Homo sapiens	134-138
33513620-7	2021	Therefore, our results suggest that low-dose TSA can activate the Akt/Nrf2 pathway and upregulate expression of HO-1, SOD and CAT to stimulate the cellular defense mechanism.	trichostatin A	45-48	heme oxygenase 1	Homo sapiens	112-116
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	Heme	73-77	heme oxygenase 1	Homo sapiens	91-95
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	Biliverdine	131-141	heme oxygenase 1	Homo sapiens	73-89
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	Biliverdine	131-141	heme oxygenase 1	Homo sapiens	91-95
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	ammonium ferrous sulfate	143-154	heme oxygenase 1	Homo sapiens	73-89
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	ammonium ferrous sulfate	143-154	heme oxygenase 1	Homo sapiens	91-95
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	Carbon Monoxide	159-174	heme oxygenase 1	Homo sapiens	73-89
33787980-3	2021	In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide.	Carbon Monoxide	159-174	heme oxygenase 1	Homo sapiens	91-95
33787980-8	2021	We critically discuss the issue of metalloporphyrins, commonly used pharmacological modulators of HO-1 activity, and raise the issue of their important HO-1-independent activities.	Metalloporphyrins	35-52	heme oxygenase 1	Homo sapiens	98-102
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Heme	126-130	heme oxygenase 1	Homo sapiens	0-16
33781184-0	2021	Micro Composite Palmitoylethanolamide/Rutin Reduces Vascular Injury through Modulation of the Nrf2/HO-1 and NF-kB Pathways.	palmidrol	16-37	heme oxygenase 1	Homo sapiens	99-103
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Heme	126-130	heme oxygenase 1	Homo sapiens	18-22
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Carbon Monoxide	184-199	heme oxygenase 1	Homo sapiens	0-16
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Carbon Monoxide	184-199	heme oxygenase 1	Homo sapiens	18-22
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Carbon Monoxide	201-203	heme oxygenase 1	Homo sapiens	0-16
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Carbon Monoxide	201-203	heme oxygenase 1	Homo sapiens	18-22
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Biliverdine	206-216	heme oxygenase 1	Homo sapiens	0-16
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	Biliverdine	206-216	heme oxygenase 1	Homo sapiens	18-22
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	ferrous iron	221-233	heme oxygenase 1	Homo sapiens	0-16
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	ferrous iron	221-233	heme oxygenase 1	Homo sapiens	18-22
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	ammonium ferrous sulfate	235-239	heme oxygenase 1	Homo sapiens	0-16
33868304-1	2021	Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+).	ammonium ferrous sulfate	235-239	heme oxygenase 1	Homo sapiens	18-22
33868304-4	2021	Intrinsically to the cell, HO-1 activity provides antioxidant, anti-apoptotic and cytoprotective effects via its catabolites as well as clearing toxic intracellular heme.	Heme	165-169	heme oxygenase 1	Homo sapiens	27-31
33781184-0	2021	Micro Composite Palmitoylethanolamide/Rutin Reduces Vascular Injury through Modulation of the Nrf2/HO-1 and NF-kB Pathways.	Rutin	38-43	heme oxygenase 1	Homo sapiens	99-103
33625409-12	2021	d-pinitol not only significantly activated the Nrf2/ARE signaling pathway via facilitating the translocation of Nrf2 from sitoplazma to cytoblast, upregulating the protein expression levels of GCLC, GCLM, HO-1, and NQO1, but also improved the PPAR-gamma level by binding to the active site of PPAR-gamma, when suppressing NF-kappaB p65 and IkappaBalpha phosphorylation.	pinitol	0-9	heme oxygenase 1	Homo sapiens	205-209
33547170-11	2021	Inhibition of Asah2 increased p53 protein stability to upregulate Hmox1 expression to suppress lipid reactive oxygen species production to suppress ferroptosis in MDSCs.	lipid reactive oxygen species	95-124	heme oxygenase 1	Homo sapiens	66-71
33453713-0	2021	MiR-133a-3p relieves the oxidative stress induced trophoblast cell apoptosis through the BACH1/Nrf2/HO-1 signaling pathway.	mir-133a-3p	0-11	heme oxygenase 1	Homo sapiens	100-104
33453713-12	2021	It is collectively demonstrated that miR-133a-3p can relieve the oxidative stress-induced apoptosis in the trophoblast cells through the BACH1/Nrf2/HO-1 signaling pathway via targeting BACH1 directly.	mir-133a	37-45	heme oxygenase 1	Homo sapiens	148-152
33738869-8	2021	Heme oxygenase-1 (HO-1), a scavenger of ROS, was triggered by HIF-1 alpha.	Reactive Oxygen Species	40-43	heme oxygenase 1	Homo sapiens	0-16
33738869-8	2021	Heme oxygenase-1 (HO-1), a scavenger of ROS, was triggered by HIF-1 alpha.	Reactive Oxygen Species	40-43	heme oxygenase 1	Homo sapiens	18-22
33738869-9	2021	The effect of hydrogen peroxide was inhibited by HO-1 induction, whereas it was promoted by HO-1 knockdown.	Hydrogen Peroxide	14-31	heme oxygenase 1	Homo sapiens	49-53
33738869-10	2021	HO-1 inhibition by zinc protoporphyrin promoted the differentiation and increased ROS.	zinc protoporphyrin	19-38	heme oxygenase 1	Homo sapiens	0-4
33738869-10	2021	HO-1 inhibition by zinc protoporphyrin promoted the differentiation and increased ROS.	Reactive Oxygen Species	82-85	heme oxygenase 1	Homo sapiens	0-4
33738869-12	2021	Immature HL cells are inhibited from differentiation by a reduction of ROS through the induction of HO-1 via HIF-1alpha.	Reactive Oxygen Species	71-74	heme oxygenase 1	Homo sapiens	100-104
33733282-16	2021	CONCLUSIONS: A certain concentration range of CSPE can increase the expression of the downstream protein HO-1 and negatively regulate the production of ROS by upregulating the expression of Nrf2, thus protecting human retinal endothelial cells from oxidative damage caused by high glucose.	Glucose	281-288	heme oxygenase 1	Homo sapiens	105-109
33189376-7	2021	Likewise, serum Cu was positively associated with HO-1 (beta = 0.0004, P = 0.03) and negatively associated with MCP-1 (beta = -0.0006, P = 0.003) and IL-8 (beta = -0.002, P = 0.03).	Copper	16-18	heme oxygenase 1	Homo sapiens	50-54
33465425-8	2021	In addition, brusatol significantly suppressed the expression of Nrf2 and HO-1, and abrogated tBHQ-induced Nrf2 activation.	brusatol	13-21	heme oxygenase 1	Homo sapiens	74-78
33577831-0	2021	Ergothioneine alleviates senescence of fibroblasts induced by UVB damage of keratinocytes via activation of the Nrf2/HO-1 pathway and HSP70 in keratinocytes.	Ergothioneine	0-13	heme oxygenase 1	Homo sapiens	117-121
33566044-8	2021	Furthermore, the stimulating effects of PS-ALA on the PGC-1alpha/Nrf1/Tfam pathway and Nrf2/HO-1 pathway as well as its mitochondrial biogenesis promotion effects and anti-oxidative activities were abrogated by the AMPK inhibitor in OA-treated HepG2 cells.	ps-ala	40-46	heme oxygenase 1	Homo sapiens	92-96
33491566-3	2021	HIF1 pathway inhibitor digoxin blocked hypoxia-stimulated HIF1alpha activation and heme oxygenase (HMOX1) expression in HK2 cells.	Digoxin	23-30	heme oxygenase 1	Homo sapiens	99-104
33491566-4	2021	Hypoxia mimicking CoCl2 stimulated HMOX1 expression was significantly lower in Nrf2-/- RTECs than in WT counterparts.	cobaltous chloride	18-23	heme oxygenase 1	Homo sapiens	35-40
32782233-7	2021	Antioxidant response element (ARE)-reporter activity and expression of ARE-dependent genes NAD(P)H dehydrogenase [quinone] 1 (NQO1), heme oxygenase-1 (HO-1) were increased by resorcinol.	resorcinol	175-185	heme oxygenase 1	Homo sapiens	133-149
32782233-7	2021	Antioxidant response element (ARE)-reporter activity and expression of ARE-dependent genes NAD(P)H dehydrogenase [quinone] 1 (NQO1), heme oxygenase-1 (HO-1) were increased by resorcinol.	resorcinol	175-185	heme oxygenase 1	Homo sapiens	151-155
33245515-9	2021	RT-qPCR showed that GA significantly increased the mRNA levels of Heme oxygenase-1 (HO-1) and NADPH:quinone oxidoreductase1 (NQO1).	Gallium	20-22	heme oxygenase 1	Homo sapiens	66-82
33245515-9	2021	RT-qPCR showed that GA significantly increased the mRNA levels of Heme oxygenase-1 (HO-1) and NADPH:quinone oxidoreductase1 (NQO1).	Gallium	20-22	heme oxygenase 1	Homo sapiens	84-88
33571414-6	2021	Real-time qPCR quantification and Western blotting verified that the GA pretreatment elevates NAD(P)H quinone oxidoreductase-1 (NQO1) by more than 4.6-fold, heme oxygenase (HO-1) by about 1.2-fold, and the glutamate-cysteine ligase catalytic (GCLC) subunit by 0.7-fold.	ginnalin A	69-71	heme oxygenase 1	Homo sapiens	173-177
33678318-6	2021	RESULTS: In ectopic endometrial cells, caffeic acid caused a significant elevation in Nrf-2 gene expression level, NQO1, and HO-1 enzyme activities.	caffeic acid	39-51	heme oxygenase 1	Homo sapiens	125-129
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	294-299
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	Acetaldehyde	47-59	heme oxygenase 1	Homo sapiens	294-299
33058354-10	2021	Indeed, cynaropicrin increased the expression of several antioxidant genes, such as glutamate-cysteine ligase and heme oxygenase-1, by promoting the activation of the transcription factor Nrf-2.	cynaropicrin	8-20	heme oxygenase 1	Homo sapiens	114-130
33664571-0	2021	Copper Nanoparticles Induce Oxidative Stress via the Heme Oxygenase 1 Signaling Pathway in vitro Studies.	Copper	0-6	heme oxygenase 1	Homo sapiens	53-69
33647480-9	2021	Emodin treatment activated the Nuclear factorery throid 2-related factor 2/Kelch-like ECH-associated protein 1-antioxidatant response element (Nrf2/Keap1-ARE) pathway and upregulated the expression of heme oxygenase 1 (HO-1), superoxide dismutase (SOD), and catalase (CAT) in the hepatopancreas after CyHV-3 infection.	Emodin	0-6	heme oxygenase 1	Homo sapiens	201-217
33647480-9	2021	Emodin treatment activated the Nuclear factorery throid 2-related factor 2/Kelch-like ECH-associated protein 1-antioxidatant response element (Nrf2/Keap1-ARE) pathway and upregulated the expression of heme oxygenase 1 (HO-1), superoxide dismutase (SOD), and catalase (CAT) in the hepatopancreas after CyHV-3 infection.	Emodin	0-6	heme oxygenase 1	Homo sapiens	219-223
33671004-8	2021	In contrast, in ferroptosis, HO-1 may play a pro-death role via enhancing iron release.	Iron	74-78	heme oxygenase 1	Homo sapiens	29-33
33716792-6	2021	Heme oxygenase-1 (HO-1), a phase II detoxification enzyme responsible for heme catabolism, is induced by oxidative stress, among others.	Heme	74-78	heme oxygenase 1	Homo sapiens	0-16
33664571-6	2021	Subsequently, for oxidative stress parameter detection, the cells were pre-treated with hemin to induce HO-1 expression prior to CuNP treatment.	Hemin	88-93	heme oxygenase 1	Homo sapiens	104-108
33716792-6	2021	Heme oxygenase-1 (HO-1), a phase II detoxification enzyme responsible for heme catabolism, is induced by oxidative stress, among others.	Heme	74-78	heme oxygenase 1	Homo sapiens	18-22
33716792-8	2021	The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute.	Heme	23-27	heme oxygenase 1	Homo sapiens	208-212
33716792-8	2021	The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute.	Oxides	141-146	heme oxygenase 1	Homo sapiens	208-212
33716792-8	2021	The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute.	Carbon Monoxide	354-369	heme oxygenase 1	Homo sapiens	208-212
33716792-8	2021	The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute.	Biliverdine	371-381	heme oxygenase 1	Homo sapiens	208-212
33716792-8	2021	The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute.	Bilirubin	382-391	heme oxygenase 1	Homo sapiens	208-212
33716792-8	2021	The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute.	ammonium ferrous sulfate	397-401	heme oxygenase 1	Homo sapiens	208-212
33664571-8	2021	Furthermore, hemin pretreatment induced HO-1 expression in cells, which partially reduced the accumulation of reactive oxygen species induced by CuNPs and increased the levels of antioxidant enzymes.	Hemin	13-18	heme oxygenase 1	Homo sapiens	40-44
33664571-8	2021	Furthermore, hemin pretreatment induced HO-1 expression in cells, which partially reduced the accumulation of reactive oxygen species induced by CuNPs and increased the levels of antioxidant enzymes.	Oxygen	119-125	heme oxygenase 1	Homo sapiens	40-44
33664571-8	2021	Furthermore, hemin pretreatment induced HO-1 expression in cells, which partially reduced the accumulation of reactive oxygen species induced by CuNPs and increased the levels of antioxidant enzymes.	cunps	145-150	heme oxygenase 1	Homo sapiens	40-44
33579280-0	2021	AITC inhibits fibroblast-myofibroblast transition via TRPA1-independent MAPK and NRF2/HO-1 pathways and reverses corticosteroids insensitivity in human lung fibroblasts.	allyl isothiocyanate	0-4	heme oxygenase 1	Homo sapiens	86-90
33316526-0	2021	Activation of the ROS/HO-1/NQO1 signaling pathway contributes to the copper-induced oxidative stress and autophagy in duck renal tubular epithelial cells.	Reactive Oxygen Species	18-21	heme oxygenase 1	Homo sapiens	22-26
33316526-0	2021	Activation of the ROS/HO-1/NQO1 signaling pathway contributes to the copper-induced oxidative stress and autophagy in duck renal tubular epithelial cells.	Copper	69-75	heme oxygenase 1	Homo sapiens	22-26
33316526-1	2021	The aim of this study was to investigate the crosstalk between oxidative stress and autophagy through the ROS/HO-1/NQO1 pathway caused by copper (Cu).	Reactive Oxygen Species	106-109	heme oxygenase 1	Homo sapiens	110-114
33316526-1	2021	The aim of this study was to investigate the crosstalk between oxidative stress and autophagy through the ROS/HO-1/NQO1 pathway caused by copper (Cu).	Copper	138-144	heme oxygenase 1	Homo sapiens	110-114
33316526-1	2021	The aim of this study was to investigate the crosstalk between oxidative stress and autophagy through the ROS/HO-1/NQO1 pathway caused by copper (Cu).	Copper	146-148	heme oxygenase 1	Homo sapiens	110-114
33316526-5	2021	In summary, our findings indicated that excessive Cu could induce oxidative stress and autophagy by activating the ROS/HO-1/NQO1 pathway, and inhibition of HO-1 might attenuate Cu-induced oxidative stress and autophagy in duck renal tubular epithelial cells.	Copper	50-52	heme oxygenase 1	Homo sapiens	119-123
33316526-5	2021	In summary, our findings indicated that excessive Cu could induce oxidative stress and autophagy by activating the ROS/HO-1/NQO1 pathway, and inhibition of HO-1 might attenuate Cu-induced oxidative stress and autophagy in duck renal tubular epithelial cells.	Reactive Oxygen Species	115-118	heme oxygenase 1	Homo sapiens	119-123
33316526-5	2021	In summary, our findings indicated that excessive Cu could induce oxidative stress and autophagy by activating the ROS/HO-1/NQO1 pathway, and inhibition of HO-1 might attenuate Cu-induced oxidative stress and autophagy in duck renal tubular epithelial cells.	Copper	177-179	heme oxygenase 1	Homo sapiens	119-123
33316526-5	2021	In summary, our findings indicated that excessive Cu could induce oxidative stress and autophagy by activating the ROS/HO-1/NQO1 pathway, and inhibition of HO-1 might attenuate Cu-induced oxidative stress and autophagy in duck renal tubular epithelial cells.	Copper	177-179	heme oxygenase 1	Homo sapiens	156-160
33643023-2	2021	Biliverdin is derived from heme through a reaction mediated by HO-1 and protects cells from oxidative stress.	Biliverdine	0-10	heme oxygenase 1	Homo sapiens	63-67
33643023-2	2021	Biliverdin is derived from heme through a reaction mediated by HO-1 and protects cells from oxidative stress.	Heme	27-31	heme oxygenase 1	Homo sapiens	63-67
33643023-3	2021	However, iron and carbon monoxide produced by the catabolism of HO-1 exert detrimental effects on patients with PD.	Iron	9-13	heme oxygenase 1	Homo sapiens	64-68
33643023-3	2021	However, iron and carbon monoxide produced by the catabolism of HO-1 exert detrimental effects on patients with PD.	Carbon Monoxide	18-33	heme oxygenase 1	Homo sapiens	64-68
33669070-4	2021	Biochemical studies showed that Zn(II)-curc treatment increased the NRF2 protein levels along with its targets, heme oxygenase-1 (HO-1) and p62/SQSTM1, while markedly reduced the levels of Keap1 (Kelch-like ECH-associated protein 1), the NRF2 inhibitor, in the cancer cell lines analyzed.	zn(ii)	32-38	heme oxygenase 1	Homo sapiens	112-128
33669070-4	2021	Biochemical studies showed that Zn(II)-curc treatment increased the NRF2 protein levels along with its targets, heme oxygenase-1 (HO-1) and p62/SQSTM1, while markedly reduced the levels of Keap1 (Kelch-like ECH-associated protein 1), the NRF2 inhibitor, in the cancer cell lines analyzed.	zn(ii)	32-38	heme oxygenase 1	Homo sapiens	130-134
33668397-0	2021	Protective Effects of 6,7,4"-Trihydroxyflavanone on Hypoxia-Induced Neurotoxicity by Enhancement of HO-1 through Nrf2 Signaling Pathway.	6,7,4'-Trihydroxyflavanone	22-48	heme oxygenase 1	Homo sapiens	100-104
33668397-7	2021	We revealed that treatment with THF promotes HO-1 expression through Nrf2 nuclear translocation.	tetrahydrofuran	32-35	heme oxygenase 1	Homo sapiens	45-49
33668397-8	2021	An inhibitor assay using tin protoporphyrin IX (SnPP) confirmed that the enhancement of HO-1 by pre-treatment with THF protects SH-SY5y cells from CoCl2-induced neurotoxicity under hypoxic conditions.	tin protoporphyrin IX	25-46	heme oxygenase 1	Homo sapiens	88-92
33668397-8	2021	An inhibitor assay using tin protoporphyrin IX (SnPP) confirmed that the enhancement of HO-1 by pre-treatment with THF protects SH-SY5y cells from CoCl2-induced neurotoxicity under hypoxic conditions.	S-Nitroso-N-propionyl-D,L-penicillamine	48-52	heme oxygenase 1	Homo sapiens	88-92
33668397-8	2021	An inhibitor assay using tin protoporphyrin IX (SnPP) confirmed that the enhancement of HO-1 by pre-treatment with THF protects SH-SY5y cells from CoCl2-induced neurotoxicity under hypoxic conditions.	tetrahydrofuran	115-118	heme oxygenase 1	Homo sapiens	88-92
33668397-8	2021	An inhibitor assay using tin protoporphyrin IX (SnPP) confirmed that the enhancement of HO-1 by pre-treatment with THF protects SH-SY5y cells from CoCl2-induced neurotoxicity under hypoxic conditions.	cobaltous chloride	147-152	heme oxygenase 1	Homo sapiens	88-92
33668397-9	2021	Our results demonstrate the advantageous effects of THF against hypoxia-induced neurotoxicity through the HO-1/Nrf2 signaling pathway and provide a therapeutic insight for neurodegenerative disorders.	tetrahydrofuran	52-55	heme oxygenase 1	Homo sapiens	106-110
33579280-8	2021	AITC significantly increased phosphorylated- extracellular signal-regulated kinase (ERK) 1/2 and heme oxygenase (HO)-1 protein expressions (P < 0.05) in TGF-beta1-treated cells.	allyl isothiocyanate	0-4	heme oxygenase 1	Homo sapiens	97-118
33579280-12	2021	CONCLUSION: We found that AITC exerts protective effect on TGF-beta1-induced alpha-SMA induction by activating ERK1/2 MAPK and NRF2/HO-1 pathways in lung fibroblasts.	allyl isothiocyanate	26-30	heme oxygenase 1	Homo sapiens	132-136
33581965-9	2021	Results from qRT-PCR indicated that the suppression of Nrf2 and HO-1 following AGEs stimulation was reversed by Magnolol.	magnolol	112-120	heme oxygenase 1	Homo sapiens	64-68
33546257-7	2021	Two peptides and their combination treatment resulted in the increased heme oxygenase-1 (HO-1), a phase II detoxifying enzyme, through the activation of nuclear transcription factor-erythroid 2-related factor (Nrf2).	Peptides	4-12	heme oxygenase 1	Homo sapiens	89-93
33546433-6	2021	Differential array analysis revealed early modulation of stress response gene expression in both A375 melanoma and PANC-1 adenocarcinoma cells elicited by D2O (90%; <=6 h) (upregulated: CDKN1A, DDIT3, EGR1, GADD45A, HMOX1, NFKBIA, or SOD2 (up to 9-fold; p < 0.01)) confirmed by independent RT-qPCR analysis.	Deuterium Oxide	155-158	heme oxygenase 1	Homo sapiens	216-221
33546257-7	2021	Two peptides and their combination treatment resulted in the increased heme oxygenase-1 (HO-1), a phase II detoxifying enzyme, through the activation of nuclear transcription factor-erythroid 2-related factor (Nrf2).	Peptides	4-12	heme oxygenase 1	Homo sapiens	71-87
33569875-5	2021	Green tea catechins especially epigallocatechin gallate (EGCG) elucidated the protective role of Nrf2 and its downstream molecules in various disorders through Keap-1, HO-1, NQO-1, GPx, GCLc, GCLm, NF-kB cross-link, kinases, and apoptotic proteins.	Catechin	10-19	heme oxygenase 1	Homo sapiens	168-172
33569875-5	2021	Green tea catechins especially epigallocatechin gallate (EGCG) elucidated the protective role of Nrf2 and its downstream molecules in various disorders through Keap-1, HO-1, NQO-1, GPx, GCLc, GCLm, NF-kB cross-link, kinases, and apoptotic proteins.	epigallocatechin gallate	31-55	heme oxygenase 1	Homo sapiens	168-172
33569875-5	2021	Green tea catechins especially epigallocatechin gallate (EGCG) elucidated the protective role of Nrf2 and its downstream molecules in various disorders through Keap-1, HO-1, NQO-1, GPx, GCLc, GCLm, NF-kB cross-link, kinases, and apoptotic proteins.	epigallocatechin gallate	57-61	heme oxygenase 1	Homo sapiens	168-172
33547785-12	2022	Two thirds of intervention studies (50% dietary, such as using resistant starch) reported an increase of NRF2, NQO1, or HO-1.	Starch	73-79	heme oxygenase 1	Homo sapiens	120-124
33603823-5	2021	Mechanistic studies revealed that the protective effects of GFE were related to its activation of Nrf2 and HO-1 signaling in HaCaT cells.	1-(3,4-dichlorophenyl)-6,6-dimethyl-1,3,5-triazine-2,4-diamine	60-63	heme oxygenase 1	Homo sapiens	107-111
33347928-7	2021	Besides, polysaccharides show protective effects through certain signaling pathways including PI3K/Akt, MAPK, and NF-kappaB, PARP-1/AIF, JNK3/c-Jun/Fas-L, and Nrf2/HO-1 signaling pathways.	Polysaccharides	9-24	heme oxygenase 1	Homo sapiens	164-168
32372266-8	2021	Resveratrol directly upregulates antioxidative capacity by increasing antioxidant genes such as heme oxygenase-1, superoxide dismutase, catalase, and glutathione.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	96-112
33645502-13	2021	Introduction of high concentration of fisetin promoted the translocation of Nrf2 from the cytoplasm into the nucleus, increasing protein expression of its downstream elements, at least HO-1 in IR liver tissues and hepatocytes after HR.	fisetin	38-45	heme oxygenase 1	Homo sapiens	185-189
33645502-15	2021	CONCLUSION: Fisetin alleviates liver damage, cell apoptosis, and oxidative stress induced by liver IRI, at least through Nrf2/HO-1 signaling pathway, suggesting that fisetin could be considered as a targeted drug for liver IRI treatment.	fisetin	12-19	heme oxygenase 1	Homo sapiens	126-130
33645502-15	2021	CONCLUSION: Fisetin alleviates liver damage, cell apoptosis, and oxidative stress induced by liver IRI, at least through Nrf2/HO-1 signaling pathway, suggesting that fisetin could be considered as a targeted drug for liver IRI treatment.	fisetin	166-173	heme oxygenase 1	Homo sapiens	126-130
33023966-8	2021	This increase in HO-1 protein was recapitulated in human A375 melanoma cells exposed to fructose in culture.	Fructose	88-96	heme oxygenase 1	Homo sapiens	17-21
33287596-6	2021	Heme oxygenase-1 (HO-1) induction offers protection via inhibition of NADPH oxidase and promotion of cGMP generation.	Cyclic GMP	101-105	heme oxygenase 1	Homo sapiens	0-16
33287596-6	2021	Heme oxygenase-1 (HO-1) induction offers protection via inhibition of NADPH oxidase and promotion of cGMP generation.	Cyclic GMP	101-105	heme oxygenase 1	Homo sapiens	18-22
33310139-7	2021	Garcinone D (GarD) significantly upregulated AhR/Cyp1a1 and Nrf2/HO-1 protein expression and enhanced zonula occludens-1 and occludin protein levels in HT-29 cells.	garcinone	0-9	heme oxygenase 1	Homo sapiens	65-69
32964457-13	2021	The inhibitory effect on neuronal damage is achieved through the antioxidant (via inducing the Nrf2/HO-1 system) and anti-inflammatory effects (via promoting JNK/AP-1 signaling) of DHA.	Docosahexaenoic Acids	181-184	heme oxygenase 1	Homo sapiens	100-104
33355378-4	2021	However, whether 0.7% ISO affords protection against septic neuronal injury involving HO-1 activation is unclear.	iso	22-25	heme oxygenase 1	Homo sapiens	86-90
33176981-0	2021	Desaturation and heme elevation during COVID-19 infection: A potential prognostic factor of heme oxygenase-1.	Heme	17-21	heme oxygenase 1	Homo sapiens	92-108
33573363-5	2021	The obtained results showed that PPJE significantly inhibited reactive oxygen species release and increased the cellular antioxidant response, as indicated by the increased expression of cytoprotective enzymes, such as heme oxygenase-1 and NAD(P)H dehydrogenase [quinone] 1.	ppje	33-37	heme oxygenase 1	Homo sapiens	219-235
33514947-4	2021	In this Review, we present an introduction to HO-1 for immunologists, including an overview of its roles in iron metabolism and antioxidant defence, and the factors which regulate its expression.	Iron	108-112	heme oxygenase 1	Homo sapiens	46-50
33512783-12	2021	The cells and the wound tissues treated with BB showed highest Nrf2 activation and HO-1 expression than PVP-I and CHG. BB was highly efficient in wound infection control while delayed wound healing.	boeravinone B	45-47	heme oxygenase 1	Homo sapiens	83-87
33512783-12	2021	The cells and the wound tissues treated with BB showed highest Nrf2 activation and HO-1 expression than PVP-I and CHG. BB was highly efficient in wound infection control while delayed wound healing.	boeravinone B	119-121	heme oxygenase 1	Homo sapiens	83-87
33394027-9	2021	This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KmPOR HO-1 without affecting the Vmaxapp.	Bilirubin	118-127	heme oxygenase 1	Homo sapiens	36-40
33394027-9	2021	This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KmPOR HO-1 without affecting the Vmaxapp.	Bilirubin	118-127	heme oxygenase 1	Homo sapiens	104-108
33394027-9	2021	This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KmPOR HO-1 without affecting the Vmaxapp.	Bilirubin	118-127	heme oxygenase 1	Homo sapiens	104-108
33394027-10	2021	In like manner, HO-1 inhibited CYP1A1-mediated 7-ethoxyresorufin dealkylation by increasing the KmPOR CYP1A1.	ethoxyresorufin	47-64	heme oxygenase 1	Homo sapiens	16-20
33747471-0	2021	Intracellular ethanol-mediated oxidation and apoptosis in HepG2/CYP2E1 cells impaired by two active peptides from seahorse (Hippocampus kuda bleeler) protein hydrolysates via the Nrf2/HO-1 and akt pathways.	Ethanol	14-21	heme oxygenase 1	Homo sapiens	184-188
33246336-15	2021	MAIN RESULTS AND THE ROLE OF CHANCE: After 1-week grafting, the relative expression of Sod1, Hmox1 and Cat was significantly higher in the group receiving 150 mg/kg NAC (NAC150-treated group) compared to controls (P = 0.04, P = 0.03, and P = 0.01, respectively), whereas the expression levels of Tnf-alpha, Il1-beta and Il6 were reduced.	nac150	170-176	heme oxygenase 1	Homo sapiens	93-98
33502605-9	2021	Mechanically, aloin further enforced the activation of the NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling.	alloin	14-19	heme oxygenase 1	Homo sapiens	89-105
33502605-9	2021	Mechanically, aloin further enforced the activation of the NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling.	alloin	14-19	heme oxygenase 1	Homo sapiens	107-111
33585534-12	2020	LPP treatment improved cell survival rate, reduced intracellular LDH and MDA levels, increased intracellular SOD, CAT, GSH levels, down-regulated Bax, caspases-3, Nrf2, HO-1 expression, and up-regulated Bcl-2 expression.	Linalyl diphosphate	0-3	heme oxygenase 1	Homo sapiens	169-173
33584308-0	2020	Mitochondrial Iron Overload-Mediated Inhibition of Nrf2-HO-1/GPX4 Assisted ALI-Induced Nephrotoxicity.	Iron	14-18	heme oxygenase 1	Homo sapiens	56-60
33584308-0	2020	Mitochondrial Iron Overload-Mediated Inhibition of Nrf2-HO-1/GPX4 Assisted ALI-Induced Nephrotoxicity.	aristolactam I	75-78	heme oxygenase 1	Homo sapiens	56-60
33584308-11	2020	In conclusion, our results demonstrated that mitochondrial iron overload-mediated antioxidant system inhibition would assist ALI-induced ferroptosis in renal tubular epithelial cells, and Nrf2-HO-1/GPX4 antioxidative system could be an important intervention target to prevent medicine containing ALI-induced nephropathy.	aristolactam I	297-300	heme oxygenase 1	Homo sapiens	193-197
33472699-7	2021	In addition, TPP-Niacin markedly enhanced the expression of transcription factors (PGC-1alpha and NRF2) and antioxidant-associated genes (especially HO-1 and NQO-1).	tpp-niacin	13-23	heme oxygenase 1	Homo sapiens	149-153
33472699-9	2021	TPP-Niacin is believed to protect against mitochondrial dysfunction by upregulating antioxidant-related genes, such as PGC-1alpha, NRF2, HO-1, and NQO-1, in RPE cells.	tpp-niacin	0-10	heme oxygenase 1	Homo sapiens	137-141
33585534-0	2020	Protective Effect of Lemon Peel Polyphenols on Oxidative Stress-Induced Damage to Human Keratinocyte HaCaT Cells Through Activation of the Nrf2/HO-1 Signaling Pathway.	Polyphenols	32-43	heme oxygenase 1	Homo sapiens	144-148
33505436-8	2020	Moreover, Zn-protoporphyrin-IX, an inhibitor of heme oxygenase-1, reduced the protective effect of Nrf1 overexpression on OGD/R-induced TEC oxidative stress and pyroptosis.	zn-protoporphyrin-ix	10-30	heme oxygenase 1	Homo sapiens	48-64
33096358-10	2021	The present study further enriches and perfects the mechanism theory of HgCl2 toxicity and suggest that the CYP450 signaling and Nrf2/HO-1 pathway is important in shedding light on curcumin"s hepatoprotective effects in HgCl2 toxicity.	Curcumin	181-189	heme oxygenase 1	Homo sapiens	134-138
33254827-8	2021	Simultaneously, flow cytometry also showed that NaHS could prevent mic-PS-induced accumulation of reactive oxygen species (ROS) by increasing the expression of HO-1 and NQO1.	sodium bisulfide	48-52	heme oxygenase 1	Homo sapiens	160-164
33254827-8	2021	Simultaneously, flow cytometry also showed that NaHS could prevent mic-PS-induced accumulation of reactive oxygen species (ROS) by increasing the expression of HO-1 and NQO1.	Reactive Oxygen Species	123-126	heme oxygenase 1	Homo sapiens	160-164
33254827-9	2021	Furthermore, inhibition of HO-1 could reverse the hepatic protective effects of NaHS during mic-PS exposure.	sodium bisulfide	80-84	heme oxygenase 1	Homo sapiens	27-31
33254827-10	2021	Mechanistically, H2S elevating the HO-1 and NQO1 expression by facilitating nuclear accumulation of Nrf2, and consequently reducing mic-PS-induced hepatic apoptosis and inflammation.	Deuterium	17-20	heme oxygenase 1	Homo sapiens	35-39
33278384-5	2021	This study was mainly aimed to explore whether the rhythm gene "brain and muscle ARNT-like 1" (BMAL1) was involved in regulating oxidative stress-related NRF2/HO-1 pathway to reduce the formation of urinary calcium oxalate stones.	Calcium	207-214	heme oxygenase 1	Homo sapiens	159-163
33278384-6	2021	In vitro experiment found that the activation of NRF2/HO-1 can significantly reduce the oxalate-induced oxidative damage and urinary calcium oxalate stone formation, and the relative expression of BMAL1 was increased.	Oxalates	88-95	heme oxygenase 1	Homo sapiens	54-58
33278384-6	2021	In vitro experiment found that the activation of NRF2/HO-1 can significantly reduce the oxalate-induced oxidative damage and urinary calcium oxalate stone formation, and the relative expression of BMAL1 was increased.	Calcium	133-140	heme oxygenase 1	Homo sapiens	54-58
33278384-8	2021	In the hyperoxaluria animal model, the BMAL1 expression level decreased obviously, and the production of calcium oxalate stones was significantly reduced after activating NRF2/HO-1.	Calcium Oxalate	105-120	heme oxygenase 1	Homo sapiens	176-180
33152749-3	2021	Here, we found that cell-free heme suppresses human B cell plasmablast/plasma cell differentiation by inhibiting the DOCK8/STAT3 signaling pathway, which is critical for B cell activation, as well as by upregulating heme oxygenase 1 (HO-1) through its enzymatic byproducts, carbon monoxide and biliverdin.	Heme	30-34	heme oxygenase 1	Homo sapiens	216-232
33152749-3	2021	Here, we found that cell-free heme suppresses human B cell plasmablast/plasma cell differentiation by inhibiting the DOCK8/STAT3 signaling pathway, which is critical for B cell activation, as well as by upregulating heme oxygenase 1 (HO-1) through its enzymatic byproducts, carbon monoxide and biliverdin.	Heme	30-34	heme oxygenase 1	Homo sapiens	234-238
33444090-7	2021	Under ICH pathological conditions, such as overproduction of reactive oxygen species (ROS), Nrf2 is translocated into the nucleus where it up-regulates the expression of several anti-oxidative phase II enzymes such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	61-84	heme oxygenase 1	Homo sapiens	218-234
33444090-7	2021	Under ICH pathological conditions, such as overproduction of reactive oxygen species (ROS), Nrf2 is translocated into the nucleus where it up-regulates the expression of several anti-oxidative phase II enzymes such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	61-84	heme oxygenase 1	Homo sapiens	236-240
33444090-7	2021	Under ICH pathological conditions, such as overproduction of reactive oxygen species (ROS), Nrf2 is translocated into the nucleus where it up-regulates the expression of several anti-oxidative phase II enzymes such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	86-89	heme oxygenase 1	Homo sapiens	218-234
33444090-7	2021	Under ICH pathological conditions, such as overproduction of reactive oxygen species (ROS), Nrf2 is translocated into the nucleus where it up-regulates the expression of several anti-oxidative phase II enzymes such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	86-89	heme oxygenase 1	Homo sapiens	236-240
33520087-7	2021	More importantly, berbamine increased the intracellular reactive oxygen species (ROS) level through the downregulation of antioxidative genes such as Nrf2, HO-1, SOD2, and GPX-1.	berbamine	18-27	heme oxygenase 1	Homo sapiens	156-160
33520087-7	2021	More importantly, berbamine increased the intracellular reactive oxygen species (ROS) level through the downregulation of antioxidative genes such as Nrf2, HO-1, SOD2, and GPX-1.	Reactive Oxygen Species	81-84	heme oxygenase 1	Homo sapiens	156-160
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Heme	97-101	heme oxygenase 1	Homo sapiens	0-16
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Heme	97-101	heme oxygenase 1	Homo sapiens	18-22
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Carbon Monoxide	166-181	heme oxygenase 1	Homo sapiens	0-16
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Carbon Monoxide	166-181	heme oxygenase 1	Homo sapiens	18-22
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Carbon Monoxide	183-185	heme oxygenase 1	Homo sapiens	0-16
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Carbon Monoxide	183-185	heme oxygenase 1	Homo sapiens	18-22
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Iron	193-197	heme oxygenase 1	Homo sapiens	0-16
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Iron	193-197	heme oxygenase 1	Homo sapiens	18-22
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Biliverdine	202-212	heme oxygenase 1	Homo sapiens	0-16
33440611-1	2021	Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin.	Biliverdine	202-212	heme oxygenase 1	Homo sapiens	18-22
33440611-6	2021	We provide a brief background on the current understanding of the mechanisms underlying how HO-1 leaves the sER membrane and migrates to the nucleus, the circumstances under which it does so and, maybe the most important and unknown aspect, what the function of HO-1 in the nucleus is.	Serine	108-111	heme oxygenase 1	Homo sapiens	92-96
33271149-5	2021	Kaempferol (25 muM) mediated downregulation of GST, NQO1 and HO1 expression is also observed even after stimulation of Nrf2 by tert-butylhydroquinone (tBHQ).	kaempferol	0-10	heme oxygenase 1	Homo sapiens	61-64
33096358-0	2021	Curcumin ameliorates mercuric chloride-induced liver injury via modulating cytochrome P450 signaling and Nrf2/HO-1 pathway.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	110-114
33096358-0	2021	Curcumin ameliorates mercuric chloride-induced liver injury via modulating cytochrome P450 signaling and Nrf2/HO-1 pathway.	Mercuric Chloride	21-38	heme oxygenase 1	Homo sapiens	110-114
33096358-7	2021	Furthermore, curcumin significantly increased the nuclear translocation of nuclear factor E2-related factor 2 (Nrf2) and consequently upregulated the expression of heme oxygenase 1 (HO-1) under HgCl2 treatment.	Curcumin	13-21	heme oxygenase 1	Homo sapiens	164-180
33096358-7	2021	Furthermore, curcumin significantly increased the nuclear translocation of nuclear factor E2-related factor 2 (Nrf2) and consequently upregulated the expression of heme oxygenase 1 (HO-1) under HgCl2 treatment.	Curcumin	13-21	heme oxygenase 1	Homo sapiens	182-186
33096358-8	2021	Meanwhile, inhibition of HO-1 by zinc protoporphyria could abolish the cytoprotective effects of curcumin in HgCl2-treated L02 hepatocytes.	Curcumin	97-105	heme oxygenase 1	Homo sapiens	25-29
33096358-8	2021	Meanwhile, inhibition of HO-1 by zinc protoporphyria could abolish the cytoprotective effects of curcumin in HgCl2-treated L02 hepatocytes.	Mercuric Chloride	109-114	heme oxygenase 1	Homo sapiens	25-29
33096358-9	2021	In conclusion, our data identify that curcumin could enhance Nrf2-mediated HO-1 to upregulate antioxidant ability, which might be associate with CYP450 signaling to suppress liver damage induced by HgCl2.	Curcumin	38-46	heme oxygenase 1	Homo sapiens	75-79
33628184-7	2020	Furthermore, Pristimerin suppressed NF-kappaB and MAPK signaling pathways, reduced reactive oxygen species (ROS) production and activated the nuclear factor erythroid 2-related factor 2/heme oxygenase 1 (Nrf2/HO-1) signaling during osteoclastogenesis.	pristimerin	13-24	heme oxygenase 1	Homo sapiens	209-213
33411783-11	2021	However, pretreatment of a HO-1 inhibitor reduced the protective effect of Formononetin on hyperoxic ALI.	formononetin	75-87	heme oxygenase 1	Homo sapiens	27-31
33435366-8	2021	Chrysoeriol also markedly enhanced key transcription factors (Nrf2) and antioxidant-associated genes (particularly HO-1 and NQO-1).	chrysoeriol	0-11	heme oxygenase 1	Homo sapiens	115-119
33411783-12	2021	Cell study showed that the Formononetin-induced upregulation of HO-1 was abolished when the Nrf2 was silenced.	formononetin	27-39	heme oxygenase 1	Homo sapiens	64-68
33396673-0	2020	Dimethyl Fumarate Promotes the Survival of Retinal Ganglion Cells after Optic Nerve Injury, Possibly through the Nrf2/HO-1 Pathway.	Dimethyl Fumarate	0-17	heme oxygenase 1	Homo sapiens	118-122
33411783-13	2021	CONCLUSIONS: Formononetin pretreatment reduces hyperoxia-induced ALI via Nrf2/HO-1-mediated antioxidant and anti-inflammatory effects.	formononetin	13-25	heme oxygenase 1	Homo sapiens	78-82
33605427-11	2021	CONCLUSIONS: These results suggest that genistein exerts a neuroprotective effect on SH-SY5Y cells in vitro via Nrf2/HO-1/PI3K signaling, providing a foundation for the application of genistein in the treatment of neurodegenerative diseases related to Nrf2/HO-1/PI3K signaling.	Genistein	40-49	heme oxygenase 1	Homo sapiens	117-121
33605427-11	2021	CONCLUSIONS: These results suggest that genistein exerts a neuroprotective effect on SH-SY5Y cells in vitro via Nrf2/HO-1/PI3K signaling, providing a foundation for the application of genistein in the treatment of neurodegenerative diseases related to Nrf2/HO-1/PI3K signaling.	Genistein	40-49	heme oxygenase 1	Homo sapiens	257-261
33605427-11	2021	CONCLUSIONS: These results suggest that genistein exerts a neuroprotective effect on SH-SY5Y cells in vitro via Nrf2/HO-1/PI3K signaling, providing a foundation for the application of genistein in the treatment of neurodegenerative diseases related to Nrf2/HO-1/PI3K signaling.	Genistein	184-193	heme oxygenase 1	Homo sapiens	117-121
33442403-0	2021	Inhibition of Nrf2/HO-1 signaling pathway by Dextran Sulfate suppresses angiogenesis of Gastric Cancer.	Dextran Sulfate	45-60	heme oxygenase 1	Homo sapiens	19-23
32820550-6	2021	Other studies also demonstrated that the analgesic effects of opioids and cannabinoids are improved when these drugs are coadministered with CO-RMs, HO-1 or Nrf2 activators in different preclinical pain models and that these improvements are generally mediated by upregulation or prevention of the downregulation of micro-opioid receptors, delta-opioid receptors and/or cannabinoid 2 receptors in the setting of chronic pain.	Cannabinoids	74-86	heme oxygenase 1	Homo sapiens	149-153
32820550-8	2021	In summary, activation of the Nrf2/HO-1/carbon monoxide signaling pathway alone and/or in combination with the administration of specific analgesics is a valid strategy for the treatment of chronic pain and some associated emotional disorders.	Carbon Monoxide	40-55	heme oxygenase 1	Homo sapiens	35-39
33075721-0	2021	Role of heme oxygenase-1 in human placenta on iron supply to fetus.	Iron	46-50	heme oxygenase 1	Homo sapiens	8-24
33075721-2	2021	Recently, increasing evidence has shown that heme oxygenase (HO)-1, which is an inducible isoform of the rate-limiting enzyme in the heme degradation pathway, may be involved in the effective reutilization of iron.	Iron	209-213	heme oxygenase 1	Homo sapiens	45-66
33075721-9	2021	Placenta with fetal death (miscarriage) in the first and second trimester indicate significantly higher ratio of ho-1 gene for iron production to the fpn-1 gene for iron excretion than normal.	Iron	127-131	heme oxygenase 1	Homo sapiens	113-117
33075721-11	2021	DISCUSSION: These findings suggest that HO-1 in placenta plays an important role in iron supplying system in the second trimester to support fetal development.	Iron	84-88	heme oxygenase 1	Homo sapiens	40-44
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Heme	87-91	heme oxygenase 1	Homo sapiens	0-16
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Heme	87-91	heme oxygenase 1	Homo sapiens	18-22
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Heme	119-123	heme oxygenase 1	Homo sapiens	0-16
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Heme	119-123	heme oxygenase 1	Homo sapiens	18-22
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Carbon Monoxide	199-214	heme oxygenase 1	Homo sapiens	0-16
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Carbon Monoxide	199-214	heme oxygenase 1	Homo sapiens	18-22
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Biliverdine	219-229	heme oxygenase 1	Homo sapiens	0-16
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Biliverdine	219-229	heme oxygenase 1	Homo sapiens	18-22
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Bilirubin	230-239	heme oxygenase 1	Homo sapiens	0-16
33184238-4	2020	Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis.	Bilirubin	230-239	heme oxygenase 1	Homo sapiens	18-22
33383653-8	2020	Furthermore, cycloheximide treatment increased HO-1 abundance in p53 KO cells suggesting that p53 modulates HO-1 protein stability.	Cycloheximide	13-26	heme oxygenase 1	Homo sapiens	47-51
33383653-8	2020	Furthermore, cycloheximide treatment increased HO-1 abundance in p53 KO cells suggesting that p53 modulates HO-1 protein stability.	Cycloheximide	13-26	heme oxygenase 1	Homo sapiens	108-112
33289541-12	2020	TFNA treatment in IL-1beta-induced chondrocytes reduced apoptosis by activating the BCL2/BAX/caspase-3 pathway, inhibited oxidative stress by regulating the Nrf2/HO-1-signaling pathway, and enhanced autophagy through upregulated LC3-II, Beclin1, and Atg7.	4-(Trifluoromethyl)nicotinic acid	0-4	heme oxygenase 1	Homo sapiens	162-166
33414780-6	2020	Plasma levels of heme and its scavenger hemopexin and degrading enzyme heme-oxygenase-1 (HO-1) were measured in 48 STEC-HUS patients.	Heme	17-21	heme oxygenase 1	Homo sapiens	89-93
33414780-10	2020	Interestingly, especially patients with high heme levels (n = 12, heme levels above 75 quartile range) had high plasma HO-1 levels with median of 332.5 (86-720) ng/ml (p = 0.008).	Heme	45-49	heme oxygenase 1	Homo sapiens	119-123
33414780-10	2020	Interestingly, especially patients with high heme levels (n = 12, heme levels above 75 quartile range) had high plasma HO-1 levels with median of 332.5 (86-720) ng/ml (p = 0.008).	Heme	66-70	heme oxygenase 1	Homo sapiens	119-123
33248029-10	2021	Modulation of oxidative stress-induced response involves the regulation of genes that encode for antioxidant proteins such as catalase and heme oxygenase-1; regulation that functions as a critical protection mechanism against oxidative cell damage induced by HEMA and TEGDMA.	hydroxyethyl methacrylate	259-263	heme oxygenase 1	Homo sapiens	139-155
33248029-10	2021	Modulation of oxidative stress-induced response involves the regulation of genes that encode for antioxidant proteins such as catalase and heme oxygenase-1; regulation that functions as a critical protection mechanism against oxidative cell damage induced by HEMA and TEGDMA.	triethylene glycol dimethacrylate	268-274	heme oxygenase 1	Homo sapiens	139-155
33220236-5	2021	Our data revealed that esculetin played an antioxidant role not only through its antioxidant activity, but also by highly inducing Nrf-2 translocation to the nucleus, which in turn, enhanced Nrf2 signaling regulated antioxidant genes (HO-1, NQO1, GCLM, SOD1 and SOD2) mRNA expression levels in H2O2-treated HCE cells.	esculetin	23-32	heme oxygenase 1	Homo sapiens	235-239
33605427-0	2021	Genistein exerts a cell-protective effect via Nrf2/HO-1/PI3K signaling in Abeta25-35-induced Alzheimer"s disease models in vitro.	Genistein	0-9	heme oxygenase 1	Homo sapiens	51-55
33605427-8	2021	RESULTS: Genistein enhanced the HO-1expression at both the mRNA and protein levels, as well as the PI3K p85 phosphorylation level.	Genistein	9-18	heme oxygenase 1	Homo sapiens	32-36
33605427-9	2021	In addition, genistein increased the survival of SH-SY5Y cells treated with Abeta25-35via HO-1 signaling.	Genistein	13-22	heme oxygenase 1	Homo sapiens	90-94
33442403-1	2021	Purpose: To investigate the role of Nrf2/HO-1 signaling pathway in angiogenesis and whether dextran sulfate (DS) could suppress angiogenesis by inhibiting Nrf2/HO-1 signaling pathway in gastric cancer.	Dextran Sulfate	92-107	heme oxygenase 1	Homo sapiens	160-164
33442403-1	2021	Purpose: To investigate the role of Nrf2/HO-1 signaling pathway in angiogenesis and whether dextran sulfate (DS) could suppress angiogenesis by inhibiting Nrf2/HO-1 signaling pathway in gastric cancer.	Dextran Sulfate	109-111	heme oxygenase 1	Homo sapiens	160-164
33442403-4	2021	Immunofluorescence,western blot and qPCR analyzed the effects of DS on the expression of Nrf2, HO-1 and VEGF under gradient hypoxia time.	Dextran Sulfate	65-67	heme oxygenase 1	Homo sapiens	95-99
33442403-10	2021	DS reduced the angiogenic potential and the expression of Nrf2, HO-1 and VEGF in HGC-27 cells.	Dextran Sulfate	0-2	heme oxygenase 1	Homo sapiens	64-68
33357768-0	2021	MitoQ protects against high glucose-induced brain microvascular endothelial cells injury via the Nrf2/HO-1 pathway.	mitoquinone	0-5	heme oxygenase 1	Homo sapiens	102-106
33357768-6	2021	Moreover, we found that MitoQ treatment significantly upregulated the expression of Nrf2 and HO-1 in HG-induced BMECs, which is accompanied by improved mitochondrial membrane potential and decreased MtROS production.	mitoquinone	24-29	heme oxygenase 1	Homo sapiens	93-97
33357768-9	2021	In conclusion, our results suggest that MitoQ exerts protective effect on HG-induced BMECs injury via activating Nrf2/HO-1 pathway.	mitoquinone	40-45	heme oxygenase 1	Homo sapiens	118-122
33357768-9	2021	In conclusion, our results suggest that MitoQ exerts protective effect on HG-induced BMECs injury via activating Nrf2/HO-1 pathway.	Mercury	74-76	heme oxygenase 1	Homo sapiens	118-122
33373320-5	2020	NMN administration significantly increased NAD+ levels, SIRT1 protein expression, and heme oxygenase-1 (HO-1) expression.	Nicotinamide Mononucleotide	0-3	heme oxygenase 1	Homo sapiens	86-102
33373320-5	2020	NMN administration significantly increased NAD+ levels, SIRT1 protein expression, and heme oxygenase-1 (HO-1) expression.	Nicotinamide Mononucleotide	0-3	heme oxygenase 1	Homo sapiens	104-108
33396673-1	2020	This study aimed to verify whether dimethyl fumarate (DMF) promotes the survival of retinal ganglion cells (RGCs) after optic nerve crush (ONC) accompanied by activation of the NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway.	Dimethyl Fumarate	35-52	heme oxygenase 1	Homo sapiens	207-223
33396673-1	2020	This study aimed to verify whether dimethyl fumarate (DMF) promotes the survival of retinal ganglion cells (RGCs) after optic nerve crush (ONC) accompanied by activation of the NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway.	Dimethyl Fumarate	35-52	heme oxygenase 1	Homo sapiens	225-229
33396673-1	2020	This study aimed to verify whether dimethyl fumarate (DMF) promotes the survival of retinal ganglion cells (RGCs) after optic nerve crush (ONC) accompanied by activation of the NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway.	Dimethyl Fumarate	54-57	heme oxygenase 1	Homo sapiens	207-223
33396673-1	2020	This study aimed to verify whether dimethyl fumarate (DMF) promotes the survival of retinal ganglion cells (RGCs) after optic nerve crush (ONC) accompanied by activation of the NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway.	Dimethyl Fumarate	54-57	heme oxygenase 1	Homo sapiens	225-229
33396673-3	2020	Furthermore, immunohistochemical and immunoblotting analyses were performed to study the activation of the Nrf2/HO-1 pathway using retinas treated with daily administration of DMF.	Dimethyl Fumarate	176-179	heme oxygenase 1	Homo sapiens	112-116
33396673-5	2020	Immunohistochemical analysis showed that DMF administration increased the immunoreactivity for Nrf2 and HO-1, a potent antioxidant enzyme, in RGCs immunolabeled with RNA-binding protein with multiple splicing (RBPMS).	Dimethyl Fumarate	41-44	heme oxygenase 1	Homo sapiens	104-108
33396673-6	2020	Immunoblotting analysis revealed an increase in the nuclear expression of Nrf2 and marked upregulation of HO-1 after DMF administration.	Dimethyl Fumarate	117-120	heme oxygenase 1	Homo sapiens	106-110
33344146-9	2020	In addition, intracellular cholesterol load interfered with the balance between NADPH oxidase activity and HO-1 expression.	Cholesterol	27-38	heme oxygenase 1	Homo sapiens	107-111
33051205-1	2020	Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network.	Heme	45-49	heme oxygenase 1	Homo sapiens	31-34
33051205-1	2020	Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network.	Biliverdine	65-75	heme oxygenase 1	Homo sapiens	31-34
33051205-1	2020	Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network.	Carbon Monoxide	77-79	heme oxygenase 1	Homo sapiens	31-34
33051205-1	2020	Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network.	Iron	85-89	heme oxygenase 1	Homo sapiens	31-34
33051205-1	2020	Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network.	Heme	124-128	heme oxygenase 1	Homo sapiens	31-34
33051205-2	2020	Tight regulation of the cellular levels and catalytic activities of HO1 and HO2 is important for maintaining heme homeostasis.	Heme	109-113	heme oxygenase 1	Homo sapiens	68-71
33287198-4	2020	According to the results, PGFE suppressed pro-inflammatory cytokines such as tumor necrosis factor-alpha, interleukin (IL)-1beta, and IL-6, and pro-inflammatory mediators such as inducible nitric oxide synthase and cyclooxygenase-2 through heme oxygenase-1 expression in human periodontal ligament cells stimulated with Porphyromonas gingivalis lipopolysaccharide (PG-LPS).	pgfe	26-30	heme oxygenase 1	Homo sapiens	240-256
33333908-0	2020	Novel Heme Oxygenase-1 (HO-1) Inducers Based on Dimethyl Fumarate Structure.	Dimethyl Fumarate	48-65	heme oxygenase 1	Homo sapiens	6-22
33333908-0	2020	Novel Heme Oxygenase-1 (HO-1) Inducers Based on Dimethyl Fumarate Structure.	Dimethyl Fumarate	48-65	heme oxygenase 1	Homo sapiens	24-28
33333908-1	2020	Novel heme oxygenase-1 (HO-1) inducers based on dimethyl fumarate (DMF) structure are reported in this paper.	Dimethyl Fumarate	48-65	heme oxygenase 1	Homo sapiens	6-22
33333908-1	2020	Novel heme oxygenase-1 (HO-1) inducers based on dimethyl fumarate (DMF) structure are reported in this paper.	Dimethyl Fumarate	48-65	heme oxygenase 1	Homo sapiens	24-28
33333908-1	2020	Novel heme oxygenase-1 (HO-1) inducers based on dimethyl fumarate (DMF) structure are reported in this paper.	Dimethyl Fumarate	67-70	heme oxygenase 1	Homo sapiens	6-22
33333908-1	2020	Novel heme oxygenase-1 (HO-1) inducers based on dimethyl fumarate (DMF) structure are reported in this paper.	Dimethyl Fumarate	67-70	heme oxygenase 1	Homo sapiens	24-28
33327226-8	2020	The increase in heme in vivo induces HO-1 production, a heme-degrading enzyme.	Heme	16-20	heme oxygenase 1	Homo sapiens	37-41
33327226-8	2020	The increase in heme in vivo induces HO-1 production, a heme-degrading enzyme.	Heme	56-60	heme oxygenase 1	Homo sapiens	37-41
33343802-0	2020	Induction of HO-1 by 5, 8-Dihydroxy-4",7-Dimethoxyflavone via Activation of ROS/p38 MAPK/Nrf2 Attenuates Thrombin-Induced Connective Tissue Growth Factor Expression in Human Cardiac Fibroblasts.	5, 8-dihydroxy-4",7-dimethoxyflavone	21-57	heme oxygenase 1	Homo sapiens	13-17
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	0-16
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	18-22
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Carbon Monoxide	111-113	heme oxygenase 1	Homo sapiens	0-16
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Carbon Monoxide	111-113	heme oxygenase 1	Homo sapiens	18-22
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Iron	121-125	heme oxygenase 1	Homo sapiens	0-16
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Iron	121-125	heme oxygenase 1	Homo sapiens	18-22
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Biliverdine	131-141	heme oxygenase 1	Homo sapiens	0-16
33276470-1	2020	Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin.	Biliverdine	131-141	heme oxygenase 1	Homo sapiens	18-22
31851841-13	2020	Furthermore, taraxasterol induced the Nrf2 nuclear accumulation and expressions of HO-1, NQO-1 and GPx-3 in OGD/R-induced hippocampal neurons.	taraxasterol	13-25	heme oxygenase 1	Homo sapiens	83-87
32954935-9	2020	Recombinant DEL-1 augmented AMP-activated protein kinase (AMPK) phosphorylation and haem oxygenase (HO)-1 expression to alleviating inflammation and impairment of insulin signalling in 3T3-L1 adipocytes treated with palmitate.	Palmitates	216-225	heme oxygenase 1	Homo sapiens	84-105
33343802-0	2020	Induction of HO-1 by 5, 8-Dihydroxy-4",7-Dimethoxyflavone via Activation of ROS/p38 MAPK/Nrf2 Attenuates Thrombin-Induced Connective Tissue Growth Factor Expression in Human Cardiac Fibroblasts.	Reactive Oxygen Species	76-79	heme oxygenase 1	Homo sapiens	13-17
33343802-2	2020	Flavonoids have been demonstrated to display anti-inflammatory and antioxidant effects through the induction of HO-1.	Flavonoids	0-10	heme oxygenase 1	Homo sapiens	112-116
33343802-5	2020	Here, we found that DDF time- and concentration-dependently induced HO-1 protein and mRNA expression, which was attenuated by pretreatment with reactive oxygen species (ROS) scavenger N-acetyl cysteine (NAC) in HCFs.	Reactive Oxygen Species	144-167	heme oxygenase 1	Homo sapiens	68-72
33343802-5	2020	Here, we found that DDF time- and concentration-dependently induced HO-1 protein and mRNA expression, which was attenuated by pretreatment with reactive oxygen species (ROS) scavenger N-acetyl cysteine (NAC) in HCFs.	Reactive Oxygen Species	169-172	heme oxygenase 1	Homo sapiens	68-72
33343802-5	2020	Here, we found that DDF time- and concentration-dependently induced HO-1 protein and mRNA expression, which was attenuated by pretreatment with reactive oxygen species (ROS) scavenger N-acetyl cysteine (NAC) in HCFs.	Acetylcysteine	184-201	heme oxygenase 1	Homo sapiens	68-72
33343802-5	2020	Here, we found that DDF time- and concentration-dependently induced HO-1 protein and mRNA expression, which was attenuated by pretreatment with reactive oxygen species (ROS) scavenger N-acetyl cysteine (NAC) in HCFs.	Acetylcysteine	203-206	heme oxygenase 1	Homo sapiens	68-72
33343802-7	2020	Interestingly, pretreatment with glutathione (GSH) inhibited DDF-induced HO-1 expression.	Glutathione	33-44	heme oxygenase 1	Homo sapiens	73-77
33343802-7	2020	Interestingly, pretreatment with glutathione (GSH) inhibited DDF-induced HO-1 expression.	Glutathione	46-49	heme oxygenase 1	Homo sapiens	73-77
33343802-7	2020	Interestingly, pretreatment with glutathione (GSH) inhibited DDF-induced HO-1 expression.	ddf	61-64	heme oxygenase 1	Homo sapiens	73-77
33343802-9	2020	DDF-induced HO-1 expression was attenuated by an inhibitor of p38 MAPK (p38i VIII) or siRNA, but not by MEK1/2 (PD98059) or JNK1/2 (SP600125).	ddf	0-3	heme oxygenase 1	Homo sapiens	12-16
33343802-11	2020	Moreover, DDF-induced HO-1 expression was mediated through Nrf2 phosphorylation and translocation into the nucleus which was attenuated by NAC or p38 siRNA.	Acetylcysteine	139-142	heme oxygenase 1	Homo sapiens	22-26
33343802-13	2020	Interaction between Nrf2 and the ARE-binding sites on the HO-1 promoter was revealed by chromatin immunoprecipitation assay, which was attenuated by NAC, GSH, or p38i VIII.	Acetylcysteine	149-152	heme oxygenase 1	Homo sapiens	58-62
33343802-13	2020	Interaction between Nrf2 and the ARE-binding sites on the HO-1 promoter was revealed by chromatin immunoprecipitation assay, which was attenuated by NAC, GSH, or p38i VIII.	Glutathione	154-157	heme oxygenase 1	Homo sapiens	58-62
33343802-16	2020	These results suggested that DDF-induced HO-1 expression is, at least, mediated through the activation of the ROS-dependent p38 MAPK/Nrf2 signaling pathway in HCFs.	Reactive Oxygen Species	110-113	heme oxygenase 1	Homo sapiens	41-45
32623920-6	2020	We further showed that H2O2-induced oxidative stress was reduced by curcumin via the Nrf2/HO-1 pathway in human neuroblastoma cells.	Hydrogen Peroxide	23-27	heme oxygenase 1	Homo sapiens	90-94
33199994-9	2020	DMF also increased the anti-inflammatory and antioxidative ability of NP cells by promoting the activity of the Nrf2/HO-1 and PI3K/Akt signaling pathways, thus delaying IVDD.	Dimethyl Fumarate	0-3	heme oxygenase 1	Homo sapiens	117-121
33378016-0	2020	MiRNA-15a-3p inhibits the metastasis of hepatocellular carcinoma by interacting with HMOX1.	mirna-15a-3p	0-12	heme oxygenase 1	Homo sapiens	85-90
32623920-6	2020	We further showed that H2O2-induced oxidative stress was reduced by curcumin via the Nrf2/HO-1 pathway in human neuroblastoma cells.	Curcumin	68-76	heme oxygenase 1	Homo sapiens	90-94
33045867-9	2020	Subsequently, activation of MAPK-Nrf2/ARE signaling was readily induced by vitexin treatment, as evidenced by upregulation of antioxidant genes including heme oxygenase 1 (HO-1) and superoxide dismutase (SOD).	vitexin	75-82	heme oxygenase 1	Homo sapiens	154-170
33045867-9	2020	Subsequently, activation of MAPK-Nrf2/ARE signaling was readily induced by vitexin treatment, as evidenced by upregulation of antioxidant genes including heme oxygenase 1 (HO-1) and superoxide dismutase (SOD).	vitexin	75-82	heme oxygenase 1	Homo sapiens	172-176
33035580-0	2020	Effects of taraxasterol against ethanol and high-fat diet-induced liver injury by regulating TLR4/MyD88/NF-kappaB and Nrf2/HO-1 signaling pathways.	taraxasterol	11-23	heme oxygenase 1	Homo sapiens	123-127
33456997-11	2020	Crocin also increased the expression of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1), decreased TAZ in MNNG-treated GES-1 cells.	crocin	0-6	heme oxygenase 1	Homo sapiens	95-111
33456997-11	2020	Crocin also increased the expression of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1), decreased TAZ in MNNG-treated GES-1 cells.	crocin	0-6	heme oxygenase 1	Homo sapiens	113-117
33035580-6	2020	Production of CYP2E1, Nrf2 and HO-1, which produced in response to increased oxidative stress, were regulated in TAR treated, ethanol-induced hepatocytes.	Ethanol	126-133	heme oxygenase 1	Homo sapiens	31-35
33256538-0	2022	Aloperine protects human retinal pigment epithelial cells against hydrogen peroxide-induced oxidative stress and apoptosis through activation of Nrf2/HO-1 pathway.	aloperine	0-9	heme oxygenase 1	Homo sapiens	150-154
32942007-5	2020	Moreover, we evaluated the relationship between glucose concentration and concentration of intracellular ROS, as well as the effects of glucose concentration on the induction of Nrf2-dependent genes such as Glutathione S-transferases, Heme-oxygenase-1, and Glutathione peroxidase-4).	Glucose	136-143	heme oxygenase 1	Homo sapiens	235-251
33157356-5	2020	HO-1 induction by transfection of HO-1 over-expression plasmid or treatment with cobalt protoporphyrin (CoPP), a potent HO-1 inducer, could inhibit DTMUV replication effectively.	cobaltiprotoporphyrin	81-102	heme oxygenase 1	Homo sapiens	0-4
33157356-5	2020	HO-1 induction by transfection of HO-1 over-expression plasmid or treatment with cobalt protoporphyrin (CoPP), a potent HO-1 inducer, could inhibit DTMUV replication effectively.	cobaltiprotoporphyrin	104-108	heme oxygenase 1	Homo sapiens	0-4
33157356-7	2020	Furthermore, we found that ferric ion (Fe3+) but not biliverdin and carbon monoxide, products of heme degradation by HO-1, mediated the HO-1-induced anti-DTMUV effect.	Ferric enterobactin ion	27-33	heme oxygenase 1	Homo sapiens	136-140
33157356-7	2020	Furthermore, we found that ferric ion (Fe3+) but not biliverdin and carbon monoxide, products of heme degradation by HO-1, mediated the HO-1-induced anti-DTMUV effect.	ferric sulfate	39-43	heme oxygenase 1	Homo sapiens	136-140
33157356-7	2020	Furthermore, we found that ferric ion (Fe3+) but not biliverdin and carbon monoxide, products of heme degradation by HO-1, mediated the HO-1-induced anti-DTMUV effect.	Heme	97-101	heme oxygenase 1	Homo sapiens	136-140
33256538-0	2022	Aloperine protects human retinal pigment epithelial cells against hydrogen peroxide-induced oxidative stress and apoptosis through activation of Nrf2/HO-1 pathway.	Hydrogen Peroxide	66-83	heme oxygenase 1	Homo sapiens	150-154
33256538-15	2022	Moreover, aloperine treatment enhanced the expression levels of Nrf2 in nuclear fraction and the HO-1 expression in lysates.	aloperine	10-19	heme oxygenase 1	Homo sapiens	97-101
33256538-17	2022	In conclusion, these findings demonstrated that aloperine protected ARPE-19 cells from H2O2-induced oxidative stress and apoptosis in part via activating the Nrf2/HO-1 signaling pathway.	aloperine	48-57	heme oxygenase 1	Homo sapiens	163-167
33256538-17	2022	In conclusion, these findings demonstrated that aloperine protected ARPE-19 cells from H2O2-induced oxidative stress and apoptosis in part via activating the Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	87-91	heme oxygenase 1	Homo sapiens	163-167
32812103-4	2020	Additionally, coumarin-pi promoted nuclear factor erythroid 2-related factor 2 (Nrf2) expression and upregulated the protein expression of antioxidantenzymes, including heme oxygenase-1 (HO-1), NAD(P)H: quinone oxidase (NQO1), glutamyl cysteine ligase catalytic subunit (GCLC), and glutamate-cysteine ligase regulatory subunit (GCLM).	coumarin	14-22	heme oxygenase 1	Homo sapiens	169-185
32812103-4	2020	Additionally, coumarin-pi promoted nuclear factor erythroid 2-related factor 2 (Nrf2) expression and upregulated the protein expression of antioxidantenzymes, including heme oxygenase-1 (HO-1), NAD(P)H: quinone oxidase (NQO1), glutamyl cysteine ligase catalytic subunit (GCLC), and glutamate-cysteine ligase regulatory subunit (GCLM).	coumarin	14-22	heme oxygenase 1	Homo sapiens	187-191
32976958-7	2020	Both HFD-fed mice and PA/OA-induced HepG2 cells displayed ferroptosis-based panel of biomarkers such as iron overload with the up-regulation of TFR1 and the down-regulation of FTH1, lipid peroxidation and inhibition of Nrf2 activity, which further induced GPX4 and HO-1 levels.	Iron	104-108	heme oxygenase 1	Homo sapiens	265-269
33266044-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide.	Biliverdine	99-109	heme oxygenase 1	Homo sapiens	0-16
33266044-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide.	Biliverdine	99-109	heme oxygenase 1	Homo sapiens	18-22
33266044-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide.	Iron	111-115	heme oxygenase 1	Homo sapiens	0-16
33266044-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide.	Iron	111-115	heme oxygenase 1	Homo sapiens	18-22
33266044-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	0-16
33266044-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	18-22
33381031-0	2020	Suppression of Urokinase-Type Plasminogen Activator Receptor by Docosahexaenoic Acid Mediated by Heme Oxygenase-1 in 12-O-Tetradecanoylphorbol-13-Acetate-Induced Human Endothelial Cells.	Docosahexaenoic Acids	64-84	heme oxygenase 1	Homo sapiens	97-113
33260980-1	2020	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that catalyzes heme group degradation.	Heme	74-78	heme oxygenase 1	Homo sapiens	0-16
33260980-1	2020	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that catalyzes heme group degradation.	Heme	74-78	heme oxygenase 1	Homo sapiens	18-22
33381031-0	2020	Suppression of Urokinase-Type Plasminogen Activator Receptor by Docosahexaenoic Acid Mediated by Heme Oxygenase-1 in 12-O-Tetradecanoylphorbol-13-Acetate-Induced Human Endothelial Cells.	Tetradecanoylphorbol Acetate	117-153	heme oxygenase 1	Homo sapiens	97-113
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	fepp	47-51	heme oxygenase 1	Homo sapiens	13-17
33381031-4	2020	The aim of this study was to investigate the effect of DHA on 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced uPAR expression and potential role of heme oxygenase-1 (HO-1) in DHA-induced inhibition of uPAR in human endothelial ECV304 cells.	Docosahexaenoic Acids	178-181	heme oxygenase 1	Homo sapiens	151-167
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	fepp	47-51	heme oxygenase 1	Homo sapiens	144-148
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	Tetradecanoylphorbol Acetate	63-66	heme oxygenase 1	Homo sapiens	13-17
33381031-4	2020	The aim of this study was to investigate the effect of DHA on 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced uPAR expression and potential role of heme oxygenase-1 (HO-1) in DHA-induced inhibition of uPAR in human endothelial ECV304 cells.	Docosahexaenoic Acids	178-181	heme oxygenase 1	Homo sapiens	169-173
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	Tetradecanoylphorbol Acetate	63-66	heme oxygenase 1	Homo sapiens	144-148
33381031-6	2020	Moreover, treatment with DHA induced HO-1 expression in a time- and concentration-dependent manner.	Docosahexaenoic Acids	25-28	heme oxygenase 1	Homo sapiens	37-41
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	tin protoporphyrin IX	159-180	heme oxygenase 1	Homo sapiens	13-17
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	tin protoporphyrin IX	159-180	heme oxygenase 1	Homo sapiens	144-148
33381031-7	2020	In addition, DHA-induced inhibition of uPAR expression and cell invasion in TPA-stimulated cells was reversed by si-HO-1 RNA.	Docosahexaenoic Acids	13-16	heme oxygenase 1	Homo sapiens	116-120
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	S-Nitroso-N-propionyl-D,L-penicillamine	182-186	heme oxygenase 1	Homo sapiens	13-17
33381031-7	2020	In addition, DHA-induced inhibition of uPAR expression and cell invasion in TPA-stimulated cells was reversed by si-HO-1 RNA.	Tetradecanoylphorbol Acetate	76-79	heme oxygenase 1	Homo sapiens	116-120
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	S-Nitroso-N-propionyl-D,L-penicillamine	182-186	heme oxygenase 1	Homo sapiens	144-148
33381031-8	2020	Induction of HO-1 by ferric protoporphyrin IX (FePP) inhibited TPA-induced uPAR expression, and this effect was abolished by treatment with the HO-1 inhibitor tin protoporphyrin IX (SnPP).	ferric protoporphyrin ix	21-45	heme oxygenase 1	Homo sapiens	13-17
33381031-9	2020	Additionally, carbon monoxide, an HO-1 product, attenuated TPA-induced uPAR expression and cell invasion.	Carbon Monoxide	14-29	heme oxygenase 1	Homo sapiens	34-38
33381031-9	2020	Additionally, carbon monoxide, an HO-1 product, attenuated TPA-induced uPAR expression and cell invasion.	Tetradecanoylphorbol Acetate	59-62	heme oxygenase 1	Homo sapiens	34-38
33381031-10	2020	Collectively, these data suggest a novel role of DHA-induced HO-1 in reducing uPAR expression and cell invasion in human endothelial ECV304 cells.	Docosahexaenoic Acids	49-52	heme oxygenase 1	Homo sapiens	61-65
33238962-7	2020	Serum HO-1 correlated with serum total bilirubin (R = 0.454, P <  0.001) and serum LDH (R = 0.500, P <  0.001).	Bilirubin	39-48	heme oxygenase 1	Homo sapiens	6-10
33232319-0	2020	LncRNA MIR4435-2HG mediates cisplatin resistance in HCT116 cells by regulating Nrf2 and HO-1.	Cisplatin	28-37	heme oxygenase 1	Homo sapiens	88-92
33232319-9	2020	Furthermore, Nrf2 and HO-1 mRNA levels, as critical molecules in the oxidative stress pathway, were inhibited by siRNAs targeting MIR4435-2HG, suggesting that MIR4435-2HG-mediated cisplatin resistance occurs through the Nrf2/HO-1 pathway.	mir4435	130-137	heme oxygenase 1	Homo sapiens	22-26
33232319-9	2020	Furthermore, Nrf2 and HO-1 mRNA levels, as critical molecules in the oxidative stress pathway, were inhibited by siRNAs targeting MIR4435-2HG, suggesting that MIR4435-2HG-mediated cisplatin resistance occurs through the Nrf2/HO-1 pathway.	mir4435	130-137	heme oxygenase 1	Homo sapiens	225-229
33232319-9	2020	Furthermore, Nrf2 and HO-1 mRNA levels, as critical molecules in the oxidative stress pathway, were inhibited by siRNAs targeting MIR4435-2HG, suggesting that MIR4435-2HG-mediated cisplatin resistance occurs through the Nrf2/HO-1 pathway.	mir4435	159-166	heme oxygenase 1	Homo sapiens	22-26
33232319-9	2020	Furthermore, Nrf2 and HO-1 mRNA levels, as critical molecules in the oxidative stress pathway, were inhibited by siRNAs targeting MIR4435-2HG, suggesting that MIR4435-2HG-mediated cisplatin resistance occurs through the Nrf2/HO-1 pathway.	mir4435	159-166	heme oxygenase 1	Homo sapiens	225-229
33232319-9	2020	Furthermore, Nrf2 and HO-1 mRNA levels, as critical molecules in the oxidative stress pathway, were inhibited by siRNAs targeting MIR4435-2HG, suggesting that MIR4435-2HG-mediated cisplatin resistance occurs through the Nrf2/HO-1 pathway.	Cisplatin	180-189	heme oxygenase 1	Homo sapiens	22-26
33232319-9	2020	Furthermore, Nrf2 and HO-1 mRNA levels, as critical molecules in the oxidative stress pathway, were inhibited by siRNAs targeting MIR4435-2HG, suggesting that MIR4435-2HG-mediated cisplatin resistance occurs through the Nrf2/HO-1 pathway.	Cisplatin	180-189	heme oxygenase 1	Homo sapiens	225-229
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Heme	98-102	heme oxygenase 1	Homo sapiens	0-16
33222098-8	2022	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 muM) smothered the preventive impacts brought about by edaravone with respect to mitochondrial function and inflammation.	zinc protoporphyrin	56-78	heme oxygenase 1	Homo sapiens	22-38
33222098-8	2022	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 muM) smothered the preventive impacts brought about by edaravone with respect to mitochondrial function and inflammation.	zinc protoporphyrin	56-78	heme oxygenase 1	Homo sapiens	40-44
33222098-8	2022	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 muM) smothered the preventive impacts brought about by edaravone with respect to mitochondrial function and inflammation.	zinc protoporphyrin	80-87	heme oxygenase 1	Homo sapiens	22-38
33222098-8	2022	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 muM) smothered the preventive impacts brought about by edaravone with respect to mitochondrial function and inflammation.	zinc protoporphyrin	80-87	heme oxygenase 1	Homo sapiens	40-44
33222098-8	2022	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 muM) smothered the preventive impacts brought about by edaravone with respect to mitochondrial function and inflammation.	Edaravone	147-156	heme oxygenase 1	Homo sapiens	22-38
33222098-8	2022	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 muM) smothered the preventive impacts brought about by edaravone with respect to mitochondrial function and inflammation.	Edaravone	147-156	heme oxygenase 1	Homo sapiens	40-44
33222098-9	2022	After this examination, it can be concluded that edaravone caused cytoprotective impacts in an HO-1-dependent manner in SH-SY5Y cells against ZnO NPs-induced toxicity.	Edaravone	49-58	heme oxygenase 1	Homo sapiens	95-99
33222098-9	2022	After this examination, it can be concluded that edaravone caused cytoprotective impacts in an HO-1-dependent manner in SH-SY5Y cells against ZnO NPs-induced toxicity.	Zinc Oxide	142-145	heme oxygenase 1	Homo sapiens	95-99
33274001-7	2020	In conclusion, our study suggested that delphinidin, as an effective antioxidant, protected HepG2 cells from oxidative stress by regulating the expression of Nrf2/HO-1.	delphinidin	40-51	heme oxygenase 1	Homo sapiens	163-167
33228202-8	2020	HO-1 degrades the prooxidant heme and generates molecules with antioxidative and anti-inflammatory properties, resulting in decreased oxidative stress and inflammation.	Heme	29-33	heme oxygenase 1	Homo sapiens	0-4
32900489-6	2020	Furthermore, ADA modulated the expressions of SOD2, HO-1 and Gpx1 as antioxidant enzymes.	adrenic acid	13-16	heme oxygenase 1	Homo sapiens	52-56
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Heme	98-102	heme oxygenase 1	Homo sapiens	18-22
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Carbon Monoxide	106-121	heme oxygenase 1	Homo sapiens	0-16
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Carbon Monoxide	106-121	heme oxygenase 1	Homo sapiens	18-22
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Carbon Monoxide	123-125	heme oxygenase 1	Homo sapiens	0-16
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Carbon Monoxide	123-125	heme oxygenase 1	Homo sapiens	18-22
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Iron	128-132	heme oxygenase 1	Homo sapiens	0-16
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Iron	128-132	heme oxygenase 1	Homo sapiens	18-22
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Biliverdine	138-148	heme oxygenase 1	Homo sapiens	0-16
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Biliverdine	138-148	heme oxygenase 1	Homo sapiens	18-22
33210267-2	2021	The current study, demonstrated that 5-ALA induced ferroptosis via glutathione peroxidase 4 (GPX4) and heme oxygenase 1 (HMOX1) and had an antitumor effect in esophageal squamous cell carcinoma (ESCC).	5-amino levulinic acid	37-42	heme oxygenase 1	Homo sapiens	103-119
33210267-2	2021	The current study, demonstrated that 5-ALA induced ferroptosis via glutathione peroxidase 4 (GPX4) and heme oxygenase 1 (HMOX1) and had an antitumor effect in esophageal squamous cell carcinoma (ESCC).	5-amino levulinic acid	37-42	heme oxygenase 1	Homo sapiens	121-126
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Biliverdine	150-152	heme oxygenase 1	Homo sapiens	0-16
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Biliverdine	150-152	heme oxygenase 1	Homo sapiens	18-22
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Bilirubin	191-200	heme oxygenase 1	Homo sapiens	0-16
33228260-1	2020	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase.	Bilirubin	191-200	heme oxygenase 1	Homo sapiens	18-22
33228260-4	2020	HO-1 may function as a pleiotropic modulator of inflammatory signaling, via the removal of heme, and generation of its enzymatic degradation-products.	Heme	91-95	heme oxygenase 1	Homo sapiens	0-4
33185862-0	2021	Piperlongumine Inhibits Zika Virus Replication In vitro and Promotes Up-Regulation of HO-1 Expression, Suggesting An Implication of Oxidative Stress.	piperlonguminine	0-14	heme oxygenase 1	Homo sapiens	86-90
33217990-6	2020	Curcumin quenches free radicals, induces antioxidant enzymes (catalase, superoxide dismutase, glutathione peroxidase), and upregulates antioxidative protein markers-Nrf2 and HO-1 that lead to the suppression of cellular oxidative stress.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	174-178
33202598-10	2020	Moreover, chronic obesity also results in the reduction of antioxidant genes such as heme oxygenase-1 (HO-1), increasing adipocyte susceptibility to ROS and cytokines.	Reactive Oxygen Species	149-152	heme oxygenase 1	Homo sapiens	85-101
33223823-0	2020	Eldecalcitol Inhibits LPS-Induced NLRP3 Inflammasome-Dependent Pyroptosis in Human Gingival Fibroblasts by Activating the Nrf2/HO-1 Signaling Pathway.	eldecalcitol	0-12	heme oxygenase 1	Homo sapiens	127-131
33223823-12	2020	Pretreatment with ED-71 effectively inhibited the LPS-induced pyroptosis and was associated with activation of the Nrf2/HO-1 signaling pathway.	eldecalcitol	18-23	heme oxygenase 1	Homo sapiens	120-124
33294119-0	2020	Transcriptome Investigation and In Vitro Verification of Curcumin-Induced HO-1 as a Feature of Ferroptosis in Breast Cancer Cells.	Curcumin	57-65	heme oxygenase 1	Homo sapiens	74-78
33294119-7	2020	Curcumin upregulates a variety of ferroptosis target genes related to redox regulation, especially heme oxygenase-1 (HO-1).	Curcumin	0-8	heme oxygenase 1	Homo sapiens	99-115
33294119-7	2020	Curcumin upregulates a variety of ferroptosis target genes related to redox regulation, especially heme oxygenase-1 (HO-1).	Curcumin	0-8	heme oxygenase 1	Homo sapiens	117-121
33294119-9	2020	Therefore, these data demonstrate that curcumin triggers the molecular and cytological characteristics of ferroptosis in breast cancer cells, and HO-1 promotes curcumin-induced ferroptosis.	Curcumin	160-168	heme oxygenase 1	Homo sapiens	146-150
33185862-5	2021	PL also significantly increased heme oxygenase-1 (HO-1) gene expression, while silencing HO-1 expression and using the reactive oxygen species scavenger, N-acetylcysteine, attenuated the inhibitory effect of PL on Zika virus replication.	piperlonguminine	0-2	heme oxygenase 1	Homo sapiens	32-48
33185862-5	2021	PL also significantly increased heme oxygenase-1 (HO-1) gene expression, while silencing HO-1 expression and using the reactive oxygen species scavenger, N-acetylcysteine, attenuated the inhibitory effect of PL on Zika virus replication.	piperlonguminine	0-2	heme oxygenase 1	Homo sapiens	50-54
33185862-5	2021	PL also significantly increased heme oxygenase-1 (HO-1) gene expression, while silencing HO-1 expression and using the reactive oxygen species scavenger, N-acetylcysteine, attenuated the inhibitory effect of PL on Zika virus replication.	piperlonguminine	208-210	heme oxygenase 1	Homo sapiens	89-93
32885420-0	2020	Protective role of HO-1 against acute kidney injury caused by cutaneous exposure to arsenicals.	Arsenicals	84-94	heme oxygenase 1	Homo sapiens	19-23
33148696-11	2021	Whereas BRET data suggested substantial inhibition of CYP1A2-mediated 7-ethoxyresorufin deethylation in the presence of HO-1, its activity was actually stimulated at subsaturating POR.	ethoxyresorufin	70-87	heme oxygenase 1	Homo sapiens	120-124
33148696-12	2021	In contrast, HO-1-mediated heme metabolism was inhibited at subsaturating POR.	Heme	27-31	heme oxygenase 1	Homo sapiens	13-17
33959213-5	2020	In THP-1 macrophage-derived foam cells, treatment with BCA upregulated ATP-binding cassette (ABC) transporter A1 (ABCA1) and ABCG1 expression and facilitated subsequent cholesterol efflux and diminished intracellular cholesterol contents by activating the peroxisome proliferator-activated receptor gamma (PPARgamma)/liver X receptor alpha (LXRalpha) and PPARgamma/heme oxygenase 1 (HO-1) pathways.	biochanin A	55-58	heme oxygenase 1	Homo sapiens	355-381
33959213-5	2020	In THP-1 macrophage-derived foam cells, treatment with BCA upregulated ATP-binding cassette (ABC) transporter A1 (ABCA1) and ABCG1 expression and facilitated subsequent cholesterol efflux and diminished intracellular cholesterol contents by activating the peroxisome proliferator-activated receptor gamma (PPARgamma)/liver X receptor alpha (LXRalpha) and PPARgamma/heme oxygenase 1 (HO-1) pathways.	biochanin A	55-58	heme oxygenase 1	Homo sapiens	383-387
33174867-7	2020	Importantly, memantine also promoted the expression of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) antioxidant signaling pathway.	Memantine	13-22	heme oxygenase 1	Homo sapiens	110-126
33174867-7	2020	Importantly, memantine also promoted the expression of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) antioxidant signaling pathway.	Memantine	13-22	heme oxygenase 1	Homo sapiens	128-132
32885420-8	2020	Indeed, HO-1 induction with cobalt protoporphyrin (CoPP) treatment in arsenical-treated HEK293 cells afforded cytoprotection by attenuating CHOP-associated apoptosis and cytokine mRNA levels.	cobaltiprotoporphyrin	28-49	heme oxygenase 1	Homo sapiens	8-12
32885420-8	2020	Indeed, HO-1 induction with cobalt protoporphyrin (CoPP) treatment in arsenical-treated HEK293 cells afforded cytoprotection by attenuating CHOP-associated apoptosis and cytokine mRNA levels.	cobaltiprotoporphyrin	51-55	heme oxygenase 1	Homo sapiens	8-12
32885420-8	2020	Indeed, HO-1 induction with cobalt protoporphyrin (CoPP) treatment in arsenical-treated HEK293 cells afforded cytoprotection by attenuating CHOP-associated apoptosis and cytokine mRNA levels.	Arsenicals	70-79	heme oxygenase 1	Homo sapiens	8-12
32784000-6	2020	Moreover, CB08035-SCA and CB08035-SYP treatments reduced significantly Bax, BNIP3, APAF1, ERK1, JNK1, MAPK1, NFkappaB1, TNFalpha, IL-6, IL-1beta and HO-1 gene expressions of apoptosis, proinflammation and oxidative stress induced by t-BOOH.	SMSF0006723	10-17	heme oxygenase 1	Homo sapiens	149-153
32239675-6	2020	Autophagy inhibitor 3-MA pretreatment reversed the anti-senescent and protective effects on the mitochondrial function of HO-1, which promoted the degradation of the extracellular matrix (ECM) in the intervertebral disc.	3-methyladenine	20-24	heme oxygenase 1	Homo sapiens	122-126
32784000-6	2020	Moreover, CB08035-SCA and CB08035-SYP treatments reduced significantly Bax, BNIP3, APAF1, ERK1, JNK1, MAPK1, NFkappaB1, TNFalpha, IL-6, IL-1beta and HO-1 gene expressions of apoptosis, proinflammation and oxidative stress induced by t-BOOH.	SMSF0006723	26-33	heme oxygenase 1	Homo sapiens	149-153
33039895-9	2020	Conversely, genetic or pharmacologic inhibition of HO-1 in TAMs restored the M1-like polarization.	tams	59-63	heme oxygenase 1	Homo sapiens	51-55
31983246-0	2020	Thymoquinone and Curcumin combination protects cisplatin-induced Kidney Injury, Nephrotoxicity by attenuating NFkB, KIM-1 and ameliorating Nrf2/HO-1 signaling.	Cisplatin	47-56	heme oxygenase 1	Homo sapiens	144-148
31983246-10	2020	Tq + Cur treatment increased the expressions of phosphorylated Akt, Nrf2 and HO-1 proteins while decreasing the levels of cleaved caspase 3 and NFkB in kidney homogenates.	thymoquinone	0-2	heme oxygenase 1	Homo sapiens	77-81
31983246-10	2020	Tq + Cur treatment increased the expressions of phosphorylated Akt, Nrf2 and HO-1 proteins while decreasing the levels of cleaved caspase 3 and NFkB in kidney homogenates.	Curcumin	5-8	heme oxygenase 1	Homo sapiens	77-81
31983246-11	2020	In summary, Tq + Cur had protective effects on cisplatin-induced nephrotoxicity and renal injury, which could be mediated by up-regulation of survival signals like Akt, Nrf2/HO-1, and attenuation of KIM-1, NFkB.	thymoquinone	12-14	heme oxygenase 1	Homo sapiens	174-178
31983246-11	2020	In summary, Tq + Cur had protective effects on cisplatin-induced nephrotoxicity and renal injury, which could be mediated by up-regulation of survival signals like Akt, Nrf2/HO-1, and attenuation of KIM-1, NFkB.	Curcumin	17-20	heme oxygenase 1	Homo sapiens	174-178
31983246-11	2020	In summary, Tq + Cur had protective effects on cisplatin-induced nephrotoxicity and renal injury, which could be mediated by up-regulation of survival signals like Akt, Nrf2/HO-1, and attenuation of KIM-1, NFkB.	Cisplatin	47-56	heme oxygenase 1	Homo sapiens	174-178
33052744-0	2020	Fisetin Suppresses Pulmonary Inflammatory Responses through Heme Oxygenase-1 Mediated Downregulation of Inducible Nitric Oxide Synthase.	fisetin	0-7	heme oxygenase 1	Homo sapiens	60-76
33052744-2	2020	Using lipopolysaccharide (LPS)-activated human pulmonary artery endothelial cells (HPAECs), we determined the effects of fisetin on the induction of heme oxygenase-1 (HO-1), inducible nitric oxide synthase (iNOS), and cyclooxygenase-2 (COX-2).	fisetin	121-128	heme oxygenase 1	Homo sapiens	149-165
33052744-2	2020	Using lipopolysaccharide (LPS)-activated human pulmonary artery endothelial cells (HPAECs), we determined the effects of fisetin on the induction of heme oxygenase-1 (HO-1), inducible nitric oxide synthase (iNOS), and cyclooxygenase-2 (COX-2).	fisetin	121-128	heme oxygenase 1	Homo sapiens	167-171
32891672-8	2020	Furthermore, we observed that neuroprotective effects of curcumin and riluzole are mediated through Nrf2/HO-1 signaling.	Curcumin	57-65	heme oxygenase 1	Homo sapiens	105-109
32891672-8	2020	Furthermore, we observed that neuroprotective effects of curcumin and riluzole are mediated through Nrf2/HO-1 signaling.	Riluzole	70-78	heme oxygenase 1	Homo sapiens	105-109
31983246-0	2020	Thymoquinone and Curcumin combination protects cisplatin-induced Kidney Injury, Nephrotoxicity by attenuating NFkB, KIM-1 and ameliorating Nrf2/HO-1 signaling.	thymoquinone	0-12	heme oxygenase 1	Homo sapiens	144-148
31983246-0	2020	Thymoquinone and Curcumin combination protects cisplatin-induced Kidney Injury, Nephrotoxicity by attenuating NFkB, KIM-1 and ameliorating Nrf2/HO-1 signaling.	Curcumin	17-25	heme oxygenase 1	Homo sapiens	144-148
32716561-7	2020	The potentiation effect of phyllanthin seen with the three ER stressors was related to suppression of survival p-Nrf-2/HO-1 expression, resulting in increased activation of the eIF-2alpha/ATF-4/CHOP pathway.	phyllanthin	27-38	heme oxygenase 1	Homo sapiens	119-123
33012373-0	2020	Retraction Notice to "Ketamine Reduces LPS-Induced HMGB1 Through HO-1 and Nrf2/ p38 MAPK" [Journal of Surgical Research 194 (2015) 599-613].	Ketamine	22-30	heme oxygenase 1	Homo sapiens	65-69
33254548-5	2020	HO-1 is induced by hemin, a well-tolerated molecule, used for decades in the treatment of acute intermittent porphyria.	Hemin	19-24	heme oxygenase 1	Homo sapiens	0-4
33039895-11	2020	Inhibition of HO-1 overexpression in TAMs may provoke a robust anti-tumor immune response, thereby potentiating the efficacy of chemotherapy.	tams	37-41	heme oxygenase 1	Homo sapiens	14-18
32814076-0	2020	Ghrelin mitigates MPP+-induced cytotoxicity: involvement of ERK1/2-mediated Nrf2/HO-1 and endoplasmic reticulum stress PERK signaling pathway.	Ghrelin	0-7	heme oxygenase 1	Homo sapiens	81-85
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	Biliverdine	110-120	heme oxygenase 1	Homo sapiens	30-35
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	Biliverdine	139-149	heme oxygenase 1	Homo sapiens	29-45
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	Biliverdine	139-149	heme oxygenase 1	Homo sapiens	47-52
32558263-6	2020	Transcription of HMOX1 and other NFE2L2-dependent genes is increased in response to electrophilic and reactive oxygen species (ROS).	Reactive Oxygen Species	102-125	heme oxygenase 1	Homo sapiens	17-22
32558263-6	2020	Transcription of HMOX1 and other NFE2L2-dependent genes is increased in response to electrophilic and reactive oxygen species (ROS).	Reactive Oxygen Species	127-130	heme oxygenase 1	Homo sapiens	17-22
32558263-9	2020	Transcriptional induction of HMOX1 through derepression of Bach1 with cobalt protoporphyrin (CoPP) or transcriptional activation of HMOX2 by oncogenic B-RafV600E results in increased melanosphere formation.	cobaltiprotoporphyrin	70-91	heme oxygenase 1	Homo sapiens	29-34
33000859-0	2020	Madecassoside protects  retinal pigment epithelial cells against hydrogen peroxide induced oxidative stress and apoptosis through the activation of Nrf2/HO-1 pathway.	madecassoside	0-13	heme oxygenase 1	Homo sapiens	153-157
33000859-10	2020	Furthermore, H2O2-induced increase in expression levels of HO-1 and nuclear Nrf2 were enhanced by MADE treatment.	Hydrogen Peroxide	13-17	heme oxygenase 1	Homo sapiens	59-63
33000859-12	2020	In conclusion, these findings demonstrated that MADE protected ARPE-19 cells from H2O2-induced oxidative stress and apoptosis by inducing the activation of Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	82-86	heme oxygenase 1	Homo sapiens	161-165
33110194-5	2020	Growth and differentiation of cells induced by heme-albumin was dependent on heme-oxygenase 1 (HO-1) function and was accompanied with an increase of the intracellular labile iron pool (LIP).	Heme	47-51	heme oxygenase 1	Homo sapiens	77-93
33110194-5	2020	Growth and differentiation of cells induced by heme-albumin was dependent on heme-oxygenase 1 (HO-1) function and was accompanied with an increase of the intracellular labile iron pool (LIP).	Heme	47-51	heme oxygenase 1	Homo sapiens	95-99
33110194-5	2020	Growth and differentiation of cells induced by heme-albumin was dependent on heme-oxygenase 1 (HO-1) function and was accompanied with an increase of the intracellular labile iron pool (LIP).	Iron	175-179	heme oxygenase 1	Homo sapiens	95-99
33079284-6	2022	Additionally, sulforaphane increased the mRNA levels of nuclear factor erythroid-derived 2-like 2 (Nrf2) and heme oxygenase-1 (HO1), both of which mediate several cytoprotective responses.	sulforaphane	14-26	heme oxygenase 1	Homo sapiens	109-125
33079284-6	2022	Additionally, sulforaphane increased the mRNA levels of nuclear factor erythroid-derived 2-like 2 (Nrf2) and heme oxygenase-1 (HO1), both of which mediate several cytoprotective responses.	sulforaphane	14-26	heme oxygenase 1	Homo sapiens	127-130
33079284-9	2022	Interestingly, the anti-inflammatory and antioxidant effects of sulforaphane were blocked by HO1 pharmacological inhibition, suggesting its dependence on HO1 activity.	sulforaphane	64-76	heme oxygenase 1	Homo sapiens	93-96
33079284-9	2022	Interestingly, the anti-inflammatory and antioxidant effects of sulforaphane were blocked by HO1 pharmacological inhibition, suggesting its dependence on HO1 activity.	sulforaphane	64-76	heme oxygenase 1	Homo sapiens	154-157
33092263-4	2020	The proline adduct was the most active compound, it showed anti-leukemic activity, upregulated heme oxygenase 1 (HMOX1) and the primary stress-inducible isoform of the heath shock 70 kDa protein 1 (HSPA1A), and downregulated NFkB1 transcription, it was also found to be about 270 times more water soluble than dehydroleucodine.	Proline	4-11	heme oxygenase 1	Homo sapiens	95-111
33092263-4	2020	The proline adduct was the most active compound, it showed anti-leukemic activity, upregulated heme oxygenase 1 (HMOX1) and the primary stress-inducible isoform of the heath shock 70 kDa protein 1 (HSPA1A), and downregulated NFkB1 transcription, it was also found to be about 270 times more water soluble than dehydroleucodine.	Proline	4-11	heme oxygenase 1	Homo sapiens	113-118
33178028-9	2020	Moreover, UDCA promoted the expression of nuclear Nrf2, HO-1, and NQO1, although arsenic regulated nuclear translocation of Nrf2 positively.	Ursodeoxycholic Acid	10-14	heme oxygenase 1	Homo sapiens	56-60
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	Heme	29-33	heme oxygenase 1	Homo sapiens	47-52
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	29-45
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	47-52
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	ammonium ferrous sulfate	130-134	heme oxygenase 1	Homo sapiens	29-45
32558263-4	2020	Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin.	ammonium ferrous sulfate	130-134	heme oxygenase 1	Homo sapiens	47-52
33142756-8	2020	Furthermore, the mRNA levels of redox-sensitive heme oxygenase (Hmox1), catalase (Cat) and glutamate-cysteine ligase (Gclc) and the total cellular glutathione content were lower in taurine-supplemented cells than they were in the control cells.	Taurine	181-188	heme oxygenase 1	Homo sapiens	64-69
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	Heme	65-69	heme oxygenase 1	Homo sapiens	12-28
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	Heme	65-69	heme oxygenase 1	Homo sapiens	30-35
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	Carbon Monoxide	75-90	heme oxygenase 1	Homo sapiens	12-28
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	Carbon Monoxide	75-90	heme oxygenase 1	Homo sapiens	30-35
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	ferrous iron	92-104	heme oxygenase 1	Homo sapiens	12-28
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	ferrous iron	92-104	heme oxygenase 1	Homo sapiens	30-35
33066778-1	2020	BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin.	Biliverdine	110-120	heme oxygenase 1	Homo sapiens	12-28
33076330-3	2020	To identify protection strategies for ADMSCs, this study investigated the influence of the non-psychoactive phytocannabinoid cannabidiol (CBD) and the endocannabinoid analogue R(+)-methanandamide (MA) on the induction of heme oxygenase-1 (HO-1) and autophagy under serum-free conditions.	methanandamide	176-195	heme oxygenase 1	Homo sapiens	221-237
33076330-4	2020	At a concentration of 3 microM, CBD induced an upregulation of HO-1 mRNA and protein within 6 h, whereas for MA only a late and comparatively lower increase in the HO-1 protein could be detected after 48 h. In addition, both cannabinoids induced time- and concentration-dependent increases in LC3A/B-II protein, a marker of autophagy, and in metabolic activity.	Cannabidiol	32-35	heme oxygenase 1	Homo sapiens	63-67
33076330-6	2020	Similarly, knockdown of HO-1 by siRNA or inhibition of HO-1 activity by tin protoporphyrin IX (SnPPIX) had no effect on CBD-induced autophagy and metabolic activity.	tin protoporphyrin IX	72-93	heme oxygenase 1	Homo sapiens	55-59
33076330-6	2020	Similarly, knockdown of HO-1 by siRNA or inhibition of HO-1 activity by tin protoporphyrin IX (SnPPIX) had no effect on CBD-induced autophagy and metabolic activity.	tin protoporphyrin IX	95-101	heme oxygenase 1	Homo sapiens	55-59
33076330-9	2020	Remarkably, inhibition of HO-1 by SnPPIX under conditions of autophagy deficit led to a significant reversal of apoptosis in cannabinoid-treated cells.	tin protoporphyrin IX	34-40	heme oxygenase 1	Homo sapiens	26-30
33076330-9	2020	Remarkably, inhibition of HO-1 by SnPPIX under conditions of autophagy deficit led to a significant reversal of apoptosis in cannabinoid-treated cells.	Cannabinoids	125-136	heme oxygenase 1	Homo sapiens	26-30
33076330-10	2020	In conclusion, the investigated cannabinoids increase metabolic viability of ADMSCs under serum-free conditions by inducing HO-1-independent autophagy but contribute to apoptosis under conditions of additional autophagy deficit via an HO-1-dependent pathway.	Cannabinoids	32-44	heme oxygenase 1	Homo sapiens	124-128
33076330-10	2020	In conclusion, the investigated cannabinoids increase metabolic viability of ADMSCs under serum-free conditions by inducing HO-1-independent autophagy but contribute to apoptosis under conditions of additional autophagy deficit via an HO-1-dependent pathway.	Cannabinoids	32-44	heme oxygenase 1	Homo sapiens	235-239
33066365-6	2020	Exposure to low O3 concentrations down in the degradation of the explanted adipose tissue and induced a concomitant increase in the protein abundance of Nrf2 and in the expression of its target gene Hmox1.	Ozone	16-18	heme oxygenase 1	Homo sapiens	199-204
32860873-3	2020	Endogenously, CO is synthesized upon degradation of heme by heme oxygenases (HOs) of which two enzymatically active isoenzymes are known in mammals; the stress-inducible HO-1 and the constitutively expressed HO-2.	Carbon Monoxide	14-16	heme oxygenase 1	Homo sapiens	170-174
32860873-3	2020	Endogenously, CO is synthesized upon degradation of heme by heme oxygenases (HOs) of which two enzymatically active isoenzymes are known in mammals; the stress-inducible HO-1 and the constitutively expressed HO-2.	Heme	52-56	heme oxygenase 1	Homo sapiens	170-174
33081396-0	2020	Calcium Ionophore-Induced Extracellular Vesicles Mediate Cytoprotection against Simulated Ischemia/Reperfusion Injury in Cardiomyocyte-Derived Cell Lines by Inducing Heme Oxygenase 1.	Calcium	0-7	heme oxygenase 1	Homo sapiens	166-182
33081396-10	2020	Calcium ionophore-induced EVs exert cytoprotection by inducing HO-1 in a TLR4-independent manner.	Calcium	0-7	heme oxygenase 1	Homo sapiens	63-67
32860873-4	2020	Among other pathways, HO-1 expression is stimulated by the Nrf2/Keap1 system which senses electrophilic compounds including alkylating agents and reactive oxygen species (ROS) such as superoxide or hydrogen peroxide.	Reactive Oxygen Species	146-169	heme oxygenase 1	Homo sapiens	22-26
33053761-7	2020	Geraniol treatment also activated the Keap1/Nrf2/heme oxygenase-1 (HO-1) pathway, increased antioxidant enzyme activities, modulated the PI3K/Akt/mTOR pathway, and ameliorated myocardial autophagy, inflammation, and apoptosis.	geraniol	0-8	heme oxygenase 1	Homo sapiens	49-65
32860873-4	2020	Among other pathways, HO-1 expression is stimulated by the Nrf2/Keap1 system which senses electrophilic compounds including alkylating agents and reactive oxygen species (ROS) such as superoxide or hydrogen peroxide.	Reactive Oxygen Species	171-174	heme oxygenase 1	Homo sapiens	22-26
32860873-4	2020	Among other pathways, HO-1 expression is stimulated by the Nrf2/Keap1 system which senses electrophilic compounds including alkylating agents and reactive oxygen species (ROS) such as superoxide or hydrogen peroxide.	Superoxides	184-194	heme oxygenase 1	Homo sapiens	22-26
32860873-4	2020	Among other pathways, HO-1 expression is stimulated by the Nrf2/Keap1 system which senses electrophilic compounds including alkylating agents and reactive oxygen species (ROS) such as superoxide or hydrogen peroxide.	Hydrogen Peroxide	198-215	heme oxygenase 1	Homo sapiens	22-26
32860873-5	2020	In context with ROS, HO-1 expression has been associated with antioxidant defense related to the heme-metabolite redox pair biliverdin/bilirubin.	Reactive Oxygen Species	16-19	heme oxygenase 1	Homo sapiens	21-25
32860873-5	2020	In context with ROS, HO-1 expression has been associated with antioxidant defense related to the heme-metabolite redox pair biliverdin/bilirubin.	Heme	97-101	heme oxygenase 1	Homo sapiens	21-25
32860873-5	2020	In context with ROS, HO-1 expression has been associated with antioxidant defense related to the heme-metabolite redox pair biliverdin/bilirubin.	Biliverdine	124-134	heme oxygenase 1	Homo sapiens	21-25
32860873-5	2020	In context with ROS, HO-1 expression has been associated with antioxidant defense related to the heme-metabolite redox pair biliverdin/bilirubin.	Bilirubin	135-144	heme oxygenase 1	Homo sapiens	21-25
32866568-4	2020	Arsenite stimulated an oxidative stress response as detected by Nrf-2 nuclear accumulation and induction of HMOX-1 and NQO1, which was not detected with up to 30 muM uranyl acetate.	arsenite	0-8	heme oxygenase 1	Homo sapiens	108-114
33053761-7	2020	Geraniol treatment also activated the Keap1/Nrf2/heme oxygenase-1 (HO-1) pathway, increased antioxidant enzyme activities, modulated the PI3K/Akt/mTOR pathway, and ameliorated myocardial autophagy, inflammation, and apoptosis.	geraniol	0-8	heme oxygenase 1	Homo sapiens	67-71
32745467-8	2020	In addition, suppressive effects of gAcrp on ROS production and NADPH oxidase activation, both of which critically contribute to leptin-induced inflammasomes activation, disappeared by inhibition of HO-1 signaling.	gacrp	36-41	heme oxygenase 1	Homo sapiens	199-203
33023074-6	2020	Pretreatment with LY294002 (Akt inhibitor) and PD980559 (ERK inhibitor) inhibited LPS-induced Nrf2 nuclear translocation and HO-1 protein expression in ELF-EMF-exposed cells.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	18-26	heme oxygenase 1	Homo sapiens	125-129
33023074-6	2020	Pretreatment with LY294002 (Akt inhibitor) and PD980559 (ERK inhibitor) inhibited LPS-induced Nrf2 nuclear translocation and HO-1 protein expression in ELF-EMF-exposed cells.	pd980559	47-55	heme oxygenase 1	Homo sapiens	125-129
32745467-11	2020	In summary, treatment with gAcrp prevents leptin-induced cancer cell growth by modulating inflammasome activation, which is mediated, at least in part, via HO-1 induction and modulation of ER-alpha signaling.	gacrp	27-32	heme oxygenase 1	Homo sapiens	156-160
33155244-12	2020	The activity of the NRF2/HO-1 pathway was inhibited by miR-34a-5p, possibly via FOXM1.	mir-34a-5p	55-65	heme oxygenase 1	Homo sapiens	25-29
33155244-13	2020	CONCLUSIONS: MiR-34a-5p inhibition attenuates LPS-induced EC injury by targeting FOXM1 via activation of the NRF2/HO-1 pathway.	mir-34a-5p	13-23	heme oxygenase 1	Homo sapiens	114-118
32897647-0	2020	miR-141-3p inhibits vascular smooth muscle cell proliferation and migration via regulating Keap1/Nrf2/HO-1 pathway.	mir-141-3p	0-10	heme oxygenase 1	Homo sapiens	102-106
32945449-10	2020	Treatment with zinc protoporphyrin-9, a specific inhibitor of heme oxygenase-1 (HO-1), markedly attenuated the cell death induced by MI-463 plus auranofin.	zinc protoporphyrin	15-36	heme oxygenase 1	Homo sapiens	62-78
32945449-10	2020	Treatment with zinc protoporphyrin-9, a specific inhibitor of heme oxygenase-1 (HO-1), markedly attenuated the cell death induced by MI-463 plus auranofin.	zinc protoporphyrin	15-36	heme oxygenase 1	Homo sapiens	80-84
32945449-10	2020	Treatment with zinc protoporphyrin-9, a specific inhibitor of heme oxygenase-1 (HO-1), markedly attenuated the cell death induced by MI-463 plus auranofin.	Auranofin	145-154	heme oxygenase 1	Homo sapiens	62-78
32945449-10	2020	Treatment with zinc protoporphyrin-9, a specific inhibitor of heme oxygenase-1 (HO-1), markedly attenuated the cell death induced by MI-463 plus auranofin.	Auranofin	145-154	heme oxygenase 1	Homo sapiens	80-84
32945449-12	2020	In addition, the potent induction of HO-1 contributed to the synergistic effects of MI-463 plus auranofin.	Auranofin	96-105	heme oxygenase 1	Homo sapiens	37-41
32897647-11	2020	miR-141-3p also inhibited the expressions of IL-6, IL-beta, TNF-alpha and Keap1 but promoted the expressions of Nrf2 and HO-1.	mir-141-3p	0-10	heme oxygenase 1	Homo sapiens	121-125
32897647-13	2020	miR-141-3p is down-regulated during AS, and it can alleviate VSMCs" dysfunction by targeting the Keap1/Nrf2/HO-1 axis.	mir-141-3p	0-10	heme oxygenase 1	Homo sapiens	108-112
32712291-6	2020	In addition, hemistepsin A markedly promoted the activation of nuclear factor-erythroid-2-related factor 2 (Nrf2), which was associated with the enhanced expression and activity of heme oxygenase-1 (HO-1) in the presence of 500 muM H2O2.	Hydrogen Peroxide	232-236	heme oxygenase 1	Homo sapiens	181-197
32602595-5	2020	HG stimulation-caused the decrease in the expression levels of p-Akt, nuclear Nrf2, and HO-1 was elevated after spiraeoside treatment in AC16 cells.	Mercury	0-2	heme oxygenase 1	Homo sapiens	88-92
32602595-5	2020	HG stimulation-caused the decrease in the expression levels of p-Akt, nuclear Nrf2, and HO-1 was elevated after spiraeoside treatment in AC16 cells.	spiraeoside	112-123	heme oxygenase 1	Homo sapiens	88-92
32128811-5	2020	We found that BRUP-1 up-regulated the expression level of heme oxygenase-1 (HO-1), one of the rate-limiting enzyme of bilirubin production via nuclear factor erythroid 2-related factor 2 (Nrf2) activation.	Bilirubin	118-127	heme oxygenase 1	Homo sapiens	58-74
32128811-5	2020	We found that BRUP-1 up-regulated the expression level of heme oxygenase-1 (HO-1), one of the rate-limiting enzyme of bilirubin production via nuclear factor erythroid 2-related factor 2 (Nrf2) activation.	Bilirubin	118-127	heme oxygenase 1	Homo sapiens	76-80
33001278-0	2020	The DPP-IV inhibitor saxagliptin promotes the migration and invasion of papillary thyroid carcinoma cells via the NRF2/HO1 pathway.	saxagliptin	21-32	heme oxygenase 1	Homo sapiens	119-122
32707369-19	2020	SCDG medicated serum promoted protein expressions of nuclear Nrf2 and total HO-1, and inhibited translocation of p65.	scdg	0-4	heme oxygenase 1	Homo sapiens	76-80
33001278-17	2020	Saxagliptin enhanced the migratory and invasive ability of human thyroid carcinoma cells, as well as the expression of MMP2 and VEGF, by activating the NRF2/HO1 pathway.	saxagliptin	0-11	heme oxygenase 1	Homo sapiens	157-160
32712291-6	2020	In addition, hemistepsin A markedly promoted the activation of nuclear factor-erythroid-2-related factor 2 (Nrf2), which was associated with the enhanced expression and activity of heme oxygenase-1 (HO-1) in the presence of 500 muM H2O2.	Hydrogen Peroxide	232-236	heme oxygenase 1	Homo sapiens	199-203
33134292-0	2020	Celecoxib Exerts Neuroprotective Effects in beta-Amyloid-Treated SH-SY5Y Cells Through the Regulation of Heme Oxygenase-1: Novel Insights for an Old Drug.	Celecoxib	0-9	heme oxygenase 1	Homo sapiens	105-121
33134292-5	2020	Both sAbeta (6.25-50 nM) and fAbeta (1.25-50 nM) dose-dependently over-expressed inducible HO (HO-1) after 24 h of incubation, reaching statistical significance at 25 and 6.25 nM, respectively.	sabeta	5-11	heme oxygenase 1	Homo sapiens	95-99
32993497-3	2020	H2S release is triggered by carbon monoxide (CO) from the catabolism of heme by inducible heme oxygenase (HO-1) and heme proteins possess catalytic activity necessary for the H2S signalling by protein persulfidation.	Deuterium	0-3	heme oxygenase 1	Homo sapiens	106-110
32993497-3	2020	H2S release is triggered by carbon monoxide (CO) from the catabolism of heme by inducible heme oxygenase (HO-1) and heme proteins possess catalytic activity necessary for the H2S signalling by protein persulfidation.	Carbon Monoxide	28-43	heme oxygenase 1	Homo sapiens	106-110
32993497-3	2020	H2S release is triggered by carbon monoxide (CO) from the catabolism of heme by inducible heme oxygenase (HO-1) and heme proteins possess catalytic activity necessary for the H2S signalling by protein persulfidation.	Carbon Monoxide	45-47	heme oxygenase 1	Homo sapiens	106-110
32993497-3	2020	H2S release is triggered by carbon monoxide (CO) from the catabolism of heme by inducible heme oxygenase (HO-1) and heme proteins possess catalytic activity necessary for the H2S signalling by protein persulfidation.	Heme	72-76	heme oxygenase 1	Homo sapiens	106-110
32993497-3	2020	H2S release is triggered by carbon monoxide (CO) from the catabolism of heme by inducible heme oxygenase (HO-1) and heme proteins possess catalytic activity necessary for the H2S signalling by protein persulfidation.	Deuterium	175-178	heme oxygenase 1	Homo sapiens	106-110
32993497-9	2020	Finally, an array of therapeutic interventions with the potential to clinically modulate the HO-1/CO/H2S axis is already available or under development.	Carbon Monoxide	98-100	heme oxygenase 1	Homo sapiens	93-97
32993497-9	2020	Finally, an array of therapeutic interventions with the potential to clinically modulate the HO-1/CO/H2S axis is already available or under development.	Deuterium	101-104	heme oxygenase 1	Homo sapiens	93-97
33134292-5	2020	Both sAbeta (6.25-50 nM) and fAbeta (1.25-50 nM) dose-dependently over-expressed inducible HO (HO-1) after 24 h of incubation, reaching statistical significance at 25 and 6.25 nM, respectively.	fabeta	29-35	heme oxygenase 1	Homo sapiens	95-99
33134292-7	2020	Furthermore, 10 muM CXB counteracted the Abeta-induced ROS production with a mechanism fully dependent on HO-1 up-regulation; nevertheless, 10 muM CXB significantly counteracted only 25 nM sAbeta-induced lipid peroxidation damage in SH-SY5Y neurons by modulating HO-1.	Celecoxib	20-23	heme oxygenase 1	Homo sapiens	106-110
33134292-7	2020	Furthermore, 10 muM CXB counteracted the Abeta-induced ROS production with a mechanism fully dependent on HO-1 up-regulation; nevertheless, 10 muM CXB significantly counteracted only 25 nM sAbeta-induced lipid peroxidation damage in SH-SY5Y neurons by modulating HO-1.	Celecoxib	20-23	heme oxygenase 1	Homo sapiens	263-267
33134292-7	2020	Furthermore, 10 muM CXB counteracted the Abeta-induced ROS production with a mechanism fully dependent on HO-1 up-regulation; nevertheless, 10 muM CXB significantly counteracted only 25 nM sAbeta-induced lipid peroxidation damage in SH-SY5Y neurons by modulating HO-1.	Celecoxib	147-150	heme oxygenase 1	Homo sapiens	263-267
33134292-7	2020	Furthermore, 10 muM CXB counteracted the Abeta-induced ROS production with a mechanism fully dependent on HO-1 up-regulation; nevertheless, 10 muM CXB significantly counteracted only 25 nM sAbeta-induced lipid peroxidation damage in SH-SY5Y neurons by modulating HO-1.	sabeta	189-195	heme oxygenase 1	Homo sapiens	263-267
32968051-0	2020	Heme oxygenase 1 protects human colonocytes against ROS formation, oxidative DNA damage and cytotoxicity induced by heme iron, but not inorganic iron.	Reactive Oxygen Species	52-55	heme oxygenase 1	Homo sapiens	0-16
32992548-9	2020	In conclusion, MG inhibited hepatic steatosis-induced NLRP3 inflammasome activation through the restoration of autophagy to promote HO-1 signaling capable of ameliorating oxidative stress and inflammatory responses.	magnolol	15-17	heme oxygenase 1	Homo sapiens	132-136
32992548-0	2020	Involvement of HO-1 and Autophagy in the Protective Effect of Magnolol in Hepatic Steatosis-Induced NLRP3 Inflammasome Activation In Vivo and In Vitro.	magnolol	62-70	heme oxygenase 1	Homo sapiens	15-19
32968051-11	2020	Chemical inhibition or genetic knockdown of HO-1 potentiated hemin-triggered ROS generation and oxidative DNA damage preferentially in HCEC.	Hemin	61-66	heme oxygenase 1	Homo sapiens	44-48
32968051-0	2020	Heme oxygenase 1 protects human colonocytes against ROS formation, oxidative DNA damage and cytotoxicity induced by heme iron, but not inorganic iron.	Heme	116-120	heme oxygenase 1	Homo sapiens	0-16
32968051-11	2020	Chemical inhibition or genetic knockdown of HO-1 potentiated hemin-triggered ROS generation and oxidative DNA damage preferentially in HCEC.	Reactive Oxygen Species	77-80	heme oxygenase 1	Homo sapiens	44-48
32968051-0	2020	Heme oxygenase 1 protects human colonocytes against ROS formation, oxidative DNA damage and cytotoxicity induced by heme iron, but not inorganic iron.	Iron	121-125	heme oxygenase 1	Homo sapiens	0-16
32968051-12	2020	Furthermore, HO-1 abrogation strongly augmented the cytotoxic effects of hemin in HCEC, revealing its pivotal function in colonocytes and highlighting the toxicity of free intracellular heme iron.	Hemin	73-78	heme oxygenase 1	Homo sapiens	13-17
32968051-12	2020	Furthermore, HO-1 abrogation strongly augmented the cytotoxic effects of hemin in HCEC, revealing its pivotal function in colonocytes and highlighting the toxicity of free intracellular heme iron.	Heme	186-190	heme oxygenase 1	Homo sapiens	13-17
32968051-9	2020	Hemin caused stabilization and nuclear translocation of Nrf2, which induced heme oxygenase-1 (HO-1) and ferritin heavy chain (FtH).	Hemin	0-5	heme oxygenase 1	Homo sapiens	76-92
32968051-12	2020	Furthermore, HO-1 abrogation strongly augmented the cytotoxic effects of hemin in HCEC, revealing its pivotal function in colonocytes and highlighting the toxicity of free intracellular heme iron.	Iron	191-195	heme oxygenase 1	Homo sapiens	13-17
32968051-9	2020	Hemin caused stabilization and nuclear translocation of Nrf2, which induced heme oxygenase-1 (HO-1) and ferritin heavy chain (FtH).	Hemin	0-5	heme oxygenase 1	Homo sapiens	94-98
32968051-14	2020	Importantly, HO-1 conferred protection against the detrimental effects of hemin.	Hemin	74-79	heme oxygenase 1	Homo sapiens	13-17
32967203-12	2020	Our results indicate that piperine may be an effective molecule for the prophylactic treatment of colon carcinogenesis by targeting the NF-kappaB/Nrf-2/Keap-1/HO-1 pathway as a progressive strategy in the preclusion and effective treatment of colorectal cancer.	piperine	26-34	heme oxygenase 1	Homo sapiens	159-163
32971746-1	2020	Heme oxygenase-1 is induced by many cellular stressors and catalyzes the breakdown of heme to generate carbon monoxide and bilirubin, which confer cytoprotection.	Heme	86-90	heme oxygenase 1	Homo sapiens	0-16
32971746-1	2020	Heme oxygenase-1 is induced by many cellular stressors and catalyzes the breakdown of heme to generate carbon monoxide and bilirubin, which confer cytoprotection.	Carbon Monoxide	103-118	heme oxygenase 1	Homo sapiens	0-16
32971746-1	2020	Heme oxygenase-1 is induced by many cellular stressors and catalyzes the breakdown of heme to generate carbon monoxide and bilirubin, which confer cytoprotection.	Bilirubin	123-132	heme oxygenase 1	Homo sapiens	0-16
32971746-8	2020	Our results suggest that regulation of heme may be an equally significant role of HO-1.	Heme	39-43	heme oxygenase 1	Homo sapiens	82-86
32967203-9	2020	We found that piperine inhibited NF-kappaB by the activation of Nrf-2, blocking downstream inflammatory mediators/cytokines (TNF-alpha, IL-6, IL-1beta, Cox-2, PGE-2, iNOS, NO, MPO), triggering an antioxidant response machinery (HO-1, NQO-1, GSH, GR, GPx, CAT, SOD), scavenging ROS, and decreasing lipid peroxidation.	piperine	14-22	heme oxygenase 1	Homo sapiens	228-232
32553625-8	2020	We also found that DMF inhibited the extracellular release of high mobility group box 1, associated with an up-regulation of heme oxygenase-1, likely mediated through Nrf2 activation.	Dimethyl Fumarate	19-22	heme oxygenase 1	Homo sapiens	125-141
32615411-0	2020	Nrf2/HO-1 partially regulates cytoprotective effects of carbon monoxide against urban particulate matter-induced inflammatory responses in oral keratinocytes.	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	5-9
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	Heme	73-77	heme oxygenase 1	Homo sapiens	0-16
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	Heme	73-77	heme oxygenase 1	Homo sapiens	18-22
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	Biliverdine	81-91	heme oxygenase 1	Homo sapiens	0-16
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	Biliverdine	81-91	heme oxygenase 1	Homo sapiens	18-22
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	0-16
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	18-22
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	ferrous iron	118-130	heme oxygenase 1	Homo sapiens	0-16
32880973-1	2021	Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders.	ferrous iron	118-130	heme oxygenase 1	Homo sapiens	18-22
32611235-2	2020	In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes.	Heme	31-35	heme oxygenase 1	Homo sapiens	208-224
32611235-2	2020	In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes.	Heme	31-35	heme oxygenase 1	Homo sapiens	226-231
32611235-2	2020	In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes.	Heme	31-35	heme oxygenase 1	Homo sapiens	233-237
32611235-2	2020	In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes.	Adenosine	49-58	heme oxygenase 1	Homo sapiens	208-224
32611235-2	2020	In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes.	Adenosine	49-58	heme oxygenase 1	Homo sapiens	226-231
32611235-2	2020	In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes.	Adenosine	49-58	heme oxygenase 1	Homo sapiens	233-237
32913257-5	2020	Methylglyoxal treatment also significantly decreased the mRNA expression of the slit diaphragm markers ZO-1 and NEPH1 and significantly increased the mRNA expression of the oxidative stress marker HO-1.	Pyruvaldehyde	0-13	heme oxygenase 1	Homo sapiens	197-201
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Carbon Monoxide	63-78	heme oxygenase 1	Homo sapiens	0-16
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Carbon Monoxide	63-78	heme oxygenase 1	Homo sapiens	18-22
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Carbon Monoxide	80-82	heme oxygenase 1	Homo sapiens	0-16
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Carbon Monoxide	80-82	heme oxygenase 1	Homo sapiens	18-22
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Iron	85-89	heme oxygenase 1	Homo sapiens	0-16
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Iron	85-89	heme oxygenase 1	Homo sapiens	18-22
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	0-16
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	18-22
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Bilirubin	139-148	heme oxygenase 1	Homo sapiens	0-16
32899732-1	2020	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin.	Bilirubin	139-148	heme oxygenase 1	Homo sapiens	18-22
32899732-4	2020	The vasoprotection evoked by HO-1 is largely ascribed to the generation of CO and/or the bile pigments, biliverdin and bilirubin, which exert potent antioxidant and anti-inflammatory effects.	Carbon Monoxide	75-77	heme oxygenase 1	Homo sapiens	29-33
32899732-4	2020	The vasoprotection evoked by HO-1 is largely ascribed to the generation of CO and/or the bile pigments, biliverdin and bilirubin, which exert potent antioxidant and anti-inflammatory effects.	Biliverdine	104-114	heme oxygenase 1	Homo sapiens	29-33
32899732-4	2020	The vasoprotection evoked by HO-1 is largely ascribed to the generation of CO and/or the bile pigments, biliverdin and bilirubin, which exert potent antioxidant and anti-inflammatory effects.	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	29-33
32899732-6	2020	Several therapeutic strategies are currently being pursued that may allow for the targeting of HO-1 in arterial remodeling in various pathologies, including the use of gene delivery approaches, the development of novel inducers of the enzyme, and the administration of unique formulations of CO and bilirubin.	Carbon Monoxide	292-294	heme oxygenase 1	Homo sapiens	95-99
32899732-6	2020	Several therapeutic strategies are currently being pursued that may allow for the targeting of HO-1 in arterial remodeling in various pathologies, including the use of gene delivery approaches, the development of novel inducers of the enzyme, and the administration of unique formulations of CO and bilirubin.	Bilirubin	299-308	heme oxygenase 1	Homo sapiens	95-99
32574971-7	2020	The underlying mechanisms of monotropein on alleviating cisplatin-induced AKI were associated with the activation of Nrf2/HO-1 pathway against oxidative stress and the inhibition on NF-kappaB signaling to suppress inflammation as well as the regulation on the expressions of proteins in apoptosis pathway in this renal injury model.	Cisplatin	56-65	heme oxygenase 1	Homo sapiens	122-126
32500379-3	2020	Additionally, COVID-19"s heme reduction may contribute to even lower HO-1.	Heme	25-29	heme oxygenase 1	Homo sapiens	69-73
32500379-9	2020	Therapies with anti-viral properties that raise HO-1 include certain anesthetics (sevoflurane or isoflurane), hemin, estrogen, statins, curcumin, resveratrol, and melatonin.	Sevoflurane	82-93	heme oxygenase 1	Homo sapiens	48-52
32500379-9	2020	Therapies with anti-viral properties that raise HO-1 include certain anesthetics (sevoflurane or isoflurane), hemin, estrogen, statins, curcumin, resveratrol, and melatonin.	Isoflurane	97-107	heme oxygenase 1	Homo sapiens	48-52
32500379-9	2020	Therapies with anti-viral properties that raise HO-1 include certain anesthetics (sevoflurane or isoflurane), hemin, estrogen, statins, curcumin, resveratrol, and melatonin.	Curcumin	136-144	heme oxygenase 1	Homo sapiens	48-52
32500379-9	2020	Therapies with anti-viral properties that raise HO-1 include certain anesthetics (sevoflurane or isoflurane), hemin, estrogen, statins, curcumin, resveratrol, and melatonin.	Resveratrol	146-157	heme oxygenase 1	Homo sapiens	48-52
32500379-9	2020	Therapies with anti-viral properties that raise HO-1 include certain anesthetics (sevoflurane or isoflurane), hemin, estrogen, statins, curcumin, resveratrol, and melatonin.	Melatonin	163-172	heme oxygenase 1	Homo sapiens	48-52
32293791-0	2020	Emodin protected against synaptic impairment and oxidative stress induced by fluoride in SH-SY5Y cells by modulating ERK1/2/Nrf2/HO-1 pathway.	Emodin	0-6	heme oxygenase 1	Homo sapiens	129-133
32293791-0	2020	Emodin protected against synaptic impairment and oxidative stress induced by fluoride in SH-SY5Y cells by modulating ERK1/2/Nrf2/HO-1 pathway.	Fluorides	77-85	heme oxygenase 1	Homo sapiens	129-133
32615411-3	2020	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	78-94
32615411-3	2020	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	96-100
32615411-3	2020	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	78-94
32615411-3	2020	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	96-100
32615411-3	2020	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant.	Heme	34-38	heme oxygenase 1	Homo sapiens	78-94
32615411-3	2020	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant.	Heme	34-38	heme oxygenase 1	Homo sapiens	96-100
32347305-11	2020	OUTCOMES: HO-1 exerts some protective effects on the placentation, probably by a combination of factors, including its interrelation with the PGC-1alpha/PPAR pathway and the sFlt1/PlGF balance, and through its primary metabolites, notably carbon monoxide and bilirubin.	Carbon Monoxide	239-254	heme oxygenase 1	Homo sapiens	10-14
31830562-4	2020	Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin.	Carbon Dioxide	141-143	heme oxygenase 1	Homo sapiens	47-63
31830562-4	2020	Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin.	Carbon Dioxide	141-143	heme oxygenase 1	Homo sapiens	65-69
31830562-4	2020	Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin.	Biliverdine	145-155	heme oxygenase 1	Homo sapiens	47-63
31830562-4	2020	Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin.	Biliverdine	145-155	heme oxygenase 1	Homo sapiens	65-69
31830562-4	2020	Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin.	Bilirubin	160-169	heme oxygenase 1	Homo sapiens	47-63
31830562-4	2020	Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin.	Bilirubin	160-169	heme oxygenase 1	Homo sapiens	65-69
32347305-11	2020	OUTCOMES: HO-1 exerts some protective effects on the placentation, probably by a combination of factors, including its interrelation with the PGC-1alpha/PPAR pathway and the sFlt1/PlGF balance, and through its primary metabolites, notably carbon monoxide and bilirubin.	Bilirubin	259-268	heme oxygenase 1	Homo sapiens	10-14
32940965-1	2020	BACKGROUND: Tin protoporphyrin (SnPP), a heme oxygenase 1 (HO-1) inhibitor, triggers adaptive tissue responses that confer potent protection against acute renal- and extra-renal tissue injuries.	tin protoporphyrin IX	12-30	heme oxygenase 1	Homo sapiens	41-57
32540488-9	2020	Moreover, the nuclear factor erythoid 2-related 2 (Nrf2) and HO-1 expression were lower in 3% DSS+ Ferr-1 group than 3% DSS group (P < 0.05).	Dextran Sulfate	94-97	heme oxygenase 1	Homo sapiens	61-65
32540488-10	2020	These data revealed that suppressing ferroptosis could effectively ameliorate DSS-induced UC involved in blocking Nrf2/HO-1 signaling pathway.	Dextran Sulfate	78-81	heme oxygenase 1	Homo sapiens	119-123
32782567-0	2020	Enhancement of piperlongumine chemosensitivity by silencing heme oxygenase-1 expression in cholangiocarcinoma cell lines.	piperlonguminine	15-29	heme oxygenase 1	Homo sapiens	60-76
32782567-3	2020	The aim of the present study was to investigate the molecular mechanisms of PL-induced heme oxygenase-1 (HO-1) expression in CCA cell lines.	piperlonguminine	76-78	heme oxygenase 1	Homo sapiens	87-103
32782567-3	2020	The aim of the present study was to investigate the molecular mechanisms of PL-induced heme oxygenase-1 (HO-1) expression in CCA cell lines.	piperlonguminine	76-78	heme oxygenase 1	Homo sapiens	105-109
32782567-10	2020	Dose-dependent upregulation of HO-1 expression via PI3K/Akt activation was detected in PL-treated CCA cells.	piperlonguminine	87-89	heme oxygenase 1	Homo sapiens	31-35
32782567-11	2020	Inhibition of HO-1 eliminated the antioxidant defense mechanisms, leading to increased anti-cancer activity of PL in the CCA cell lines via an increase in intracellular ROS levels and apoptotic protein expression.	piperlonguminine	111-113	heme oxygenase 1	Homo sapiens	14-18
32782567-11	2020	Inhibition of HO-1 eliminated the antioxidant defense mechanisms, leading to increased anti-cancer activity of PL in the CCA cell lines via an increase in intracellular ROS levels and apoptotic protein expression.	Reactive Oxygen Species	169-172	heme oxygenase 1	Homo sapiens	14-18
32782567-12	2020	These observations indicated that HO-1 inhibition had a chemosensitizing effect on CCA to PL.	piperlonguminine	90-92	heme oxygenase 1	Homo sapiens	34-38
32540488-0	2020	Ferroptosis mediated DSS-induced ulcerative colitis associated with Nrf2/HO-1 signaling pathway.	Dextran Sulfate	21-24	heme oxygenase 1	Homo sapiens	73-77
32645628-0	2020	DL0410 attenuates oxidative stress and neuroinflammation via BDNF/TrkB/ERK/CREB and Nrf2/HO-1 activation.	DL0410	0-6	heme oxygenase 1	Homo sapiens	89-93
32940965-1	2020	BACKGROUND: Tin protoporphyrin (SnPP), a heme oxygenase 1 (HO-1) inhibitor, triggers adaptive tissue responses that confer potent protection against acute renal- and extra-renal tissue injuries.	tin protoporphyrin IX	12-30	heme oxygenase 1	Homo sapiens	59-63
32940965-1	2020	BACKGROUND: Tin protoporphyrin (SnPP), a heme oxygenase 1 (HO-1) inhibitor, triggers adaptive tissue responses that confer potent protection against acute renal- and extra-renal tissue injuries.	S-Nitroso-N-propionyl-D,L-penicillamine	32-36	heme oxygenase 1	Homo sapiens	41-57
32940965-1	2020	BACKGROUND: Tin protoporphyrin (SnPP), a heme oxygenase 1 (HO-1) inhibitor, triggers adaptive tissue responses that confer potent protection against acute renal- and extra-renal tissue injuries.	S-Nitroso-N-propionyl-D,L-penicillamine	32-36	heme oxygenase 1	Homo sapiens	59-63
32150044-12	2020	Dual inhibition of both miR-24-3p and miR-145-5p prior to hypoxia-reoxygenation caused significant upregulation of SOD2 and HMOX1 protein; fold-change of 3.17 (p<=0.05) and 6.97 (p<=0.05) respectively.	mir-24-3p	24-33	heme oxygenase 1	Homo sapiens	124-129
32506039-4	2020	In keratinocytes, DHA-exposure performed at low millimolar concentrations did not impair viability while causing a pronounced cellular stress response as obvious from rapid activation of phospho-protein signal transduction [p-p38, p-Hsp27(S15/S78), p-eIF2alpha] and gene expression changes (HSPA6, HMOX1, CRYAB, CCL3), not observable upon exposure to the non-ketose, tanning-inactive DHA-control glycerol.	Dihydroxyacetone	18-21	heme oxygenase 1	Homo sapiens	298-303
32506039-6	2020	In human epidermal reconstructs a topical use-relevant DHA-dose regimen elicited a comparable stress response as revealed by gene expression array (HSPA1A, HSPA6, HSPD1, IL6, DDIT3, EGR1) and immunohistochemical analysis (CEL, HO-1, p-Hsp27-S78).	Dihydroxyacetone	55-58	heme oxygenase 1	Homo sapiens	227-231
32828015-6	2020	In addition, the leukocytes from people with HIV with CWP had attenuated levels of the heme metabolizing enzyme, heme oxygenase-1, which metabolizes free heme to carbon-monoxide and biliverdin.	Heme	87-91	heme oxygenase 1	Homo sapiens	113-129
32828015-6	2020	In addition, the leukocytes from people with HIV with CWP had attenuated levels of the heme metabolizing enzyme, heme oxygenase-1, which metabolizes free heme to carbon-monoxide and biliverdin.	Carbon Monoxide	162-177	heme oxygenase 1	Homo sapiens	113-129
32828015-6	2020	In addition, the leukocytes from people with HIV with CWP had attenuated levels of the heme metabolizing enzyme, heme oxygenase-1, which metabolizes free heme to carbon-monoxide and biliverdin.	Biliverdine	182-192	heme oxygenase 1	Homo sapiens	113-129
32982786-5	2020	HO-1 and HO-2 catalyze the rate-limiting step of cellular heme degradation and, similar to SirT1, HO-1 exerts beneficial effects in the vasculature through the activation of anti-oxidant, anti-inflammatory, anti-apoptotic, and anti-proliferative signaling pathways.	Heme	58-62	heme oxygenase 1	Homo sapiens	0-4
32982732-0	2020	Jian-Pi-Bu-Xue-Formula Alleviates Cyclophosphamide-Induced Myelosuppression via Up-Regulating NRF2/HO1/NQO1 Signaling.	jian-pi-bu-xue	0-14	heme oxygenase 1	Homo sapiens	99-102
32982732-0	2020	Jian-Pi-Bu-Xue-Formula Alleviates Cyclophosphamide-Induced Myelosuppression via Up-Regulating NRF2/HO1/NQO1 Signaling.	Cyclophosphamide	34-50	heme oxygenase 1	Homo sapiens	99-102
32854434-0	2020	Cudratricusxanthone O Inhibits H2O2-Induced Cell Damage by Activating Nrf2/HO-1 Pathway in Human Chondrocytes.	cudratricusxanthone	0-19	heme oxygenase 1	Homo sapiens	75-79
32854434-0	2020	Cudratricusxanthone O Inhibits H2O2-Induced Cell Damage by Activating Nrf2/HO-1 Pathway in Human Chondrocytes.	Hydrogen Peroxide	31-35	heme oxygenase 1	Homo sapiens	75-79
32854434-2	2020	Although induced-heme oxygenase-1 (HO-1) has been found to protect cells against oxygen radical damage, little information is available regarding the use of bioactive compounds from natural sources for regulating the HO-1 pathway to treat OA.	Oxygen	22-28	heme oxygenase 1	Homo sapiens	35-39
32854434-3	2020	In this study, we explored the inhibitory effects of cudratricusxanthone O (CTO) isolated from the Maclura tricuspidata Bureau (Moraceae) on H2O2-induced damage of SW1353 chondrocytes via regulation of the HO-1 pathway.	cudratricusxanthone o	53-74	heme oxygenase 1	Homo sapiens	206-210
32854434-3	2020	In this study, we explored the inhibitory effects of cudratricusxanthone O (CTO) isolated from the Maclura tricuspidata Bureau (Moraceae) on H2O2-induced damage of SW1353 chondrocytes via regulation of the HO-1 pathway.	cto	76-79	heme oxygenase 1	Homo sapiens	206-210
32854434-7	2020	Treatment with the HO-1 inhibitor tin-protoporphyrin IX revealed that these protective effects were exerted due to an increase in HO-1 expression induced by CTO.	tin protoporphyrin IX	34-55	heme oxygenase 1	Homo sapiens	19-23
32908872-0	2020	Retracted: Involvement of Nrf2-Mediated Upregulation of Heme Oxygenase-1 in Mollugin-Induced Growth Inhibition and Apoptosis in Human Oral Cancer Cells.	rubimaillin	76-84	heme oxygenase 1	Homo sapiens	56-72
32854434-7	2020	Treatment with the HO-1 inhibitor tin-protoporphyrin IX revealed that these protective effects were exerted due to an increase in HO-1 expression induced by CTO.	tin protoporphyrin IX	34-55	heme oxygenase 1	Homo sapiens	130-134
32854434-7	2020	Treatment with the HO-1 inhibitor tin-protoporphyrin IX revealed that these protective effects were exerted due to an increase in HO-1 expression induced by CTO.	cto	157-160	heme oxygenase 1	Homo sapiens	19-23
32854434-7	2020	Treatment with the HO-1 inhibitor tin-protoporphyrin IX revealed that these protective effects were exerted due to an increase in HO-1 expression induced by CTO.	cto	157-160	heme oxygenase 1	Homo sapiens	130-134
32842569-7	2020	Besides, BA downregulated the phosphorylation of the p38, JNK, and ERK proteins, while it upregulated the expression of the Nrf2 and HO-1 proteins in thymus tissues.	betulinic acid	9-11	heme oxygenase 1	Homo sapiens	133-137
32908636-6	2020	HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin.	Carbon Monoxide	37-52	heme oxygenase 1	Homo sapiens	0-4
32908636-6	2020	HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin.	Carbon Monoxide	54-56	heme oxygenase 1	Homo sapiens	0-4
32908636-6	2020	HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin.	Iron	64-68	heme oxygenase 1	Homo sapiens	0-4
32908636-6	2020	HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin.	Biliverdine	78-88	heme oxygenase 1	Homo sapiens	0-4
32908636-6	2020	HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin.	Bilirubin	124-133	heme oxygenase 1	Homo sapiens	0-4
32913552-5	2020	This study was designed to examine the role of HO-1 in lead acetate (PbAc)-induced renal tubular cell injury in vitro.	lead acetate	55-67	heme oxygenase 1	Homo sapiens	47-51
32818234-11	2020	RSG cotreatment significantly protected against HQ-induced necrosis and apoptosis, prevented HQ-reduced mitochondrial bioenergetics, decreased HQ-induced reactive oxygen species production, improved HQ-disrupted mitochondrial membrane potential, reduced F-actin aggregates, decreased phosphorylation of P38 and heat shock protein 27, and further upregulated HQ-induced heme oxygenase-1 protein levels.	rsg	0-3	heme oxygenase 1	Homo sapiens	369-385
32913552-5	2020	This study was designed to examine the role of HO-1 in lead acetate (PbAc)-induced renal tubular cell injury in vitro.	pbac	69-73	heme oxygenase 1	Homo sapiens	47-51
32913552-8	2020	In addition, pretreatment with 3-methyladenine, an inhibitor of autophagy, aggravated apoptosis and abolished renoprotection by HO-1, suggesting that the anti-apoptotic effect of HO-1 in Pb-induced nephrotoxicity is dependent on enhanced autophagy.	3-methyladenine	31-46	heme oxygenase 1	Homo sapiens	128-132
32913552-8	2020	In addition, pretreatment with 3-methyladenine, an inhibitor of autophagy, aggravated apoptosis and abolished renoprotection by HO-1, suggesting that the anti-apoptotic effect of HO-1 in Pb-induced nephrotoxicity is dependent on enhanced autophagy.	3-methyladenine	31-46	heme oxygenase 1	Homo sapiens	179-183
32913552-8	2020	In addition, pretreatment with 3-methyladenine, an inhibitor of autophagy, aggravated apoptosis and abolished renoprotection by HO-1, suggesting that the anti-apoptotic effect of HO-1 in Pb-induced nephrotoxicity is dependent on enhanced autophagy.	Lead	187-189	heme oxygenase 1	Homo sapiens	179-183
32913552-12	2020	Our findings suggest that HO-1 alleviates Pb-induced nephrotoxicity via enhanced autophagy, which involves activation of the AMPK/mTORC1 signaling pathway.	Lead	42-44	heme oxygenase 1	Homo sapiens	26-30
32801826-9	2020	We established a central role for L-cystine, as changes in the expression of the anti-oxidative gene hmox1 were L-cystine-dependent.	Cystine	34-43	heme oxygenase 1	Homo sapiens	101-106
32801826-9	2020	We established a central role for L-cystine, as changes in the expression of the anti-oxidative gene hmox1 were L-cystine-dependent.	Cystine	112-121	heme oxygenase 1	Homo sapiens	101-106
32817372-7	2020	In parallel with decreased GULP1 expression, we observed increased expression of NRF2, HMOX1, and other candidate antioxidant genes in cisplatin-resistant cells.	Cisplatin	135-144	heme oxygenase 1	Homo sapiens	87-92
32416241-3	2020	The present work tested the hypothesis that zinc is necessary in the neuronal defense response against dopamine (DA)-induced oxidative stress, in particular through heme oxygenase-1 (HO-1) upregulation.	Dopamine	103-111	heme oxygenase 1	Homo sapiens	183-187
32416241-3	2020	The present work tested the hypothesis that zinc is necessary in the neuronal defense response against dopamine (DA)-induced oxidative stress, in particular through heme oxygenase-1 (HO-1) upregulation.	Dopamine	113-115	heme oxygenase 1	Homo sapiens	165-181
32416241-3	2020	The present work tested the hypothesis that zinc is necessary in the neuronal defense response against dopamine (DA)-induced oxidative stress, in particular through heme oxygenase-1 (HO-1) upregulation.	Dopamine	113-115	heme oxygenase 1	Homo sapiens	183-187
32416241-5	2020	Human IMR-32 neuroblastoma cells responded to high DA concentrations (100 muM) by upregulating HO-1.	Dopamine	51-53	heme oxygenase 1	Homo sapiens	95-99
32416241-7	2020	DA-mediated induction of HO-1 expression was dependent on the concentration of zinc in the medium.	Dopamine	0-2	heme oxygenase 1	Homo sapiens	25-29
32416241-12	2020	Results suggest that zinc is crucial in the neuronal response to DA-induced oxidative stress in part through its role in the modulation of the Nrf2-and Bach-1-driven upregulation of HO-1 expression.	Dopamine	65-67	heme oxygenase 1	Homo sapiens	182-186
32567157-8	2020	ATX and LiCl treatment raised the protein levels of p-Akt, p-GSK3beta, nucleus Nrf2 and haeme oxygenase 1 (HO-1).	astaxanthine	0-3	heme oxygenase 1	Homo sapiens	88-105
32567157-8	2020	ATX and LiCl treatment raised the protein levels of p-Akt, p-GSK3beta, nucleus Nrf2 and haeme oxygenase 1 (HO-1).	astaxanthine	0-3	heme oxygenase 1	Homo sapiens	107-111
32567157-8	2020	ATX and LiCl treatment raised the protein levels of p-Akt, p-GSK3beta, nucleus Nrf2 and haeme oxygenase 1 (HO-1).	Lithium Chloride	8-12	heme oxygenase 1	Homo sapiens	88-105
32567157-8	2020	ATX and LiCl treatment raised the protein levels of p-Akt, p-GSK3beta, nucleus Nrf2 and haeme oxygenase 1 (HO-1).	Lithium Chloride	8-12	heme oxygenase 1	Homo sapiens	107-111
32559798-1	2020	OBJECTIVE:  We examined the interaction of polymorphisms in the genes heme oxygenase-1 (HMOX1) and nitric oxide synthase (NOS3) in patients with preeclampsia (PE) as well as the responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	196-206	heme oxygenase 1	Homo sapiens	88-93
32407842-0	2020	Excessive reactive oxygen species induce apoptosis via the APPL1-Nrf2/HO-1 antioxidant signalling pathway in trophoblasts with missed abortion.	Reactive Oxygen Species	10-33	heme oxygenase 1	Homo sapiens	70-74
31833548-8	2020	In Vitro assay revealed that mutant IDH indirectly reduced the amount of exogenous 5-ALA-derived protoporphyrinogen IX in glioma cells by increasing activity of ferrochelatase and heme oxygenase 1.	Aminolevulinic Acid	83-88	heme oxygenase 1	Homo sapiens	180-196
32155298-0	2020	Ampelopsin inhibits high glucose-induced extracellular matrix accumulation and oxidative stress in mesangial cells through activating the Nrf2/HO-1 pathway.	Glucose	25-32	heme oxygenase 1	Homo sapiens	143-147
32155298-9	2020	Furthermore, AMP elevated the expression levels of nuclear Nrf2 and heme oxygenase-1 (HO-1), as well as increased the mRNA levels of Nrf2-driven genes NAD(P)H dehydrogenase quinone-1 (NQO-1) and HO-1 in HG-treated MCs.	ampelopsin	13-16	heme oxygenase 1	Homo sapiens	68-84
32155298-9	2020	Furthermore, AMP elevated the expression levels of nuclear Nrf2 and heme oxygenase-1 (HO-1), as well as increased the mRNA levels of Nrf2-driven genes NAD(P)H dehydrogenase quinone-1 (NQO-1) and HO-1 in HG-treated MCs.	ampelopsin	13-16	heme oxygenase 1	Homo sapiens	86-90
32155298-9	2020	Furthermore, AMP elevated the expression levels of nuclear Nrf2 and heme oxygenase-1 (HO-1), as well as increased the mRNA levels of Nrf2-driven genes NAD(P)H dehydrogenase quinone-1 (NQO-1) and HO-1 in HG-treated MCs.	ampelopsin	13-16	heme oxygenase 1	Homo sapiens	195-199
32155298-11	2020	In conclusion, these findings indicated that AMP protected MCs from HG-induced oxidative damage and ECM accumulation, which might be mediated by Nrf2/HO-1 pathway.	ampelopsin	45-48	heme oxygenase 1	Homo sapiens	150-154
32559798-4	2020	CONCLUSION:  We found interactions between the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that the HMOX1 polymorphism affects the levels of enzyme HO-1 in responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	91-101	heme oxygenase 1	Homo sapiens	47-53
32559798-4	2020	CONCLUSION:  We found interactions between the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that the HMOX1 polymorphism affects the levels of enzyme HO-1 in responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	91-101	heme oxygenase 1	Homo sapiens	115-120
32559798-4	2020	CONCLUSION:  We found interactions between the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that the HMOX1 polymorphism affects the levels of enzyme HO-1 in responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	91-101	heme oxygenase 1	Homo sapiens	163-167
32559798-4	2020	CONCLUSION:  We found interactions between the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that the HMOX1 polymorphism affects the levels of enzyme HO-1 in responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	189-199	heme oxygenase 1	Homo sapiens	47-53
32559798-4	2020	CONCLUSION:  We found interactions between the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that the HMOX1 polymorphism affects the levels of enzyme HO-1 in responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	189-199	heme oxygenase 1	Homo sapiens	115-120
32559798-3	2020	RESULTS:  We found interactions between genotypes of the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that PE genotyped as AT presents lower levels of protein HO-1 compared with AA.	Methyldopa	101-111	heme oxygenase 1	Homo sapiens	57-63
32559798-4	2020	CONCLUSION:  We found interactions between the HMOX-1 and NOS3 genes and responsiveness to methyldopa and that the HMOX1 polymorphism affects the levels of enzyme HO-1 in responsiveness to methyldopa and to total antihypertensive therapy.	Methyldopa	189-199	heme oxygenase 1	Homo sapiens	163-167
32850957-0	2020	Melatonin Inhibits Oxidative Stress and Apoptosis in Cryopreserved Ovarian Tissues via Nrf2/HO-1 Signaling Pathway.	Melatonin	0-9	heme oxygenase 1	Homo sapiens	92-96
32737955-7	2020	We identified the levels of expression of ABCG2 transporters, ferrochelatase (FECH), and heme oxygenase (HO-1) as predictive biomarkers for 5-ALA-PDT.	5-amino levulinic acid	140-145	heme oxygenase 1	Homo sapiens	105-109
32731542-7	2020	The results indicate that the interaction between 147CC514 and heme-HO-1 is considerably weak, and the enzymatic activity of 147CC514 is markedly weaker than that of CPR.	147cc514	50-58	heme oxygenase 1	Homo sapiens	68-72
32223225-6	2020	Vaped GLY also causes an increase in cellular stress signals HMOX1, NQO1, and carbonylated proteins when the e-cig device is operated at high wattages.	Glycerol	6-9	heme oxygenase 1	Homo sapiens	61-66
32774680-12	2020	Noteworthily, the renal Nrf2/HO-1 pathway was activated and autophagy was enhanced after hUCBMNC injection.	hucbmnc	89-96	heme oxygenase 1	Homo sapiens	29-33
32774685-6	2020	Additionally, H2O2 at 1 mM significantly decreased the mRNA expression levels of Nrf2, CAT, SOD1, SOD2, HO-1, GST-pi, NQO1, and GLCM in ARPE-19 cells; however, treatment with EE-TT reversed the downregulated mRNA expression levels of all these genes induced by H2O2.	Hydrogen Peroxide	14-18	heme oxygenase 1	Homo sapiens	104-108
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Heme	17-21	heme oxygenase 1	Homo sapiens	35-39
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	17-33
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	35-39
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	ferrous iron	103-115	heme oxygenase 1	Homo sapiens	17-33
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	ferrous iron	103-115	heme oxygenase 1	Homo sapiens	35-39
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Carbon Monoxide	121-136	heme oxygenase 1	Homo sapiens	17-33
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Carbon Monoxide	121-136	heme oxygenase 1	Homo sapiens	35-39
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Carbon Monoxide	138-140	heme oxygenase 1	Homo sapiens	17-33
32717801-1	2020	Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO).	Carbon Monoxide	138-140	heme oxygenase 1	Homo sapiens	35-39
32792954-0	2020	Kaempferol Protects Blood Vessels From Damage Induced by Oxidative Stress and Inflammation in Association With the Nrf2/HO-1 Signaling Pathway.	kaempferol	0-10	heme oxygenase 1	Homo sapiens	120-124
32792954-6	2020	Finally, we observed that kaempferol corrected the levels of antioxidants and elevated the protein levels of Nrf2 and HO-1 in aortic tissues and HUVECs.	kaempferol	26-36	heme oxygenase 1	Homo sapiens	118-122
32792954-7	2020	Collectively, our findings prove that kaempferol protects blood vessels from damage induced by oxidative stress and inflammation and that the Nrf2/HO-1 signaling pathway plays a key role in mediating these effects.	kaempferol	38-48	heme oxygenase 1	Homo sapiens	147-151
32692767-1	2020	Heme oxygenase (HO-1) mediates the enzymatic cleavage of heme, a molecule with proinflammatory and prooxidant properties.	Heme	57-61	heme oxygenase 1	Homo sapiens	16-20
32530271-0	2020	Albumin Protects Lung Cells against Acrolein Cytotoxicity and Acrolein-adducted Albumin Increases Heme Oxygenase 1 Transcripts.	Acrolein	62-70	heme oxygenase 1	Homo sapiens	98-114
32708430-5	2020	The inflammatory response manifested by increased cytokine levels and reactive oxygen species results in inhibition of heme oxygenase (HO-1), with a subsequent loss of cytoprotection.	Oxygen	79-85	heme oxygenase 1	Homo sapiens	135-139
32530271-6	2020	In addition, albumin inhibited acrolein-induced increase of transcripts associated with cellular stress response, activating transcription factor 3 (ATF3), and antioxidant response, heme oxygenase 1 (HMOX1) in HAEC cells.	Acrolein	31-39	heme oxygenase 1	Homo sapiens	182-198
32530271-6	2020	In addition, albumin inhibited acrolein-induced increase of transcripts associated with cellular stress response, activating transcription factor 3 (ATF3), and antioxidant response, heme oxygenase 1 (HMOX1) in HAEC cells.	Acrolein	31-39	heme oxygenase 1	Homo sapiens	200-205
32530271-7	2020	Acrolein-adducted albumin itself increased HMOX1 transcripts but not ATF3 transcripts.	Acrolein	0-8	heme oxygenase 1	Homo sapiens	43-48
32530271-8	2020	The HMOX1 transcript increase was inhibited by hydralazine, a carbonyl scavenger, suggesting that the carbonyl group of acrolein-adducted albumin mediated HMOX1 transcript increase.	Hydralazine	47-58	heme oxygenase 1	Homo sapiens	4-9
32530271-8	2020	The HMOX1 transcript increase was inhibited by hydralazine, a carbonyl scavenger, suggesting that the carbonyl group of acrolein-adducted albumin mediated HMOX1 transcript increase.	Hydralazine	47-58	heme oxygenase 1	Homo sapiens	155-160
32530271-8	2020	The HMOX1 transcript increase was inhibited by hydralazine, a carbonyl scavenger, suggesting that the carbonyl group of acrolein-adducted albumin mediated HMOX1 transcript increase.	Acrolein	120-128	heme oxygenase 1	Homo sapiens	4-9
32530271-8	2020	The HMOX1 transcript increase was inhibited by hydralazine, a carbonyl scavenger, suggesting that the carbonyl group of acrolein-adducted albumin mediated HMOX1 transcript increase.	Acrolein	120-128	heme oxygenase 1	Homo sapiens	155-160
32765809-4	2020	In this study, we firstly reported that brusatol exerted the growth-inhibitory effects on HER2-positive cancer cells by regressing Nrf2/HO-1 and HER2-AKT/ERK1/2 signaling pathways in these cells.	brusatol	40-48	heme oxygenase 1	Homo sapiens	136-140
32709140-8	2020	We observed that combined treatment with AZD0364 and ZSTK474 affected nuclear factor-kappaB (NF-kappaB) and antioxidant protein levels: NF-E2-related factor 2 (NRF2), heme oxygenase-1 (HO-1), thioredoxin (Trx), thioredoxin reductase (TrxR), and the reduced glutathione/oxidized glutathione (GSH/GSSG) ratio.	N-(3-(4-chlorophenyl)-2-(3-cyanophenyl)-1-methylpropyl)-2-methyl-2-((5-(trifluoromethyl)pyridin-2-yl)oxy)propanamide	41-48	heme oxygenase 1	Homo sapiens	167-183
32709140-8	2020	We observed that combined treatment with AZD0364 and ZSTK474 affected nuclear factor-kappaB (NF-kappaB) and antioxidant protein levels: NF-E2-related factor 2 (NRF2), heme oxygenase-1 (HO-1), thioredoxin (Trx), thioredoxin reductase (TrxR), and the reduced glutathione/oxidized glutathione (GSH/GSSG) ratio.	N-(3-(4-chlorophenyl)-2-(3-cyanophenyl)-1-methylpropyl)-2-methyl-2-((5-(trifluoromethyl)pyridin-2-yl)oxy)propanamide	41-48	heme oxygenase 1	Homo sapiens	185-189
32765809-0	2020	Nrf2 Inhibitor, Brusatol in Combination with Trastuzumab Exerts Synergistic Antitumor Activity in HER2-Positive Cancers by Inhibiting Nrf2/HO-1 and HER2-AKT/ERK1/2 Pathways.	brusatol	16-24	heme oxygenase 1	Homo sapiens	139-143
32709140-8	2020	We observed that combined treatment with AZD0364 and ZSTK474 affected nuclear factor-kappaB (NF-kappaB) and antioxidant protein levels: NF-E2-related factor 2 (NRF2), heme oxygenase-1 (HO-1), thioredoxin (Trx), thioredoxin reductase (TrxR), and the reduced glutathione/oxidized glutathione (GSH/GSSG) ratio.	ZSTK474	53-60	heme oxygenase 1	Homo sapiens	167-183
32709140-8	2020	We observed that combined treatment with AZD0364 and ZSTK474 affected nuclear factor-kappaB (NF-kappaB) and antioxidant protein levels: NF-E2-related factor 2 (NRF2), heme oxygenase-1 (HO-1), thioredoxin (Trx), thioredoxin reductase (TrxR), and the reduced glutathione/oxidized glutathione (GSH/GSSG) ratio.	ZSTK474	53-60	heme oxygenase 1	Homo sapiens	185-189
32765809-5	2020	More importantly, we found that brusatol synergistically enhanced the antitumor activity of trastuzumab against HER2-positive SK-OV-3 and BT-474 cells, which may be attributed to the inhibition of Nrf2/HO-1 and HER2-AKT/ERK1/2 signaling pathways.	brusatol	32-40	heme oxygenase 1	Homo sapiens	202-206
32708634-0	2020	Cannabidiol Promotes Endothelial Cell Survival by Heme Oxygenase-1-Mediated Autophagy.	Cannabidiol	0-11	heme oxygenase 1	Homo sapiens	50-66
32709035-10	2020	Conclusions: Our results suggest the presence of molecular stages of PA, defined according to the over-expression (first stage) or under-expression (second stage) of the HMOX1, SOD1, IL-6, and IFNgamma genes in abnormal skin tissue.	Protactinium	69-71	heme oxygenase 1	Homo sapiens	170-175
32708634-2	2020	This study investigated the influence of CBD on the expression of heme oxygenase-1 (HO-1) and its functional role in regulating metabolic, autophagic, and apoptotic processes of human umbilical vein endothelial cells (HUVEC).	Cannabidiol	41-44	heme oxygenase 1	Homo sapiens	66-82
32708634-4	2020	CBD-induced HO-1 expression was not decreased by antagonists of cannabinoid-activated receptors (CB1, CB2, transient receptor potential vanilloid 1), but by the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine (NAC).	Cannabidiol	0-3	heme oxygenase 1	Homo sapiens	12-16
32708634-2	2020	This study investigated the influence of CBD on the expression of heme oxygenase-1 (HO-1) and its functional role in regulating metabolic, autophagic, and apoptotic processes of human umbilical vein endothelial cells (HUVEC).	Cannabidiol	41-44	heme oxygenase 1	Homo sapiens	84-88
32708634-4	2020	CBD-induced HO-1 expression was not decreased by antagonists of cannabinoid-activated receptors (CB1, CB2, transient receptor potential vanilloid 1), but by the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine (NAC).	Reactive Oxygen Species	186-189	heme oxygenase 1	Homo sapiens	12-16
32708634-3	2020	Concentrations up to 10 microM CBD showed a concentration-dependent increase of HO-1 mRNA and protein and an increase of the HO-1-regulating transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2).	Cannabidiol	31-34	heme oxygenase 1	Homo sapiens	80-84
32708634-4	2020	CBD-induced HO-1 expression was not decreased by antagonists of cannabinoid-activated receptors (CB1, CB2, transient receptor potential vanilloid 1), but by the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine (NAC).	Acetylcysteine	201-220	heme oxygenase 1	Homo sapiens	12-16
32708634-3	2020	Concentrations up to 10 microM CBD showed a concentration-dependent increase of HO-1 mRNA and protein and an increase of the HO-1-regulating transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2).	Cannabidiol	31-34	heme oxygenase 1	Homo sapiens	125-129
32708634-4	2020	CBD-induced HO-1 expression was not decreased by antagonists of cannabinoid-activated receptors (CB1, CB2, transient receptor potential vanilloid 1), but by the reactive oxygen species (ROS) scavenger N-acetyl-L-cysteine (NAC).	Acetylcysteine	222-225	heme oxygenase 1	Homo sapiens	12-16
32376267-0	2020	Heme oxygenase-1 alleviated non-alcoholic fatty liver disease via suppressing ROS-dependent endoplasmic reticulum stress.	ros	78-81	heme oxygenase 1	Homo sapiens	0-16
32708634-9	2020	On the other hand, the inhibition of HO-1 activity with tin protoporphyrin IX (SnPPIX) or knockdown of HO-1 expression by Nrf2 siRNA was associated with a decrease in CBD-mediated autophagy and apoptosis.	tin protoporphyrin IX	56-77	heme oxygenase 1	Homo sapiens	37-41
32708634-9	2020	On the other hand, the inhibition of HO-1 activity with tin protoporphyrin IX (SnPPIX) or knockdown of HO-1 expression by Nrf2 siRNA was associated with a decrease in CBD-mediated autophagy and apoptosis.	tin protoporphyrin IX	79-85	heme oxygenase 1	Homo sapiens	37-41
32708634-9	2020	On the other hand, the inhibition of HO-1 activity with tin protoporphyrin IX (SnPPIX) or knockdown of HO-1 expression by Nrf2 siRNA was associated with a decrease in CBD-mediated autophagy and apoptosis.	Cannabidiol	167-170	heme oxygenase 1	Homo sapiens	37-41
32708634-9	2020	On the other hand, the inhibition of HO-1 activity with tin protoporphyrin IX (SnPPIX) or knockdown of HO-1 expression by Nrf2 siRNA was associated with a decrease in CBD-mediated autophagy and apoptosis.	Cannabidiol	167-170	heme oxygenase 1	Homo sapiens	103-107
32708634-10	2020	In summary, our data show for the first time ROS-mediated HO-1 expression in endothelial cells as a mechanism by which CBD mediates protective autophagy, which at higher CBD concentrations, however, can no longer prevent cell death inducing apoptosis.	Reactive Oxygen Species	45-48	heme oxygenase 1	Homo sapiens	58-62
32708634-10	2020	In summary, our data show for the first time ROS-mediated HO-1 expression in endothelial cells as a mechanism by which CBD mediates protective autophagy, which at higher CBD concentrations, however, can no longer prevent cell death inducing apoptosis.	Cannabidiol	119-122	heme oxygenase 1	Homo sapiens	58-62
32708634-10	2020	In summary, our data show for the first time ROS-mediated HO-1 expression in endothelial cells as a mechanism by which CBD mediates protective autophagy, which at higher CBD concentrations, however, can no longer prevent cell death inducing apoptosis.	Cannabidiol	170-173	heme oxygenase 1	Homo sapiens	58-62
32209424-0	2020	New insights into the protection of growth hormone in cisplatin-induced nephrotoxicity: The impact of IGF-1 on the Keap1-Nrf2/HO-1 signaling.	Cisplatin	54-63	heme oxygenase 1	Homo sapiens	126-130
32209424-7	2020	Cisplatin upregulated the HMGB-1/NF-kappaB and downregulated Nrf2/HO-1 pathways which were reversed by hGH and aligned with increased renal IGF-1 expression.	Cisplatin	0-9	heme oxygenase 1	Homo sapiens	66-70
32209424-10	2020	SIGNIFICANCE: these results concluded that hGH can attenuate the inflammation and oxidative stress attained by CDDP probably through inhibition of Nrf2/HO-1 pathway.	Cisplatin	111-115	heme oxygenase 1	Homo sapiens	152-156
32209424-11	2020	We also suggested that Keap1/Nrf2-mediated upregulation of the antioxidant HO-1 might inhibit HMGB-1/NF-kappaB signaling and thus provide the principal protection mechanism offered by hGH against CDDP-induced kidney injury.	Cisplatin	196-200	heme oxygenase 1	Homo sapiens	75-79
32335165-10	2020	Piperine inhibited iNOS expression concomitant with enhanced expression levels of Nrf2, HO1 and the total antioxidant capacity in the hippocampal tissue.	piperine	0-8	heme oxygenase 1	Homo sapiens	88-91
32695819-0	2020	Antioxidant Effects and Cytoprotective Potentials of Herbal Tea against H2O2-Induced Oxidative Damage by Activating Heme Oxygenase1 Pathway.	Hydrogen Peroxide	72-76	heme oxygenase 1	Homo sapiens	116-131
32760278-6	2020	The non-resolving hyper-inflammation in CF lungs is attributed to an impairment of several signaling pathways associated with resolution of the inflammatory response, including the heme oxygenase-1/carbon monoxide (HO-1/CO) pathway.	Carbon Monoxide	198-213	heme oxygenase 1	Homo sapiens	181-197
32760278-6	2020	The non-resolving hyper-inflammation in CF lungs is attributed to an impairment of several signaling pathways associated with resolution of the inflammatory response, including the heme oxygenase-1/carbon monoxide (HO-1/CO) pathway.	Carbon Monoxide	198-213	heme oxygenase 1	Homo sapiens	215-219
32760278-7	2020	HO-1 is an enzyme that degrades heme groups, leading to the production of potent antioxidant, anti-inflammatory, and bactericidal mediators, such as biliverdin, bilirubin, and CO.	Heme	32-36	heme oxygenase 1	Homo sapiens	0-4
32760278-7	2020	HO-1 is an enzyme that degrades heme groups, leading to the production of potent antioxidant, anti-inflammatory, and bactericidal mediators, such as biliverdin, bilirubin, and CO.	Biliverdine	149-159	heme oxygenase 1	Homo sapiens	0-4
32760278-7	2020	HO-1 is an enzyme that degrades heme groups, leading to the production of potent antioxidant, anti-inflammatory, and bactericidal mediators, such as biliverdin, bilirubin, and CO.	Bilirubin	161-170	heme oxygenase 1	Homo sapiens	0-4
32760278-13	2020	Finally, we discuss recent studies highlighting how endogenous HO-1 can be induced by administration of controlled doses of CO to reduce lung hyper-inflammation, oxidative stress, bacterial infection, and dysfunctional ion transport, which are all hallmarks of CF lung disease.	Carbon Monoxide	124-126	heme oxygenase 1	Homo sapiens	63-67
32733250-9	2020	In the tumor necrosis factor alpha (TNF)-alpha/interferon (IFN)-gamma-stimulated HaCaT cells, CBT inhibited the production of pro-inflammatory cytokines and chemokines and elevated the nuclear translocation of NF-E2 p45 related factors 2 (Nrf2) and subsequent production of heme oxygenase-1 (HO-1).	N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE	94-97	heme oxygenase 1	Homo sapiens	274-290
32733250-9	2020	In the tumor necrosis factor alpha (TNF)-alpha/interferon (IFN)-gamma-stimulated HaCaT cells, CBT inhibited the production of pro-inflammatory cytokines and chemokines and elevated the nuclear translocation of NF-E2 p45 related factors 2 (Nrf2) and subsequent production of heme oxygenase-1 (HO-1).	N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE	94-97	heme oxygenase 1	Homo sapiens	292-296
31927051-10	2020	These results indicate that nifedipine inhibited inflammation and oxidative stress in chondrocytes via activation of Nrf-2/HO-1 signaling.	Nifedipine	28-38	heme oxygenase 1	Homo sapiens	123-127
32695819-6	2020	Furthermore, enrichment analysis of differentially expressed genes revealed that heme oxygenase1 (HMOX1) was a key gene for protective effect of WHT on oxidative stress-induced cell damage.	wht	145-148	heme oxygenase 1	Homo sapiens	81-96
32695819-6	2020	Furthermore, enrichment analysis of differentially expressed genes revealed that heme oxygenase1 (HMOX1) was a key gene for protective effect of WHT on oxidative stress-induced cell damage.	wht	145-148	heme oxygenase 1	Homo sapiens	98-103
32344355-0	2020	Akebia Saponin D ameliorated kidney injury and exerted anti-inflammatory and anti-apoptotic effects in diabetic nephropathy by activation of NRF2/HO-1 and inhibition of NF-KB pathway.	akebia saponin D	0-16	heme oxygenase 1	Homo sapiens	146-150
32801467-5	2020	Furthermore, enzymatically synthesized glycogen increased in the expression level of heme oxygenase-1, NAD(P)H: quinone oxidoreductase 1, and NF-E2-related factor 2, a transcriptional factor for heme oxygenase-1 and NAD(P)H: quinone oxidoreductase 1.	Glycogen	39-47	heme oxygenase 1	Homo sapiens	85-101
32319555-4	2020	CA and its natural derivative, 2-methoxycinnamaldehyde (MCA), markedly increased the cellular protein level of heme oxygenase-1 (HO-1) and promoted the translocation of nuclear factor erythroid 2-related factor 2 (Nrf2) to the nucleus.	2-methoxycinnamaldehyde	31-54	heme oxygenase 1	Homo sapiens	111-127
32319555-4	2020	CA and its natural derivative, 2-methoxycinnamaldehyde (MCA), markedly increased the cellular protein level of heme oxygenase-1 (HO-1) and promoted the translocation of nuclear factor erythroid 2-related factor 2 (Nrf2) to the nucleus.	2-methoxycinnamaldehyde	31-54	heme oxygenase 1	Homo sapiens	129-133
32319555-4	2020	CA and its natural derivative, 2-methoxycinnamaldehyde (MCA), markedly increased the cellular protein level of heme oxygenase-1 (HO-1) and promoted the translocation of nuclear factor erythroid 2-related factor 2 (Nrf2) to the nucleus.	2-methoxycinnamaldehyde	56-59	heme oxygenase 1	Homo sapiens	111-127
32319555-4	2020	CA and its natural derivative, 2-methoxycinnamaldehyde (MCA), markedly increased the cellular protein level of heme oxygenase-1 (HO-1) and promoted the translocation of nuclear factor erythroid 2-related factor 2 (Nrf2) to the nucleus.	2-methoxycinnamaldehyde	56-59	heme oxygenase 1	Homo sapiens	129-133
32319555-5	2020	CA-mediated Nrf2/HO-1 activation protected the HUVECs from H2O2-induced oxidative stress, which promotes apoptosis.	Hydrogen Peroxide	59-63	heme oxygenase 1	Homo sapiens	17-21
32801466-10	2020	On the other hand, ESG increased nuclear translocation of Nrf2 and expression of antioxidant proteins, HO-1 and NQO1.	L-Gamma-Glutamyl-S-[(3s)-1-Ethyl-2,5-Dioxopyrrolidin-3-Yl]-L-Cysteinylglycine	19-22	heme oxygenase 1	Homo sapiens	103-107
32240302-0	2020	JUND-dependent upregulation of HMOX1 is associated with cisplatin resistance in muscle-invasive bladder cancer.	Cisplatin	56-65	heme oxygenase 1	Homo sapiens	31-36
32240302-6	2020	This CDDP resistance was further demonstrated to be mediated, at least in part, by transactivation of HMOX1 [the gene encoding heme oxygenase-1 (HO-1)], one of the most important antioxidant signaling pathways of cell adaptation to stress.	cddp	5-9	heme oxygenase 1	Homo sapiens	102-107
32240302-6	2020	This CDDP resistance was further demonstrated to be mediated, at least in part, by transactivation of HMOX1 [the gene encoding heme oxygenase-1 (HO-1)], one of the most important antioxidant signaling pathways of cell adaptation to stress.	cddp	5-9	heme oxygenase 1	Homo sapiens	127-143
32240302-6	2020	This CDDP resistance was further demonstrated to be mediated, at least in part, by transactivation of HMOX1 [the gene encoding heme oxygenase-1 (HO-1)], one of the most important antioxidant signaling pathways of cell adaptation to stress.	cddp	5-9	heme oxygenase 1	Homo sapiens	145-149
32240302-7	2020	One mutation within the HMOX1 promoter successfully abolished oxidative stress-enhanced and JUND-driven HMOX1 promoter activation, suggesting that this unique site synergized for maximal HO-1 induction in CDDP-challenged BC cells.	cddp	205-209	heme oxygenase 1	Homo sapiens	24-29
32240302-7	2020	One mutation within the HMOX1 promoter successfully abolished oxidative stress-enhanced and JUND-driven HMOX1 promoter activation, suggesting that this unique site synergized for maximal HO-1 induction in CDDP-challenged BC cells.	cddp	205-209	heme oxygenase 1	Homo sapiens	104-109
32240302-7	2020	One mutation within the HMOX1 promoter successfully abolished oxidative stress-enhanced and JUND-driven HMOX1 promoter activation, suggesting that this unique site synergized for maximal HO-1 induction in CDDP-challenged BC cells.	cddp	205-209	heme oxygenase 1	Homo sapiens	187-191
32801467-5	2020	Furthermore, enzymatically synthesized glycogen increased in the expression level of heme oxygenase-1, NAD(P)H: quinone oxidoreductase 1, and NF-E2-related factor 2, a transcriptional factor for heme oxygenase-1 and NAD(P)H: quinone oxidoreductase 1.	Glycogen	39-47	heme oxygenase 1	Homo sapiens	195-211
32801467-7	2020	Knockdown of heme oxygenase-1 and NAD(P)H: quinone oxidoreductase 1 canceled enzymatically synthesized glycogen-suppressed reactive oxygen species accumulation in normal human epidermal keratinocytes.	Glycogen	103-111	heme oxygenase 1	Homo sapiens	13-29
32801467-7	2020	Knockdown of heme oxygenase-1 and NAD(P)H: quinone oxidoreductase 1 canceled enzymatically synthesized glycogen-suppressed reactive oxygen species accumulation in normal human epidermal keratinocytes.	Reactive Oxygen Species	123-146	heme oxygenase 1	Homo sapiens	13-29
32801467-8	2020	It is, therefore, concluded that enzymatically synthesized glycogen inhibited ultraviolet B-induced oxidative stress through increasing the expression level of heme oxygenase-1 and NAD(P)H: quinone oxidoreductase 1 through the NF-E2-related factor 2 pathway in normal human epidermal keratinocytes.	Glycogen	59-67	heme oxygenase 1	Homo sapiens	160-176
32336667-7	2020	We observed a clear additive effect of O3 and DEE in combination with UV in increasing levels of several oxidative (4HNE, HO-1) and inflammatory (COX2, NF-kappaB) markers and loss of barrier-associated proteins, such as filaggrin and involucrin.	Ozone	39-41	heme oxygenase 1	Homo sapiens	122-126
32319645-9	2020	Additionally, treatment with petatewalide B activated AMPK in the OGD/R-exposed SH-SY5Y cells and upregulated activation of the downstream transcription factor Nrf2, which accompanied heme oxygenase 1 (HO-1) and NAD(P)H quinone dehydrogenase 1 (NQO1) expression.	petatewalide b	29-43	heme oxygenase 1	Homo sapiens	184-200
32319645-9	2020	Additionally, treatment with petatewalide B activated AMPK in the OGD/R-exposed SH-SY5Y cells and upregulated activation of the downstream transcription factor Nrf2, which accompanied heme oxygenase 1 (HO-1) and NAD(P)H quinone dehydrogenase 1 (NQO1) expression.	petatewalide b	29-43	heme oxygenase 1	Homo sapiens	202-206
32319645-10	2020	Furthermore, silencing AMPK, Nrf2, HO-1 and NQO1 expression inhibited petatewalide B"s protective effect against apoptosis in the OGD/R-exposed SH-SY5Y cells.	petatewalide b	70-84	heme oxygenase 1	Homo sapiens	35-39
32629871-6	2020	NRF2 knockdown reversed 5-FU resistance of PDAC cells via suppression of ABCG2 and HO-1.	Fluorouracil	24-28	heme oxygenase 1	Homo sapiens	83-87
32695110-4	2020	Heme is a chemoattractant, activates the complement system, modulates host defense mechanisms through the activation of innate immune receptors and the heme oxygenase-1/ferritin system, and induces innate immune memory.	Heme	0-4	heme oxygenase 1	Homo sapiens	152-168
32655974-6	2020	However, these processes could be inactivated by compound C (inhibitor of AMPK) and zinc protoporphyrin-1 (ZnPP-1; inhibitor of HO-1).	znpp-1	107-113	heme oxygenase 1	Homo sapiens	128-132
32706194-11	2020	At the same time, N-hydroxy-N"-(4-butyl-2-methylphenyl)-formamidine protects SH-SY5Y cells against oxygen-glucose deprivation and reoxygenation-induced injury partly through the inhibition of microRNA-27-a-5p and promotion of the Bach1/HO-1 signaling pathway.	n-hydroxy-n"-(4-butyl-2-methylphenyl)-formamidine	18-67	heme oxygenase 1	Homo sapiens	236-240
32655823-7	2020	In addition, the activation of NF-kappaB pathway was suppressed by 4SC-202, while up-regulation of HO-1 significantly weakened the 4SC-202-induced suppression of the NF-kappaB pathway, thereby attenuating the efficacy of 4SC-202.	domatinostat	131-138	heme oxygenase 1	Homo sapiens	99-103
32655974-6	2020	However, these processes could be inactivated by compound C (inhibitor of AMPK) and zinc protoporphyrin-1 (ZnPP-1; inhibitor of HO-1).	zinc protoporphyrin-1	84-105	heme oxygenase 1	Homo sapiens	128-132
32630570-10	2020	After H2O2 treatment, translocation of Nrf2 into the nucleus and the subsequent increase of Heme Oxygenase-1 (HO-1) were observed earlier in CGA-treated cells.	Hydrogen Peroxide	6-10	heme oxygenase 1	Homo sapiens	110-114
32581238-6	2020	Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls.	Hemin	21-26	heme oxygenase 1	Homo sapiens	13-17
32581238-6	2020	Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls.	Hemin	21-26	heme oxygenase 1	Homo sapiens	234-238
32581238-6	2020	Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls.	COPP protocol	30-34	heme oxygenase 1	Homo sapiens	13-17
32581238-6	2020	Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls.	COPP protocol	30-34	heme oxygenase 1	Homo sapiens	234-238
32581238-6	2020	Induction of HO-1 by hemin or CoPP in vitro reduced production of IFN-gamma and IL-10 from healthy human PBMCs and decreased bacterial clearance activity of whole blood from healthy controls and beta-thalassaemia, while inhibition of HO-1 by SnPP enhanced both functions in healthy controls.	S-Nitroso-N-propionyl-D,L-penicillamine	242-246	heme oxygenase 1	Homo sapiens	13-17
32581238-8	2020	Our results suggest a mechanism that excess hemin of beta-thalassaemia patients is a significant cause of immune suppression via HO-1 induction and may underlie the susceptibility of these individuals to severe bacterial infection.	Hemin	44-49	heme oxygenase 1	Homo sapiens	129-133
32655823-6	2020	Here, we reported that 4SC-202 could down-regulate the expression of HO-1, and up-regulation of HO-1 could significantly attenuate the 4SC-202-induced apoptosis in SKM-1 cells.	domatinostat	23-30	heme oxygenase 1	Homo sapiens	69-73
32655823-6	2020	Here, we reported that 4SC-202 could down-regulate the expression of HO-1, and up-regulation of HO-1 could significantly attenuate the 4SC-202-induced apoptosis in SKM-1 cells.	domatinostat	135-142	heme oxygenase 1	Homo sapiens	96-100
32655823-7	2020	In addition, the activation of NF-kappaB pathway was suppressed by 4SC-202, while up-regulation of HO-1 significantly weakened the 4SC-202-induced suppression of the NF-kappaB pathway, thereby attenuating the efficacy of 4SC-202.	domatinostat	131-138	heme oxygenase 1	Homo sapiens	99-103
32595528-6	2020	Compared with OGD-treated cells, xanomeline inhibited apoptosis, reduced ROS production, attenuated the OGD-induced HIF-1alpha increase and partially reversed the reduction of HO-1, Sirtuin-1, Bcl-2, PARP, and p-Akt induced by OGD.	xanomeline	33-43	heme oxygenase 1	Homo sapiens	176-180
32670766-5	2020	Herein, lipid-polymer hybrid nanoparticle (hNP) is loaded with tin mesoporphyrin (SnMP), a HO1-inhibitor, and non-covalently modified with an engineered antibody for leukemic cell-targeted delivery.	lipid-polymer	8-21	heme oxygenase 1	Homo sapiens	91-94
32506967-2	2022	Although BaP is one of the most extensively studied pollutants, the underlying mechanisms through which BaP affects reactive oxygen species (ROS)/hypoxia-inducible factor 1alpha (HIF-1alpha)/heme oxygenase 1(HO-1) signaling during lung or breast carcinogenesis are not yet fully understood.	Benzo(a)pyrene	104-107	heme oxygenase 1	Homo sapiens	191-207
32506967-2	2022	Although BaP is one of the most extensively studied pollutants, the underlying mechanisms through which BaP affects reactive oxygen species (ROS)/hypoxia-inducible factor 1alpha (HIF-1alpha)/heme oxygenase 1(HO-1) signaling during lung or breast carcinogenesis are not yet fully understood.	Benzo(a)pyrene	104-107	heme oxygenase 1	Homo sapiens	208-212
32506967-3	2022	In this study, we analyzed the effects of 0 (control), 1, 5, or 25 microM BaP exposure on A549 and MCF-7 cancer cells, by evaluating cell viability, cell cycle, and regulatory protein expression, metabolic gene expression, and ROS/HIF-1alpha/HO-1 signaling.	Benzo(a)pyrene	74-77	heme oxygenase 1	Homo sapiens	242-246
32526964-0	2020	Baicalein Inhibits Benzo[a]pyrene-Induced Toxic Response by Downregulating Src Phosphorylation and by Upregulating NRF2-HMOX1 System.	baicalein	0-9	heme oxygenase 1	Homo sapiens	120-125
32526964-0	2020	Baicalein Inhibits Benzo[a]pyrene-Induced Toxic Response by Downregulating Src Phosphorylation and by Upregulating NRF2-HMOX1 System.	Benzo(a)pyrene	19-33	heme oxygenase 1	Homo sapiens	120-125
32526964-6	2020	In addition, BAI activated antioxidative system nuclear factor-erythroid 2-related factor-2 (NRF2) and heme oxygenase 1 (HMOX1), leading the reduction of BaP-induced ROS production.	Benzo(a)pyrene	154-157	heme oxygenase 1	Homo sapiens	103-119
32526964-6	2020	In addition, BAI activated antioxidative system nuclear factor-erythroid 2-related factor-2 (NRF2) and heme oxygenase 1 (HMOX1), leading the reduction of BaP-induced ROS production.	Benzo(a)pyrene	154-157	heme oxygenase 1	Homo sapiens	121-126
32526964-6	2020	In addition, BAI activated antioxidative system nuclear factor-erythroid 2-related factor-2 (NRF2) and heme oxygenase 1 (HMOX1), leading the reduction of BaP-induced ROS production.	Reactive Oxygen Species	166-169	heme oxygenase 1	Homo sapiens	121-126
32526964-9	2020	These results indicate that BAI and BAI-containing herbal drugs may be useful for inhibiting the toxic effects of BaP via dual AHR-CYP1A1-inhibiting and NRF2-HMOX1-activating activities.	Benzo(a)pyrene	114-117	heme oxygenase 1	Homo sapiens	158-163
32506967-7	2022	Moreover, the induction of ROS and the modulation of HIF-1alpha and HO-1 were observed after BaP exposure.	Benzo(a)pyrene	93-96	heme oxygenase 1	Homo sapiens	68-72
32506967-8	2022	Taken together, these findings suggest that BaP affects proliferation with reference to metabolic genes and ROS/HIF-1alpha/HO-1 signaling in A549 and MCF-7 cancer cells.	Benzo(a)pyrene	44-47	heme oxygenase 1	Homo sapiens	123-127
32724648-4	2020	Furthermore, COS treatment significantly upregulated the expression of Nrf2 and its downstream target genes HO-1, NQO1, and CAT.	carbonyl sulfide	13-16	heme oxygenase 1	Homo sapiens	108-112
32369450-3	2020	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme that catabolizes free heme.	Heme	74-78	heme oxygenase 1	Homo sapiens	0-16
32369450-3	2020	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme that catabolizes free heme.	Heme	74-78	heme oxygenase 1	Homo sapiens	18-22
32369450-6	2020	Herein, we show that HO-1 is highly expressed in monocytic cells in the tumor microenvironment (TME) once they differentiate into TAMs.	tams	130-134	heme oxygenase 1	Homo sapiens	21-25
32670766-10	2020	Collectively, HO1-inhibiting dual cell-targeted T-hNP/SnMP has a strong potential as a novel therapeutic in AML.	tin mesoporphyrin	54-58	heme oxygenase 1	Homo sapiens	14-17
32167970-15	2020	RTV-treated HIV+ women had further increases in cystatin C (n = 20; p = 0.05), with parallel elevation of HO-1.	Ritonavir	0-3	heme oxygenase 1	Homo sapiens	106-110
32222619-0	2020	Chromatograpic resolution of phenylethanolic-azole racemic compounds highlighted stereoselective inhibition of heme oxygenase-1 by (R)-enantiomers.	phenylethanolic	29-44	heme oxygenase 1	Homo sapiens	111-127
32222619-0	2020	Chromatograpic resolution of phenylethanolic-azole racemic compounds highlighted stereoselective inhibition of heme oxygenase-1 by (R)-enantiomers.	Azoles	45-50	heme oxygenase 1	Homo sapiens	111-127
31990992-0	2020	Inhibition of microRNA-199a-5p ameliorates oxygen-glucose deprivation/reoxygenation-induced apoptosis and oxidative stress in HT22 neurons by targeting Brg1 to activate Nrf2/HO-1 signaling.	Oxygen	43-49	heme oxygenase 1	Homo sapiens	174-178
32514269-0	2020	Asiaticoside inhibits TGF-beta1-induced mesothelial-mesenchymal transition and oxidative stress via the Nrf2/HO-1 signaling pathway in the human peritoneal mesothelial cell line HMrSV5.	asiaticoside	0-12	heme oxygenase 1	Homo sapiens	109-113
32633385-8	2020	In addition, HBSP also increased the activity of the Nrf2/HO-1 signaling pathway and ML385 reduced the protective effect of HBSP on BEAS-2B cells.	hbsp	13-17	heme oxygenase 1	Homo sapiens	58-62
32234671-0	2020	Cryptochlorogenic acid attenuates LPS-induced inflammatory response and oxidative stress via upregulation of the Nrf2/HO-1 signaling pathway in RAW 264.7 macrophages.	Cryptochlorogenic acid	0-22	heme oxygenase 1	Homo sapiens	118-122
32234491-5	2020	The liver serum biomarkers such as ALT and AST, elated levels of free radicals inducing oxidative stress characterized by a surge in Nrf-2, FOXO-1 and HO-1 genes and diminution of anti-oxidant activity characterized by a decline in SOD, GPx, and CAT genes.	Free Radicals	65-78	heme oxygenase 1	Homo sapiens	151-155
31820335-12	2020	Further, lutein protected high glucose-mediated down-regulation of a redox-sensitive transcription factor, Nrf2, and antioxidant enzymes, SOD2, HO-1, and catalase.	Lutein	9-15	heme oxygenase 1	Homo sapiens	144-162
31820335-12	2020	Further, lutein protected high glucose-mediated down-regulation of a redox-sensitive transcription factor, Nrf2, and antioxidant enzymes, SOD2, HO-1, and catalase.	Glucose	31-38	heme oxygenase 1	Homo sapiens	144-162
32108297-0	2020	The Secretion from Bone Marrow Mesenchymal Stem Cells Pretreated with Berberine Rescues Neurons with Oxidative Damage Through Activation of the Keap1-Nrf2-HO-1 Signaling Pathway.	Berberine	70-79	heme oxygenase 1	Homo sapiens	155-159
32429564-6	2020	Mechanically, WFA inhibits matrix metalloproteinase (MMP)-2 and MMP-9 activities but induces mRNA expression for a group of antioxidant genes, such as nuclear factor, erythroid 2-like 2 (NFE2L2), heme oxygenase 1 (HMOX1), glutathione-disulfide reductase (GSR), and NAD(P)H quinone dehydrogenase 1 (NQO1)) in Ca9-22 cells.	withaferin A	14-17	heme oxygenase 1	Homo sapiens	196-212
32546967-0	2020	Glycine Improves Ischemic Stroke Through miR-19a-3p/AMPK/GSK-3beta/HO-1 Pathway.	Glycine	0-7	heme oxygenase 1	Homo sapiens	67-71
32546967-14	2020	Rescue experiments demonstrated that glycine improved cell apoptosis, inflammatory response and glucose metabolism disorder of ischemic stroke through miR-19a-3p/AMPK/GSK-3beta/HO-1 pathway.	Glycine	37-44	heme oxygenase 1	Homo sapiens	177-181
32546967-15	2020	Conclusion: Glycine improves ischemic stroke through miR-19a-3p/AMPK/GSK-3beta/HO-1 pathway.	Glycine	12-19	heme oxygenase 1	Homo sapiens	79-83
32536057-1	2020	Objective: To investigate the effect of rosiglitazone (RGZ) on the expression of peroxisome proliferator-activated receptor gamma (PPARgamma) and heme oxygenase-1 (HO-1) in hepatic stellate cells (HSCs).	Rosiglitazone	40-53	heme oxygenase 1	Homo sapiens	164-168
32536057-1	2020	Objective: To investigate the effect of rosiglitazone (RGZ) on the expression of peroxisome proliferator-activated receptor gamma (PPARgamma) and heme oxygenase-1 (HO-1) in hepatic stellate cells (HSCs).	Rosiglitazone	55-58	heme oxygenase 1	Homo sapiens	146-162
32536057-1	2020	Objective: To investigate the effect of rosiglitazone (RGZ) on the expression of peroxisome proliferator-activated receptor gamma (PPARgamma) and heme oxygenase-1 (HO-1) in hepatic stellate cells (HSCs).	Rosiglitazone	55-58	heme oxygenase 1	Homo sapiens	164-168
32536057-11	2020	HO-1 mRNA (1.80 +- 0.36) and protein (0.61 +- 0.09) relative expression was significantly increased in RGZ + ZnPP-IX group as compared to blank control group (P < 0.05).	Rosiglitazone	103-106	heme oxygenase 1	Homo sapiens	0-4
32536057-11	2020	HO-1 mRNA (1.80 +- 0.36) and protein (0.61 +- 0.09) relative expression was significantly increased in RGZ + ZnPP-IX group as compared to blank control group (P < 0.05).	zinc protoporphyrin	109-116	heme oxygenase 1	Homo sapiens	0-4
32536057-13	2020	Conclusion: The effect of rosiglitazone on inducing increased expression of PPARgamma, and then inhibiting HSC proliferation activity and collagen production may be realized by regulating its downstream HO-1 expression.	Rosiglitazone	26-39	heme oxygenase 1	Homo sapiens	203-207
32485912-0	2020	Roles of JNK/Nrf2 Pathway on Hemin-Induced Heme Oxygenase-1 Activation in MCF-7 Human Breast Cancer Cells.	Hemin	29-34	heme oxygenase 1	Homo sapiens	43-59
32485912-2	2020	In this study, we investigated that the mechanisms of hemin-induced HO-1 expression and its signaling pathways in human breast cancer cell.	Hemin	54-59	heme oxygenase 1	Homo sapiens	68-72
32485912-4	2020	Hemin increased HO-1 expression in MCF-7 cells in a dose- and time-dependent manner.	Hemin	0-5	heme oxygenase 1	Homo sapiens	16-20
32485912-5	2020	Hemin enhanced HO-1 expression through the activation of c-Jun N-terminal kinases (JNK) signaling pathway.	Hemin	0-5	heme oxygenase 1	Homo sapiens	15-19
32485912-6	2020	Hemin also induced activation of Nrf2, a major transcription factor of HO-1 expression.	Hemin	0-5	heme oxygenase 1	Homo sapiens	71-75
32485912-7	2020	These responses in MCF-7 cells were completely blocked by pretreatment with brazilin, a HO-1 regulator.	brazilin	76-84	heme oxygenase 1	Homo sapiens	88-92
32485912-8	2020	These results indicated that brazilin inhibits hemin-induced HO-1 expressions through inactivation of JNK/Nrf2 in MCF-7 cells.	brazilin	29-37	heme oxygenase 1	Homo sapiens	61-65
32485912-8	2020	These results indicated that brazilin inhibits hemin-induced HO-1 expressions through inactivation of JNK/Nrf2 in MCF-7 cells.	Hemin	47-52	heme oxygenase 1	Homo sapiens	61-65
32485912-9	2020	Thus, our findings suggest that HO-1 is an important anticancer-target of brazilin in human breast cancer.	brazilin	74-82	heme oxygenase 1	Homo sapiens	32-36
32455831-4	2020	HO-1 catalyzes the enzymatic degradation of heme with the simultaneous release of carbon monoxide (CO), ferrous iron (Fe2+), and biliverdin.	Carbon Monoxide	82-97	heme oxygenase 1	Homo sapiens	0-4
32455831-4	2020	HO-1 catalyzes the enzymatic degradation of heme with the simultaneous release of carbon monoxide (CO), ferrous iron (Fe2+), and biliverdin.	Carbon Monoxide	99-101	heme oxygenase 1	Homo sapiens	0-4
32455831-4	2020	HO-1 catalyzes the enzymatic degradation of heme with the simultaneous release of carbon monoxide (CO), ferrous iron (Fe2+), and biliverdin.	ferrous iron	104-116	heme oxygenase 1	Homo sapiens	0-4
32455831-4	2020	HO-1 catalyzes the enzymatic degradation of heme with the simultaneous release of carbon monoxide (CO), ferrous iron (Fe2+), and biliverdin.	ammonium ferrous sulfate	118-122	heme oxygenase 1	Homo sapiens	0-4
32455831-4	2020	HO-1 catalyzes the enzymatic degradation of heme with the simultaneous release of carbon monoxide (CO), ferrous iron (Fe2+), and biliverdin.	Biliverdine	129-139	heme oxygenase 1	Homo sapiens	0-4
32536057-0	2020	[Rosiglitazone inhibits hepatic stellate cell proliferation by regulating peroxisome proliferator-activated receptor gamma/ heme oxygenase-1 expression].	Rosiglitazone	1-14	heme oxygenase 1	Homo sapiens	124-140
32536057-1	2020	Objective: To investigate the effect of rosiglitazone (RGZ) on the expression of peroxisome proliferator-activated receptor gamma (PPARgamma) and heme oxygenase-1 (HO-1) in hepatic stellate cells (HSCs).	Rosiglitazone	40-53	heme oxygenase 1	Homo sapiens	146-162
32509156-4	2020	Besides, it was also expounded that nuclear factor-erythroid 2 (NF-E2)-related factor 2/BTB domain and CNC homolog 1 (Nrf2/Bach1) might be involved in the regulation of HO-1 and the quantum effect of photon altered ROS generation.	Reactive Oxygen Species	215-218	heme oxygenase 1	Homo sapiens	169-173
32429564-6	2020	Mechanically, WFA inhibits matrix metalloproteinase (MMP)-2 and MMP-9 activities but induces mRNA expression for a group of antioxidant genes, such as nuclear factor, erythroid 2-like 2 (NFE2L2), heme oxygenase 1 (HMOX1), glutathione-disulfide reductase (GSR), and NAD(P)H quinone dehydrogenase 1 (NQO1)) in Ca9-22 cells.	withaferin A	14-17	heme oxygenase 1	Homo sapiens	214-219
32499710-9	2020	Comparing to the UVA radiation, PF pre-treatment could prominently increase the MTS activity, decrease cell apoptosis, reduce the generations of ROS and MDA, increase the activity of SOD and increase the expression of Nrf2 and its target genes HO-1 and NQ-O1.	peoniflorin	32-34	heme oxygenase 1	Homo sapiens	244-248
32509141-0	2020	Apatinib, a Novel Tyrosine Kinase Inhibitor, Promotes ROS-Dependent Apoptosis and Autophagy via the Nrf2/HO-1 Pathway in Ovarian Cancer Cells.	apatinib	0-8	heme oxygenase 1	Homo sapiens	105-109
32509141-5	2020	Mechanistically, we showed that apatinib suppressed glutathione to generate ROS via the downregulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway and maintained an antitumor effect at a low level of VEGFR2 in ovarian cancer, suggesting that combination of apatinib with Nrf2 inhibitor may be a promising therapy strategy for patients with ovarian cancer.	apatinib	32-40	heme oxygenase 1	Homo sapiens	161-177
32509141-5	2020	Mechanistically, we showed that apatinib suppressed glutathione to generate ROS via the downregulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway and maintained an antitumor effect at a low level of VEGFR2 in ovarian cancer, suggesting that combination of apatinib with Nrf2 inhibitor may be a promising therapy strategy for patients with ovarian cancer.	apatinib	32-40	heme oxygenase 1	Homo sapiens	179-183
32509141-5	2020	Mechanistically, we showed that apatinib suppressed glutathione to generate ROS via the downregulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway and maintained an antitumor effect at a low level of VEGFR2 in ovarian cancer, suggesting that combination of apatinib with Nrf2 inhibitor may be a promising therapy strategy for patients with ovarian cancer.	Glutathione	52-63	heme oxygenase 1	Homo sapiens	161-177
32105681-0	2020	Upregulation of heme oxygenase-1 by Brahma-related gene 1 through Nrf2 signaling confers protective effect against high glucose-induced oxidative damage of retinal ganglion cells.	Glucose	120-127	heme oxygenase 1	Homo sapiens	16-32
32509141-5	2020	Mechanistically, we showed that apatinib suppressed glutathione to generate ROS via the downregulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway and maintained an antitumor effect at a low level of VEGFR2 in ovarian cancer, suggesting that combination of apatinib with Nrf2 inhibitor may be a promising therapy strategy for patients with ovarian cancer.	ros	76-79	heme oxygenase 1	Homo sapiens	161-177
32509141-5	2020	Mechanistically, we showed that apatinib suppressed glutathione to generate ROS via the downregulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway and maintained an antitumor effect at a low level of VEGFR2 in ovarian cancer, suggesting that combination of apatinib with Nrf2 inhibitor may be a promising therapy strategy for patients with ovarian cancer.	ros	76-79	heme oxygenase 1	Homo sapiens	179-183
32509141-5	2020	Mechanistically, we showed that apatinib suppressed glutathione to generate ROS via the downregulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway and maintained an antitumor effect at a low level of VEGFR2 in ovarian cancer, suggesting that combination of apatinib with Nrf2 inhibitor may be a promising therapy strategy for patients with ovarian cancer.	Glutathione	52-63	heme oxygenase 1	Homo sapiens	179-183
32291269-13	2020	p21 responses to high-dose SnPP and HO-1 responses to low-dose SnPP were significantly suppressed in participants with CKD versus healthy volunteers.	S-Nitroso-N-propionyl-D,L-penicillamine	63-67	heme oxygenase 1	Homo sapiens	36-40
32494130-8	2020	Meanwhile, we showed that CuONPs exposure induced oxidative stress, indicated by the increase of cellular levels of superoxide anions, the upregulation of protein levels of heme oxygenase-1 (HO-1) and glutamate-cysteine ligase modifier subunit (GCLM), the elevation of the levels of malondialdehyde (MDA), but the reduction of glutathione to glutathione disulfide ratio.	cuonps	26-32	heme oxygenase 1	Homo sapiens	173-189
32494130-8	2020	Meanwhile, we showed that CuONPs exposure induced oxidative stress, indicated by the increase of cellular levels of superoxide anions, the upregulation of protein levels of heme oxygenase-1 (HO-1) and glutamate-cysteine ligase modifier subunit (GCLM), the elevation of the levels of malondialdehyde (MDA), but the reduction of glutathione to glutathione disulfide ratio.	cuonps	26-32	heme oxygenase 1	Homo sapiens	191-195
32393788-3	2020	The fasting-mimicking diet selectivity reverses vitamin C-induced up-regulation of heme-oxygenase-1 and ferritin in KRAS-mutant cancer cells, consequently increasing reactive iron, oxygen species, and cell death; an effect further potentiated by chemotherapy.	Ascorbic Acid	48-57	heme oxygenase 1	Homo sapiens	83-99
32393788-3	2020	The fasting-mimicking diet selectivity reverses vitamin C-induced up-regulation of heme-oxygenase-1 and ferritin in KRAS-mutant cancer cells, consequently increasing reactive iron, oxygen species, and cell death; an effect further potentiated by chemotherapy.	Iron	175-179	heme oxygenase 1	Homo sapiens	83-99
32397146-7	2020	Furthermore, 12-EPAHSA increased the expression of Nrf2-dependent antioxidant enzyme genes (NQO1, GCLM, GCLC, SOD-1, and HO-1).	12-EPAHSA	13-22	heme oxygenase 1	Homo sapiens	121-125
32084418-11	2020	The results showed that agomelatine and melatonin decreased neuronal injury and promoted the Nrf2-HO-1 signalling pathway.	agomelatine	24-35	heme oxygenase 1	Homo sapiens	98-102
32084418-11	2020	The results showed that agomelatine and melatonin decreased neuronal injury and promoted the Nrf2-HO-1 signalling pathway.	Melatonin	40-49	heme oxygenase 1	Homo sapiens	98-102
32156661-2	2020	As a response, heme induces its metabolic degradation via heme oxygenase-1 (HO-1), activated by NF-E2-related factor 2 (NRF2), the master stress response transcription factor.	Heme	15-19	heme oxygenase 1	Homo sapiens	58-74
32124251-6	2020	Pathway analysis demonstrated that the ROS/Nrf2/HO-1-SOD2-NQO-1-GCLC signaling axis is a key axis through which curcumin activates the Nrf2/ARE pathway in TMJ inflammatory chondrocytes.	ros	39-42	heme oxygenase 1	Homo sapiens	48-57
31900049-6	2020	Our study has shown that IMP could regulate the signaling pathways including MAPK, PI3K/Akt, NF-kappaB, and Nrf2/HO-1 to release the inflammatory responses.	imperatorin	25-28	heme oxygenase 1	Homo sapiens	113-117
31900049-7	2020	IMP might attenuate airway remodeling by the down-regulation of Nrf2/HO-1/ROS/PI3K/Akt, Nrf2/HO-1/ROS/MAPK, and Nrf2/HO-1/ROS/NF-kappaB signaling pathways.	imperatorin	0-3	heme oxygenase 1	Homo sapiens	69-73
31900049-7	2020	IMP might attenuate airway remodeling by the down-regulation of Nrf2/HO-1/ROS/PI3K/Akt, Nrf2/HO-1/ROS/MAPK, and Nrf2/HO-1/ROS/NF-kappaB signaling pathways.	imperatorin	0-3	heme oxygenase 1	Homo sapiens	93-97
31900049-7	2020	IMP might attenuate airway remodeling by the down-regulation of Nrf2/HO-1/ROS/PI3K/Akt, Nrf2/HO-1/ROS/MAPK, and Nrf2/HO-1/ROS/NF-kappaB signaling pathways.	imperatorin	0-3	heme oxygenase 1	Homo sapiens	93-97
32124251-6	2020	Pathway analysis demonstrated that the ROS/Nrf2/HO-1-SOD2-NQO-1-GCLC signaling axis is a key axis through which curcumin activates the Nrf2/ARE pathway in TMJ inflammatory chondrocytes.	Curcumin	112-120	heme oxygenase 1	Homo sapiens	48-57
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Heme	44-48	heme oxygenase 1	Homo sapiens	11-27
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Heme	44-48	heme oxygenase 1	Homo sapiens	29-33
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Carbon Monoxide	52-54	heme oxygenase 1	Homo sapiens	11-27
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Carbon Monoxide	52-54	heme oxygenase 1	Homo sapiens	29-33
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Iron	56-60	heme oxygenase 1	Homo sapiens	11-27
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Iron	56-60	heme oxygenase 1	Homo sapiens	29-33
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Biliverdine	66-76	heme oxygenase 1	Homo sapiens	11-27
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Biliverdine	66-76	heme oxygenase 1	Homo sapiens	29-33
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Bilirubin	77-86	heme oxygenase 1	Homo sapiens	11-27
32006543-1	2020	OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin.	Bilirubin	77-86	heme oxygenase 1	Homo sapiens	29-33
32006543-2	2020	Although serum bilirubin levels were often reported in patients with coronary artery disease (CAD), HO-1 levels in patients with CAD and the association between HO-1 and bilirubin levels have not been clarified.	Bilirubin	170-179	heme oxygenase 1	Homo sapiens	161-165
32006543-8	2020	In multivariate analysis, HO-1 levels were a significant factor for CAD independent of atherosclerotic risk factors and bilirulin levels.	bilirulin	120-129	heme oxygenase 1	Homo sapiens	26-30
32112801-4	2020	This was associated with reduced ferritin induction by hemoglobin; expression of heme oxygenase-1, which catalyzes iron release from heme, was not altered.	Iron	115-119	heme oxygenase 1	Homo sapiens	81-97
32004978-8	2020	We observed that brusatol, an NRF2 inhibitor, as well as small interfering RNA (siRNA)-mediated knockdown of NRF2 in DLD-1 cells suppressed compound 3-induced HO-1 expression.	brusatol	17-25	heme oxygenase 1	Homo sapiens	159-163
32363357-7	2020	Quercetin added apically to the endothelial cells upregulated HO-1 and downregulated PDK4 both in monoculture and in co-culture, but the total PDK4 levels were higher in the presence of HepG2 cells.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	62-66
32278282-0	2020	Canagliflozin inhibits vascular smooth muscle cell proliferation and migration: Role of heme oxygenase-1.	Canagliflozin	0-13	heme oxygenase 1	Homo sapiens	88-104
32108290-8	2020	Our results showed that hemin was able to induce both HO-1 gene and protein expression in a cell-dependent manner being A172 more responsive to pharmacological upregulation of HO-1.	Hemin	24-29	heme oxygenase 1	Homo sapiens	54-58
32108290-8	2020	Our results showed that hemin was able to induce both HO-1 gene and protein expression in a cell-dependent manner being A172 more responsive to pharmacological upregulation of HO-1.	Hemin	24-29	heme oxygenase 1	Homo sapiens	176-180
32278282-5	2020	Canagliflozin also resulted in the induction of heme oxygenase-1 (HO-1) expression, and a rise in HO activity in vascular SMCs, whereas, empagliflozin or dapagliflozin had no effect on HO activity.	Canagliflozin	0-13	heme oxygenase 1	Homo sapiens	48-64
32278282-5	2020	Canagliflozin also resulted in the induction of heme oxygenase-1 (HO-1) expression, and a rise in HO activity in vascular SMCs, whereas, empagliflozin or dapagliflozin had no effect on HO activity.	Canagliflozin	0-13	heme oxygenase 1	Homo sapiens	66-70
32278282-6	2020	Canagliflozin also activated the HO-1 promoter and this was abrogated by mutating the antioxidant responsive element or by overexpressing dominant-negative NF-E2-related factor-2 (Nrf2).	Canagliflozin	0-13	heme oxygenase 1	Homo sapiens	33-37
32278282-7	2020	The induction of HO-1 by canagliflozin relied on reactive oxygen species (ROS) formation and was negated by antioxidants.	Canagliflozin	25-38	heme oxygenase 1	Homo sapiens	17-21
32278282-7	2020	The induction of HO-1 by canagliflozin relied on reactive oxygen species (ROS) formation and was negated by antioxidants.	Reactive Oxygen Species	49-72	heme oxygenase 1	Homo sapiens	17-21
32278282-7	2020	The induction of HO-1 by canagliflozin relied on reactive oxygen species (ROS) formation and was negated by antioxidants.	Reactive Oxygen Species	74-77	heme oxygenase 1	Homo sapiens	17-21
32278282-8	2020	Finally, silencing HO-1 expression partially rescued the proliferative and migratory response of canagliflozin-treated SMCs, and this was reversed by carbon monoxide and bilirubin.	Canagliflozin	97-110	heme oxygenase 1	Homo sapiens	19-23
32278282-8	2020	Finally, silencing HO-1 expression partially rescued the proliferative and migratory response of canagliflozin-treated SMCs, and this was reversed by carbon monoxide and bilirubin.	Carbon Monoxide	150-165	heme oxygenase 1	Homo sapiens	19-23
32278282-8	2020	Finally, silencing HO-1 expression partially rescued the proliferative and migratory response of canagliflozin-treated SMCs, and this was reversed by carbon monoxide and bilirubin.	Bilirubin	170-179	heme oxygenase 1	Homo sapiens	19-23
32278282-10	2020	Moreover, it demonstrates that canagliflozin stimulates the expression of HO-1 in vascular SMCs via the ROS-Nrf2 pathway, and that the induction of HO-1 contributes to the cellular actions of canagliflozin.	Canagliflozin	31-44	heme oxygenase 1	Homo sapiens	74-78
32278282-10	2020	Moreover, it demonstrates that canagliflozin stimulates the expression of HO-1 in vascular SMCs via the ROS-Nrf2 pathway, and that the induction of HO-1 contributes to the cellular actions of canagliflozin.	Reactive Oxygen Species	104-107	heme oxygenase 1	Homo sapiens	74-78
32278282-10	2020	Moreover, it demonstrates that canagliflozin stimulates the expression of HO-1 in vascular SMCs via the ROS-Nrf2 pathway, and that the induction of HO-1 contributes to the cellular actions of canagliflozin.	Canagliflozin	192-205	heme oxygenase 1	Homo sapiens	148-152
32411596-9	2020	Importantly, SOX8 might be a potential regulator of reactive oxygen species (ROS) homeostasis, as SOX8 regulated the expression of antioxidant enzymes (GPX1, HMOX1) and reduced drug-induced ROS accumulation in GTN cell models.	Reactive Oxygen Species	52-75	heme oxygenase 1	Homo sapiens	158-163
32410998-0	2020	Paeoniflorin Resists H2O2-Induced Oxidative Stress in Melanocytes by JNK/Nrf2/HO-1 Pathway.	peoniflorin	0-12	heme oxygenase 1	Homo sapiens	78-82
32410998-0	2020	Paeoniflorin Resists H2O2-Induced Oxidative Stress in Melanocytes by JNK/Nrf2/HO-1 Pathway.	Hydrogen Peroxide	21-25	heme oxygenase 1	Homo sapiens	78-82
32410998-5	2020	Furthermore, PF activated c-Jun amino terminal kinase (JNK) and the nuclear factor E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway to counteract H2O2-induced oxidative damage in PIG1 and PIG3V.	Hydrogen Peroxide	156-160	heme oxygenase 1	Homo sapiens	110-126
32410998-5	2020	Furthermore, PF activated c-Jun amino terminal kinase (JNK) and the nuclear factor E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway to counteract H2O2-induced oxidative damage in PIG1 and PIG3V.	Hydrogen Peroxide	156-160	heme oxygenase 1	Homo sapiens	128-132
32410998-6	2020	Taken together, our study firstly demonstrates that PF resists H2O2-induced oxidative stress in melanocytes probably by activating JNK/Nrf2/HO-1 signaling, suggesting a potential therapeutic application of PF on vitiligo.	Hydrogen Peroxide	63-67	heme oxygenase 1	Homo sapiens	140-144
32411596-9	2020	Importantly, SOX8 might be a potential regulator of reactive oxygen species (ROS) homeostasis, as SOX8 regulated the expression of antioxidant enzymes (GPX1, HMOX1) and reduced drug-induced ROS accumulation in GTN cell models.	Reactive Oxygen Species	77-80	heme oxygenase 1	Homo sapiens	158-163
32411596-9	2020	Importantly, SOX8 might be a potential regulator of reactive oxygen species (ROS) homeostasis, as SOX8 regulated the expression of antioxidant enzymes (GPX1, HMOX1) and reduced drug-induced ROS accumulation in GTN cell models.	Reactive Oxygen Species	190-193	heme oxygenase 1	Homo sapiens	158-163
32298237-5	2020	Downregulation of HO-1 using pharmacological inhibitor ZnPPIX or siRNA knockdown significantly enhanced myeloma cell sensitivity to bortezomib in human primary CD138+ cells, U266 and RPMI8226 cell lines.	Bortezomib	132-142	heme oxygenase 1	Homo sapiens	18-22
32361557-16	2020	4,5-CQME also regulated the Keap1/Nrf2 signaling pathway and enhanced both the mRNA and protein expressions of HO-1 and NQO1.	4,5-cqme	0-8	heme oxygenase 1	Homo sapiens	111-115
32387991-7	2020	Moreover, the nuclear factor E2 related factor (Nrf2) protein expression in the ferulic acid group positively correlated with the HO-1, GCLC and NQO1 protein levels.	ferulic acid	80-92	heme oxygenase 1	Homo sapiens	130-134
32298237-0	2020	Heme oxygenase-1 inhibition mediates Gas6 to enhance bortezomib-sensitivity in multiple myeloma via ERK/STAT3 axis.	Bortezomib	53-63	heme oxygenase 1	Homo sapiens	0-16
32298237-3	2020	Here we aim to investigate the role and mechanism of HO-1 in bortezomib-sensitivity to myeloma cells.	Bortezomib	61-71	heme oxygenase 1	Homo sapiens	53-57
32410860-0	2020	Carbon Monoxide-Releasing Molecule-3 Suppresses Tumor Necrosis Factor-alpha- and Interleukin-1beta-Induced Expression of Junctional Molecules on Human Gingival Fibroblasts via the Heme Oxygenase-1 Pathway.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	180-196
32321531-0	2020	Alantolactone suppresses inflammation, apoptosis and oxidative stress in cigarette smoke-induced human bronchial epithelial cells through activation of Nrf2/HO-1 and inhibition of the NF-kappaB pathways.	alantolactone	0-13	heme oxygenase 1	Homo sapiens	157-161
32298237-7	2020	Combination with HO-1 inhibition increased bortezomib-induced apoptosis and antiproliferative effects via suppressing Gas6 production.	Bortezomib	43-53	heme oxygenase 1	Homo sapiens	17-21
32298237-5	2020	Downregulation of HO-1 using pharmacological inhibitor ZnPPIX or siRNA knockdown significantly enhanced myeloma cell sensitivity to bortezomib in human primary CD138+ cells, U266 and RPMI8226 cell lines.	zinc protoporphyrin	55-61	heme oxygenase 1	Homo sapiens	18-22
32298237-8	2020	These findings suggest that combination of bortezomib and HO-1 inhibitor may serve as a promising therapeutic target against bortezomib-resistant MM.	Bortezomib	125-135	heme oxygenase 1	Homo sapiens	58-62
32308771-10	2020	In vitro, beta-elemene in combination with cetuximab was shown to induce iron-dependent reactive oxygen species (ROS) accumulation, glutathione (GSH) depletion, lipid peroxidation, upregulation of HO-1 and transferrin, and downregulation of negative regulatory proteins for ferroptosis (GPX4, SLC7A11, FTH1, glutaminase, and SLC40A1) in KRAS mutant CRC cells.	beta-elemene	10-22	heme oxygenase 1	Homo sapiens	197-201
32264868-8	2020	EMPA and DAPA (100 muM) significantly reduced SA-induced inflammation (IL1beta, TNFalpha, MCP1), oxidant stress (SOD2, TXN, HO1), but not apoptosis in MAC.	empagliflozin	0-4	heme oxygenase 1	Homo sapiens	124-127
32264868-8	2020	EMPA and DAPA (100 muM) significantly reduced SA-induced inflammation (IL1beta, TNFalpha, MCP1), oxidant stress (SOD2, TXN, HO1), but not apoptosis in MAC.	dapagliflozin	9-13	heme oxygenase 1	Homo sapiens	124-127
32293500-7	2020	BIX-01294 treatment or siRNA-mediated G9a knockdown led to the activation of the PERK/NRF2 pathway and HO-1 upregulation in KG1 cells.	BIX 01294	0-9	heme oxygenase 1	Homo sapiens	103-107
32377300-5	2020	According to recently published data, increased endogenous CO production by inducible HO-1, its delivery by novel pharmacological CO-releasing agents, or even the direct inhalation of CO has been considered a promising alternative in future experimental and clinical therapies against various GI disorders.	Carbon Monoxide	59-61	heme oxygenase 1	Homo sapiens	86-90
32334435-11	2020	Resveratrol in combination with HQ significantly upregulated HO-1 mRNA expression above that of HQ-treated cells alone.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	61-65
31981945-11	2020	In particular, OXC treatment significantly enhanced expressions of nuclear factor erythroid 2-related factor 2 (Nrf2) and its downstream protein heme oxygenase-1 in ischemic CA1.	Oxcarbazepine	15-18	heme oxygenase 1	Homo sapiens	145-161
32228565-0	2020	Activation of the Nrf2/HO-1 pathway by curcumin inhibits oxidative stress in human nasal fibroblasts exposed to urban particulate matter.	Curcumin	39-47	heme oxygenase 1	Homo sapiens	23-27
31964465-0	2020	15d-PGJ2 inhibits NF-kappaB and AP-1-mediated MMP-9 expression and invasion of breast cancer cell by means of a heme oxygenase-1-dependent mechanism.	15-deoxyprostaglandin J2	0-8	heme oxygenase 1	Homo sapiens	112-128
31964465-5	2020	In this study, we investigated the effects of induction of HO-1 by PPARgamma on TPAinduced MMP-9 expression and cell invasion using MCF-7 breast cancer cells.	tpainduced	80-90	heme oxygenase 1	Homo sapiens	59-63
31964465-8	2020	15d-PGJ2 induced HO-1 expression in a dose-dependent manner.	15-deoxyprostaglandin J2	0-8	heme oxygenase 1	Homo sapiens	17-21
31964465-9	2020	Interestingly, HO-1 siRNA significantly attenuated the inhibition of TPA-induced MMP-9 protein expression and cell invasion by 15d-PGJ2.	15-deoxyprostaglandin J2	127-135	heme oxygenase 1	Homo sapiens	15-19
31964465-10	2020	These results suggest that 15d-PGJ2 inhibits TPA-induced MMP- 9 expression and invasion of MCF-7 cells by means of a heme oxygenase-1-dependent mechanism.	15-deoxyprostaglandin J2	27-35	heme oxygenase 1	Homo sapiens	117-133
31978617-9	2020	In addition, RSV reduced the levels of senescence-associated secretory phenotype (SASP), gene markers associated with senescence (P53, P16, and P21), intracellular ROS levels and increased gene expression of enzymes protecting cells from oxidative damage (HMOX1 and SOD3).	resveratrol	13-16	heme oxygenase 1	Homo sapiens	256-261
32023790-10	2020	In addition, BPA treatment enhanced gene expression of antioxidant enzymes, heme oxygenase(HO)-1, catalase, superoxide dismutase(SOD) 1 and 2.	bisphenol A	13-16	heme oxygenase 1	Homo sapiens	76-106
31376303-0	2020	HO-1 downregulation favors BRAFV600 melanoma cell death induced by Vemurafenib/PLX4032 and increases NK recognition.	Vemurafenib	67-78	heme oxygenase 1	Homo sapiens	0-4
31376303-0	2020	HO-1 downregulation favors BRAFV600 melanoma cell death induced by Vemurafenib/PLX4032 and increases NK recognition.	Vemurafenib	79-86	heme oxygenase 1	Homo sapiens	0-4
31376303-4	2020	We have investigated the role of HO-1 expression in Vemurafenib-treated BRAFV600 melanoma cells in modulating their susceptibility to NK cell-mediated recognition.	Vemurafenib	52-63	heme oxygenase 1	Homo sapiens	33-37
31376303-7	2020	HO-1 silencing/inhibition was able to induce a further significant reduction of Vemurafenib-treated melanoma viability.	Vemurafenib	80-91	heme oxygenase 1	Homo sapiens	0-4
31376303-9	2020	Furthermore, melanoma cell treatment with Vemurafenib downregulated the expression of ligands of NKp30 and NKG2D activating receptors, and HO-1 silencing/inhibition was able to restore their expression.	Vemurafenib	42-53	heme oxygenase 1	Homo sapiens	107-143
31376303-10	2020	Our results indicate that HO-1 downregulation can both improve the efficacy of Vemurafenib on melanoma cells and favor melanoma susceptibility to NK cell-mediated recognition and killing.	Vemurafenib	79-90	heme oxygenase 1	Homo sapiens	26-30
31895874-9	2020	In addition, EGCG prevents enhanced oxidative stress via the Nrf2/HO-1 pathway.	epigallocatechin gallate	13-17	heme oxygenase 1	Homo sapiens	66-70
32163836-7	2020	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase (FECH) and heme oxygenase-1 (HO-1) and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	21-25	heme oxygenase 1	Homo sapiens	154-170
32163836-7	2020	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase (FECH) and heme oxygenase-1 (HO-1) and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	21-25	heme oxygenase 1	Homo sapiens	172-176
32163836-7	2020	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase (FECH) and heme oxygenase-1 (HO-1) and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	111-115	heme oxygenase 1	Homo sapiens	154-170
32163836-7	2020	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase (FECH) and heme oxygenase-1 (HO-1) and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	111-115	heme oxygenase 1	Homo sapiens	172-176
32163836-7	2020	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase (FECH) and heme oxygenase-1 (HO-1) and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	111-115	heme oxygenase 1	Homo sapiens	154-170
32163836-7	2020	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase (FECH) and heme oxygenase-1 (HO-1) and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	111-115	heme oxygenase 1	Homo sapiens	172-176
32163836-8	2020	Based on the availability of compounds targeting these proteins and inhibiting them, in this study we used modulators such as genistein, an isoflavone able to inhibit ABCG2; deferoxamine, which chelate iron ions impairing FECH activity and tin protoporphyrin IX (SnPP), the specific HO-1 inhibitor.	Genistein	126-135	heme oxygenase 1	Homo sapiens	283-287
32163836-8	2020	Based on the availability of compounds targeting these proteins and inhibiting them, in this study we used modulators such as genistein, an isoflavone able to inhibit ABCG2; deferoxamine, which chelate iron ions impairing FECH activity and tin protoporphyrin IX (SnPP), the specific HO-1 inhibitor.	Deferoxamine	174-186	heme oxygenase 1	Homo sapiens	283-287
32420127-0	2020	Proteomic analysis of oxidative stress response in human umbilical vein endothelial cells (HUVECs): role of heme oxygenase 1 (HMOX1) in hypoxanthine-induced oxidative stress in HUVECs.	Hypoxanthine	136-148	heme oxygenase 1	Homo sapiens	108-124
32420127-0	2020	Proteomic analysis of oxidative stress response in human umbilical vein endothelial cells (HUVECs): role of heme oxygenase 1 (HMOX1) in hypoxanthine-induced oxidative stress in HUVECs.	Hypoxanthine	136-148	heme oxygenase 1	Homo sapiens	126-131
32420127-11	2020	Conclusions: We found that HMOX1 was closely related to the oxidative stress response induced by hypoxanthine.	Hypoxanthine	97-109	heme oxygenase 1	Homo sapiens	27-32
31868938-7	2020	Furthermore, GCN2 knockdown reduced cell apoptosis and enhanced the activation of nuclear factor E2-related factor 2/heme oxygenase-1 (Nrf2/HO-1) pathway in high glucose-stimulated ARPE-19 cells.	Glucose	162-169	heme oxygenase 1	Homo sapiens	140-144
31868938-9	2020	Taken together, our findings suggest that knockdown of GCN2 inhibits high glucose-induced oxidative stress and apoptosis in ARPE-19 cells through activation of the Nrf2/HO-1 pathway.	Glucose	74-81	heme oxygenase 1	Homo sapiens	169-173
31541463-0	2020	Acetaminophen sensitizing erastin-induced ferroptosis via modulation of Nrf2/heme oxygenase-1 signaling pathway in non-small-cell lung cancer.	Acetaminophen	0-13	heme oxygenase 1	Homo sapiens	77-93
31541463-6	2020	As a downstream gene of Nrf2, heme oxygenase-1 expression decreased significantly with the cotreatment of erastin and APAP, which could be rescued by BM.	Acetaminophen	118-122	heme oxygenase 1	Homo sapiens	30-46
31541463-6	2020	As a downstream gene of Nrf2, heme oxygenase-1 expression decreased significantly with the cotreatment of erastin and APAP, which could be rescued by BM.	bardoxolone methyl	150-152	heme oxygenase 1	Homo sapiens	30-46
32259676-12	2020	Moreover, limonin induced activation of Nrf2 and increased protein expression and mRNA levels of its downstream targets, including HO-1, NQO1 and GCLC/GCLM.	limonin	10-17	heme oxygenase 1	Homo sapiens	131-135
32228565-10	2020	Nrf2 production was also promoted to increase the expression of HO-1 and SOD2 by curcumin.	Curcumin	81-89	heme oxygenase 1	Homo sapiens	64-68
32225089-7	2020	Oxidative stress response was also impaired in HACE1 fibroblasts, as shown by the reduced NQO1 and Hmox1 mRNA levels observed in H2O2-treated cells.	Hydrogen Peroxide	129-133	heme oxygenase 1	Homo sapiens	99-104
32231654-5	2020	The results demonstrated that induction of HO-1 via cobalt-protoporphyrin (CoPP) markedly suppressed PRV replication, while HO-1 specific small interfering RNA or inhibitor zinc-protoporphyrin partially reversed the inhibitory effect of CoPP on PRV replication.	cobaltiprotoporphyrin	52-73	heme oxygenase 1	Homo sapiens	43-47
32204510-4	2020	Ectopic overexpression of HO-1 not only attenuated cell proliferation in vitro and in vivo, but also blocked the reactive oxygen species (ROS) induced by H2O2 and the pyocyanin in HepG2 or Hep3B cells.	Reactive Oxygen Species	113-136	heme oxygenase 1	Homo sapiens	26-30
32204510-4	2020	Ectopic overexpression of HO-1 not only attenuated cell proliferation in vitro and in vivo, but also blocked the reactive oxygen species (ROS) induced by H2O2 and the pyocyanin in HepG2 or Hep3B cells.	Reactive Oxygen Species	138-141	heme oxygenase 1	Homo sapiens	26-30
32204510-4	2020	Ectopic overexpression of HO-1 not only attenuated cell proliferation in vitro and in vivo, but also blocked the reactive oxygen species (ROS) induced by H2O2 and the pyocyanin in HepG2 or Hep3B cells.	Hydrogen Peroxide	154-158	heme oxygenase 1	Homo sapiens	26-30
32204510-4	2020	Ectopic overexpression of HO-1 not only attenuated cell proliferation in vitro and in vivo, but also blocked the reactive oxygen species (ROS) induced by H2O2 and the pyocyanin in HepG2 or Hep3B cells.	Pyocyanine	167-176	heme oxygenase 1	Homo sapiens	26-30
32188144-4	2020	Mechanistic investigations found that the downregulation of cellular IAP 1 (cIAP1)/X-chromosome-linked IAP (XIAP) and upregulation of heme oxygenase-1 (HO-1) were critical for DMC-induced caspase-8/-9/-3 activation and apoptotic cell death.	demethoxycurcumin	176-179	heme oxygenase 1	Homo sapiens	134-150
32188144-4	2020	Mechanistic investigations found that the downregulation of cellular IAP 1 (cIAP1)/X-chromosome-linked IAP (XIAP) and upregulation of heme oxygenase-1 (HO-1) were critical for DMC-induced caspase-8/-9/-3 activation and apoptotic cell death.	demethoxycurcumin	176-179	heme oxygenase 1	Homo sapiens	152-156
32188144-5	2020	Moreover, p38 mitogen-activated protein kinase (MAPK) and c-Jun N-terminal kinase (JNK)1/2 were activated by DMC treatment in OSCC cells, and only the inhibition of p38 MAPK significantly abolished DMC-induced HO-1 expression and caspase-8/-9/-3 activation.	demethoxycurcumin	109-112	heme oxygenase 1	Homo sapiens	210-214
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Heme	52-56	heme oxygenase 1	Homo sapiens	0-16
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Heme	52-56	heme oxygenase 1	Homo sapiens	18-22
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Biliverdine	62-72	heme oxygenase 1	Homo sapiens	0-16
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Biliverdine	62-72	heme oxygenase 1	Homo sapiens	18-22
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Biliverdine	74-76	heme oxygenase 1	Homo sapiens	0-16
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Biliverdine	74-76	heme oxygenase 1	Homo sapiens	18-22
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Iron	79-83	heme oxygenase 1	Homo sapiens	0-16
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Iron	79-83	heme oxygenase 1	Homo sapiens	18-22
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	0-16
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	18-22
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Carbon Monoxide	105-107	heme oxygenase 1	Homo sapiens	0-16
32231654-2	2020	Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors.	Carbon Monoxide	105-107	heme oxygenase 1	Homo sapiens	18-22
32231654-5	2020	The results demonstrated that induction of HO-1 via cobalt-protoporphyrin (CoPP) markedly suppressed PRV replication, while HO-1 specific small interfering RNA or inhibitor zinc-protoporphyrin partially reversed the inhibitory effect of CoPP on PRV replication.	cobaltiprotoporphyrin	75-79	heme oxygenase 1	Homo sapiens	43-47
32168943-0	2020	New Arylethanolimidazole Derivatives as HO-1 Inhibitors with Cytotoxicity against MCF-7 Breast Cancer Cells.	arylethanolimidazole	4-24	heme oxygenase 1	Homo sapiens	40-44
32168943-1	2020	In this paper, a novel series of imidazole-based heme oxygenase-1 (HO-1) inhibitors is reported.	imidazole	33-42	heme oxygenase 1	Homo sapiens	49-65
32168943-1	2020	In this paper, a novel series of imidazole-based heme oxygenase-1 (HO-1) inhibitors is reported.	imidazole	33-42	heme oxygenase 1	Homo sapiens	67-71
31604020-0	2020	Salvianolic acid B exerts a protective effect in acute liver injury by regulating the Nrf2/HO-1 signaling pathway.	salvianolic acid B	0-18	heme oxygenase 1	Homo sapiens	91-95
31972171-2	2020	Treatment of mouse epidermal JB-6 cells with curcumin resulted in the induction of HO-1 expression, and this was abrogated in cells transiently transfected with Nrf2 siRNA.	Curcumin	45-53	heme oxygenase 1	Homo sapiens	83-87
32121588-1	2020	Mevastatin (MVS) has been previously shown to induce heme oxygenase (HO)-1 expression through Nox/ROS-dependent PDGFRalpha/PI3K/Akt/Nrf2/ARE axis in human pulmonary alveolar epithelial cells (HPAEpiCs).	mevastatin	0-10	heme oxygenase 1	Homo sapiens	53-74
32121588-1	2020	Mevastatin (MVS) has been previously shown to induce heme oxygenase (HO)-1 expression through Nox/ROS-dependent PDGFRalpha/PI3K/Akt/Nrf2/ARE axis in human pulmonary alveolar epithelial cells (HPAEpiCs).	mevastatin	12-15	heme oxygenase 1	Homo sapiens	53-74
32121588-1	2020	Mevastatin (MVS) has been previously shown to induce heme oxygenase (HO)-1 expression through Nox/ROS-dependent PDGFRalpha/PI3K/Akt/Nrf2/ARE axis in human pulmonary alveolar epithelial cells (HPAEpiCs).	ros	98-101	heme oxygenase 1	Homo sapiens	53-74
31846839-10	2020	Vinp reduced activation of NF-kappaB, MAPK, and AKT signaling during osteoclastogenesis and prevented the production of reactive oxygen species with increased nuclear factor erythroid 2-related factor 2, heme oxygenase 1, and NAD(P)H:quinone acceptor oxidoreductase 1 expression.	vinpocetine	0-4	heme oxygenase 1	Homo sapiens	204-220
31604020-3	2020	The objective of this study was to investigate the underlying mechanism of Sal B in CCl4-induced acute liver injury, especially its effect on the Nrf2/HO-1 signaling pathway.	salvianolic acid B	75-80	heme oxygenase 1	Homo sapiens	151-155
31981961-8	2020	The miR-548a-3p might regulate the cellular response to hydrogen peroxide through HO-1 and HIF-1pathway.	Hydrogen Peroxide	56-73	heme oxygenase 1	Homo sapiens	82-86
32111854-5	2020	The autophagy inhibitor bafilomycin caused a significant decrease in the production of Nrf2, HO-1 and NQO1 compared to DEPs treatment, whereas the Nrf2 activator sulforaphane increased the LC3B (p = 0.020) levels.	bafilomycin	24-35	heme oxygenase 1	Homo sapiens	93-97
32056044-0	2020	Non-competitive heme oxygenase-1 activity inhibitor reduces non-small cell lung cancer glutathione content and regulates cell proliferation.	Glutathione	87-98	heme oxygenase 1	Homo sapiens	16-32
32056044-4	2020	NSCLC cell line (A549) was treated with the HO-1 activity inhibitor VP13/47 (10 microM) and we further evaluated cell viability, apoptosis, mitochondrial dysfunction and oxidative stress.	vp13/47	68-75	heme oxygenase 1	Homo sapiens	44-48
31965713-7	2020	In addition, TMS could activate ERK/Nrf2/HO-1 signaling which increased the expression of ATP-binding cassette transporters.	Adenosine Triphosphate	90-93	heme oxygenase 1	Homo sapiens	41-45
31972252-6	2020	In high glucose-incubated vascular endothelial cells, NO donor attenuated oxidative stress and endothelial dysfunction via the inhibition of NADPH oxidase, where a heme oxygenase-1 (HO-1)-dependent mechanism was demonstrated for the antioxidant abilities of NO.	Glucose	8-15	heme oxygenase 1	Homo sapiens	164-180
31972252-6	2020	In high glucose-incubated vascular endothelial cells, NO donor attenuated oxidative stress and endothelial dysfunction via the inhibition of NADPH oxidase, where a heme oxygenase-1 (HO-1)-dependent mechanism was demonstrated for the antioxidant abilities of NO.	NADP	141-146	heme oxygenase 1	Homo sapiens	164-180
32274105-8	2020	Also, Sch A downregulated the expression of IL-8 and upregulated the expression of HO-1 mRNA in lung epithelial cells and cell supernatants, and resulted in the downregulation of the protein expression level of phosphorylated nuclear factor-kappaB.	schizandrin A	6-11	heme oxygenase 1	Homo sapiens	83-87
32035862-2	2020	In living organisms, it is produced endogenously during the degradation of heme by oxygenase, which occurs in three isoforms: HO-1, HO-2 and HO-3.	Heme	75-79	heme oxygenase 1	Homo sapiens	126-130
32106617-3	2020	Pretreatment with blueberry anthocyanin extract, malvidin, malvidin-3-glucoside, and malvidin-3-galactoside significantly ameliorated high-glucose-induced damage by enhancing endogenous antioxidant superoxide dismutase (SOD) and heme oxygenase-1 (HO-1), lowering reactive oxygen species (ROS) generation and NADPH oxidase isoform 4 (NOX4) expression, and increasing the cell vitalities.	Anthocyanins	28-39	heme oxygenase 1	Homo sapiens	229-245
32106617-3	2020	Pretreatment with blueberry anthocyanin extract, malvidin, malvidin-3-glucoside, and malvidin-3-galactoside significantly ameliorated high-glucose-induced damage by enhancing endogenous antioxidant superoxide dismutase (SOD) and heme oxygenase-1 (HO-1), lowering reactive oxygen species (ROS) generation and NADPH oxidase isoform 4 (NOX4) expression, and increasing the cell vitalities.	Glucose	139-146	heme oxygenase 1	Homo sapiens	229-245
32318125-0	2020	Erratum to "Tetrandrine Ameliorates Airway Remodeling of Chronic Asthma by Interfering TGF-beta1/Nrf-2/HO-1 Signaling Pathway-Mediated Oxidative Stress".	tetrandrine	12-23	heme oxygenase 1	Homo sapiens	103-107
32057253-6	2020	Astragaloside IV could increase the expression of HO-1 and Nrf2 for promoting the oxidant protective effect.Conclusion: Aastragaloside IV has an anti-inflammatory and oxidative effect via regulated NF-kappaB, MAPK and HO-1/Nrf2 signalling pathways in human bronchial epithelial cells.	aastragaloside	120-134	heme oxygenase 1	Homo sapiens	218-222
32057253-6	2020	Astragaloside IV could increase the expression of HO-1 and Nrf2 for promoting the oxidant protective effect.Conclusion: Aastragaloside IV has an anti-inflammatory and oxidative effect via regulated NF-kappaB, MAPK and HO-1/Nrf2 signalling pathways in human bronchial epithelial cells.	astragaloside A	0-13	heme oxygenase 1	Homo sapiens	50-54
32057253-6	2020	Astragaloside IV could increase the expression of HO-1 and Nrf2 for promoting the oxidant protective effect.Conclusion: Aastragaloside IV has an anti-inflammatory and oxidative effect via regulated NF-kappaB, MAPK and HO-1/Nrf2 signalling pathways in human bronchial epithelial cells.	astragaloside A	0-13	heme oxygenase 1	Homo sapiens	218-222
32015215-5	2020	These effects were reversed by treatment with the early autophagy inhibitor 3-methyl adenine, which suggests HO-1-induced autophagy suppresses IL-1beta-induced apoptosis in NPCs.	3-methyladenine	76-92	heme oxygenase 1	Homo sapiens	109-113
32057253-6	2020	Astragaloside IV could increase the expression of HO-1 and Nrf2 for promoting the oxidant protective effect.Conclusion: Aastragaloside IV has an anti-inflammatory and oxidative effect via regulated NF-kappaB, MAPK and HO-1/Nrf2 signalling pathways in human bronchial epithelial cells.	aastragaloside	120-134	heme oxygenase 1	Homo sapiens	50-54
32075047-7	2020	RosA promotes the expression of Heme oxygenase-1 (HO-1) and reduces the production of reactive oxygen species (Ros), which is induced by Dox.	rosmarinic acid	0-4	heme oxygenase 1	Homo sapiens	32-48
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Heme	83-87	heme oxygenase 1	Homo sapiens	0-16
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Heme	83-87	heme oxygenase 1	Homo sapiens	18-22
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	0-16
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	18-22
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Iron	110-114	heme oxygenase 1	Homo sapiens	0-16
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Iron	110-114	heme oxygenase 1	Homo sapiens	18-22
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	0-16
32059452-1	2020	Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	18-22
32050604-4	2020	However, the expression of hemoxygenase-1 (HO-1) protein was up-regulated upon exposure to floridoside, and two antioxidant enzymes, superoxide dismutase (SOD) and GSH-Px, were activated by floridoside.	2-galactopyranosylglycerol	91-102	heme oxygenase 1	Homo sapiens	27-47
32050604-4	2020	However, the expression of hemoxygenase-1 (HO-1) protein was up-regulated upon exposure to floridoside, and two antioxidant enzymes, superoxide dismutase (SOD) and GSH-Px, were activated by floridoside.	Glutathione	164-167	heme oxygenase 1	Homo sapiens	27-47
32050604-4	2020	However, the expression of hemoxygenase-1 (HO-1) protein was up-regulated upon exposure to floridoside, and two antioxidant enzymes, superoxide dismutase (SOD) and GSH-Px, were activated by floridoside.	2-galactopyranosylglycerol	190-201	heme oxygenase 1	Homo sapiens	27-47
31902541-0	2020	Corrigendum to "Cytoprotective effect of Fufang Lurong Jiangu capsule against hydrogen peroxide-induced oxidative stress in bone marrow stromal cell-derived osteoblasts through the Nrf2/HO-1 signaling pathway" [Biomed.	Hydrogen Peroxide	78-95	heme oxygenase 1	Homo sapiens	186-190
31848666-0	2020	Heme oxygenase-1 regulates autophagy through carbon-oxygen to alleviate deoxynivalenol-induced hepatic damage.	Carbon	45-51	heme oxygenase 1	Homo sapiens	0-16
31848666-0	2020	Heme oxygenase-1 regulates autophagy through carbon-oxygen to alleviate deoxynivalenol-induced hepatic damage.	deoxynivalenol	72-86	heme oxygenase 1	Homo sapiens	0-16
31848666-5	2020	Importantly, AAV-mediated liver-specific overexpression of HO-1 reversed DON-induced liver damages, upregulated autophagy and attenuated apoptosis in liver, while AAV-mediated HO-1 silence aggravated DON-induced liver damages, inhibited autophagy and increased apoptosis.	deoxynivalenol	73-76	heme oxygenase 1	Homo sapiens	59-63
31848666-5	2020	Importantly, AAV-mediated liver-specific overexpression of HO-1 reversed DON-induced liver damages, upregulated autophagy and attenuated apoptosis in liver, while AAV-mediated HO-1 silence aggravated DON-induced liver damages, inhibited autophagy and increased apoptosis.	deoxynivalenol	200-203	heme oxygenase 1	Homo sapiens	59-63
31848666-5	2020	Importantly, AAV-mediated liver-specific overexpression of HO-1 reversed DON-induced liver damages, upregulated autophagy and attenuated apoptosis in liver, while AAV-mediated HO-1 silence aggravated DON-induced liver damages, inhibited autophagy and increased apoptosis.	deoxynivalenol	200-203	heme oxygenase 1	Homo sapiens	176-180
31848666-8	2020	Therefore, we suppose that HO-1 might be a potential research target to protect human and animal from liver injuries induced by low dose of DON exposure.	deoxynivalenol	140-143	heme oxygenase 1	Homo sapiens	27-31
31787334-5	2020	The sR9-mediated heme oxygenase-1 siRNA (siHO-1) delivery efficiently enhanced apoptotic response to daunorubicin of AML cells and AML-targeted HO-1 silencing improved chemotherapy and prolonged survival in orthotopic myeloid leukemia model.	Daunorubicin	101-113	heme oxygenase 1	Homo sapiens	43-47
31705351-10	2020	Overexpression of HO-1 in HER2-expressing SKBR3 breast cancer cells resulted in reduced sensitivity to both pan-HER family kinase inhibitors sapatinib and lapatinib.	sapatinib	141-150	heme oxygenase 1	Homo sapiens	18-22
31705351-10	2020	Overexpression of HO-1 in HER2-expressing SKBR3 breast cancer cells resulted in reduced sensitivity to both pan-HER family kinase inhibitors sapatinib and lapatinib.	lapatinib	155-164	heme oxygenase 1	Homo sapiens	18-22
31705351-13	2020	Treatment with autophagy inhibitors was able to increase the sensitivity of the HO-1 over-expressing cells to both lapatinib and sapatinib.	lapatinib	115-124	heme oxygenase 1	Homo sapiens	80-84
31705351-13	2020	Treatment with autophagy inhibitors was able to increase the sensitivity of the HO-1 over-expressing cells to both lapatinib and sapatinib.	sapatinib	129-138	heme oxygenase 1	Homo sapiens	80-84
32141582-5	2020	Furthermore, the expression of antioxidant factor Nrf2, as well as downstream antioxidant genes, including NQO1, SOD1, SOD2, and HO1 was assessed in hydroquinone stimulated ARPE19 cells, in the presence or absence of SAC pretreatment.	hydroquinone	149-161	heme oxygenase 1	Homo sapiens	129-132
32010329-8	2020	However, S1PC was found to augment HMOX1 expression, induced by NO donors, such as NOR3.	1-propenylcysteine sulfoxide	9-13	heme oxygenase 1	Homo sapiens	35-40
32096202-12	2020	Melatonin reduced the ROS, MDA, 4-HNE, and 8-OHdG contents but further enhanced the levels of the nuclear factor E2-related factor-2 (Nrf2) and heme oxygenase (HO-1).	Melatonin	0-9	heme oxygenase 1	Homo sapiens	160-164
32096202-13	2020	Melatonin-increased viability and melatonin-decreased LDH release were also mediated by the blockage of NF-kappaB or reversed by Nrf2 or HO-1 knockdown.	Melatonin	0-9	heme oxygenase 1	Homo sapiens	137-141
32096202-13	2020	Melatonin-increased viability and melatonin-decreased LDH release were also mediated by the blockage of NF-kappaB or reversed by Nrf2 or HO-1 knockdown.	Melatonin	34-43	heme oxygenase 1	Homo sapiens	137-141
32096202-16	2020	CONCLUSIONS: Melatonin protected SH SY5Y cells from OGD/R induced oxidative stress, inflammation, apoptosis, and autophagy by blocking NF-kappaB signaling and activating Nrf2/HO-1, Akt, and mTOR/p70S6K/4E-BP-1 pathways, thereby indicating that melatonin is a potential and novel therapeutic drug for ischemic stroke.	Melatonin	13-22	heme oxygenase 1	Homo sapiens	175-179
32411446-6	2020	Nrf2/HO-1 also has the ability to modulate calcium levels to prevent ferroptosis, pyroptosis, autophagy, programmed cell necrosis, alkaliptosis, and clockophagy.	Calcium	43-50	heme oxygenase 1	Homo sapiens	5-9
32082323-6	2020	Heme oxygenase-1 (HO-1, encoded by HMOX1) produces BV by heme degradation, while biliverdin reductase-A (BLVR-A) generates BR by the subsequent conversion of BV.	Heme	57-61	heme oxygenase 1	Homo sapiens	0-22
32082323-6	2020	Heme oxygenase-1 (HO-1, encoded by HMOX1) produces BV by heme degradation, while biliverdin reductase-A (BLVR-A) generates BR by the subsequent conversion of BV.	Heme	57-61	heme oxygenase 1	Homo sapiens	35-40
32082323-6	2020	Heme oxygenase-1 (HO-1, encoded by HMOX1) produces BV by heme degradation, while biliverdin reductase-A (BLVR-A) generates BR by the subsequent conversion of BV.	Bilirubin	123-125	heme oxygenase 1	Homo sapiens	0-22
31347162-0	2020	CD73-dependent adenosine dampens interleukin 1beta-induced CXCL8 production in gingival fibroblasts: Association with heme oxygenase-1 and adenosine monophosphate-activated protein kinase.	Adenosine	15-24	heme oxygenase 1	Homo sapiens	118-134
31347162-9	2020	ATP pretreatment impaired IL-1beta-induced CXCL8 secretion and required activation of heme oxygenase-1 (HO-1) and phosphorylated adenosine monophosphate-activated protein kinase (pAMPK).	Adenosine Triphosphate	0-3	heme oxygenase 1	Homo sapiens	86-102
31347162-9	2020	ATP pretreatment impaired IL-1beta-induced CXCL8 secretion and required activation of heme oxygenase-1 (HO-1) and phosphorylated adenosine monophosphate-activated protein kinase (pAMPK).	Adenosine Triphosphate	0-3	heme oxygenase 1	Homo sapiens	104-108
31347162-11	2020	CONCLUSIONS: CD73-generated adenosine dampens IL-1beta-induced CXCL8 in HGFs and involves HO-1 and pAMPK signaling.	Adenosine	28-37	heme oxygenase 1	Homo sapiens	90-94
31974615-5	2020	It was demonstrated that crocetin significantly attenuated the activities of pro-inflammatory cytokines and nuclear factor erythroid-2 related factor 2 (Nrf2)/heme oxygenase-1 signaling.	crocetin	25-33	heme oxygenase 1	Homo sapiens	159-175
31884405-0	2020	Protective effect of Hedansanqi Tiaozhi Tang against non-alcoholic fatty liver disease in vitro and in vivo through activating Nrf2/HO-1 antioxidant signaling pathway.	hedansanqi	21-31	heme oxygenase 1	Homo sapiens	132-136
31884405-0	2020	Protective effect of Hedansanqi Tiaozhi Tang against non-alcoholic fatty liver disease in vitro and in vivo through activating Nrf2/HO-1 antioxidant signaling pathway.	tiaozhi	32-39	heme oxygenase 1	Homo sapiens	132-136
31669540-9	2020	15-Keto PGE2 activated AKT signaling, and the pharmacological AKT inhibitor, LY294002 suppressed the 15-keto PGE2-induced HO-1 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	77-85	heme oxygenase 1	Homo sapiens	122-126
32082480-6	2020	Mechanistic studies proved that farrerol could induce an inhibitory phosphorylation of GSK-3beta at Ser9 without affecting the expression level of total GSK-3beta protein and promote the nuclear translocation of Nrf2 as well as the mRNA and protein expression of its downstream target genes heme oxygenase-1 (HO-1) and NAD(P)H: quinone oxidoreductase 1 (NQO1) in EA.hy926 cells.	farrerol	32-40	heme oxygenase 1	Homo sapiens	291-307
32064026-4	2020	In piglets fed a DON-contaminated diet, dietary supplementation with BCU significantly decreased the mRNA levels of P70S6K, 4E-BP1, and HSP70 in the liver, the protein expression of HO-1 in the jejunum, and the expression of p-Nrf2 and p-NF-kappaB in the ileum but increased Mn-SOD activity in serum.	(3r)-3,4-Dihydro-2h-Chromen-3-Ylmethanol	69-72	heme oxygenase 1	Homo sapiens	182-186
31964423-12	2020	HMOX1 inhibition by tin protoporphyrin (SnPP) in normal DBMSCs resulted in a reduction in proliferation, migration, adhesion, and clone formation processes as compared to the untreated controls.	tin protoporphyrin IX	20-38	heme oxygenase 1	Homo sapiens	0-5
31964423-12	2020	HMOX1 inhibition by tin protoporphyrin (SnPP) in normal DBMSCs resulted in a reduction in proliferation, migration, adhesion, and clone formation processes as compared to the untreated controls.	tin protoporphyrin IX	40-44	heme oxygenase 1	Homo sapiens	0-5
31964423-13	2020	mRNA and protein analyses of PE-DBMSCs preconditioned with H2O2 at lower doses showed upregulation of HMOX1 expression.	Water	59-63	heme oxygenase 1	Homo sapiens	102-107
32065759-7	2020	Hyperoxia was also found to diminish DNA damage and generation of free radicals initiated in B[a]P-treated cells which was attributed to an significant rise of Nrf2, leading to elevated antioxidant activities or detoxification proteins including heme oxygenase 1 (HO-1), superoxide dismutase (SOD), glutathione peroxidase-1/2 (GPX-1/2), CAT, GST and glutathione (GSH).	Phosphorus	97-98	heme oxygenase 1	Homo sapiens	246-262
32065759-7	2020	Hyperoxia was also found to diminish DNA damage and generation of free radicals initiated in B[a]P-treated cells which was attributed to an significant rise of Nrf2, leading to elevated antioxidant activities or detoxification proteins including heme oxygenase 1 (HO-1), superoxide dismutase (SOD), glutathione peroxidase-1/2 (GPX-1/2), CAT, GST and glutathione (GSH).	Phosphorus	97-98	heme oxygenase 1	Homo sapiens	264-268
32082188-3	2020	This review aims to provide an up-to-date and critical overview of the molecular mechanisms by which bilirubin derived from plasma or from HMOX1 activation in vascular cells affects endothelial function.	Bilirubin	101-110	heme oxygenase 1	Homo sapiens	139-144
32082188-5	2020	In this context, therapeutic interventions aimed at mildly increasing serum bilirubin as well as bilirubin generated endogenously by endothelial HMOX1 should be considered.	Bilirubin	97-106	heme oxygenase 1	Homo sapiens	145-150
31991717-4	2020	In our experimental model, main carnosine beneficial effects were: (1) the modulation of nitric oxide production and metabolism; (2) the amelioration of the macrophage energy state; (3) the decrease of the expressions of pro-oxidant enzymes (Nox-2, Cox-2) and of the lipid peroxidation product malondialdehyde; (4) the restoration and/or increase of the expressions of antioxidant enzymes (Gpx1, SOD-2 and Cat); (5) the increase of the transforming growth factor-beta1 (TGF-beta1) and the down-regulation of the expressions of interleukins 1beta and 6 (IL-1beta and IL-6) and 6) the increase of the expressions of Nuclear factor (erythroid-derived 2)-like 2 (Nrf2) and heme oxygenase-1 (HO-1).	Carnosine	32-41	heme oxygenase 1	Homo sapiens	669-685
32020857-12	2020	CONCLUSIONS: The neuroprotective effects of Danshensu on rotenone-induced PD are attributed to the anti-oxidative properties by activating PI3K/AKT/Nrf2 pathway and increasing Nrf2-induced expression of HO-1, GCLC, and GCLM, at least in part.	3,4-dihydroxyphenyllactic acid	44-53	heme oxygenase 1	Homo sapiens	203-207
32020857-12	2020	CONCLUSIONS: The neuroprotective effects of Danshensu on rotenone-induced PD are attributed to the anti-oxidative properties by activating PI3K/AKT/Nrf2 pathway and increasing Nrf2-induced expression of HO-1, GCLC, and GCLM, at least in part.	Rotenone	57-65	heme oxygenase 1	Homo sapiens	203-207
31974389-3	2020	We reported that both polyphenols show antioxidant and oto-protective activity in the cochlea by up-regulating Nrf-2/HO-1 pathway and downregulating p53 phosphorylation.	Polyphenols	22-33	heme oxygenase 1	Homo sapiens	117-121
31669540-0	2020	15-Keto prostaglandin E2 induces heme oxygenase-1 expression through activation of Nrf2 in human colon epithelial CCD 841 CoN cells.	15-ketoprostaglandin E2	0-24	heme oxygenase 1	Homo sapiens	33-49
31669540-5	2020	In this study, we found that 15-keto PGE2 upregulated the expression of heme oxygenase-1 (HO-1), a representative antioxidative and anti-inflammatory enzyme, at both transcriptional and translational levels, in human colon epithelial CCD 841 CoN cells.	Dinoprostone	37-41	heme oxygenase 1	Homo sapiens	72-88
31669540-5	2020	In this study, we found that 15-keto PGE2 upregulated the expression of heme oxygenase-1 (HO-1), a representative antioxidative and anti-inflammatory enzyme, at both transcriptional and translational levels, in human colon epithelial CCD 841 CoN cells.	Dinoprostone	37-41	heme oxygenase 1	Homo sapiens	90-94
31669540-8	2020	Furthermore, the silencing of the Nrf2 gene abolished 15-keto PGE2-induced HO-1 expression in CCD 841 CoN cells.	15-ketoprostaglandin E2	54-66	heme oxygenase 1	Homo sapiens	75-79
31669540-9	2020	15-Keto PGE2 activated AKT signaling, and the pharmacological AKT inhibitor, LY294002 suppressed the 15-keto PGE2-induced HO-1 expression.	15-ketoprostaglandin E2	0-12	heme oxygenase 1	Homo sapiens	122-126
31669540-9	2020	15-Keto PGE2 activated AKT signaling, and the pharmacological AKT inhibitor, LY294002 suppressed the 15-keto PGE2-induced HO-1 expression.	15-ketoprostaglandin E2	101-113	heme oxygenase 1	Homo sapiens	122-126
31669540-11	2020	N-acetyl-l-cysteine treatment attenuated the 15-keto PGE2-induced phosphorylation of GSK3beta, transcriptional activity of Nrf2, and subsequently HO-1 expression.	Acetylcysteine	0-19	heme oxygenase 1	Homo sapiens	146-150
31669540-11	2020	N-acetyl-l-cysteine treatment attenuated the 15-keto PGE2-induced phosphorylation of GSK3beta, transcriptional activity of Nrf2, and subsequently HO-1 expression.	Dinoprostone	53-57	heme oxygenase 1	Homo sapiens	146-150
31669540-13	2020	In conclusion, 15-keto PGE2 induces HO-1 expression through Nrf2 activation in human colon epithelial cells.	15-ketoprostaglandin E2	15-27	heme oxygenase 1	Homo sapiens	36-40
31952230-10	2020	CONCLUSIONS: MVS-induced HO-1 is, at least in part, mediated through a p47phox/Nox2/ROS-dependent activation of c-Src/PDGFRalpha/PI3K/Akt-regulated Nrf2/ARE axis and suppresses the TNF-alpha-mediated inflammatory responses in HPAEpiCs.	mevastatin	13-16	heme oxygenase 1	Homo sapiens	25-29
31952230-0	2020	Induction of HO-1 by Mevastatin Mediated via a Nox/ROS-Dependent c-Src/PDGFRalpha/PI3K/Akt/Nrf2/ARE Cascade Suppresses TNF-alpha-Induced Lung Inflammation.	mevastatin	21-31	heme oxygenase 1	Homo sapiens	13-17
31677563-8	2020	In the duodenum, glyphosate remarkably increased the relative mRNA expression levels of Nrf2 (linear and quadratic, P &lt; 0.05) and NQO1 (linear and quadratic, P &lt; 0.05) and reduced the relative mRNA expression levels of GPx1, HO-1 and GCLM (linear and quadratic, P &lt; 0.05).	glyphosate	17-27	heme oxygenase 1	Homo sapiens	231-235
32668967-2	2020	The aim of the this study was to examine the effects of [Formula: see text] (a rare protopanaxatriol-type ginsenoside fraction; Rg2, Rg4, Rg6, Rh1, and Rh4) on heme oxygenase-1 (HO-1) induction and on the expression of inducible nitric oxide synthase (iNOS) and cyclooxygenase (COX-)2 in lipopolysaccharide (LPS)-activated human pulmonary artery endothelial cells (HPAECs).	protopanaxatriol	84-100	heme oxygenase 1	Homo sapiens	160-176
31952230-1	2020	BACKGROUND: Mevastatin (MVS), a 3-hydroxy-3-methylglutaryl coenzyme, a reductase (HMG-CoA) inhibitor, has anti-inflammatory effects potentially via up-regulation of heme oxygenase-1 (HO-1).	mevastatin	12-22	heme oxygenase 1	Homo sapiens	165-181
31952230-1	2020	BACKGROUND: Mevastatin (MVS), a 3-hydroxy-3-methylglutaryl coenzyme, a reductase (HMG-CoA) inhibitor, has anti-inflammatory effects potentially via up-regulation of heme oxygenase-1 (HO-1).	mevastatin	12-22	heme oxygenase 1	Homo sapiens	183-187
31952230-1	2020	BACKGROUND: Mevastatin (MVS), a 3-hydroxy-3-methylglutaryl coenzyme, a reductase (HMG-CoA) inhibitor, has anti-inflammatory effects potentially via up-regulation of heme oxygenase-1 (HO-1).	mevastatin	24-27	heme oxygenase 1	Homo sapiens	165-181
31952230-1	2020	BACKGROUND: Mevastatin (MVS), a 3-hydroxy-3-methylglutaryl coenzyme, a reductase (HMG-CoA) inhibitor, has anti-inflammatory effects potentially via up-regulation of heme oxygenase-1 (HO-1).	mevastatin	24-27	heme oxygenase 1	Homo sapiens	183-187
31952230-2	2020	However, the mechanisms underlying MVS-induced HO-1 expression remain largely unknown in human pulmonary alveolar epithelial cells (HPAEpiCs).	mevastatin	35-38	heme oxygenase 1	Homo sapiens	47-51
31952230-5	2020	RESULTS: Upregulation of HO-1 by MVS attenuated the tumor necrosis factor (TNF)-alpha-stimulated ICAM-1 expression associated with THP-1 adhesion to HPAEpiCs.	mevastatin	33-36	heme oxygenase 1	Homo sapiens	25-29
31952230-6	2020	These inhibitory effects of HO-1 were reversed by tin protoporphyrin (SnPP)IX or by transfection with HO-1 siRNA.	tin protoporphyrin IX	50-68	heme oxygenase 1	Homo sapiens	28-32
31952230-6	2020	These inhibitory effects of HO-1 were reversed by tin protoporphyrin (SnPP)IX or by transfection with HO-1 siRNA.	tin protoporphyrin IX	70-74	heme oxygenase 1	Homo sapiens	28-32
31952230-7	2020	MVS-induced HO-1 expression was mediated via NADPH oxidase (Nox)-derived reactive oxygen species (ROS) generation.	mevastatin	0-3	heme oxygenase 1	Homo sapiens	12-16
31952230-7	2020	MVS-induced HO-1 expression was mediated via NADPH oxidase (Nox)-derived reactive oxygen species (ROS) generation.	NADP	45-50	heme oxygenase 1	Homo sapiens	12-16
31952230-7	2020	MVS-induced HO-1 expression was mediated via NADPH oxidase (Nox)-derived reactive oxygen species (ROS) generation.	Oxygen	82-88	heme oxygenase 1	Homo sapiens	12-16
31678598-8	2020	Activated AMPKalpha induced activation of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1), which are proteins functioning in redox balance.	ampkalpha	10-19	heme oxygenase 1	Homo sapiens	97-113
31678598-8	2020	Activated AMPKalpha induced activation of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1), which are proteins functioning in redox balance.	ampkalpha	10-19	heme oxygenase 1	Homo sapiens	115-119
32668967-2	2020	The aim of the this study was to examine the effects of [Formula: see text] (a rare protopanaxatriol-type ginsenoside fraction; Rg2, Rg4, Rg6, Rh1, and Rh4) on heme oxygenase-1 (HO-1) induction and on the expression of inducible nitric oxide synthase (iNOS) and cyclooxygenase (COX-)2 in lipopolysaccharide (LPS)-activated human pulmonary artery endothelial cells (HPAECs).	Ginsenosides	106-117	heme oxygenase 1	Homo sapiens	160-176
31764154-10	2020	Blockade of lipoxin A4 production in mesenchymal stromal cells, and of prostaglandin E2 synthesis in mesenchymal stromal cell/macrophage cocultures, prevented upregulation of heme oxygenase-1 in macrophages (from 9.6 +- 5.5-fold to 2.3 +- 1.3 and 2.4 +- 2.3 respectively, P = 0.004).	lipoxin A4	12-22	heme oxygenase 1	Homo sapiens	175-191
31796664-6	2020	The following clusters were found in the dendrogram: Nrf2 and p21 with ATP5B and GADPH in all the tissues and with NRF1 in all except the tumor tissues with metastasis; Bach1 with ATP5B and GAPDH in the tumor tissues; Keap1 with p62 in all the tissues, with LC3 in the tumor tissues and with NRF1 and HO1 in the tumor tissues with metastasis.	gadph	81-86	heme oxygenase 1	Homo sapiens	301-304
33268671-0	2020	(-)-Epigallocatechin-3-gallate inhibits RANKL-induced osteoclastogenesis via downregulation of NFATc1 and suppression of HO-1-HMGB1-RAGE pathway.	epigallocatechin gallate	0-30	heme oxygenase 1	Homo sapiens	121-125
33268671-8	2020	We also found that EGCG upregulated heme oxygenase-1 (HO-1) and suppressed the extracellular release of high-mobility group box 1 (HMGB1).	epigallocatechin gallate	19-23	heme oxygenase 1	Homo sapiens	36-52
33268671-8	2020	We also found that EGCG upregulated heme oxygenase-1 (HO-1) and suppressed the extracellular release of high-mobility group box 1 (HMGB1).	epigallocatechin gallate	19-23	heme oxygenase 1	Homo sapiens	54-58
33268671-10	2020	In summary, our study showed that EGCG could inhibit osteoclast differentiation through the downregulation of NFATc1 and the suppression of the HO-1-HMGB1-RAGE pathway.	epigallocatechin gallate	34-38	heme oxygenase 1	Homo sapiens	144-148
31646664-4	2020	The dose-dependent protective effects against H2 O2 -induced oxidative stress of the rutin-Lys MRPs may involve the inhibition of reactive oxygen species generation, enhancement of the superoxide dismutase and catalase activities, along with the activation of the Nrf2-dependent pathway and upregulation of phase II antioxidant genes (including NQO1, HO-1, GCLG, and GCLM).	Water	46-51	heme oxygenase 1	Homo sapiens	351-355
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	Heme	88-92	heme oxygenase 1	Homo sapiens	0-16
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	Heme	88-92	heme oxygenase 1	Homo sapiens	18-22
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	ferrous iron	101-113	heme oxygenase 1	Homo sapiens	0-16
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	ferrous iron	101-113	heme oxygenase 1	Homo sapiens	18-22
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	0-16
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	18-22
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	0-16
33016915-4	2020	Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	18-22
33016915-6	2020	The beneficial roles of HO-1 overexpression in AD brains are widely accepted due to its ability to convert pro-oxidant heme to biliverdin and bilirubin (antioxidants), which promote restoration of a suitable tissue redox microenvironment.	Heme	119-123	heme oxygenase 1	Homo sapiens	24-28
33016915-6	2020	The beneficial roles of HO-1 overexpression in AD brains are widely accepted due to its ability to convert pro-oxidant heme to biliverdin and bilirubin (antioxidants), which promote restoration of a suitable tissue redox microenvironment.	Biliverdine	127-137	heme oxygenase 1	Homo sapiens	24-28
33016915-6	2020	The beneficial roles of HO-1 overexpression in AD brains are widely accepted due to its ability to convert pro-oxidant heme to biliverdin and bilirubin (antioxidants), which promote restoration of a suitable tissue redox microenvironment.	Bilirubin	142-151	heme oxygenase 1	Homo sapiens	24-28
32047536-4	2020	Furthermore, Nrf2 downstream antioxidant genes such as HO-1(heme oxygenase 1) and NQO1 (NAD (P) H: quinone oxidoreductase 1) were upregulated in SKOV3/DDP cells with VK3 treatment, which indicated VK3 activated Nrf2 signaling in SKOV3/DDP cells.	Vitamin K	166-169	heme oxygenase 1	Homo sapiens	55-59
32047536-4	2020	Furthermore, Nrf2 downstream antioxidant genes such as HO-1(heme oxygenase 1) and NQO1 (NAD (P) H: quinone oxidoreductase 1) were upregulated in SKOV3/DDP cells with VK3 treatment, which indicated VK3 activated Nrf2 signaling in SKOV3/DDP cells.	Vitamin K	166-169	heme oxygenase 1	Homo sapiens	60-76
32047536-4	2020	Furthermore, Nrf2 downstream antioxidant genes such as HO-1(heme oxygenase 1) and NQO1 (NAD (P) H: quinone oxidoreductase 1) were upregulated in SKOV3/DDP cells with VK3 treatment, which indicated VK3 activated Nrf2 signaling in SKOV3/DDP cells.	Vitamin K	197-200	heme oxygenase 1	Homo sapiens	55-59
32047536-4	2020	Furthermore, Nrf2 downstream antioxidant genes such as HO-1(heme oxygenase 1) and NQO1 (NAD (P) H: quinone oxidoreductase 1) were upregulated in SKOV3/DDP cells with VK3 treatment, which indicated VK3 activated Nrf2 signaling in SKOV3/DDP cells.	Vitamin K	197-200	heme oxygenase 1	Homo sapiens	60-76
31646664-4	2020	The dose-dependent protective effects against H2 O2 -induced oxidative stress of the rutin-Lys MRPs may involve the inhibition of reactive oxygen species generation, enhancement of the superoxide dismutase and catalase activities, along with the activation of the Nrf2-dependent pathway and upregulation of phase II antioxidant genes (including NQO1, HO-1, GCLG, and GCLM).	Rutin	85-90	heme oxygenase 1	Homo sapiens	351-355
31646664-4	2020	The dose-dependent protective effects against H2 O2 -induced oxidative stress of the rutin-Lys MRPs may involve the inhibition of reactive oxygen species generation, enhancement of the superoxide dismutase and catalase activities, along with the activation of the Nrf2-dependent pathway and upregulation of phase II antioxidant genes (including NQO1, HO-1, GCLG, and GCLM).	pentalysine	91-94	heme oxygenase 1	Homo sapiens	351-355
31882813-5	2019	Besides, Mn-TAT PTD-Ngb activated the phosphoinositide-3 kinase (PI3K)/Akt signaling pathway, which up-regulated the expression of nuclear factor E2-related factor 2 (Nrf2), Heme oxygenase-1 (HO-1), superoxide dismutase (SOD), catalase (CAT).	Superoxides	199-209	heme oxygenase 1	Homo sapiens	174-190
31411335-1	2020	Objectives The number of dinucleotide repeats (GT) nmodulate expression of heme oxygenase 1 (HMOX1), a stress response gene.	Dinucleoside Phosphates	25-37	heme oxygenase 1	Homo sapiens	75-91
31411335-1	2020	Objectives The number of dinucleotide repeats (GT) nmodulate expression of heme oxygenase 1 (HMOX1), a stress response gene.	Dinucleoside Phosphates	25-37	heme oxygenase 1	Homo sapiens	93-98
31895879-0	2020	Berberine Attenuates Cholesterol Accumulation in Macrophage Foam Cells by Suppressing AP-1 Activity and Activation of the Nrf2/HO-1 Pathway.	Berberine	0-9	heme oxygenase 1	Homo sapiens	127-131
31895879-8	2020	Mechanisms study showed that berberine can suppress scavenger receptor expression via inhibiting the activity of AP-1 and upregulate ATP-binding cassette transporter via activating Nrf2/HO-1 signaling in human macrophage.	Berberine	29-38	heme oxygenase 1	Homo sapiens	186-190
31865348-11	2020	In addition, EX4 markedly increased expression of NRF2, HO-1, and NQO-1 and significantly improved protein expression of NRF2 and HO-1 in H2O2-treated ARPE-19 cells, caused by increased nuclear NRF2 protein expression.	Water	138-142	heme oxygenase 1	Homo sapiens	130-134
31518892-5	2020	In addition, CBD induced the expression of several NRF2 target genes, with heme oxygenase 1 (HMOX1) being the gene and the protein most upregulated by CBD.	Cannabidiol	13-16	heme oxygenase 1	Homo sapiens	75-91
31518892-5	2020	In addition, CBD induced the expression of several NRF2 target genes, with heme oxygenase 1 (HMOX1) being the gene and the protein most upregulated by CBD.	Cannabidiol	13-16	heme oxygenase 1	Homo sapiens	93-98
31518892-5	2020	In addition, CBD induced the expression of several NRF2 target genes, with heme oxygenase 1 (HMOX1) being the gene and the protein most upregulated by CBD.	Cannabidiol	151-154	heme oxygenase 1	Homo sapiens	75-91
31518892-5	2020	In addition, CBD induced the expression of several NRF2 target genes, with heme oxygenase 1 (HMOX1) being the gene and the protein most upregulated by CBD.	Cannabidiol	151-154	heme oxygenase 1	Homo sapiens	93-98
31810001-7	2020	HO-1 attenuated reactive oxygen species induced by H2O2 or pyocyanin treatment in PC-3 and DU145 cells.	Oxygen	25-31	heme oxygenase 1	Homo sapiens	0-4
31810001-7	2020	HO-1 attenuated reactive oxygen species induced by H2O2 or pyocyanin treatment in PC-3 and DU145 cells.	Water	51-55	heme oxygenase 1	Homo sapiens	0-4
31810001-7	2020	HO-1 attenuated reactive oxygen species induced by H2O2 or pyocyanin treatment in PC-3 and DU145 cells.	Pyocyanine	59-68	heme oxygenase 1	Homo sapiens	0-4
31810001-8	2020	HO-1 further reduced PC-3 and DU145 cell apoptosis induced by H2O2 or serum starvation.	Water	62-66	heme oxygenase 1	Homo sapiens	0-4
31877176-0	2019	alpha-Lipoic acid prevents against cisplatin cytotoxicity via activation of the NRF2/HO-1 antioxidant pathway.	Thioctic Acid	0-17	heme oxygenase 1	Homo sapiens	85-89
31877176-0	2019	alpha-Lipoic acid prevents against cisplatin cytotoxicity via activation of the NRF2/HO-1 antioxidant pathway.	Cisplatin	35-44	heme oxygenase 1	Homo sapiens	85-89
31882813-5	2019	Besides, Mn-TAT PTD-Ngb activated the phosphoinositide-3 kinase (PI3K)/Akt signaling pathway, which up-regulated the expression of nuclear factor E2-related factor 2 (Nrf2), Heme oxygenase-1 (HO-1), superoxide dismutase (SOD), catalase (CAT).	Superoxides	199-209	heme oxygenase 1	Homo sapiens	192-196
31614142-6	2019	Sofalcone induced HO-1 protein expression, which was dependent on increased nuclear accumulation of Nrf2 in human colon carcinoma cells.	sofalcone	0-9	heme oxygenase 1	Homo sapiens	18-22
31878134-6	2019	Moreover, Nrf2 and its downstream heme oxygenase 1 (HO-1) were inhibited by Cd exposure, and Kelch-like ECH-associated protein 1 (Keap1), the inhibitory protein of Nrf2, was increased.	Cadmium	76-78	heme oxygenase 1	Homo sapiens	34-50
31878134-6	2019	Moreover, Nrf2 and its downstream heme oxygenase 1 (HO-1) were inhibited by Cd exposure, and Kelch-like ECH-associated protein 1 (Keap1), the inhibitory protein of Nrf2, was increased.	Cadmium	76-78	heme oxygenase 1	Homo sapiens	52-56
31878134-8	2019	In conclusion, the inhibition of Nrf2, HO-1, and the activation of NF-kappaB, NLRP3, and MAPKs all contribute to Cd-induced liver injury.	Cadmium	113-115	heme oxygenase 1	Homo sapiens	39-43
31729530-0	2019	Moracin attenuates LPS-induced inflammation in nucleus pulposus cells via Nrf2/HO-1 and NF-kappaB/TGF-beta pathway.	moracin C	0-7	heme oxygenase 1	Homo sapiens	79-83
31729530-7	2019	Together, our results demonstrated the ability of moracin to antagonize LPS-mediated inflammation in primary culture of nucleus pulposus in intervertebral disc by partly regulating the Nrf2/HO-1 and NF-kappaB/TGF-beta pathway in nucleus pulposus cells.	moracin C	50-57	heme oxygenase 1	Homo sapiens	190-194
31861550-4	2019	The TU-inducible transcription of Nrf1 and Nrf2, as well as GCLM (glutamate cysteine ligase modifier subunit) and HO-1 (heme oxygenase 1), was accompanied by activation of ER stress signaling networks.	Tunicamycin	4-6	heme oxygenase 1	Homo sapiens	66-136
31861550-9	2019	Furthermore,&amp;nbsp;caNrf2DeltaN also enhanced induction of PERK and IRE1 by TU, but reduced expression of ATF4 and HO-1.	Tunicamycin	79-81	heme oxygenase 1	Homo sapiens	118-122
31614142-13	2019	The protective effects of sofalcone against colon damage and inflammation were significantly inhibited by co-administration of an HO-1 inhibitor.	sofalcone	26-35	heme oxygenase 1	Homo sapiens	130-134
31614142-14	2019	In conclusion, sofalcone activated the Nrf2-HO-1 pathway by covalently binding to KEAP1 via Michael addition, and may confer anti-colitic effects by inducing Nrf2 activation.	sofalcone	15-24	heme oxygenase 1	Homo sapiens	44-48
31659617-0	2019	Grape Seed Procyanidins Attenuates Cisplatin-induced Human Embryonic Renal Cell Cytotoxicity by Modulating Heme Oxygenase-1 in Vitro.	procyanidin	11-23	heme oxygenase 1	Homo sapiens	107-123
31704097-4	2019	BVR-deficiency induces the activity of Nrf2 transcription factor and increases heme oxygenase-1 (HO-1) level, which is accompanied by the reduction of cellular heme content, increase in a free iron fraction and oxidative stress.	Heme	79-83	heme oxygenase 1	Homo sapiens	97-101
31704097-5	2019	Accordingly, the phenotype of BVR-deficient cells can be mimicked by hemin or iron overload, whereas depletion of HO-1 in BVR-deficient ECs abrogates the increase in intracellular free iron and oxidative stress, preventing the loss of endothelial markers.	Iron	185-189	heme oxygenase 1	Homo sapiens	114-118
31704097-8	2019	Collectively, the non-enzymatic activity of BVR contributes to the maintenance of healthy endothelial phenotype through the prevention of HO-1-dependent iron-overload, oxidative stress and subsequent endothelial-to-mesenchymal transition (EndMT).	Iron	153-157	heme oxygenase 1	Homo sapiens	138-142
31847280-12	2019	DHA supplementation increased (p &lt; 0.05) mRNA expression of Nrf2, HO-1, GPx1, and CAT in the ID group.	artenimol	0-3	heme oxygenase 1	Homo sapiens	69-73
31847280-13	2019	In addition, the protein expression of Nrf2 was downregulated (p &lt; 0.05) in the liver of IUGR-affected piglets and DHA supplementation increased (p &lt; 0.05) the protein content of Nrf2 and HO-1.	artenimol	118-121	heme oxygenase 1	Homo sapiens	194-198
31817533-0	2019	Dietary Curcumin Supplementation Increases Antioxidant Capacity, Upregulates Nrf2 and Hmox1 Levels in the Liver of Piglet Model with Intrauterine Growth Retardation.	Curcumin	8-16	heme oxygenase 1	Homo sapiens	86-91
31817533-8	2019	Dietary curcumin supplementation increased body-weight gain, feed intake, activities of antioxidant enzymes, and the expressions of nuclear factor, erythroid 2-like 2 (Nrf2) and heme oxygenase-1 (Hmox1) proteins in the liver of weaned piglets with IUGR.	Curcumin	8-16	heme oxygenase 1	Homo sapiens	178-194
31817533-8	2019	Dietary curcumin supplementation increased body-weight gain, feed intake, activities of antioxidant enzymes, and the expressions of nuclear factor, erythroid 2-like 2 (Nrf2) and heme oxygenase-1 (Hmox1) proteins in the liver of weaned piglets with IUGR.	Curcumin	8-16	heme oxygenase 1	Homo sapiens	196-201
31817533-10	2019	Curcumin could efficiently improve the growth, increase hepatic antioxidant capacity, and upregulate Nrf2 and Hmox1 levels in the liver of IUGR weaned piglets.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	110-115
31885818-0	2019	FA-97, a New Synthetic Caffeic Acid Phenethyl Ester Derivative, Protects against Oxidative Stress-Mediated Neuronal Cell Apoptosis and Scopolamine-Induced Cognitive Impairment by Activating Nrf2/HO-1 Signaling.	fa-97	0-5	heme oxygenase 1	Homo sapiens	195-199
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Heme	34-38	heme oxygenase 1	Homo sapiens	0-16
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Heme	34-38	heme oxygenase 1	Homo sapiens	18-22
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Biliverdine	63-81	heme oxygenase 1	Homo sapiens	0-16
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Biliverdine	63-81	heme oxygenase 1	Homo sapiens	18-22
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	0-16
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	18-22
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Carbon Monoxide	100-102	heme oxygenase 1	Homo sapiens	0-16
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Carbon Monoxide	100-102	heme oxygenase 1	Homo sapiens	18-22
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Iron	109-113	heme oxygenase 1	Homo sapiens	0-16
31704095-1	2019	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron.	Iron	109-113	heme oxygenase 1	Homo sapiens	18-22
31704095-2	2019	The HO-1/CO system confers cytoprotection in animal models of organ injury and disease, via modulation of inflammation and apoptosis.	Carbon Monoxide	9-11	heme oxygenase 1	Homo sapiens	4-8
31921135-2	2019	Based on studies showing the potential role of heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme and has anti-inflammatory properties in SLE development, we decided to explore HO-1 in LN.	Heme	47-51	heme oxygenase 1	Homo sapiens	65-69
31159593-8	2019	We found that H2O2 stimulation-evoked HUVECs oxidative damage meanwhile impeded HO-1 expression.	Hydrogen Peroxide	14-18	heme oxygenase 1	Homo sapiens	80-84
30825052-9	2019	Additionally, it was determined that Pyr-1 generates oxidative and proteotoxic stress by provoking the accumulation of ROS, resulting in the overexpression of the stress-related hmox-1 mRNA transcripts and protein and a marked increase in poly-ubiquitinated proteins.	Pyr-1	37-42	heme oxygenase 1	Homo sapiens	178-184
30825052-9	2019	Additionally, it was determined that Pyr-1 generates oxidative and proteotoxic stress by provoking the accumulation of ROS, resulting in the overexpression of the stress-related hmox-1 mRNA transcripts and protein and a marked increase in poly-ubiquitinated proteins.	Reactive Oxygen Species	119-122	heme oxygenase 1	Homo sapiens	178-184
31659617-3	2019	This study reported whether O-GSP can antagonize the cisplatin-induced cytotoxicity in HEK293 cells through inducing HO-1 protein expression.	GSP-6 glycosulfopeptide	28-33	heme oxygenase 1	Homo sapiens	117-121
31659617-3	2019	This study reported whether O-GSP can antagonize the cisplatin-induced cytotoxicity in HEK293 cells through inducing HO-1 protein expression.	Cisplatin	53-62	heme oxygenase 1	Homo sapiens	117-121
31659617-5	2019	Herein, We found that O-GSP can antagonize cisplatin nephrotoxicity through regulating the expression of HO-1.	GSP-6 glycosulfopeptide	22-27	heme oxygenase 1	Homo sapiens	105-109
31659617-5	2019	Herein, We found that O-GSP can antagonize cisplatin nephrotoxicity through regulating the expression of HO-1.	Cisplatin	43-52	heme oxygenase 1	Homo sapiens	105-109
31659617-7	2019	Interestingly, p38 MAPK plays a major role in HO-1 expression induced by O-GSP.	GSP-6 glycosulfopeptide	73-78	heme oxygenase 1	Homo sapiens	46-50
31659617-8	2019	And O-GSP can modulate the decrease of Nrf2 and HO-1 expression induced by cisplatin, and improve the cisplatin-induced activity and apoptosis rate of cells by stimulating the expression of HO-1.	GSP-6 glycosulfopeptide	4-9	heme oxygenase 1	Homo sapiens	48-52
31659617-8	2019	And O-GSP can modulate the decrease of Nrf2 and HO-1 expression induced by cisplatin, and improve the cisplatin-induced activity and apoptosis rate of cells by stimulating the expression of HO-1.	GSP-6 glycosulfopeptide	4-9	heme oxygenase 1	Homo sapiens	190-194
31659617-8	2019	And O-GSP can modulate the decrease of Nrf2 and HO-1 expression induced by cisplatin, and improve the cisplatin-induced activity and apoptosis rate of cells by stimulating the expression of HO-1.	Cisplatin	75-84	heme oxygenase 1	Homo sapiens	48-52
31659617-8	2019	And O-GSP can modulate the decrease of Nrf2 and HO-1 expression induced by cisplatin, and improve the cisplatin-induced activity and apoptosis rate of cells by stimulating the expression of HO-1.	Cisplatin	102-111	heme oxygenase 1	Homo sapiens	190-194
31659617-10	2019	Collectively, the results indicated that O-GSP induced the expression of HO-1 through p38MAPK and Nrf2 pathway in HEK293 cells.	GSP-6 glycosulfopeptide	41-46	heme oxygenase 1	Homo sapiens	73-77
31659617-0	2019	Grape Seed Procyanidins Attenuates Cisplatin-induced Human Embryonic Renal Cell Cytotoxicity by Modulating Heme Oxygenase-1 in Vitro.	Cisplatin	35-44	heme oxygenase 1	Homo sapiens	107-123
31556759-11	2019	AX-SLN reduced the p-AKT which is accountable for the reduction in the NF-kB expression and also reduced the expression of Keap1 and NF-kB along with increasing the expression of HO-1 and Nrf-2.	Amoxicillin	0-2	heme oxygenase 1	Homo sapiens	179-183
30535793-6	2019	Treatment with NAC significantly increased jejunal superoxide dismutase activity, reduced glutathione: oxidized glutathione ratio, and the mRNA abundance of nuclear respiratory factor 2, heme oxygenase 1, and superoxide dismutase 2 in the IUGR-NAC piglets compared with the IUGR-CON piglets.	Acetylcysteine	15-18	heme oxygenase 1	Homo sapiens	187-203
31347718-5	2019	Fortunately, OS preconditioning can increase the expression of superoxide dismutase, catalase, NQO1, and heme oxygenase 1 through the nuclear factor erythroid 2-related factor 2 pathway, thereby decreased the intracellular reactive oxygen species (ROS) levels, relieved the damage of ROS to mitochondria, DNA and cell membrane, enhanced the anti-OS ability of BMSCs, and promoted the survival of BMSCs under OS.	Reactive Oxygen Species	223-246	heme oxygenase 1	Homo sapiens	105-121
31950025-0	2019	Erratum: 15-Deoxy-Delta12,14-prostaglandin J2 Upregulates the Expression of 15-Hydroxyprostaglandin Dehydrogenase by Inducing AP-1 Activation and Heme Oxygenase-1 Expression in Human Colon Cancer Cells.	15-deoxy-delta(12,14)-prostaglandin J2	9-45	heme oxygenase 1	Homo sapiens	146-162
31734545-7	2019	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase and heme oxygenase-1 and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	21-25	heme oxygenase 1	Homo sapiens	147-163
31734545-7	2019	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase and heme oxygenase-1 and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	111-115	heme oxygenase 1	Homo sapiens	147-163
31734545-7	2019	We hypothesized that PpIX fluorescence intensity results from the interplay between the metabolic clearance of PpIX mediated by ferrochelatase and heme oxygenase-1 and the cellular efflux of PpIX through the ATP-binding cassette subfamily G member 2 (ABCG2).	protoporphyrin IX	111-115	heme oxygenase 1	Homo sapiens	147-163
31559456-11	2019	CONCLUSION: The cytotoxic effects of CDDP and THP were both enhanced under HO-1 knockdown conditions as well as under conditions that inhibit the activation pathway of HO-1 by EGFR inhibitors.	pirarubicin	46-49	heme oxygenase 1	Homo sapiens	75-79
31351398-9	2019	RESULTS: HaCAT cells treated with 40 muM CoCl2 could not only reduce cell viability, promote cell apoptosis, arrest G1 phase of cell cycle and increase the activity of reactive oxygen species but also downregulate the expressions of c-myc, c-fos, transforming growth factor-alpha, Nrf2, heme oxygenase-1, and gamma-glutamyl cysteine synthetase.	cobaltous chloride	41-46	heme oxygenase 1	Homo sapiens	287-303
31404677-0	2019	Photoirradiation after aminolevulinic acid treatment suppresses cancer cell proliferation through the HO-1/p21 pathway.	Aminolevulinic Acid	23-42	heme oxygenase 1	Homo sapiens	102-106
31404677-8	2019	RESULTS: mRNAs of PAI-1, HO-1, and p21 were upregulated after photoirradiation of HEK293, which was suppressed by N-acetyl-L-cysteine, a reactive oxygen species (ROS) scavenger.	Acetylcysteine	114-133	heme oxygenase 1	Homo sapiens	25-29
31661135-7	2019	In the present analysis, HMOX1 and HSPA1A were identified as the most highly upregulated genes following sulforaphane treatment, suggesting their potential value as biomarkers to guide clinical trials.	sulforaphane	105-117	heme oxygenase 1	Homo sapiens	25-30
31559456-0	2019	Epidermal growth factor receptor/heme oxygenase-1 axis is involved in chemoresistance to cisplatin and pirarubicin in HepG2 cell lines and hepatoblastoma specimens.	Cisplatin	89-98	heme oxygenase 1	Homo sapiens	33-49
31559456-0	2019	Epidermal growth factor receptor/heme oxygenase-1 axis is involved in chemoresistance to cisplatin and pirarubicin in HepG2 cell lines and hepatoblastoma specimens.	pirarubicin	103-114	heme oxygenase 1	Homo sapiens	33-49
31559456-1	2019	PURPOSE: To investigate the possibility that the antioxidant stress protein Heme oxygenase-1 (HO-1) is involved in the acquisition of chemoresistance in cisplatin and pirarubicin (CITA) therapy.	Cisplatin	153-162	heme oxygenase 1	Homo sapiens	76-92
31559456-1	2019	PURPOSE: To investigate the possibility that the antioxidant stress protein Heme oxygenase-1 (HO-1) is involved in the acquisition of chemoresistance in cisplatin and pirarubicin (CITA) therapy.	Cisplatin	153-162	heme oxygenase 1	Homo sapiens	94-98
31559456-1	2019	PURPOSE: To investigate the possibility that the antioxidant stress protein Heme oxygenase-1 (HO-1) is involved in the acquisition of chemoresistance in cisplatin and pirarubicin (CITA) therapy.	pirarubicin	167-178	heme oxygenase 1	Homo sapiens	76-92
31559456-1	2019	PURPOSE: To investigate the possibility that the antioxidant stress protein Heme oxygenase-1 (HO-1) is involved in the acquisition of chemoresistance in cisplatin and pirarubicin (CITA) therapy.	pirarubicin	167-178	heme oxygenase 1	Homo sapiens	94-98
31559456-1	2019	PURPOSE: To investigate the possibility that the antioxidant stress protein Heme oxygenase-1 (HO-1) is involved in the acquisition of chemoresistance in cisplatin and pirarubicin (CITA) therapy.	cita	180-184	heme oxygenase 1	Homo sapiens	76-92
31559456-1	2019	PURPOSE: To investigate the possibility that the antioxidant stress protein Heme oxygenase-1 (HO-1) is involved in the acquisition of chemoresistance in cisplatin and pirarubicin (CITA) therapy.	cita	180-184	heme oxygenase 1	Homo sapiens	94-98
31559456-6	2019	RESULTS: HO-1 expression in HepG2 cells was increased by the treatment of cisplatin (CDDP) and pirarubicin (THP) dose-dependently.	Cisplatin	74-83	heme oxygenase 1	Homo sapiens	9-13
31559456-6	2019	RESULTS: HO-1 expression in HepG2 cells was increased by the treatment of cisplatin (CDDP) and pirarubicin (THP) dose-dependently.	Cisplatin	85-89	heme oxygenase 1	Homo sapiens	9-13
31404677-8	2019	RESULTS: mRNAs of PAI-1, HO-1, and p21 were upregulated after photoirradiation of HEK293, which was suppressed by N-acetyl-L-cysteine, a reactive oxygen species (ROS) scavenger.	Reactive Oxygen Species	137-160	heme oxygenase 1	Homo sapiens	25-29
31404677-8	2019	RESULTS: mRNAs of PAI-1, HO-1, and p21 were upregulated after photoirradiation of HEK293, which was suppressed by N-acetyl-L-cysteine, a reactive oxygen species (ROS) scavenger.	Reactive Oxygen Species	162-165	heme oxygenase 1	Homo sapiens	25-29
31559456-11	2019	CONCLUSION: The cytotoxic effects of CDDP and THP were both enhanced under HO-1 knockdown conditions as well as under conditions that inhibit the activation pathway of HO-1 by EGFR inhibitors.	pirarubicin	46-49	heme oxygenase 1	Homo sapiens	168-172
31404677-11	2019	CONCLUSION: ALA-PDD or ALA-PDT can result in rapid ROS-induced cell death and may decrease long-term recurrence rates through several pathways including the HO-1/p21 pathway.	5-amino levulinic acid	12-15	heme oxygenase 1	Homo sapiens	157-161
31404677-11	2019	CONCLUSION: ALA-PDD or ALA-PDT can result in rapid ROS-induced cell death and may decrease long-term recurrence rates through several pathways including the HO-1/p21 pathway.	5-amino levulinic acid	23-26	heme oxygenase 1	Homo sapiens	157-161
31559456-6	2019	RESULTS: HO-1 expression in HepG2 cells was increased by the treatment of cisplatin (CDDP) and pirarubicin (THP) dose-dependently.	pirarubicin	95-106	heme oxygenase 1	Homo sapiens	9-13
31559456-6	2019	RESULTS: HO-1 expression in HepG2 cells was increased by the treatment of cisplatin (CDDP) and pirarubicin (THP) dose-dependently.	pirarubicin	108-111	heme oxygenase 1	Homo sapiens	9-13
31559456-7	2019	In HO-1 knockdown HepG2 cells, the HO-1 was not expressed and the percentage of trypan blue-positive cells (dead cells) was significantly increased after treatment of CDDP and THP.	Trypan Blue	80-91	heme oxygenase 1	Homo sapiens	3-7
31404677-11	2019	CONCLUSION: ALA-PDD or ALA-PDT can result in rapid ROS-induced cell death and may decrease long-term recurrence rates through several pathways including the HO-1/p21 pathway.	Reactive Oxygen Species	51-54	heme oxygenase 1	Homo sapiens	157-161
31319135-5	2019	Reduced expression of NADPH dehydrogenase quinone 1 (NQO-1) and heme oxygenase 1 (HO-1) genes, which are well-characterized downstream targets of Nrf2-mediated transactivation, was also confirmed by using ALA and another Nrf2 activator, marliolide.	Thioctic Acid	205-208	heme oxygenase 1	Homo sapiens	64-80
31559456-7	2019	In HO-1 knockdown HepG2 cells, the HO-1 was not expressed and the percentage of trypan blue-positive cells (dead cells) was significantly increased after treatment of CDDP and THP.	Cisplatin	167-171	heme oxygenase 1	Homo sapiens	3-7
31559456-7	2019	In HO-1 knockdown HepG2 cells, the HO-1 was not expressed and the percentage of trypan blue-positive cells (dead cells) was significantly increased after treatment of CDDP and THP.	pirarubicin	176-179	heme oxygenase 1	Homo sapiens	3-7
31559456-10	2019	In human hepatoblastoma specimens, 4 of the 5 patients (80%) showed HO-1 expression changed much stronger in the viable tumor cells after CITA therapy.	cita	138-142	heme oxygenase 1	Homo sapiens	68-72
31559456-11	2019	CONCLUSION: The cytotoxic effects of CDDP and THP were both enhanced under HO-1 knockdown conditions as well as under conditions that inhibit the activation pathway of HO-1 by EGFR inhibitors.	Cisplatin	37-41	heme oxygenase 1	Homo sapiens	75-79
31559456-11	2019	CONCLUSION: The cytotoxic effects of CDDP and THP were both enhanced under HO-1 knockdown conditions as well as under conditions that inhibit the activation pathway of HO-1 by EGFR inhibitors.	Cisplatin	37-41	heme oxygenase 1	Homo sapiens	168-172
31319135-5	2019	Reduced expression of NADPH dehydrogenase quinone 1 (NQO-1) and heme oxygenase 1 (HO-1) genes, which are well-characterized downstream targets of Nrf2-mediated transactivation, was also confirmed by using ALA and another Nrf2 activator, marliolide.	Thioctic Acid	205-208	heme oxygenase 1	Homo sapiens	82-86
31319135-5	2019	Reduced expression of NADPH dehydrogenase quinone 1 (NQO-1) and heme oxygenase 1 (HO-1) genes, which are well-characterized downstream targets of Nrf2-mediated transactivation, was also confirmed by using ALA and another Nrf2 activator, marliolide.	marliolide	237-247	heme oxygenase 1	Homo sapiens	64-80
31319135-5	2019	Reduced expression of NADPH dehydrogenase quinone 1 (NQO-1) and heme oxygenase 1 (HO-1) genes, which are well-characterized downstream targets of Nrf2-mediated transactivation, was also confirmed by using ALA and another Nrf2 activator, marliolide.	marliolide	237-247	heme oxygenase 1	Homo sapiens	82-86
31654068-9	2019	Besides, scutellarin induced the mRNA expressions of heme oxygenase-1 (HO-1) and NAD(P)H: quinone oxidoreductase 1 (NQO1).	scutellarin	9-20	heme oxygenase 1	Homo sapiens	53-69
31771519-20	2019	Bilirubin levels may become elevated as a result of heme oxygenase-1 activation, occurring in exercise-induced acute kidney injury in patients with RHUC; this phenomenon suggests renal ischemia-reperfusion injury.	Bilirubin	0-9	heme oxygenase 1	Homo sapiens	52-68
31772153-11	2019	Heme Oxygenase 1 (HMOX1) was among the top upregulated genes, whose induction was ROS-dependent and HMOX1 depletion enhanced chaetocin mediated TRAIL sensitization.	chaetocin	125-134	heme oxygenase 1	Homo sapiens	0-16
31772153-11	2019	Heme Oxygenase 1 (HMOX1) was among the top upregulated genes, whose induction was ROS-dependent and HMOX1 depletion enhanced chaetocin mediated TRAIL sensitization.	chaetocin	125-134	heme oxygenase 1	Homo sapiens	18-23
31772153-11	2019	Heme Oxygenase 1 (HMOX1) was among the top upregulated genes, whose induction was ROS-dependent and HMOX1 depletion enhanced chaetocin mediated TRAIL sensitization.	chaetocin	125-134	heme oxygenase 1	Homo sapiens	100-105
31767834-8	2019	At last we show that PGK1 expression is downregulated in human necrotic femoral head tissues of DEX-taking patients, correlating with HO1 depletion.	Dexamethasone	96-99	heme oxygenase 1	Homo sapiens	134-137
31725784-5	2019	The mineral absorption pathway genes, HMOX1 and VDR are involved in iron metabolism and response to vitamin D, respectively.	Iron	68-72	heme oxygenase 1	Homo sapiens	38-43
31885775-5	2019	Therefore, regulation of Nrf2 and HO-1 expression by the PI3K/AKT pathway plays an important role in the regulation of the antioxidant and antiapoptotic responses in DRG cells in a high-glucose culture model.	Glucose	186-193	heme oxygenase 1	Homo sapiens	34-38
31819369-5	2019	The mRNA and protein expression levels of redox transcription factor Nrf2 and the downstream effector SOD-1, SOD-2, NQO-1 and HO-1 were assayed to explore the detailed mechanism by which ICA alleviates ECM degradation.	icariin	187-190	heme oxygenase 1	Homo sapiens	126-130
31885801-8	2019	Furthermore, we report on a C-terminal truncation of HO-1, which is generally considered as a signal molecule.	Carbon	28-29	heme oxygenase 1	Homo sapiens	53-57
31644887-0	2019	Quercetin, but not rutin, attenuated hydrogen peroxide-induced cell damage via heme oxygenase-1 induction in endothelial cells.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	79-95
31644887-0	2019	Quercetin, but not rutin, attenuated hydrogen peroxide-induced cell damage via heme oxygenase-1 induction in endothelial cells.	Hydrogen Peroxide	37-54	heme oxygenase 1	Homo sapiens	79-95
31644887-5	2019	It was found that quercetin upregulated HMOX1 expression to protect endothelial cells against oxidative stress, and the protective effects of quercetin on H2O2-induced endothelial cell damage (such as loss of cell viability and reduction of nitric oxide) could be abolished by the specific small-interfering RNA against HMOX1 expression or HMOX1 activity inhibitor.	Quercetin	18-27	heme oxygenase 1	Homo sapiens	40-45
31644887-5	2019	It was found that quercetin upregulated HMOX1 expression to protect endothelial cells against oxidative stress, and the protective effects of quercetin on H2O2-induced endothelial cell damage (such as loss of cell viability and reduction of nitric oxide) could be abolished by the specific small-interfering RNA against HMOX1 expression or HMOX1 activity inhibitor.	Quercetin	18-27	heme oxygenase 1	Homo sapiens	320-325
31644887-5	2019	It was found that quercetin upregulated HMOX1 expression to protect endothelial cells against oxidative stress, and the protective effects of quercetin on H2O2-induced endothelial cell damage (such as loss of cell viability and reduction of nitric oxide) could be abolished by the specific small-interfering RNA against HMOX1 expression or HMOX1 activity inhibitor.	Quercetin	18-27	heme oxygenase 1	Homo sapiens	320-325
31815138-0	2019	Sirt5 Attenuates Cisplatin-Induced Acute Kidney Injury through Regulation of Nrf2/HO-1 and Bcl-2.	Cisplatin	17-26	heme oxygenase 1	Homo sapiens	82-86
31815138-12	2019	The levels of Nrf2, HO-1, and Bcl-2 proteins in HK-2 cells were also decreased after CDDP treatment.	Cisplatin	85-89	heme oxygenase 1	Homo sapiens	20-24
31815138-15	2019	Together, the results demonstrated that Sirt5 attenuated cisplatin-induced apoptosis and mitochondrial injury in human kidney HK-2 cells, possibly through the regulation of Nrf2/HO-1 and Bcl-2.	Cisplatin	57-66	heme oxygenase 1	Homo sapiens	178-182
31644887-6	2019	In addition, the activation of ERK/Nrf2 signaling pathway was critical to the upregulation of HMOX1 induced by quercetin.	Quercetin	111-120	heme oxygenase 1	Homo sapiens	94-99
31644887-8	2019	Therefore, quercetin could attenuate oxidative stress-induced endothelial cell damage at least partly through ERK/Nrf2/HMOX1 pathway.	Quercetin	11-20	heme oxygenase 1	Homo sapiens	119-124
31725784-5	2019	The mineral absorption pathway genes, HMOX1 and VDR are involved in iron metabolism and response to vitamin D, respectively.	Vitamin D	100-109	heme oxygenase 1	Homo sapiens	38-43
31279900-0	2019	O-GlcNAcylation-dependent upregulation of HO1 triggers ammonia-induced oxidative stress and senescence in hepatic encephalopathy.	o-glcnacylation	0-15	heme oxygenase 1	Homo sapiens	42-45
31814878-0	2019	The Nrf2/HO-1 Axis as Targets for Flavanones: Neuroprotection by Pinocembrin, Naringenin, and Eriodictyol.	eriodictyol	94-105	heme oxygenase 1	Homo sapiens	9-13
31711520-9	2019	The effects of decitabine on P15INK4B and TP53 in MDS cells after inhibiting HO-1 were detected by Western blotting.	decitabine	15-25	heme oxygenase 1	Homo sapiens	77-81
31711520-16	2019	Using the E2F inhibitor HLM006474 and the EZH2 inhibitor JQEZ5, we showed that HO-1 could regulate EZH2 expression.	HLM006474	24-33	heme oxygenase 1	Homo sapiens	79-83
31781345-0	2019	Methane Alleviates Acetaminophen-Induced Liver Injury by Inhibiting Inflammation, Oxidative Stress, Endoplasmic Reticulum Stress, and Apoptosis through the Nrf2/HO-1/NQO1 Signaling Pathway.	Methane	0-7	heme oxygenase 1	Homo sapiens	161-165
31781345-0	2019	Methane Alleviates Acetaminophen-Induced Liver Injury by Inhibiting Inflammation, Oxidative Stress, Endoplasmic Reticulum Stress, and Apoptosis through the Nrf2/HO-1/NQO1 Signaling Pathway.	Acetaminophen	19-32	heme oxygenase 1	Homo sapiens	161-165
31781345-10	2019	We found that a methane-rich medium decreased the levels of reactive oxygen species (DHE fluorescent staining), inhibited apoptosis (cell flow test), and regulated the Nrf2/HO-1/NQO1 signaling pathway.	Methane	16-23	heme oxygenase 1	Homo sapiens	173-177
31781345-11	2019	Our data indicated that MRS prevented APAP-induced hepatic injury via anti-inflammatory, antioxidant, anti-ERS, and antiapoptotic properties involving the Nrf2/HO-1/NQO1 signaling pathway.	Acetaminophen	38-42	heme oxygenase 1	Homo sapiens	160-164
31814878-0	2019	The Nrf2/HO-1 Axis as Targets for Flavanones: Neuroprotection by Pinocembrin, Naringenin, and Eriodictyol.	Flavanones	34-44	heme oxygenase 1	Homo sapiens	9-13
31814878-0	2019	The Nrf2/HO-1 Axis as Targets for Flavanones: Neuroprotection by Pinocembrin, Naringenin, and Eriodictyol.	pinocembrin	65-76	heme oxygenase 1	Homo sapiens	9-13
31462605-7	2019	Treatment with DDC for 24 hours increased the expression of heme oxygenase-1 (HO-1), and this was controlled by the activation of the Nrf2-ARE pathway.	2',3'-dihydroxy-4',6'-dimethoxychalcone	15-18	heme oxygenase 1	Homo sapiens	60-76
31462615-9	2019	Treatment with DDC for 24 h also increased the expression levels of heme oxygenase-1 (HO-1) in a concentration-dependent manner.	2',3'-dihydroxy-4',6'-dimethoxychalcone	15-18	heme oxygenase 1	Homo sapiens	68-84
31462615-9	2019	Treatment with DDC for 24 h also increased the expression levels of heme oxygenase-1 (HO-1) in a concentration-dependent manner.	2',3'-dihydroxy-4',6'-dimethoxychalcone	15-18	heme oxygenase 1	Homo sapiens	86-90
31462615-10	2019	Pretreatment with the HO-1 inhibitor followed by DDC treatment before UV-A irradiation for 24 h reduced ROS production and the cytoprotective effect.	Reactive Oxygen Species	104-107	heme oxygenase 1	Homo sapiens	22-26
31272005-10	2019	N-acetylcysteine antagonized arsenite-mediated induction of HMOX1 expression as well as reduction of neuronal and oligodendrocyte differentiation in hNPC suggesting involvement of oxidative stress in arsenite DNT.	Acetylcysteine	0-16	heme oxygenase 1	Homo sapiens	60-65
31272005-10	2019	N-acetylcysteine antagonized arsenite-mediated induction of HMOX1 expression as well as reduction of neuronal and oligodendrocyte differentiation in hNPC suggesting involvement of oxidative stress in arsenite DNT.	arsenite	29-37	heme oxygenase 1	Homo sapiens	60-65
31577640-5	2019	Mechanistic studies have revealed superoxide dismutase, heme oxygenase-1 and nuclear factor erythroid 2-related factor 2 as emerging targets for the beneficial effects of curcumin on the vasculature.	Curcumin	171-179	heme oxygenase 1	Homo sapiens	56-120
31279900-0	2019	O-GlcNAcylation-dependent upregulation of HO1 triggers ammonia-induced oxidative stress and senescence in hepatic encephalopathy.	Ammonia	55-62	heme oxygenase 1	Homo sapiens	42-45
31279900-4	2019	Mechanisms and functional consequences of HO1 upregulation were studied in NH4Cl-exposed astrocytes in vitro by western blot, qPCR and super-resolution microscopy.	Ammonium Chloride	75-80	heme oxygenase 1	Homo sapiens	42-45
31279900-5	2019	RESULTS: HO1 and the endoplasmic reticulum (ER) stress marker grp78 were upregulated, together with changes in the expression of multiple iron metabolism-related genes, in post-mortem brain samples from patients with liver cirrhosis and HE.	Iron	138-142	heme oxygenase 1	Homo sapiens	9-12
31279900-7	2019	Upregulation of HO1 by NH4Cl triggered ER stress and was associated with elevated levels of free ferrous iron and expression changes in iron metabolism-related genes, which were largely abolished after knockdown or inhibition of GS, GFAT1/2, HO1 or iron chelation.	ferrous iron	97-109	heme oxygenase 1	Homo sapiens	16-19
31279900-7	2019	Upregulation of HO1 by NH4Cl triggered ER stress and was associated with elevated levels of free ferrous iron and expression changes in iron metabolism-related genes, which were largely abolished after knockdown or inhibition of GS, GFAT1/2, HO1 or iron chelation.	Iron	105-109	heme oxygenase 1	Homo sapiens	16-19
31279900-7	2019	Upregulation of HO1 by NH4Cl triggered ER stress and was associated with elevated levels of free ferrous iron and expression changes in iron metabolism-related genes, which were largely abolished after knockdown or inhibition of GS, GFAT1/2, HO1 or iron chelation.	Iron	136-140	heme oxygenase 1	Homo sapiens	16-19
31279900-10	2019	CONCLUSION: The present study identified glucosamine synthesis-dependent protein O-GlcNAcylation as a novel mechanism in the pathogenesis of HE that triggers oxidative and ER stress, as well as senescence, through upregulation of HO1 and Nox4.	Glucosamine	41-52	heme oxygenase 1	Homo sapiens	230-233
31770287-9	2019	CONCLUSION: Propofol-based TIVA attenuated inflammatory response (elevated IL-1RA and IL-10 levels), downregulated MMP-9 response, and increased HO-1 expression with improved recovery of graft function and better microcirculation compared with desflurane anesthesia in liver transplant recipients.	Propofol	12-20	heme oxygenase 1	Homo sapiens	145-149
31415221-6	2019	We found that dermaprazole induced nuclear translocation of erythroid 2-related factor 2 (Nrf2) and significantly upregulated heme oxygenase 1 (HO1) gene and protein expression in a 3D human skin model.	dermaprazole	14-26	heme oxygenase 1	Homo sapiens	126-142
31770287-0	2019	Propofol vs desflurane on the cytokine, matrix metalloproteinase-9, and heme oxygenase-1 response during living donor liver transplantation: A pilot study.	Propofol	0-8	heme oxygenase 1	Homo sapiens	72-88
31076999-0	2019	Naringenin Inhibit the Hydrogen Peroxide-Induced SH-SY5Y Cells Injury Through Nrf2/HO-1 Pathway.	naringenin	0-10	heme oxygenase 1	Homo sapiens	83-87
31076999-0	2019	Naringenin Inhibit the Hydrogen Peroxide-Induced SH-SY5Y Cells Injury Through Nrf2/HO-1 Pathway.	Hydrogen Peroxide	23-40	heme oxygenase 1	Homo sapiens	83-87
31076999-8	2019	NGN activated both ERK and PI3 K/Akt, and treatments with the specific ERK inhibitor PD98059, the PI3 K inhibitor LY294002, and the specific Nrf2 shRNA suppressed the NGN-induced HO-1 expression.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	85-92	heme oxygenase 1	Homo sapiens	179-183
31076999-8	2019	NGN activated both ERK and PI3 K/Akt, and treatments with the specific ERK inhibitor PD98059, the PI3 K inhibitor LY294002, and the specific Nrf2 shRNA suppressed the NGN-induced HO-1 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	114-122	heme oxygenase 1	Homo sapiens	179-183
31076999-9	2019	The HO-1 inhibitor ZnPP abolished the neuroprotective effect of NGN against H2O2-induced neurotoxicity.	zinc protoporphyrin	19-23	heme oxygenase 1	Homo sapiens	4-8
31076999-9	2019	The HO-1 inhibitor ZnPP abolished the neuroprotective effect of NGN against H2O2-induced neurotoxicity.	naringenin	64-67	heme oxygenase 1	Homo sapiens	4-8
31076999-9	2019	The HO-1 inhibitor ZnPP abolished the neuroprotective effect of NGN against H2O2-induced neurotoxicity.	Hydrogen Peroxide	76-80	heme oxygenase 1	Homo sapiens	4-8
31076999-10	2019	Taken together, the present study demonstrates that regulation of Nrf2/HO-1 pathway through activation of ERK and PI3 K/Akt, and the inhibition of mitochondria-dependent apoptosis together may render NGN protect SH-SY5Y cells from H2O2-induced neurotoxicity.	Hydrogen Peroxide	231-235	heme oxygenase 1	Homo sapiens	71-75
31415221-6	2019	We found that dermaprazole induced nuclear translocation of erythroid 2-related factor 2 (Nrf2) and significantly upregulated heme oxygenase 1 (HO1) gene and protein expression in a 3D human skin model.	dermaprazole	14-26	heme oxygenase 1	Homo sapiens	144-147
31472180-9	2019	Additionally, the LCA treatment effectively counteracted TNF-alpha-mediated downregulation of silent information regulator 1 (SIRT1), nuclear factor erythroid2-related factor 2 (Nrf2), and heme oxygenase-1, which are related to oxidative stress.	Lithocholic Acid	18-21	heme oxygenase 1	Homo sapiens	189-205
31749701-9	2019	Mechanistically, we found that GAS protects HUVECs from TBHP-induced cellular apoptosis by activating the nuclear factor (erythroid-derived 2)-like 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	gastrodin	31-34	heme oxygenase 1	Homo sapiens	157-173
31648725-4	2019	In our previous study, Xanthohumol (Xn), a prenylated flavonoid extracted for hops (Humulus lupulus L), was screened from 386 natural products to inhibit PRRSV proliferation and alleviate oxidative stress induced by PRRSV via the Nrf2-HMOX1 axis in Marc-145 cells.	xanthohumol	23-34	heme oxygenase 1	Homo sapiens	235-240
31648725-4	2019	In our previous study, Xanthohumol (Xn), a prenylated flavonoid extracted for hops (Humulus lupulus L), was screened from 386 natural products to inhibit PRRSV proliferation and alleviate oxidative stress induced by PRRSV via the Nrf2-HMOX1 axis in Marc-145 cells.	xanthohumol	36-38	heme oxygenase 1	Homo sapiens	235-240
31749701-9	2019	Mechanistically, we found that GAS protects HUVECs from TBHP-induced cellular apoptosis by activating the nuclear factor (erythroid-derived 2)-like 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	gastrodin	31-34	heme oxygenase 1	Homo sapiens	175-179
31749701-9	2019	Mechanistically, we found that GAS protects HUVECs from TBHP-induced cellular apoptosis by activating the nuclear factor (erythroid-derived 2)-like 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	tert-Butylhydroperoxide	56-60	heme oxygenase 1	Homo sapiens	157-173
31749701-9	2019	Mechanistically, we found that GAS protects HUVECs from TBHP-induced cellular apoptosis by activating the nuclear factor (erythroid-derived 2)-like 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	tert-Butylhydroperoxide	56-60	heme oxygenase 1	Homo sapiens	175-179
31656916-7	2019	Furthermore, resveratrol and curcumin decreased the content of m6A and decreased the enrichment of m6A on the transcripts of tight junction proteins and on heme oxygenase-1 in the intestine.	resveratrol	13-24	heme oxygenase 1	Homo sapiens	156-172
31635102-12	2019	(4) Conclusions: Microglial HO-1 induction with endogenous CO production functions as a crucial signaling pathway in blood-induced inflammation, determining microglial MCP-1 production and the extent of neuronal cell death.	Carbon Dioxide	59-61	heme oxygenase 1	Homo sapiens	28-32
31635294-5	2019	We found that AGR pretreatment strongly inhibits the production of nitric oxide (NO), cytokines, and the enzymes inducible nitric oxide synthase (iNOS), and cyclooxygenase (COX)-2, and effectively induces the activation of heme oxygenase (HO)-1 and its regulator, nuclear factor erythroid 2-related factor 2 (Nrf-2).	alanylglycylarginine	14-17	heme oxygenase 1	Homo sapiens	223-244
31330223-5	2019	The results revealed that SA4503 treatment increased Nrf2 and HO-1 expression significantly.	SA 4503	26-32	heme oxygenase 1	Homo sapiens	62-66
31772710-0	2019	Melatonin Reduces Androgen Production and Upregulates Heme Oxygenase-1 Expression in Granulosa Cells from PCOS Patients with Hypoestrogenia and Hyperandrogenia.	Melatonin	0-9	heme oxygenase 1	Homo sapiens	54-70
31656916-7	2019	Furthermore, resveratrol and curcumin decreased the content of m6A and decreased the enrichment of m6A on the transcripts of tight junction proteins and on heme oxygenase-1 in the intestine.	Curcumin	29-37	heme oxygenase 1	Homo sapiens	156-172
31597407-7	2019	Moreover, most of the enzymes and proteins that cascade or interact in the pathway of ferroptosis such as a subunit of the cystine/glutamate transporter xc- (SLC7A11), glutathione peroxidase 4 (GPX4), and the glutamate-cysteine ligase (GCLC) iron metabolism genes transferrin receptor 1 (TfR1) ferroportin, (Fpn) heme oxygenase 1 (HO-1) and ferritin are regulated by the antioxidant response element of the transcription factor, Nrf2.	Glutamic Acid	131-140	heme oxygenase 1	Homo sapiens	313-329
31597407-7	2019	Moreover, most of the enzymes and proteins that cascade or interact in the pathway of ferroptosis such as a subunit of the cystine/glutamate transporter xc- (SLC7A11), glutathione peroxidase 4 (GPX4), and the glutamate-cysteine ligase (GCLC) iron metabolism genes transferrin receptor 1 (TfR1) ferroportin, (Fpn) heme oxygenase 1 (HO-1) and ferritin are regulated by the antioxidant response element of the transcription factor, Nrf2.	Glutamic Acid	131-140	heme oxygenase 1	Homo sapiens	331-335
31597407-7	2019	Moreover, most of the enzymes and proteins that cascade or interact in the pathway of ferroptosis such as a subunit of the cystine/glutamate transporter xc- (SLC7A11), glutathione peroxidase 4 (GPX4), and the glutamate-cysteine ligase (GCLC) iron metabolism genes transferrin receptor 1 (TfR1) ferroportin, (Fpn) heme oxygenase 1 (HO-1) and ferritin are regulated by the antioxidant response element of the transcription factor, Nrf2.	Cystine	123-130	heme oxygenase 1	Homo sapiens	313-329
31597407-7	2019	Moreover, most of the enzymes and proteins that cascade or interact in the pathway of ferroptosis such as a subunit of the cystine/glutamate transporter xc- (SLC7A11), glutathione peroxidase 4 (GPX4), and the glutamate-cysteine ligase (GCLC) iron metabolism genes transferrin receptor 1 (TfR1) ferroportin, (Fpn) heme oxygenase 1 (HO-1) and ferritin are regulated by the antioxidant response element of the transcription factor, Nrf2.	Cystine	123-130	heme oxygenase 1	Homo sapiens	331-335
31571584-6	2019	Complete heme tolerance requires a fully-operational heme degradation pathway as haplo insufficiency of HMOX1 combined with SLC48A1 inactivation causes perinatal lethality demonstrating synthetic lethal interactions between heme transport and degradation.	Heme	9-13	heme oxygenase 1	Homo sapiens	104-109
31036877-5	2019	The knockdown of intracellular PRDX6 significantly enhances LOOH and ferroptotic cell death triggered by ferroptosis inducers (Erastin and RSL-3), which is correlated with the transcriptional activation of heme oxygenase-1.	Lipid Peroxides	60-64	heme oxygenase 1	Homo sapiens	206-222
31036877-6	2019	Moreover, overexpression of heme oxygenase-1 enhances both Erastin- and RSL-3-triggered LOOH, suggesting that heme oxygenase-1 mediates PRDX6 silencing-enhanced ferroptosis.	Lipid Peroxides	88-92	heme oxygenase 1	Homo sapiens	28-44
31036877-6	2019	Moreover, overexpression of heme oxygenase-1 enhances both Erastin- and RSL-3-triggered LOOH, suggesting that heme oxygenase-1 mediates PRDX6 silencing-enhanced ferroptosis.	Lipid Peroxides	88-92	heme oxygenase 1	Homo sapiens	110-126
31243599-6	2019	Gene expression analysis revealed PL caused a > 20-fold induction of heme oxygenase-1 (HO-1), which we hypothesized was a survival mechanism for PDAC cells under enhanced oxidative stress.	piperlonguminine	34-36	heme oxygenase 1	Homo sapiens	69-85
31243599-6	2019	Gene expression analysis revealed PL caused a > 20-fold induction of heme oxygenase-1 (HO-1), which we hypothesized was a survival mechanism for PDAC cells under enhanced oxidative stress.	piperlonguminine	34-36	heme oxygenase 1	Homo sapiens	87-91
31243599-7	2019	HO-1 knockout resulted in enhanced PL-induced PDAC cell death under hypoxic conditions.	piperlonguminine	35-37	heme oxygenase 1	Homo sapiens	0-4
31243599-8	2019	Similarly, high concentrations of the HO-1 inhibitor, ZnPP (10 microM), sensitized PDAC cells to PL; however, lower concentrations ZnPP (10 nM) and high or low concentrations of SnPP both protected PDAC cells from PL-induced cell death.	zinc protoporphyrin	54-58	heme oxygenase 1	Homo sapiens	38-42
31243599-8	2019	Similarly, high concentrations of the HO-1 inhibitor, ZnPP (10 microM), sensitized PDAC cells to PL; however, lower concentrations ZnPP (10 nM) and high or low concentrations of SnPP both protected PDAC cells from PL-induced cell death.	piperlonguminine	97-99	heme oxygenase 1	Homo sapiens	38-42
31243599-9	2019	Interestingly, the JNK inhibitor significantly blocked PL-induced PDAC cell death, Nrf-2 nuclear translocation, and HMOX-1 mRNA expression.	piperlonguminine	55-57	heme oxygenase 1	Homo sapiens	116-122
31243599-10	2019	Collectively, the results demonstrate JNK signaling contributes to PL-induced PDAC cell death, and at the same time, activates Nrf-2 transcription of HMOX-1 as a compensatory survival mechanism.	piperlonguminine	67-69	heme oxygenase 1	Homo sapiens	150-156
31188648-11	2019	Cell immunofluorescence staining indicated that the fluorescence staining intensity of HO-1 in the NBP group was significantly higher than that in the control group.	3-n-butylphthalide	99-102	heme oxygenase 1	Homo sapiens	87-91
31571584-6	2019	Complete heme tolerance requires a fully-operational heme degradation pathway as haplo insufficiency of HMOX1 combined with SLC48A1 inactivation causes perinatal lethality demonstrating synthetic lethal interactions between heme transport and degradation.	Heme	53-57	heme oxygenase 1	Homo sapiens	104-109
31571584-6	2019	Complete heme tolerance requires a fully-operational heme degradation pathway as haplo insufficiency of HMOX1 combined with SLC48A1 inactivation causes perinatal lethality demonstrating synthetic lethal interactions between heme transport and degradation.	Heme	53-57	heme oxygenase 1	Homo sapiens	104-109
31422179-6	2019	Moreover, the mRNA levels of Keap1, Nrf2, Maf and HO-1 indicated that l-carnitine regulated Nrf2/Keap1 activation.	Carnitine	70-81	heme oxygenase 1	Homo sapiens	50-54
31325727-0	2019	Activation of Nrf2/HO-1 signal with Myricetin for attenuating ECM degradation in human chondrocytes and ameliorating the murine osteoarthritis.	myricetin	36-45	heme oxygenase 1	Homo sapiens	19-23
31351365-1	2019	Naringenin (NG), a flavanone extracted from various plants, has potent vasoprotective effects likely related to the induction of heme oxygenase-1 (HO-1).	naringenin	0-10	heme oxygenase 1	Homo sapiens	129-145
31351365-1	2019	Naringenin (NG), a flavanone extracted from various plants, has potent vasoprotective effects likely related to the induction of heme oxygenase-1 (HO-1).	naringenin	0-10	heme oxygenase 1	Homo sapiens	147-151
31325727-11	2019	To explore the potential mechanism, we found out that myricetin suppressed NF-kappaB signaling pathway through Nrf2/HO-1 axis in human chondrocytes.	myricetin	54-63	heme oxygenase 1	Homo sapiens	116-120
31351365-1	2019	Naringenin (NG), a flavanone extracted from various plants, has potent vasoprotective effects likely related to the induction of heme oxygenase-1 (HO-1).	naringenin	12-14	heme oxygenase 1	Homo sapiens	129-145
31351365-1	2019	Naringenin (NG), a flavanone extracted from various plants, has potent vasoprotective effects likely related to the induction of heme oxygenase-1 (HO-1).	naringenin	12-14	heme oxygenase 1	Homo sapiens	147-151
31351365-2	2019	In the current study, we investigated mechanisms underlying the effect of NG on HO-1 expression and high glucose (HG)- or free fatty acids (FFA)-induced apoptosis in human umbilical vein endothelial cells (HUVECs).	naringenin	74-76	heme oxygenase 1	Homo sapiens	80-84
31351365-3	2019	First, we found that HUVECs exposed to NG exhibited enhanced HO-1 expression in a concentration- and time-dependent manner.	naringenin	39-41	heme oxygenase 1	Homo sapiens	61-65
31351365-5	2019	LY294002 (a PI3K inhibitor) and SP600125 (a JNK inhibitor) reduced NG-induced HO-1 expression, whereas BIRB796 (a p38 inhibitor) and PD98059 (an ERK inhibitor) had no effect.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	0-8	heme oxygenase 1	Homo sapiens	78-82
31351365-5	2019	LY294002 (a PI3K inhibitor) and SP600125 (a JNK inhibitor) reduced NG-induced HO-1 expression, whereas BIRB796 (a p38 inhibitor) and PD98059 (an ERK inhibitor) had no effect.	pyrazolanthrone	32-40	heme oxygenase 1	Homo sapiens	78-82
31325727-14	2019	CONCLUSION: Taken together, our data first demonstrated that myricetin possesses the therapeutic potential on OA through PI3K/Akt mediated Nrf2/HO-1 signaling pathway.	myricetin	61-70	heme oxygenase 1	Homo sapiens	144-148
31356851-10	2019	Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells.	Hemin	86-91	heme oxygenase 1	Homo sapiens	14-30
30465316-5	2019	Stress and toxicity pathway analysis demonstrated that CAPE, in a dose- and time-related fashion, induced the expression of apoptotic and oxidative stress-response genes including growth arrest and DNA-damage inducible, alpha and gamma (GADD45A and GADD45G) and heme oxygenase-1.	caffeic acid phenethyl ester	55-59	heme oxygenase 1	Homo sapiens	262-278
32587840-1	2019	Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin.	Heme	76-80	heme oxygenase 1	Homo sapiens	0-16
32587840-1	2019	Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin.	Heme	76-80	heme oxygenase 1	Homo sapiens	18-22
32587840-1	2019	Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin.	Biliverdine	97-107	heme oxygenase 1	Homo sapiens	0-16
32587840-1	2019	Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin.	Biliverdine	97-107	heme oxygenase 1	Homo sapiens	18-22
31264739-0	2019	Overexpression of heme oxygenase-1 in microenvironment mediates vincristine resistance of B-cell acute lymphoblastic leukemia by promoting vascular endothelial growth factor secretion.	Vincristine	64-75	heme oxygenase 1	Homo sapiens	18-34
31264739-3	2019	Herein, overexpression of heme oxygenase-1 (HO-1) was found in the bone marrow stromal cells (BMSCs) from B-ALL patients developing resistance to vincristine (VCR), a chemotherapeutic agent.	Vincristine	146-157	heme oxygenase 1	Homo sapiens	26-42
31264739-3	2019	Herein, overexpression of heme oxygenase-1 (HO-1) was found in the bone marrow stromal cells (BMSCs) from B-ALL patients developing resistance to vincristine (VCR), a chemotherapeutic agent.	Vincristine	146-157	heme oxygenase 1	Homo sapiens	44-48
31356851-10	2019	Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells.	Hemin	96-101	heme oxygenase 1	Homo sapiens	14-30
31356851-10	2019	Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells.	N-methyl-4-aminoantipyrine	102-105	heme oxygenase 1	Homo sapiens	14-30
31356851-10	2019	Inhibition of heme oxygenase-1 or cytochrome P450 reductase increased the toxicity of hemin and hemin/MAA in undifferentiated, but only for hemin in differentiated HL60 cells.	Hemin	96-101	heme oxygenase 1	Homo sapiens	14-30
31425676-2	2019	In a few instances e.g., neonatal jaundice, overproduction of HO-1 and increased HO activity results in elevated levels of bilirubin requiring clinical intervention with inhibitors of HO activity.	Bilirubin	123-132	heme oxygenase 1	Homo sapiens	62-66
31425676-3	2019	In contrast HO-1 levels and HO activity are low in obesity and the HO system responds to mitigate the deleterious effects of oxidative stress through increased levels of bilirubin (anti-inflammatory) and CO (anti-apoptotic) and decreased levels of heme (pro-oxidant).	Bilirubin	170-179	heme oxygenase 1	Homo sapiens	12-16
31319021-1	2019	Interest in the therapeutic effects of carbon monoxide (CO), a product of heme degradation catalyzed by the enzyme heme oxygenase-1 (HO-1), has led to the development of CO-releasing molecules (CO-RMs) for the controlled delivery of this gas in vivo.	Carbon Monoxide	39-54	heme oxygenase 1	Homo sapiens	115-131
31067610-0	2019	Nrf2-Heme oxygenase-1 modulates autophagy and inhibits apoptosis triggered by elevated glucose levels in renal tubule cells.	Glucose	87-94	heme oxygenase 1	Homo sapiens	5-21
31067610-10	2019	Conclusion: The activation of nuclear factor E2-related factor 2 (Nrf2)-HO-1 inhibited ROS expression and subsequently attenuated autophagy and cell apoptosis after HG injury was decreased.	Reactive Oxygen Species	87-90	heme oxygenase 1	Homo sapiens	72-76
31067610-12	2019	Therefore, HO-1 activation can prevent ROS development and oxidative stress during HG injury, which considerably decreases autophagy and apoptosis.	Reactive Oxygen Species	39-42	heme oxygenase 1	Homo sapiens	11-15
31547608-8	2019	Phenolic extracts derived from RB down-regulated the expression of four genes, ICAM1, CD39, CD73 and NOX4 and up-regulated the expression of another four genes, Nrf2, NQO1, HO1 and eNOS, indicating an antioxidant/ anti-inflammatory effect for RB against endothelial dysfunction.	phenolic acid	0-8	heme oxygenase 1	Homo sapiens	173-176
31319021-1	2019	Interest in the therapeutic effects of carbon monoxide (CO), a product of heme degradation catalyzed by the enzyme heme oxygenase-1 (HO-1), has led to the development of CO-releasing molecules (CO-RMs) for the controlled delivery of this gas in vivo.	Carbon Monoxide	39-54	heme oxygenase 1	Homo sapiens	133-137
31319021-1	2019	Interest in the therapeutic effects of carbon monoxide (CO), a product of heme degradation catalyzed by the enzyme heme oxygenase-1 (HO-1), has led to the development of CO-releasing molecules (CO-RMs) for the controlled delivery of this gas in vivo.	Carbon Monoxide	56-58	heme oxygenase 1	Homo sapiens	115-131
31319021-1	2019	Interest in the therapeutic effects of carbon monoxide (CO), a product of heme degradation catalyzed by the enzyme heme oxygenase-1 (HO-1), has led to the development of CO-releasing molecules (CO-RMs) for the controlled delivery of this gas in vivo.	Carbon Monoxide	56-58	heme oxygenase 1	Homo sapiens	133-137
31319021-2	2019	We recently proposed conjugating a cobalt-based CO-RM with various activators of nuclear factor erythroid 2-related factor 2 (Nrf2), the transcription factor that regulates HO-1 expression, in order to exploit the beneficial effects of exogenous and endogenous CO.	Cobalt	35-41	heme oxygenase 1	Homo sapiens	173-177
31636810-0	2019	Lysosomal Destabilizing Drug Siramesine and the Dual Tyrosine Kinase Inhibitor Lapatinib Induce a Synergistic Ferroptosis through Reduced Heme Oxygenase-1 (HO-1) Levels.	Lu 28-179	29-39	heme oxygenase 1	Homo sapiens	138-154
31533049-0	2019	Microanatomic Distribution of Myeloid Heme Oxygenase-1 Protects against Free Radical-Mediated Immunopathology in Human Tuberculosis.	Free Radicals	72-84	heme oxygenase 1	Homo sapiens	38-54
31636810-0	2019	Lysosomal Destabilizing Drug Siramesine and the Dual Tyrosine Kinase Inhibitor Lapatinib Induce a Synergistic Ferroptosis through Reduced Heme Oxygenase-1 (HO-1) Levels.	Lu 28-179	29-39	heme oxygenase 1	Homo sapiens	156-160
31636810-0	2019	Lysosomal Destabilizing Drug Siramesine and the Dual Tyrosine Kinase Inhibitor Lapatinib Induce a Synergistic Ferroptosis through Reduced Heme Oxygenase-1 (HO-1) Levels.	Lapatinib	79-88	heme oxygenase 1	Homo sapiens	138-154
31636810-0	2019	Lysosomal Destabilizing Drug Siramesine and the Dual Tyrosine Kinase Inhibitor Lapatinib Induce a Synergistic Ferroptosis through Reduced Heme Oxygenase-1 (HO-1) Levels.	Lapatinib	79-88	heme oxygenase 1	Homo sapiens	156-160
31636810-8	2019	Overexpression of HO-1 resulted in reduction of ROS and lipid peroxidation production and cell death.	Reactive Oxygen Species	48-51	heme oxygenase 1	Homo sapiens	18-22
31636810-9	2019	Furthermore, knocking down of HO-1 combined with siramesine treatment resulted in increased cell death.	Lu 28-179	49-59	heme oxygenase 1	Homo sapiens	30-34
31319070-9	2019	Furthermore, nicorandil (3 muM) enhanced nuclear factor erythroid 2-related factor 2 (Nrf2) translocation and heme oxygenase-1 (HO-1) expression.	Nicorandil	13-23	heme oxygenase 1	Homo sapiens	110-126
31421070-6	2019	In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2.	Heme	114-118	heme oxygenase 1	Homo sapiens	9-12
31421070-6	2019	In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2.	Iron	153-157	heme oxygenase 1	Homo sapiens	9-12
31422075-6	2019	Bach1 silencing significantly enhanced sulforaphane-induced expression of HO-1 but had no effect on that of GCLC, GCLM, and NQO1 in young HBE cells.	sulforaphane	39-51	heme oxygenase 1	Homo sapiens	74-78
31422075-7	2019	In contrast, Bach1 silencing enhanced sulforaphane-induced expression of GCLC, GCLM and HO-1 but had no effect on that of NQO-1 in older HBE cells.	sulforaphane	38-50	heme oxygenase 1	Homo sapiens	88-92
31319070-9	2019	Furthermore, nicorandil (3 muM) enhanced nuclear factor erythroid 2-related factor 2 (Nrf2) translocation and heme oxygenase-1 (HO-1) expression.	Nicorandil	13-23	heme oxygenase 1	Homo sapiens	128-132
31319070-11	2019	In summary, nicorandil may protect HUVECs from DOX-induced apoptosis, in part through ATF3-mediated Nrf2/HO-1 signaling pathways, which potentially protect the vessels from severe DOX toxicity.	Nicorandil	12-22	heme oxygenase 1	Homo sapiens	105-109
31319070-11	2019	In summary, nicorandil may protect HUVECs from DOX-induced apoptosis, in part through ATF3-mediated Nrf2/HO-1 signaling pathways, which potentially protect the vessels from severe DOX toxicity.	Doxorubicin	47-50	heme oxygenase 1	Homo sapiens	105-109
31506103-0	2019	Xanthohumol inhibits PRRSV proliferation and alleviates oxidative stress induced by PRRSV via the Nrf2-HMOX1 axis.	xanthohumol	0-11	heme oxygenase 1	Homo sapiens	103-108
31506475-5	2019	DHA increased glutathione peroxidase activity (control, 3.2 +- 0.3 to 4.1 +- 0.2 nmol/min/ml/mug protein, p = 0.004; AAA, 2.3 +- 0.5 to 3.4 +- 0.5 nmol/min/ml/mug protein, p = 0.008) and heme oxygenase-1 mRNA expression (control, 1.5-fold increase, p &lt; 0.001).	Docosahexaenoic Acids	0-3	heme oxygenase 1	Homo sapiens	187-203
31487814-3	2019	Furthermore, Gln exerts potent antioxidant and anti-inflammatory effects in the circulation by inducing the expression of heme oxygenase-1, heat shock proteins, and glutathione.	Glutamine	13-16	heme oxygenase 1	Homo sapiens	122-138
31564855-8	2019	More important, the genotypes, AG, GG of GSTP1 exon5 and L/M*S, L/L of HO-1 (GT)n associated with increased 8-iso-prostaglandin F (2 alpha) (8-iso-PGF2) and malondialdehyde (MDA) concentration and decreased catalase (CAT) activity.	8-isoprostaglandin A2	108-129	heme oxygenase 1	Homo sapiens	71-75
31491954-16	2019	In conclusion, cyanate could induce oxidative stress damage and lipid deposition by inhibiting Nrf2/HO-1 pathway, which was rescued by inhibitor of Nrf2.	Cyanates	15-22	heme oxygenase 1	Homo sapiens	100-104
33448816-6	2019	HUVECs exposed to Rb-CA gels exhibited enhanced migration and tubule formation ability, increased vascular endothelial growth factor secretion, and improved activation of the nuclear factor (erythroid-derived 2)-like 2 (NRF2)/heme-oxygenase-1 (HO-1) signaling pathway.	Rubidium	18-20	heme oxygenase 1	Homo sapiens	226-242
33448816-6	2019	HUVECs exposed to Rb-CA gels exhibited enhanced migration and tubule formation ability, increased vascular endothelial growth factor secretion, and improved activation of the nuclear factor (erythroid-derived 2)-like 2 (NRF2)/heme-oxygenase-1 (HO-1) signaling pathway.	Rubidium	18-20	heme oxygenase 1	Homo sapiens	244-248
31564855-8	2019	More important, the genotypes, AG, GG of GSTP1 exon5 and L/M*S, L/L of HO-1 (GT)n associated with increased 8-iso-prostaglandin F (2 alpha) (8-iso-PGF2) and malondialdehyde (MDA) concentration and decreased catalase (CAT) activity.	8-epi-prostaglandin F2alpha	141-151	heme oxygenase 1	Homo sapiens	71-75
31564855-8	2019	More important, the genotypes, AG, GG of GSTP1 exon5 and L/M*S, L/L of HO-1 (GT)n associated with increased 8-iso-prostaglandin F (2 alpha) (8-iso-PGF2) and malondialdehyde (MDA) concentration and decreased catalase (CAT) activity.	Malondialdehyde	157-172	heme oxygenase 1	Homo sapiens	71-75
31564855-8	2019	More important, the genotypes, AG, GG of GSTP1 exon5 and L/M*S, L/L of HO-1 (GT)n associated with increased 8-iso-prostaglandin F (2 alpha) (8-iso-PGF2) and malondialdehyde (MDA) concentration and decreased catalase (CAT) activity.	Malondialdehyde	174-177	heme oxygenase 1	Homo sapiens	71-75
30861304-4	2019	Si50 (200 microg/mL) induced a time-dependent ROS formation and a postponed increase in expression of haem oxygenase (HO-1) mRNA and protein.	si50	0-4	heme oxygenase 1	Homo sapiens	118-122
31075320-7	2019	Upon application of low doses of ALA-PDT to photoaging HDFs, Nrf2 was translocated to the nucleus; in addition, the expression of Nrf2, transforming growth factor-beta1 (TGF-beta1), type I and III collagen (COL1 and COL3), heme oxygenase 1 (HO-1), and p-ERK was increased, while the expression of matrix metalloproteinase 9 (MMP-9) was decreased.	Aminolevulinic Acid	33-36	heme oxygenase 1	Homo sapiens	223-239
31146961-6	2019	On the protein-level, both cell types showed similar effects: At 5 mM HEMA, heme oxygenase-1 was induced 5.1-fold in OKF6/TERT2 cells and 4.1-fold in HGFs.	hydroxyethyl methacrylate	70-74	heme oxygenase 1	Homo sapiens	76-92
31957703-0	2019	Dexmedetomidine alleviates hepatic injury via the inhibition of oxidative stress and activation of the Nrf2/HO-1 signaling pathway.	Dexmedetomidine	0-15	heme oxygenase 1	Homo sapiens	108-112
31957703-9	2019	Moreover, Nrf2, HO-1, and Bcl-2 expression was upregulated, whereas, in contrast, transcripts for Bax, caspase3, and caspase9 were downregulated following Dex treatment under OGD/R.	Dexmedetomidine	155-158	heme oxygenase 1	Homo sapiens	16-20
31957703-11	2019	Dex protects WRL-68 cells against OGD/R-induced injury by inhibiting inflammation, oxidative stress, and cell apoptosis via the activation of Nrf2/HO-1 signaling pathway, suggesting that Dex may be a potential protector against hepatic injury.	Dexmedetomidine	0-3	heme oxygenase 1	Homo sapiens	147-151
31957703-11	2019	Dex protects WRL-68 cells against OGD/R-induced injury by inhibiting inflammation, oxidative stress, and cell apoptosis via the activation of Nrf2/HO-1 signaling pathway, suggesting that Dex may be a potential protector against hepatic injury.	Dexmedetomidine	187-190	heme oxygenase 1	Homo sapiens	147-151
31226417-0	2019	Entinostat combined with Fludarabine synergistically enhances the induction of apoptosis in TP53 mutated CLL cells via the HDAC1/HO-1 pathway.	fludarabine	25-36	heme oxygenase 1	Homo sapiens	129-133
31037501-0	2019	MiR-153 regulates cardiomyocyte apoptosis by targeting Nrf2/HO-1 signaling.	mir-153	0-7	heme oxygenase 1	Homo sapiens	60-64
31037501-8	2019	Nrf2/ heme oxygenase-1 (HO-1) signaling plays a critical role in miR-153 regulated OGD/R-induced cardiomyocyte apoptosis.	mir-153	65-72	heme oxygenase 1	Homo sapiens	6-22
31037501-8	2019	Nrf2/ heme oxygenase-1 (HO-1) signaling plays a critical role in miR-153 regulated OGD/R-induced cardiomyocyte apoptosis.	mir-153	65-72	heme oxygenase 1	Homo sapiens	24-28
31112013-0	2019	Di (2-ethylhexyl) phthalate induces cytotoxicity in HEK-293 cell line, implication of the Nrf-2/HO-1 antioxidant pathway.	Diethylhexyl Phthalate	0-27	heme oxygenase 1	Homo sapiens	96-100
31273911-8	2019	However, the process of HO-1 metabolism can be toxic owing to iron overload and the activation of succedent pathways, for example, the Fenton reaction and oxidative damage; the overall effect of HO-1 in SAH and ICH tends to be protective and harmful, respectively, given the different pathophysiological changes in these two types of haemorrhagic stroke.	Iron	62-66	heme oxygenase 1	Homo sapiens	24-28
31075320-7	2019	Upon application of low doses of ALA-PDT to photoaging HDFs, Nrf2 was translocated to the nucleus; in addition, the expression of Nrf2, transforming growth factor-beta1 (TGF-beta1), type I and III collagen (COL1 and COL3), heme oxygenase 1 (HO-1), and p-ERK was increased, while the expression of matrix metalloproteinase 9 (MMP-9) was decreased.	Aminolevulinic Acid	33-36	heme oxygenase 1	Homo sapiens	241-245
31456942-0	2019	SIRT5 Promotes Cisplatin Resistance in Ovarian Cancer by Suppressing DNA Damage in a ROS-Dependent Manner via Regulation of the Nrf2/HO-1 Pathway.	Cisplatin	15-24	heme oxygenase 1	Homo sapiens	133-137
31173751-13	2019	Collectively, the results of this study suggest that Nrf2/HO-1 pathway has a protective role against CIN and support the clinical implication of Nrf2 activators, such as sulforaphane, in CIN particularly in diabetic patients.	sulforaphane	170-182	heme oxygenase 1	Homo sapiens	58-62
31227482-0	2019	Isoflavone ME-344 Disrupts Redox Homeostasis and Mitochondrial Function by Targeting Heme Oxygenase 1.	Isoflavones	0-10	heme oxygenase 1	Homo sapiens	85-101
31227482-3	2019	Drug-induced apoptosis was linked with enhanced levels of reactive oxygen species and this initiated a nuclear erythroid factor 2-like 2 signaling response, downstream of which, heme oxygenase 1 (HO-1) was also found to be time-dependently inhibited by ME-344.	Reactive Oxygen Species	58-81	heme oxygenase 1	Homo sapiens	178-194
31227482-3	2019	Drug-induced apoptosis was linked with enhanced levels of reactive oxygen species and this initiated a nuclear erythroid factor 2-like 2 signaling response, downstream of which, heme oxygenase 1 (HO-1) was also found to be time-dependently inhibited by ME-344.	Reactive Oxygen Species	58-81	heme oxygenase 1	Homo sapiens	196-200
31555758-5	2019	This review summarizes current knowledge of molecular mechanisms underlying renoprotective roles of EGCG in CKD based on available preclinical evidence (from both in vitro and in vivo animal studies), particularly its antioxidant property through preservation of mitochondrial function and activation of Nrf2 (nuclear factor erythroid 2-related factor 2)/HO-1 (heme oxygenase-1) signaling, anti-inflammatory activity, and protective effect against epithelial mesenchymal transition.	epigallocatechin gallate	100-104	heme oxygenase 1	Homo sapiens	355-377
31181187-7	2019	Importantly, pelargonidin decreased the DNA methylation in the Nrf2 promoter region of JB6 P+ cells and increased Nrf2 downstream target genes expression, such as NAD(P)H/quinone oxidoreductase 1 (NQO1) and heme oxygenase-1 (HO-1), involved in cellular protection.	pelargonidin	13-25	heme oxygenase 1	Homo sapiens	207-223
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Heme	52-56	heme oxygenase 1	Homo sapiens	0-16
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Heme	52-56	heme oxygenase 1	Homo sapiens	18-22
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Heme	52-56	heme oxygenase 1	Homo sapiens	24-29
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Carbon Monoxide	62-77	heme oxygenase 1	Homo sapiens	0-16
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Carbon Monoxide	62-77	heme oxygenase 1	Homo sapiens	18-22
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Carbon Monoxide	62-77	heme oxygenase 1	Homo sapiens	24-29
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Carbon Monoxide	79-81	heme oxygenase 1	Homo sapiens	0-16
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Carbon Monoxide	79-81	heme oxygenase 1	Homo sapiens	18-22
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Carbon Monoxide	79-81	heme oxygenase 1	Homo sapiens	24-29
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	ammonium ferrous sulfate	84-96	heme oxygenase 1	Homo sapiens	0-16
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	ammonium ferrous sulfate	84-96	heme oxygenase 1	Homo sapiens	18-22
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	ammonium ferrous sulfate	84-96	heme oxygenase 1	Homo sapiens	24-29
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	ammonium ferrous sulfate	98-102	heme oxygenase 1	Homo sapiens	0-16
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	ammonium ferrous sulfate	98-102	heme oxygenase 1	Homo sapiens	18-22
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	ammonium ferrous sulfate	98-102	heme oxygenase 1	Homo sapiens	24-29
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Biliverdine	108-118	heme oxygenase 1	Homo sapiens	0-16
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Biliverdine	108-118	heme oxygenase 1	Homo sapiens	18-22
31276659-1	2019	Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin.	Biliverdine	108-118	heme oxygenase 1	Homo sapiens	24-29
31456942-6	2019	Mechanistically, we show that SIRT5 contributes to cisplatin resistance in ovarian cancer by suppressing cisplatin-induced DNA damage in a reactive oxygen species (ROS)-dependent manner via regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	Cisplatin	51-60	heme oxygenase 1	Homo sapiens	259-275
31456942-6	2019	Mechanistically, we show that SIRT5 contributes to cisplatin resistance in ovarian cancer by suppressing cisplatin-induced DNA damage in a reactive oxygen species (ROS)-dependent manner via regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	Cisplatin	51-60	heme oxygenase 1	Homo sapiens	277-281
31456942-6	2019	Mechanistically, we show that SIRT5 contributes to cisplatin resistance in ovarian cancer by suppressing cisplatin-induced DNA damage in a reactive oxygen species (ROS)-dependent manner via regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	Cisplatin	105-114	heme oxygenase 1	Homo sapiens	259-275
31456942-6	2019	Mechanistically, we show that SIRT5 contributes to cisplatin resistance in ovarian cancer by suppressing cisplatin-induced DNA damage in a reactive oxygen species (ROS)-dependent manner via regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	Cisplatin	105-114	heme oxygenase 1	Homo sapiens	277-281
31456942-6	2019	Mechanistically, we show that SIRT5 contributes to cisplatin resistance in ovarian cancer by suppressing cisplatin-induced DNA damage in a reactive oxygen species (ROS)-dependent manner via regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	Reactive Oxygen Species	164-167	heme oxygenase 1	Homo sapiens	259-275
31456942-6	2019	Mechanistically, we show that SIRT5 contributes to cisplatin resistance in ovarian cancer by suppressing cisplatin-induced DNA damage in a reactive oxygen species (ROS)-dependent manner via regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase 1 (HO-1) pathway.	Reactive Oxygen Species	164-167	heme oxygenase 1	Homo sapiens	277-281
31467925-0	2019	Nrf2-Heme Oxygenase-1 Attenuates High-Glucose-Induced Epithelial-to-Mesenchymal Transition of Renal Tubule Cells by Inhibiting ROS-Mediated PI3K/Akt/GSK-3beta Signaling.	Reactive Oxygen Species	127-130	heme oxygenase 1	Homo sapiens	5-21
31474865-5	2019	The present study showed that tyrosol, a phenylethanoid compound, suppresses accumulation of intracellular reactive oxygen species (ROS) caused by hyperglycemia, most plausibly by promoting heme oxygenase-1 (HO-1) expression in skeletal muscle cells.	4-hydroxyphenylethanol	30-37	heme oxygenase 1	Homo sapiens	190-206
31467925-6	2019	Treatment of HK2 cells with SFN caused HG-induced attenuation in EMT markers with activated Nrf2-HO-1.	sulforaphane	28-31	heme oxygenase 1	Homo sapiens	97-101
31467925-9	2019	Conclusion: The present study suggests that Nrf2-HO-1 signaling has an inhibitory role in the regulation of EMT through the modulation of ROS-mediated PI3K/Akt/GSK-3beta activity, highlighting Nrf2-HO-1 and GSK-3beta as potential therapeutic targets in diabetic nephropathy.	Reactive Oxygen Species	138-141	heme oxygenase 1	Homo sapiens	49-53
31467925-9	2019	Conclusion: The present study suggests that Nrf2-HO-1 signaling has an inhibitory role in the regulation of EMT through the modulation of ROS-mediated PI3K/Akt/GSK-3beta activity, highlighting Nrf2-HO-1 and GSK-3beta as potential therapeutic targets in diabetic nephropathy.	Reactive Oxygen Species	138-141	heme oxygenase 1	Homo sapiens	198-202
31073781-9	2019	HO/HMOX/HSP32, expression was notably increased, which suggested the accumulation of reactive oxygen species.	Reactive Oxygen Species	85-108	heme oxygenase 1	Homo sapiens	8-13
31141180-9	2019	These results demonstrated that 5-ALA/SFC treatment ameliorated binge alcohol exposure liver injury in a rat model of HIV-infected patients by reducing macrophage activation and expression of inflammatory cytokines/chemokines, and by inducing HO-1, HO-2, and Sirt1 expression.	5-amino levulinic acid	32-37	heme oxygenase 1	Homo sapiens	243-247
31141180-9	2019	These results demonstrated that 5-ALA/SFC treatment ameliorated binge alcohol exposure liver injury in a rat model of HIV-infected patients by reducing macrophage activation and expression of inflammatory cytokines/chemokines, and by inducing HO-1, HO-2, and Sirt1 expression.	SFC	38-41	heme oxygenase 1	Homo sapiens	243-247
31030250-9	2019	Patients harboring mutant HMOX-1 had a less frequent vaso-occlusive crisis (VOC)/lifetime, less VOC in the last year, less incidence of stroke, less frequency of hospitalization, and responded more frequently to hydroxyurea with statistically significant differences (p = 0.028, 0.007, 0.046, 0.007, and 0.011 respectively).	Hydroxyurea	212-223	heme oxygenase 1	Homo sapiens	26-32
31387260-7	2019	The activity of HO-1 was inhibited using Tin Mesoporphyrin IX (SnMP).	tin mesoporphyrin ix	41-61	heme oxygenase 1	Homo sapiens	16-20
31387260-7	2019	The activity of HO-1 was inhibited using Tin Mesoporphyrin IX (SnMP).	tin mesoporphyrin	63-67	heme oxygenase 1	Homo sapiens	16-20
30871975-5	2019	In this study we found that heme oxygenase-1, which could induce decay-accelerating factor (DAF) and inhibit the membrane-attack complex, was significantly decreased in patients with TA-TMA.	ta-tma	183-189	heme oxygenase 1	Homo sapiens	28-44
31250343-13	2019	Moreover, the astragalin-induced the upregulation of HO-1 in human lung epithelial cells was inhibited when nuclear factor erythroid-2-related factor 2 (Nrf2) was silenced by small interfering RNA.	astragalin	14-24	heme oxygenase 1	Homo sapiens	53-57
31250343-14	2019	Astragalin reduces LPS-induced ALI via activation of Nrf2/HO-1 pathway.	astragalin	0-10	heme oxygenase 1	Homo sapiens	58-62
31153982-4	2019	Simultaneously, hesperetin activated the Nrf2 signaling pathway and regulated its downstream genes, including NQO1 and HO-1.	hesperetin	16-26	heme oxygenase 1	Homo sapiens	119-123
31059786-0	2019	Lipoxin A4 restores oxidative stress-induced vascular endothelial cell injury and thrombosis-related factor expression by its receptor-mediated activation of Nrf2-HO-1 axis.	lipoxin A4	0-10	heme oxygenase 1	Homo sapiens	163-167
31059786-9	2019	Mechanism analysis substantiated that LXA4 further augmented activation of the Nrf2-HO-1 pathway.	lipoxin A4	38-42	heme oxygenase 1	Homo sapiens	84-88
31059786-10	2019	Nevertheless, blocking this signaling via si-Nrf2 transfection or HO-1 antagonist ZnPP both reversed LXA4-mediated effects against oxidative stress injury and thrombotic potential.	Silicon	28-30	heme oxygenase 1	Homo sapiens	66-70
31059786-10	2019	Nevertheless, blocking this signaling via si-Nrf2 transfection or HO-1 antagonist ZnPP both reversed LXA4-mediated effects against oxidative stress injury and thrombotic potential.	zinc protoporphyrin	82-86	heme oxygenase 1	Homo sapiens	66-70
31059786-11	2019	Cessation of the LXA4 receptor pathway by its inhibitor Boc2 not only counteracted LXA4-evoked activation of the Nrf2-HO-1, but also reversed LXA4-mediated anti-oxidative stress and thrombosis-related factor expression.	boc2	56-60	heme oxygenase 1	Homo sapiens	118-122
31059786-12	2019	Accordingly, this study suggests that LXA4 may ameliorate vascular endothelial cell oxidative stress injury and subsequent thrombotic response via LXA4 receptor-dependent activation of the Nrf2-HO-1 signaling, implying a promising strategy for DVT and its complication.	lipoxin A4	38-42	heme oxygenase 1	Homo sapiens	194-198
31202006-11	2019	Finally, only CY could lead to an increase in heme oxygenase 1 (HMOX1) expression.	Cyclophosphamide	14-16	heme oxygenase 1	Homo sapiens	46-62
31172435-5	2019	Among the three types of SOA, m-xylene-derived SOA showed the strongest induction of the HMOX1 and IL8 genes, and transcriptional activity via the antioxidant response element (ARE).	Xylenes	32-38	heme oxygenase 1	Homo sapiens	89-94
31202006-11	2019	Finally, only CY could lead to an increase in heme oxygenase 1 (HMOX1) expression.	Cyclophosphamide	14-16	heme oxygenase 1	Homo sapiens	64-69
31389609-11	2019	High glucose notably lowered the protein expression levels of Nrf2, HO-1, and gamma-GCS in the cells (p<0.01).	Glucose	5-12	heme oxygenase 1	Homo sapiens	68-72
30842612-3	2019	These alterations in HO-1 and NO markers were prevented by cotreatment with the polyphenol resveratrol, which also improved GSH levels.	polyphenol resveratrol	80-102	heme oxygenase 1	Homo sapiens	21-25
30842612-3	2019	These alterations in HO-1 and NO markers were prevented by cotreatment with the polyphenol resveratrol, which also improved GSH levels.	Glutathione	124-127	heme oxygenase 1	Homo sapiens	21-25
31143972-0	2019	Salsalate ameliorates the atherosclerotic response through HO-1- and SIRT1-mediated suppression of ER stress and inflammation.	salicylsalicylic acid	0-9	heme oxygenase 1	Homo sapiens	59-63
31356549-0	2019	Curdione Ameliorated Doxorubicin-Induced Cardiotoxicity Through Suppressing Oxidative Stress and Activating Nrf2/HO-1 Pathway.	curdione	0-8	heme oxygenase 1	Homo sapiens	113-117
31143972-12	2019	CONCLUSIONS: Salsalate ameliorates LPS-induced atherosclerotic reactions via HO-1 and SIRT1-dependent reduction of inflammation and ER stress.	salicylsalicylic acid	13-22	heme oxygenase 1	Homo sapiens	77-81
31356549-0	2019	Curdione Ameliorated Doxorubicin-Induced Cardiotoxicity Through Suppressing Oxidative Stress and Activating Nrf2/HO-1 Pathway.	Doxorubicin	21-32	heme oxygenase 1	Homo sapiens	113-117
31199053-2	2019	In the presence of stimulation by cobalt protoporphyrin (CoPP), an HO-1 inducer, apoptotic characteristics were observed, including DNA laddering, hypodiploid cells, and cleavages of caspase (Casp)-3 and poly(ADP) ribose polymerase (PARP) proteins in human colon carcinoma COLO205, HCT-15, LOVO and HT-29 cells in serum-free (SF) conditions with increased HO-1, but not heat shock protein 70 (HSP70) or HSP90.	cobaltiprotoporphyrin	34-55	heme oxygenase 1	Homo sapiens	67-71
31199053-2	2019	In the presence of stimulation by cobalt protoporphyrin (CoPP), an HO-1 inducer, apoptotic characteristics were observed, including DNA laddering, hypodiploid cells, and cleavages of caspase (Casp)-3 and poly(ADP) ribose polymerase (PARP) proteins in human colon carcinoma COLO205, HCT-15, LOVO and HT-29 cells in serum-free (SF) conditions with increased HO-1, but not heat shock protein 70 (HSP70) or HSP90.	cobaltiprotoporphyrin	34-55	heme oxygenase 1	Homo sapiens	356-360
31199053-2	2019	In the presence of stimulation by cobalt protoporphyrin (CoPP), an HO-1 inducer, apoptotic characteristics were observed, including DNA laddering, hypodiploid cells, and cleavages of caspase (Casp)-3 and poly(ADP) ribose polymerase (PARP) proteins in human colon carcinoma COLO205, HCT-15, LOVO and HT-29 cells in serum-free (SF) conditions with increased HO-1, but not heat shock protein 70 (HSP70) or HSP90.	cobaltiprotoporphyrin	57-61	heme oxygenase 1	Homo sapiens	67-71
31199053-2	2019	In the presence of stimulation by cobalt protoporphyrin (CoPP), an HO-1 inducer, apoptotic characteristics were observed, including DNA laddering, hypodiploid cells, and cleavages of caspase (Casp)-3 and poly(ADP) ribose polymerase (PARP) proteins in human colon carcinoma COLO205, HCT-15, LOVO and HT-29 cells in serum-free (SF) conditions with increased HO-1, but not heat shock protein 70 (HSP70) or HSP90.	cobaltiprotoporphyrin	57-61	heme oxygenase 1	Homo sapiens	356-360
31356549-9	2019	Further study indicated that curdione decreased DOX-induced phosphorylation of extracellular signal-regulated kinase1/2 (Erk1/2) and c-Jun-N-terminal kinase and activated nuclear factor-erythroid 2-related factor 2/heme oxygenase 1 (Nrf2/HO-1) signal pathway.	curdione	29-37	heme oxygenase 1	Homo sapiens	238-242
31356549-9	2019	Further study indicated that curdione decreased DOX-induced phosphorylation of extracellular signal-regulated kinase1/2 (Erk1/2) and c-Jun-N-terminal kinase and activated nuclear factor-erythroid 2-related factor 2/heme oxygenase 1 (Nrf2/HO-1) signal pathway.	Doxorubicin	48-51	heme oxygenase 1	Homo sapiens	238-242
30951941-6	2019	In addition, TBBPA promoted the expression of antioxidant genes related to Nrf2, such as quinone oxidoreductase 1 (NQO1), catalase (CAT), and heme oxygenase 1 (HO-1).	tetrabromobisphenol A	13-18	heme oxygenase 1	Homo sapiens	142-158
30770549-0	2019	Curcumin prevents high glucose damage in retinal pigment epithelial cells through ERK1/2-mediated activation of the Nrf2/HO-1 pathway.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	121-125
30770549-5	2019	Further, curcumin was able to induce HO-1 expression via Nrf2 activation and counteracts the damage elicited by HG.	Curcumin	9-17	heme oxygenase 1	Homo sapiens	37-41
30770549-6	2019	The present study demonstrated that curcumin provides protection against HG-induced damage in RPE cells through the activation of Nrf2/HO-1 signaling that involves the ERK pathway, suggesting that curcumin may have therapeutic value in the treatment of diabetic retinopathy.	Curcumin	36-44	heme oxygenase 1	Homo sapiens	135-139
30770549-6	2019	The present study demonstrated that curcumin provides protection against HG-induced damage in RPE cells through the activation of Nrf2/HO-1 signaling that involves the ERK pathway, suggesting that curcumin may have therapeutic value in the treatment of diabetic retinopathy.	Curcumin	197-205	heme oxygenase 1	Homo sapiens	135-139
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Heme	83-87	heme oxygenase 1	Homo sapiens	0-16
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Heme	83-87	heme oxygenase 1	Homo sapiens	18-22
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Iron	100-112	heme oxygenase 1	Homo sapiens	0-16
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Iron	100-112	heme oxygenase 1	Homo sapiens	18-22
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	114-129	heme oxygenase 1	Homo sapiens	0-16
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	114-129	heme oxygenase 1	Homo sapiens	18-22
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	131-133	heme oxygenase 1	Homo sapiens	0-16
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	131-133	heme oxygenase 1	Homo sapiens	18-22
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Biliverdine	140-150	heme oxygenase 1	Homo sapiens	0-16
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Biliverdine	140-150	heme oxygenase 1	Homo sapiens	18-22
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Bilirubin	187-196	heme oxygenase 1	Homo sapiens	0-16
31344980-1	2019	Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin.	Bilirubin	187-196	heme oxygenase 1	Homo sapiens	18-22
31344980-5	2019	In atherosclerosis, HO-1 may play a protective role against the progression of atherosclerosis, mainly due to the degradation of pro-oxidant heme, the generation of anti-oxidants biliverdin and bilirubin and the production of vasodilator CO.	Heme	141-145	heme oxygenase 1	Homo sapiens	20-24
31344980-5	2019	In atherosclerosis, HO-1 may play a protective role against the progression of atherosclerosis, mainly due to the degradation of pro-oxidant heme, the generation of anti-oxidants biliverdin and bilirubin and the production of vasodilator CO.	Biliverdine	179-189	heme oxygenase 1	Homo sapiens	20-24
31344980-5	2019	In atherosclerosis, HO-1 may play a protective role against the progression of atherosclerosis, mainly due to the degradation of pro-oxidant heme, the generation of anti-oxidants biliverdin and bilirubin and the production of vasodilator CO.	Bilirubin	194-203	heme oxygenase 1	Homo sapiens	20-24
31214670-5	2019	Furthermore, DHA promoted the nuclear translocation of nuclear factor E2-related factor 2 (Nrf2), wherein Nrf2 further mediated the expression of multiple antioxidant enzymes such as, heme oxygenase-1 (HO-1), NAD(P)H: quinone oxidoreductase-1 (NQO1) and catalase, which are closely related with redox homeostasis.	Docosahexaenoic Acids	13-16	heme oxygenase 1	Homo sapiens	184-200
31396016-4	2019	Both conditions can be accompanied by decreased levels of heme oxygenase-1 (HMOX1), cytoprotective, heme-degrading enzyme.	Heme	58-62	heme oxygenase 1	Homo sapiens	76-81
31396016-10	2019	On the other hand, the only one that induced heme oxygenase-1 expression was sulforaphane, a known activator of a HMOX1 inducer-NRF2.	sulforaphane	77-89	heme oxygenase 1	Homo sapiens	45-61
31396016-10	2019	On the other hand, the only one that induced heme oxygenase-1 expression was sulforaphane, a known activator of a HMOX1 inducer-NRF2.	sulforaphane	77-89	heme oxygenase 1	Homo sapiens	114-119
30776144-3	2019	The heme oxygenase 1, encoded by the HMOX1 gene and NADH:quinone oxidoreductase 1, encoded by the NQO1 gene are crucial mediators of cellular defense against ROS.	Reactive Oxygen Species	158-161	heme oxygenase 1	Homo sapiens	4-20
30776144-3	2019	The heme oxygenase 1, encoded by the HMOX1 gene and NADH:quinone oxidoreductase 1, encoded by the NQO1 gene are crucial mediators of cellular defense against ROS.	Reactive Oxygen Species	158-161	heme oxygenase 1	Homo sapiens	37-42
30776144-4	2019	The present study aimed to investigate the associations between HMOX1 and NQO1 polymorphisms and ATLI in Chinese anti-TB treatment population.	Terbium	118-120	heme oxygenase 1	Homo sapiens	64-69
30776144-9	2019	WHAT IS NEW AND CONCLUSION: This is the first study to explore the relationship between HMOX1, NQO1 polymorphisms and ATLI in Chinese anti-TB treatment population.	Terbium	139-141	heme oxygenase 1	Homo sapiens	88-93
31423266-0	2019	Stimulated upregulation of HO-1 is associated with inadequate response of gastric and ovarian cancer cell lines to hyperthermia and cisplatin treatment.	Cisplatin	132-141	heme oxygenase 1	Homo sapiens	27-31
31423266-4	2019	In OVCAR-3 cells, cisplatin increased HO-1 mRNA expression by 3.73-fold under normothermia and 2.4-fold under hyperthermia; furthermore, these factors similarly increased HO-1 protein expression levels.	Cisplatin	18-27	heme oxygenase 1	Homo sapiens	38-42
31423266-4	2019	In OVCAR-3 cells, cisplatin increased HO-1 mRNA expression by 3.73-fold under normothermia and 2.4-fold under hyperthermia; furthermore, these factors similarly increased HO-1 protein expression levels.	Cisplatin	18-27	heme oxygenase 1	Homo sapiens	171-175
31423266-6	2019	HO-1-silencing under normothermia increased apoptotic rates in cisplatin-treated OVCAR-3 cells by 2.07-fold, and hyperthermia enhanced the effect by 3.09-fold.	Cisplatin	63-72	heme oxygenase 1	Homo sapiens	0-4
31423266-13	2019	In tumors with highly inducible HO-1, prior silencing of this gene could improve the cellular response to hyperthermia and cisplatin.	Cisplatin	123-132	heme oxygenase 1	Homo sapiens	32-36
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Heme	43-47	heme oxygenase 1	Homo sapiens	0-22
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	0-22
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Carbon Monoxide	70-72	heme oxygenase 1	Homo sapiens	0-22
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Iron	83-87	heme oxygenase 1	Homo sapiens	0-22
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	0-22
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Biliverdine	105-107	heme oxygenase 1	Homo sapiens	0-22
31396090-3	2019	Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR).	Bilirubin	109-118	heme oxygenase 1	Homo sapiens	0-22
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	5-amino levulinic acid	0-21	heme oxygenase 1	Homo sapiens	147-163
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	5-amino levulinic acid	0-21	heme oxygenase 1	Homo sapiens	165-169
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	5-amino levulinic acid	23-26	heme oxygenase 1	Homo sapiens	147-163
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	5-amino levulinic acid	23-26	heme oxygenase 1	Homo sapiens	165-169
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	Ferromia	42-64	heme oxygenase 1	Homo sapiens	147-163
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	Ferromia	42-64	heme oxygenase 1	Homo sapiens	165-169
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	SFC	66-69	heme oxygenase 1	Homo sapiens	147-163
31332208-2	2019	5-Aminolevulinic acid (ALA) combined with sodium ferrous citrate (SFC) was reported to enhance haem production, leading to respiratory complex and haem oxygenase-1 (HO-1) upregulation.	SFC	66-69	heme oxygenase 1	Homo sapiens	165-169
31332208-9	2019	Thus, our findings indicate that ALA/SFC is effective in elevating OXPHOS, HO-1 protein, and mtDNA copy number, resulting in an increase in OCR and ATP levels, which represents a promising therapeutic option for mitochondrial diseases.	SFC	37-40	heme oxygenase 1	Homo sapiens	75-79
31379570-9	2019	Moreover, TTB potentially prolonged the activation state of the nuclear factor erythroid 2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway and maintained the protection against oxidative stress in OGD/R-induced astrocytes by inducing the nuclear translocation and up-regulation of Nrf2 along with the enhanced expression of the downstream target gene HO-1.	Thenoyltrifluoroacetone	10-13	heme oxygenase 1	Homo sapiens	115-131
31257023-3	2019	Nrf2 accumulation in lung cancers causes the stabilization of Bach1 by inducing Ho1, the enzyme catabolizing heme.	Heme	109-113	heme oxygenase 1	Homo sapiens	80-83
31360208-4	2019	We also noticed that BP restored Ox-LDL-stimulated HUVECs oxidative stress, by induced antioxidant gene expressions, including Heme oxygenase-1 and its upstream mediator, Nrf2, which were mediated by the activation of the phosphorylation of PI3K/Akt/mTOR.	Benzo(a)pyrene	21-23	heme oxygenase 1	Homo sapiens	127-143
31360208-5	2019	Pretreatment with wortmannin, PI3K/AKT inhibitor, abolished BP induced Nrf2 nuclear translocation and HO-1 level.	Wortmannin	18-28	heme oxygenase 1	Homo sapiens	102-106
31360208-6	2019	Our results demonstrated that BP protected HUVECs against oxidative damage partly via PI3K/Akt/mTOR-mediated Nrf/HO-1 pathway, which might be applied into preventing Ox-LDL mediated cardiovascular diseases.	Benzo(a)pyrene	30-32	heme oxygenase 1	Homo sapiens	113-117
31277394-4	2019	Moreover, piceatannol treatment induced NF-E2-related factor 2 (Nrf2) signaling activation, which was evidenced by increased transcription of anti-oxidant genes, glutamate-cysteine ligase catalytic subunit (GCLc), SOD, and HO-1.	3,3',4,5'-tetrahydroxystilbene	10-21	heme oxygenase 1	Homo sapiens	223-227
31277394-5	2019	Knockdown of Nrf2 through targeted siRNA alleviated piceatannol-mediated HO-1 transcription, and significantly abolished piceatannol-mediated cytoprotection.	3,3',4,5'-tetrahydroxystilbene	52-63	heme oxygenase 1	Homo sapiens	73-77
31277394-6	2019	LY294002 (PI3K inhibitor) dramatically blocked piceatannol-mediated increasing of Nrf2 nuclear translocation, HO-1 expression, and cytoprotective activity, indicating the involvement of PI3K/Akt pathway in the cytoprotective effect of piceatannol.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	0-8	heme oxygenase 1	Homo sapiens	110-114
31277394-6	2019	LY294002 (PI3K inhibitor) dramatically blocked piceatannol-mediated increasing of Nrf2 nuclear translocation, HO-1 expression, and cytoprotective activity, indicating the involvement of PI3K/Akt pathway in the cytoprotective effect of piceatannol.	3,3',4,5'-tetrahydroxystilbene	47-58	heme oxygenase 1	Homo sapiens	110-114
31219431-0	2019	Activation of the Nrf2/HO-1 signaling pathway contributes to the protective effects of coptisine against oxidative stress-induced DNA damage and apoptosis in HaCaT keratinocytes.	coptisine	87-96	heme oxygenase 1	Homo sapiens	23-27
31035147-9	2019	Furthermore, as the downstream components of Nrf2 pathway, catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GPX) and heme oxygenase-1 (HO-1) were significantly synergistically induced by formaldehyde and acrolein mixtures.	Formaldehyde	209-221	heme oxygenase 1	Homo sapiens	139-155
31035147-9	2019	Furthermore, as the downstream components of Nrf2 pathway, catalase (CAT), superoxide dismutase (SOD) and glutathione peroxidase (GPX) and heme oxygenase-1 (HO-1) were significantly synergistically induced by formaldehyde and acrolein mixtures.	Acrolein	226-234	heme oxygenase 1	Homo sapiens	139-155
31219431-7	2019	Furthermore, the protective effects of coptisine against H2O2-induced cytotoxicity were abolished by ZnPP, indicating that coptisine protects keratinocytes against oxidative stress-induced injury through activation of the Nrf2/HO-1 signaling pathway.	coptisine	39-48	heme oxygenase 1	Homo sapiens	227-231
31219431-7	2019	Furthermore, the protective effects of coptisine against H2O2-induced cytotoxicity were abolished by ZnPP, indicating that coptisine protects keratinocytes against oxidative stress-induced injury through activation of the Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	57-61	heme oxygenase 1	Homo sapiens	227-231
31219431-4	2019	Interestingly, the expressions of nuclear factor-erythroid-2-related factor 2 (Nrf2) and its active form, phosphorylated Nrf2, were strikingly promoted by coptisine in the presence of H2O2, which was associated with a marked increase in the expression of heme oxygenase-1 (HO-1).	coptisine	155-164	heme oxygenase 1	Homo sapiens	255-271
31219431-7	2019	Furthermore, the protective effects of coptisine against H2O2-induced cytotoxicity were abolished by ZnPP, indicating that coptisine protects keratinocytes against oxidative stress-induced injury through activation of the Nrf2/HO-1 signaling pathway.	zinc protoporphyrin	101-105	heme oxygenase 1	Homo sapiens	227-231
31219431-4	2019	Interestingly, the expressions of nuclear factor-erythroid-2-related factor 2 (Nrf2) and its active form, phosphorylated Nrf2, were strikingly promoted by coptisine in the presence of H2O2, which was associated with a marked increase in the expression of heme oxygenase-1 (HO-1).	coptisine	155-164	heme oxygenase 1	Homo sapiens	273-277
31219431-7	2019	Furthermore, the protective effects of coptisine against H2O2-induced cytotoxicity were abolished by ZnPP, indicating that coptisine protects keratinocytes against oxidative stress-induced injury through activation of the Nrf2/HO-1 signaling pathway.	coptisine	123-132	heme oxygenase 1	Homo sapiens	227-231
31219431-4	2019	Interestingly, the expressions of nuclear factor-erythroid-2-related factor 2 (Nrf2) and its active form, phosphorylated Nrf2, were strikingly promoted by coptisine in the presence of H2O2, which was associated with a marked increase in the expression of heme oxygenase-1 (HO-1).	Hydrogen Peroxide	184-188	heme oxygenase 1	Homo sapiens	255-271
31219431-4	2019	Interestingly, the expressions of nuclear factor-erythroid-2-related factor 2 (Nrf2) and its active form, phosphorylated Nrf2, were strikingly promoted by coptisine in the presence of H2O2, which was associated with a marked increase in the expression of heme oxygenase-1 (HO-1).	Hydrogen Peroxide	184-188	heme oxygenase 1	Homo sapiens	273-277
31219431-5	2019	However, coptisine-induced HO-1 expression was completely abrogated by Nrf2-specific small interfering RNA (Nrf2-siRNA), which suggests that the increased expression of HO-1 by coptisine is Nrf2-dependent.	coptisine	9-18	heme oxygenase 1	Homo sapiens	27-31
31219431-5	2019	However, coptisine-induced HO-1 expression was completely abrogated by Nrf2-specific small interfering RNA (Nrf2-siRNA), which suggests that the increased expression of HO-1 by coptisine is Nrf2-dependent.	coptisine	9-18	heme oxygenase 1	Homo sapiens	169-173
31219431-5	2019	However, coptisine-induced HO-1 expression was completely abrogated by Nrf2-specific small interfering RNA (Nrf2-siRNA), which suggests that the increased expression of HO-1 by coptisine is Nrf2-dependent.	coptisine	177-186	heme oxygenase 1	Homo sapiens	27-31
31219431-5	2019	However, coptisine-induced HO-1 expression was completely abrogated by Nrf2-specific small interfering RNA (Nrf2-siRNA), which suggests that the increased expression of HO-1 by coptisine is Nrf2-dependent.	coptisine	177-186	heme oxygenase 1	Homo sapiens	169-173
31115551-0	2019	Glycyrrhizin protects human melanocytes from H2O2-induced oxidative damage via the Nrf2-dependent induction of HO-1.	Glycyrrhizic Acid	0-12	heme oxygenase 1	Homo sapiens	111-115
31115551-0	2019	Glycyrrhizin protects human melanocytes from H2O2-induced oxidative damage via the Nrf2-dependent induction of HO-1.	Hydrogen Peroxide	45-49	heme oxygenase 1	Homo sapiens	111-115
31115551-11	2019	The knockdown of Nrf2 by small interfering RNA or the inhibition of HO-1 by ZnPP reversed the protective effect of GR on melanocytes against H2O2-induced cytotoxicity and apoptosis.	zinc protoporphyrin	76-80	heme oxygenase 1	Homo sapiens	68-72
31115551-11	2019	The knockdown of Nrf2 by small interfering RNA or the inhibition of HO-1 by ZnPP reversed the protective effect of GR on melanocytes against H2O2-induced cytotoxicity and apoptosis.	Hydrogen Peroxide	141-145	heme oxygenase 1	Homo sapiens	68-72
31251786-4	2019	In this study we found that HBZ activates expression of Heme Oxygenase 1 (HMOX-1), a component of the oxidative stress response that functions to detoxify free heme.	Heme	160-164	heme oxygenase 1	Homo sapiens	56-72
31261663-0	2019	Carbon Monoxide Releasing Molecule-2-Upregulated ROS-Dependent Heme Oxygenase-1 Axis Suppresses Lipopolysaccharide-Induced Airway Inflammation.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	63-79
31251786-4	2019	In this study we found that HBZ activates expression of Heme Oxygenase 1 (HMOX-1), a component of the oxidative stress response that functions to detoxify free heme.	Heme	160-164	heme oxygenase 1	Homo sapiens	74-80
31261663-0	2019	Carbon Monoxide Releasing Molecule-2-Upregulated ROS-Dependent Heme Oxygenase-1 Axis Suppresses Lipopolysaccharide-Induced Airway Inflammation.	Reactive Oxygen Species	49-52	heme oxygenase 1	Homo sapiens	63-79
31251786-8	2019	Consistent with this model, we found that HMOX-1 is upregulated in HTLV-1-transformed T-cell lines and confers these cells with resistance to heme-induced cytotoxicity.	Heme	142-146	heme oxygenase 1	Homo sapiens	42-48
31261663-1	2019	The up-regulation of heme oxygenase-1 (HO-1) is mediated through nicotinamaide adenine dinucleotide phosphate (NADPH) oxidases (Nox) and reactive oxygen species (ROS) generation, which could provide cytoprotection against inflammation.	Reactive Oxygen Species	137-160	heme oxygenase 1	Homo sapiens	21-37
31261663-1	2019	The up-regulation of heme oxygenase-1 (HO-1) is mediated through nicotinamaide adenine dinucleotide phosphate (NADPH) oxidases (Nox) and reactive oxygen species (ROS) generation, which could provide cytoprotection against inflammation.	Reactive Oxygen Species	137-160	heme oxygenase 1	Homo sapiens	39-43
31208152-8	2019	CHA79 attenuated MG-induced ROS production and enhanced the antioxidant defense including nuclear factor erythroid 2-related factor 2 (Nrf2), HO-1, SOD and GSH.	cha79	0-5	heme oxygenase 1	Homo sapiens	142-146
31261663-1	2019	The up-regulation of heme oxygenase-1 (HO-1) is mediated through nicotinamaide adenine dinucleotide phosphate (NADPH) oxidases (Nox) and reactive oxygen species (ROS) generation, which could provide cytoprotection against inflammation.	Reactive Oxygen Species	162-165	heme oxygenase 1	Homo sapiens	21-37
31261663-1	2019	The up-regulation of heme oxygenase-1 (HO-1) is mediated through nicotinamaide adenine dinucleotide phosphate (NADPH) oxidases (Nox) and reactive oxygen species (ROS) generation, which could provide cytoprotection against inflammation.	Reactive Oxygen Species	162-165	heme oxygenase 1	Homo sapiens	39-43
31261663-2	2019	However, the molecular mechanisms of carbon monoxide-releasing molecule (CORM)-2-induced HO-1 expression in human tracheal smooth muscle cells (HTSMCs) remain unknown.	Carbon Monoxide	37-52	heme oxygenase 1	Homo sapiens	89-93
31261663-6	2019	We found that CORM-2 induced HO-1 expression via the activation of protein kinase C (PKC)alpha and proline-rich tyrosine kinase (Pyk2), which was mediated through Nox-derived ROS generation using pharmacological inhibitors or small interfering ribonucleic acids (siRNAs).	nicotine 1-N-oxide	163-166	heme oxygenase 1	Homo sapiens	29-33
31261663-6	2019	We found that CORM-2 induced HO-1 expression via the activation of protein kinase C (PKC)alpha and proline-rich tyrosine kinase (Pyk2), which was mediated through Nox-derived ROS generation using pharmacological inhibitors or small interfering ribonucleic acids (siRNAs).	Reactive Oxygen Species	175-178	heme oxygenase 1	Homo sapiens	29-33
31261663-10	2019	These results suggested that in HTSMCs, CORM-2 activates PKCalpha/Pyk2-dependent Nox/ROS/ERK1/2/AP-1, leading to HO-1 up-regulation, which suppresses the lipopolysaccharide (LPS)-induced airway inflammation.	nicotine 1-N-oxide	81-84	heme oxygenase 1	Homo sapiens	113-117
31261663-10	2019	These results suggested that in HTSMCs, CORM-2 activates PKCalpha/Pyk2-dependent Nox/ROS/ERK1/2/AP-1, leading to HO-1 up-regulation, which suppresses the lipopolysaccharide (LPS)-induced airway inflammation.	Reactive Oxygen Species	85-88	heme oxygenase 1	Homo sapiens	113-117
31056260-10	2019	Importantly, CDDP combined with LY294002, inhibitor of phosphoinositide 3-kinase (PI3K)/AKT serine/threonine kinase (AKT) signaling, markedly decreased the expression of NRF2, HO-1, NQO1 and GCLC in drug-resistant cervical cancer cells.	Cisplatin	13-17	heme oxygenase 1	Homo sapiens	176-180
31056260-10	2019	Importantly, CDDP combined with LY294002, inhibitor of phosphoinositide 3-kinase (PI3K)/AKT serine/threonine kinase (AKT) signaling, markedly decreased the expression of NRF2, HO-1, NQO1 and GCLC in drug-resistant cervical cancer cells.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	32-40	heme oxygenase 1	Homo sapiens	176-180
31029788-6	2019	Heme oxygenase-1 (HO-1) was induced by quercetin but not its conjugates, but was not implicated in the glucose uptake stimulation since hemin, a classical inducer of HO-1, did not affect glucose metabolism.	Quercetin	39-48	heme oxygenase 1	Homo sapiens	0-16
30773786-7	2019	The HO-1 inhibitor tin protoporphyrin IX prevented the anti-senescence action evoked by Ang-(1-7) or recombinant klotho.	tin protoporphyrin IX	19-40	heme oxygenase 1	Homo sapiens	4-8
30991050-8	2019	Notably, silencing of Nrf2 (siRNA transfection) significantly diminished CoQ10-mediated anti-melanogenic activity, as evidenced by impaired antioxidant HO-1 gene, uncontrolled ROS generation, and alpha-MSH production following UVA irradiation.	coenzyme Q10	73-78	heme oxygenase 1	Homo sapiens	152-156
31163581-1	2019	(1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects.	Heme	49-53	heme oxygenase 1	Homo sapiens	16-32
31163581-1	2019	(1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects.	Heme	49-53	heme oxygenase 1	Homo sapiens	34-38
31163581-1	2019	(1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	16-32
31163581-1	2019	(1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	34-38
31163581-1	2019	(1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects.	Carbon Monoxide	85-87	heme oxygenase 1	Homo sapiens	16-32
31163581-1	2019	(1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects.	Carbon Monoxide	85-87	heme oxygenase 1	Homo sapiens	34-38
31163602-13	2019	extract promotes an oxidative cellular microenvironment resulting in CaCo2 cell death by ferroptosis mediated by HO-1 hyper-expression.	caco2	69-74	heme oxygenase 1	Homo sapiens	113-117
30965051-5	2019	Here, we report that Sulforaphane is an inducer of heme oxygenase (HO)-1, a cytoprotective enzyme that catalyzes the degradation of heme through signaling pathways in human monocytes.	sulforaphane	21-33	heme oxygenase 1	Homo sapiens	51-72
30841754-4	2019	We now show that increasing total NAD+ content in astrocytes leads to the activation of the transcription factor nuclear factor, erythroid-derived 2, like 2 (Nfe2l2 or Nrf2) and up-regulation of the antioxidant proteins heme oxygenase 1 (HO-1) and sulfiredoxin 1 (SRXN1).	NAD	34-38	heme oxygenase 1	Homo sapiens	220-236
31029788-6	2019	Heme oxygenase-1 (HO-1) was induced by quercetin but not its conjugates, but was not implicated in the glucose uptake stimulation since hemin, a classical inducer of HO-1, did not affect glucose metabolism.	Quercetin	39-48	heme oxygenase 1	Homo sapiens	18-22
31261522-1	2019	Heme oxygenase-1 (HO-1) is an important catalytic enzyme in heme degradation, which increases during stressful conditions.	Heme	60-64	heme oxygenase 1	Homo sapiens	0-16
30907046-10	2019	Increased intracellular ROS resulted in nuclear factor kappa B (NF-kappaB) activation and upregulated expression of cyclooxygenase-2 (COX-2), hemeoxygenase-1 (HO-1), interleukin-1beta (IL-1beta), and intercellular adhesion molecule-1 (ICAM-1).	Reactive Oxygen Species	24-27	heme oxygenase 1	Homo sapiens	142-163
30884345-0	2019	A novel chalcone derivative, L2H17, ameliorates lipopolysaccharide-induced acute lung injury via upregulating HO-1 activity.	Chalcone	8-16	heme oxygenase 1	Homo sapiens	110-114
30884345-0	2019	A novel chalcone derivative, L2H17, ameliorates lipopolysaccharide-induced acute lung injury via upregulating HO-1 activity.	l2h17	29-34	heme oxygenase 1	Homo sapiens	110-114
30884345-13	2019	We also found that the inhibitory effect of L2H17 on the inflammatory responses was attenuated by an inhibitor of HO-1 activity, Tin protoporphyrin IX (SnPP).	l2h17	44-49	heme oxygenase 1	Homo sapiens	114-118
30884345-13	2019	We also found that the inhibitory effect of L2H17 on the inflammatory responses was attenuated by an inhibitor of HO-1 activity, Tin protoporphyrin IX (SnPP).	tin protoporphyrin IX	129-150	heme oxygenase 1	Homo sapiens	114-118
30884345-13	2019	We also found that the inhibitory effect of L2H17 on the inflammatory responses was attenuated by an inhibitor of HO-1 activity, Tin protoporphyrin IX (SnPP).	S-Nitroso-N-propionyl-D,L-penicillamine	152-156	heme oxygenase 1	Homo sapiens	114-118
30758914-10	2019	ALA treatment decreased ROS production in UPM-exposed fibroblasts via the Nrf2, HO-1, and NQO-1 pathways.	Thioctic Acid	0-3	heme oxygenase 1	Homo sapiens	80-84
30758914-10	2019	ALA treatment decreased ROS production in UPM-exposed fibroblasts via the Nrf2, HO-1, and NQO-1 pathways.	Reactive Oxygen Species	24-27	heme oxygenase 1	Homo sapiens	80-84
30629288-0	2019	Brusatol inhibits amyloid-beta-induced neurotoxicity in U-251 cells via regulating the Nrf2/HO-1 pathway.	brusatol	0-8	heme oxygenase 1	Homo sapiens	92-96
30629288-7	2019	Furthermore, BR induced the Nrf2/HO-1 pathway by inhibiting the PI3K/AKT/mTOR pathway to inhibit neurotoxicity elicited by Abeta.	brusatol	13-15	heme oxygenase 1	Homo sapiens	33-37
30817082-7	2019	Hesperidin also obviously upregulates Nrf2 antioxidant pathway and increases the protein expression of HO-1 and NQO1.	Hesperidin	0-10	heme oxygenase 1	Homo sapiens	103-107
31261522-1	2019	Heme oxygenase-1 (HO-1) is an important catalytic enzyme in heme degradation, which increases during stressful conditions.	Heme	60-64	heme oxygenase 1	Homo sapiens	18-22
31137785-0	2019	Heme Oxygenase-1 Inhibition Sensitizes Human Prostate Cancer Cells towards Glucose Deprivation and Metformin-Mediated Cell Death.	Glucose	75-82	heme oxygenase 1	Homo sapiens	0-16
31146323-5	2019	We showed that SB could significantly protect SH-SY5Y cells against 6-OHDA-induced cellular damage by inhibiting cell apoptosis and oxidative stress through PI3K/Akt, MAPK, caspase cascade modulation and Nrf2/HO-1 cascade modulation, respectively.	stellettin B	15-17	heme oxygenase 1	Homo sapiens	209-213
31137785-4	2019	The present work was directed to determine whether use of a specific inhibitor of HO-1 activity, alone or in combination with metformin, affected metastatic prostate cancer cell viability under different concentrations of glucose.	Glucose	222-229	heme oxygenase 1	Homo sapiens	82-86
31137785-7	2019	The activity of HO-1 was inhibited using a selective imidazole-based inhibitor; genes associated with antioxidant systems and cell death were evaluated by qRT-PCR.	imidazole	53-62	heme oxygenase 1	Homo sapiens	16-20
31137785-0	2019	Heme Oxygenase-1 Inhibition Sensitizes Human Prostate Cancer Cells towards Glucose Deprivation and Metformin-Mediated Cell Death.	Metformin	99-108	heme oxygenase 1	Homo sapiens	0-16
31137785-9	2019	Disrupting the antioxidant HO-1 activity, especially under low glucose concentration, could be an attractive approach to potentiate metformin antineoplastic effects and could provide a biochemical basis for developing HO-1-targeting drugs against solid tumors.	Glucose	63-70	heme oxygenase 1	Homo sapiens	27-31
31120979-2	2019	Recently, an increased number of dinucleotide repeats in the HMOX1 gene were reported to associate with development of AKI in cardiac surgery.	Dinucleoside Phosphates	33-45	heme oxygenase 1	Homo sapiens	61-66
31137785-9	2019	Disrupting the antioxidant HO-1 activity, especially under low glucose concentration, could be an attractive approach to potentiate metformin antineoplastic effects and could provide a biochemical basis for developing HO-1-targeting drugs against solid tumors.	Metformin	132-141	heme oxygenase 1	Homo sapiens	27-31
31193778-4	2019	Resveratrol at concentrations as low as 0.001 muMu increased HO-1 expression as well as membrane cofactor protein (MCP, CD46) and decay-accelerating factor (DAF, CD55) expression with no-effect on CD59.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	61-65
31120979-5	2019	We genotyped 300 patients with severe AKI (KDIGO 2 or 3) and 353 controls without AKI (KDIGO 0) for the guanine-thymine (GTn) repeat in the promoter region of the HMOX1 gene.	Guanine	104-111	heme oxygenase 1	Homo sapiens	163-168
31120979-5	2019	We genotyped 300 patients with severe AKI (KDIGO 2 or 3) and 353 controls without AKI (KDIGO 0) for the guanine-thymine (GTn) repeat in the promoter region of the HMOX1 gene.	Thymine	112-119	heme oxygenase 1	Homo sapiens	163-168
31120979-5	2019	We genotyped 300 patients with severe AKI (KDIGO 2 or 3) and 353 controls without AKI (KDIGO 0) for the guanine-thymine (GTn) repeat in the promoter region of the HMOX1 gene.	Nitroglycerin	121-124	heme oxygenase 1	Homo sapiens	163-168
30944174-6	2019	Here, using hydrogen-deuterium exchange MS, size-exclusion chromatography, and sedimentation velocity, we investigated how these divergent regions impact the dynamics and structure of the apo and heme-bound forms of HO1 and HO2.	Heme	196-200	heme oxygenase 1	Homo sapiens	216-219
31049492-0	2019	Wheat alkylresorcinols protect human retinal pigment epithelial cells against H2O2-induced oxidative damage through Akt-dependent Nrf2/HO-1 signaling.	wheat alkylresorcinols	0-22	heme oxygenase 1	Homo sapiens	135-139
31049492-0	2019	Wheat alkylresorcinols protect human retinal pigment epithelial cells against H2O2-induced oxidative damage through Akt-dependent Nrf2/HO-1 signaling.	Hydrogen Peroxide	78-82	heme oxygenase 1	Homo sapiens	135-139
31049492-3	2019	Moreover, ARs treatment increased NF-E2-related factor 2 (Nrf2) signaling activation, which was evidenced by increased transcription of anti-oxidant responsive genes GCL, NQO1 and HO-1.	Alizarin Red S	10-13	heme oxygenase 1	Homo sapiens	180-184
30944174-7	2019	Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket.	Heme	24-28	heme oxygenase 1	Homo sapiens	63-66
30944174-7	2019	Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket.	Heme	192-196	heme oxygenase 1	Homo sapiens	63-66
30898432-3	2019	Patrolling monocytes, which normally scavenge damaged cells and debris from the vasculature, express higher levels of anti-inflammatory heme oxygenase 1 (HO-1), a heme degrading enzyme with anti-cytotoxic and anti-inflammatory properties.	Heme	136-140	heme oxygenase 1	Homo sapiens	154-158
30084650-5	2019	Homocysteine (Hcy) downregulated HuR expression, reduced the binding of HuR to the 3"-UTR of HO-1, and thereafter decreased HO-1 expression.	Homocysteine	0-12	heme oxygenase 1	Homo sapiens	93-97
30084650-5	2019	Homocysteine (Hcy) downregulated HuR expression, reduced the binding of HuR to the 3"-UTR of HO-1, and thereafter decreased HO-1 expression.	Homocysteine	0-12	heme oxygenase 1	Homo sapiens	124-128
30084650-5	2019	Homocysteine (Hcy) downregulated HuR expression, reduced the binding of HuR to the 3"-UTR of HO-1, and thereafter decreased HO-1 expression.	Homocysteine	14-17	heme oxygenase 1	Homo sapiens	93-97
30084650-5	2019	Homocysteine (Hcy) downregulated HuR expression, reduced the binding of HuR to the 3"-UTR of HO-1, and thereafter decreased HO-1 expression.	Homocysteine	14-17	heme oxygenase 1	Homo sapiens	124-128
30084650-6	2019	Administration of the HO-1 inducer cobalt protoporphyrin-IX significantly hindered Hhcy-augmented reactive oxygen species production and renal fibrotic lesions.	cobaltiprotoporphyrin	35-59	heme oxygenase 1	Homo sapiens	22-26
30084650-6	2019	Administration of the HO-1 inducer cobalt protoporphyrin-IX significantly hindered Hhcy-augmented reactive oxygen species production and renal fibrotic lesions.	Oxygen	107-113	heme oxygenase 1	Homo sapiens	22-26
30576222-0	2019	Klotho protein inhibits H2O2-induced oxidative injury in endothelial cells via regulation of PI3K/AKT/Nrf2/HO-1 pathways.	Hydrogen Peroxide	24-28	heme oxygenase 1	Homo sapiens	107-111
30576222-7	2019	Klotho protein also activated phosphorylation of protein kinase B (AKT), whereas the addition of LY294002, a pharmacological inhibitor of phosphatidylinositol 3-kinase (PI3K), blocked Klotho-protein-induced Nrf2/HO-1 activation and cytoprotection.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	97-105	heme oxygenase 1	Homo sapiens	212-216
30576222-8	2019	Klotho protein enhanced the antioxidant defense ability of the cells by activating the PI3K/AKT pathway, which upregulated the expression of Nrf2/HO-1, thereby inhibiting H2O2-induced oxidative damage.	Hydrogen Peroxide	171-175	heme oxygenase 1	Homo sapiens	146-150
30653942-0	2019	Enhancing responsiveness of pancreatic cancer cells to gemcitabine treatment under hypoxia by heme oxygenase-1 inhibition.	gemcitabine	55-66	heme oxygenase 1	Homo sapiens	94-110
30653942-5	2019	Our results showed that hypoxia upregulates the expression of HO-1 in PDAC cells, and HO-1 inhibition using the HO-1 inhibitors zinc protoporphyrin, tin protoporphyrin IX (SnPP), and HO-1 knockout using CRISPR/Cas9 suppresses the proliferation of PDAC cells under hypoxia and sensitize them to gemcitabine under in vitro conditions.	zinc protoporphyrin	128-147	heme oxygenase 1	Homo sapiens	86-90
30653942-5	2019	Our results showed that hypoxia upregulates the expression of HO-1 in PDAC cells, and HO-1 inhibition using the HO-1 inhibitors zinc protoporphyrin, tin protoporphyrin IX (SnPP), and HO-1 knockout using CRISPR/Cas9 suppresses the proliferation of PDAC cells under hypoxia and sensitize them to gemcitabine under in vitro conditions.	zinc protoporphyrin	128-147	heme oxygenase 1	Homo sapiens	86-90
30653942-5	2019	Our results showed that hypoxia upregulates the expression of HO-1 in PDAC cells, and HO-1 inhibition using the HO-1 inhibitors zinc protoporphyrin, tin protoporphyrin IX (SnPP), and HO-1 knockout using CRISPR/Cas9 suppresses the proliferation of PDAC cells under hypoxia and sensitize them to gemcitabine under in vitro conditions.	zinc protoporphyrin	128-147	heme oxygenase 1	Homo sapiens	86-90
30653942-5	2019	Our results showed that hypoxia upregulates the expression of HO-1 in PDAC cells, and HO-1 inhibition using the HO-1 inhibitors zinc protoporphyrin, tin protoporphyrin IX (SnPP), and HO-1 knockout using CRISPR/Cas9 suppresses the proliferation of PDAC cells under hypoxia and sensitize them to gemcitabine under in vitro conditions.	S-Nitroso-N-propionyl-D,L-penicillamine	172-176	heme oxygenase 1	Homo sapiens	86-90
30653942-5	2019	Our results showed that hypoxia upregulates the expression of HO-1 in PDAC cells, and HO-1 inhibition using the HO-1 inhibitors zinc protoporphyrin, tin protoporphyrin IX (SnPP), and HO-1 knockout using CRISPR/Cas9 suppresses the proliferation of PDAC cells under hypoxia and sensitize them to gemcitabine under in vitro conditions.	S-Nitroso-N-propionyl-D,L-penicillamine	172-176	heme oxygenase 1	Homo sapiens	86-90
30653942-5	2019	Our results showed that hypoxia upregulates the expression of HO-1 in PDAC cells, and HO-1 inhibition using the HO-1 inhibitors zinc protoporphyrin, tin protoporphyrin IX (SnPP), and HO-1 knockout using CRISPR/Cas9 suppresses the proliferation of PDAC cells under hypoxia and sensitize them to gemcitabine under in vitro conditions.	S-Nitroso-N-propionyl-D,L-penicillamine	172-176	heme oxygenase 1	Homo sapiens	86-90
30653942-7	2019	Mechanistically, inhibition of HO-1 increased the production of reactive oxygen species as demonstrated by increased dihydroethidium, and Mitosox, disrupted glutathione cycle, and enhanced apoptosis.	Reactive Oxygen Species	64-87	heme oxygenase 1	Homo sapiens	31-35
30653942-7	2019	Mechanistically, inhibition of HO-1 increased the production of reactive oxygen species as demonstrated by increased dihydroethidium, and Mitosox, disrupted glutathione cycle, and enhanced apoptosis.	dihydroethidium	117-132	heme oxygenase 1	Homo sapiens	31-35
30653942-7	2019	Mechanistically, inhibition of HO-1 increased the production of reactive oxygen species as demonstrated by increased dihydroethidium, and Mitosox, disrupted glutathione cycle, and enhanced apoptosis.	5-(6'-triphenylphosphoniumhexyl)-5,6-dihydro-6-phenyl-3,8-phenanthridinediammine	138-145	heme oxygenase 1	Homo sapiens	31-35
30653942-7	2019	Mechanistically, inhibition of HO-1 increased the production of reactive oxygen species as demonstrated by increased dihydroethidium, and Mitosox, disrupted glutathione cycle, and enhanced apoptosis.	Glutathione	157-168	heme oxygenase 1	Homo sapiens	31-35
30653942-9	2019	In addition, inhibiting HO-1 reduced expression of stemness markers (CD133, and CD44) as compared to control or gemcitabine.	gemcitabine	112-123	heme oxygenase 1	Homo sapiens	24-28
30807827-10	2019	iHAEs showed relatively high resistance to ROS stimulation, which can be attributed to the high SOD2 expression and up-regulation of Nrf2, HO-1 after x-rays exposure.	Reactive Oxygen Species	43-46	heme oxygenase 1	Homo sapiens	139-143
30924710-7	2019	Interestingly, antioxidant enzymes, including heme oxygenase-1 (HO-1) and NAD(P)H: quinone oxidoreductase, were prominently induced by glyceollins in p53 wild-type xenografts, compared with p53 null xenografts.	glyceollin	135-146	heme oxygenase 1	Homo sapiens	46-62
30924710-8	2019	These results suggest that a high dose of glyceollins possibly promotes the growth of p53 wild-type colon cancer through activation of the Nrf2-mediated signaling pathway and, in particular, strong induction of HO-1 expression.	glyceollin	42-53	heme oxygenase 1	Homo sapiens	211-215
31052354-7	2019	The ectopic expression of HO-1 recovered YD-15 cells from TW-37-induced apoptosis by reducing intracellular levels of ROS.	Reactive Oxygen Species	118-121	heme oxygenase 1	Homo sapiens	26-30
31010200-0	2019	Marine Compound 3-bromo-4,5-dihydroxybenzaldehyde Protects Skin Cells against Oxidative Damage via the Nrf2/HO-1 Pathway.	3-bromo-4,5-dihydroxybenzaldehyde	16-49	heme oxygenase 1	Homo sapiens	108-112
31010200-1	2019	In this study, we aimed to illustrate the potential bio-effects of 3-bromo-4,5-dihydroxybenzaldehyde (3-BDB) on the antioxidant/cytoprotective enzyme heme oxygenase-1 (HO-1) in keratinocytes.	3-bromo-4,5-dihydroxybenzaldehyde	67-100	heme oxygenase 1	Homo sapiens	150-166
31010200-5	2019	Moreover, 3-BDB induced the phosphorylation of ERK and Akt, while inhibitors of ERK and Akt abrogated the 3-BDB-enhanced levels of HO-1 and Nrf2.	3-bromo-4,5-dihydroxybenzaldehyde	106-111	heme oxygenase 1	Homo sapiens	131-135
31010200-1	2019	In this study, we aimed to illustrate the potential bio-effects of 3-bromo-4,5-dihydroxybenzaldehyde (3-BDB) on the antioxidant/cytoprotective enzyme heme oxygenase-1 (HO-1) in keratinocytes.	3-bromo-4,5-dihydroxybenzaldehyde	67-100	heme oxygenase 1	Homo sapiens	168-172
31010200-8	2019	The present results indicate that 3-BDB activated Nrf2 signaling cascades in keratinocytes, which was mediated by ERK and Akt, upregulated HO-1, and induced cytoprotective effects against oxidative stress.	3-bromo-4,5-dihydroxybenzaldehyde	34-39	heme oxygenase 1	Homo sapiens	139-143
31010200-1	2019	In this study, we aimed to illustrate the potential bio-effects of 3-bromo-4,5-dihydroxybenzaldehyde (3-BDB) on the antioxidant/cytoprotective enzyme heme oxygenase-1 (HO-1) in keratinocytes.	3-bromo-4,5-dihydroxybenzaldehyde	102-107	heme oxygenase 1	Homo sapiens	150-166
31010200-1	2019	In this study, we aimed to illustrate the potential bio-effects of 3-bromo-4,5-dihydroxybenzaldehyde (3-BDB) on the antioxidant/cytoprotective enzyme heme oxygenase-1 (HO-1) in keratinocytes.	3-bromo-4,5-dihydroxybenzaldehyde	102-107	heme oxygenase 1	Homo sapiens	168-172
31010200-2	2019	The antioxidant effects of 3-BDB were examined via reverse transcription PCR, Western blotting, HO-1 activity assay, and immunocytochemistry.	3-bromo-4,5-dihydroxybenzaldehyde	27-32	heme oxygenase 1	Homo sapiens	96-100
30876940-6	2019	Hemin or ZnPP was combined to regulate heme oxygenase-1 (HO-1), and a pathway inhibitor was added to measure changes in the JNK/AP-1 signaling pathway.	Hemin	0-5	heme oxygenase 1	Homo sapiens	39-55
30851935-3	2019	The cell oxidative stress models were incubated with Hemin (an inducer of HO-1), then, the HTR8/SVneo cells were transfected by ZO-1 small interfering RNA (siRNA).	Hemin	53-58	heme oxygenase 1	Homo sapiens	74-78
30851935-6	2019	In both the trophoblastic and HUVEC oxidative stress models, HO-1 ZO-1 and occludin were increased incubated with Hemin.	Hemin	114-119	heme oxygenase 1	Homo sapiens	61-65
30995787-1	2019	Reactive oxygen species (ROS) induce nuclear factor erythroid 2-related factor 2 (Nrf2) activation as an adaptive defense mechanism, determining the synthesis of antioxidant molecules, including heme-oxygenase-1 (HO-1).	Reactive Oxygen Species	0-23	heme oxygenase 1	Homo sapiens	195-211
30995787-1	2019	Reactive oxygen species (ROS) induce nuclear factor erythroid 2-related factor 2 (Nrf2) activation as an adaptive defense mechanism, determining the synthesis of antioxidant molecules, including heme-oxygenase-1 (HO-1).	Reactive Oxygen Species	0-23	heme oxygenase 1	Homo sapiens	213-217
30995787-1	2019	Reactive oxygen species (ROS) induce nuclear factor erythroid 2-related factor 2 (Nrf2) activation as an adaptive defense mechanism, determining the synthesis of antioxidant molecules, including heme-oxygenase-1 (HO-1).	Reactive Oxygen Species	25-28	heme oxygenase 1	Homo sapiens	195-211
30995787-1	2019	Reactive oxygen species (ROS) induce nuclear factor erythroid 2-related factor 2 (Nrf2) activation as an adaptive defense mechanism, determining the synthesis of antioxidant molecules, including heme-oxygenase-1 (HO-1).	Reactive Oxygen Species	25-28	heme oxygenase 1	Homo sapiens	213-217
30995787-2	2019	HO-1 protects cells against oxidative injury, degrading free heme and inhibiting ROS production.	Heme	61-65	heme oxygenase 1	Homo sapiens	0-4
30995787-2	2019	HO-1 protects cells against oxidative injury, degrading free heme and inhibiting ROS production.	Reactive Oxygen Species	81-84	heme oxygenase 1	Homo sapiens	0-4
31013932-0	2019	Protective Effect of Phloroglucinol on Oxidative Stress-Induced DNA Damage and Apoptosis through Activation of the Nrf2/HO-1 Signaling Pathway in HaCaT Human Keratinocytes.	Phloroglucinol	21-35	heme oxygenase 1	Homo sapiens	120-124
30876940-6	2019	Hemin or ZnPP was combined to regulate heme oxygenase-1 (HO-1), and a pathway inhibitor was added to measure changes in the JNK/AP-1 signaling pathway.	Hemin	0-5	heme oxygenase 1	Homo sapiens	57-61
31013932-4	2019	The results showed that PG significantly inhibited the H2O2-induced growth inhibition in HaCaT cells, which was associated with increased expression of heme oxygenase-1 (HO-1) by the activation of nuclear factor erythroid 2-related factor-2 (Nrf2).	Phloroglucinol	24-26	heme oxygenase 1	Homo sapiens	152-168
31013932-4	2019	The results showed that PG significantly inhibited the H2O2-induced growth inhibition in HaCaT cells, which was associated with increased expression of heme oxygenase-1 (HO-1) by the activation of nuclear factor erythroid 2-related factor-2 (Nrf2).	Phloroglucinol	24-26	heme oxygenase 1	Homo sapiens	170-174
30784878-3	2019	Under these conditions, HO-1 exerts its strong cytoprotective activities and plays a crucial role in stimulating cell survival by removing the pro-oxidant heme and by producing carbon monoxide and biliverdin (promptly reduced to bilirubin).	Heme	155-159	heme oxygenase 1	Homo sapiens	24-28
31013932-4	2019	The results showed that PG significantly inhibited the H2O2-induced growth inhibition in HaCaT cells, which was associated with increased expression of heme oxygenase-1 (HO-1) by the activation of nuclear factor erythroid 2-related factor-2 (Nrf2).	Hydrogen Peroxide	55-59	heme oxygenase 1	Homo sapiens	152-168
31013932-4	2019	The results showed that PG significantly inhibited the H2O2-induced growth inhibition in HaCaT cells, which was associated with increased expression of heme oxygenase-1 (HO-1) by the activation of nuclear factor erythroid 2-related factor-2 (Nrf2).	Hydrogen Peroxide	55-59	heme oxygenase 1	Homo sapiens	170-174
31013932-8	2019	However, the inhibition of HO-1 function using zinc protoporphyrin, a HO-1 inhibitor, markedly attenuated these protective effects of PG against H2O2.	zinc protoporphyrin	47-66	heme oxygenase 1	Homo sapiens	27-31
31013932-8	2019	However, the inhibition of HO-1 function using zinc protoporphyrin, a HO-1 inhibitor, markedly attenuated these protective effects of PG against H2O2.	zinc protoporphyrin	47-66	heme oxygenase 1	Homo sapiens	70-74
31013932-8	2019	However, the inhibition of HO-1 function using zinc protoporphyrin, a HO-1 inhibitor, markedly attenuated these protective effects of PG against H2O2.	Phloroglucinol	134-136	heme oxygenase 1	Homo sapiens	27-31
31013932-8	2019	However, the inhibition of HO-1 function using zinc protoporphyrin, a HO-1 inhibitor, markedly attenuated these protective effects of PG against H2O2.	Phloroglucinol	134-136	heme oxygenase 1	Homo sapiens	70-74
31013932-8	2019	However, the inhibition of HO-1 function using zinc protoporphyrin, a HO-1 inhibitor, markedly attenuated these protective effects of PG against H2O2.	Hydrogen Peroxide	145-149	heme oxygenase 1	Homo sapiens	27-31
31013932-9	2019	Overall, our results suggest that PG is able to protect HaCaT keratinocytes against oxidative stress-induced DNA damage and apoptosis through activating the Nrf2/HO-1 signaling pathway.	Phloroglucinol	34-36	heme oxygenase 1	Homo sapiens	162-166
30965670-3	2019	Gene silencing (siRNA-mediated) was performed to examine the responses of Nrf2-target genes (i.e., heme oxygenase-1, NAD(P)H:quinone oxidoreductase1) to siRNA depletion of Nrf2 in MPP+-induced dopaminergic cell death.	mangion-purified polysaccharide (Candida albicans)	180-184	heme oxygenase 1	Homo sapiens	99-148
31089407-4	2019	It was found that HEMA stimulation promoted nuclear translocation of Nrf2 and increased Nrf2 and heme oxygenase-1 (HO-1) expression, which was further enhanced by Nrf2 activator tert-butylhydroquinone (tBHQ), but suppressed by Nrf2 inhibitor ML385.	hydroxyethyl methacrylate	18-22	heme oxygenase 1	Homo sapiens	97-113
31089407-4	2019	It was found that HEMA stimulation promoted nuclear translocation of Nrf2 and increased Nrf2 and heme oxygenase-1 (HO-1) expression, which was further enhanced by Nrf2 activator tert-butylhydroquinone (tBHQ), but suppressed by Nrf2 inhibitor ML385.	2-tert-butylhydroquinone	202-206	heme oxygenase 1	Homo sapiens	97-113
31089407-4	2019	It was found that HEMA stimulation promoted nuclear translocation of Nrf2 and increased Nrf2 and heme oxygenase-1 (HO-1) expression, which was further enhanced by Nrf2 activator tert-butylhydroquinone (tBHQ), but suppressed by Nrf2 inhibitor ML385.	ML385	242-247	heme oxygenase 1	Homo sapiens	97-113
30974805-0	2019	Ethanol-Mediated Stress Promotes Autophagic Survival and Aggressiveness of Colon Cancer Cells via Activation of Nrf2/HO-1 Pathway.	Ethanol	0-7	heme oxygenase 1	Homo sapiens	117-121
30974805-6	2019	EtOH treatment also upregulates the antioxidant enzymes SOD, catalase, and heme oxygenase (HO-1) and promotes the nuclear translocation of both Nrf2 and HO-1.	Ethanol	0-4	heme oxygenase 1	Homo sapiens	91-95
30974805-6	2019	EtOH treatment also upregulates the antioxidant enzymes SOD, catalase, and heme oxygenase (HO-1) and promotes the nuclear translocation of both Nrf2 and HO-1.	Ethanol	0-4	heme oxygenase 1	Homo sapiens	153-157
30974805-8	2019	Nrf2 silencing or preventing HO-1 nuclear translocation by the protease inhibitor E64d abrogates the EtOH-induced increase in the antioxidant enzyme levels as well as the migration markers.	aloxistatin	82-86	heme oxygenase 1	Homo sapiens	29-33
30974805-8	2019	Nrf2 silencing or preventing HO-1 nuclear translocation by the protease inhibitor E64d abrogates the EtOH-induced increase in the antioxidant enzyme levels as well as the migration markers.	Ethanol	101-105	heme oxygenase 1	Homo sapiens	29-33
30974805-9	2019	Taken together, our results suggest that EtOH mediates both the activation of Nrf2 and HO-1 to sustain colon cancer cell survival, thus leading to the acquisition of a more aggressive phenotype.	Ethanol	41-45	heme oxygenase 1	Homo sapiens	87-91
30594636-8	2019	This led to HO-1 protein downregulation in H2O2-treated human pancreatic beta-cells, which was also observed in NRF2-silenced beta-cells.	Hydrogen Peroxide	43-47	heme oxygenase 1	Homo sapiens	12-16
30784878-3	2019	Under these conditions, HO-1 exerts its strong cytoprotective activities and plays a crucial role in stimulating cell survival by removing the pro-oxidant heme and by producing carbon monoxide and biliverdin (promptly reduced to bilirubin).	Carbon Monoxide	177-192	heme oxygenase 1	Homo sapiens	24-28
30784878-3	2019	Under these conditions, HO-1 exerts its strong cytoprotective activities and plays a crucial role in stimulating cell survival by removing the pro-oxidant heme and by producing carbon monoxide and biliverdin (promptly reduced to bilirubin).	Biliverdine	197-207	heme oxygenase 1	Homo sapiens	24-28
30784878-3	2019	Under these conditions, HO-1 exerts its strong cytoprotective activities and plays a crucial role in stimulating cell survival by removing the pro-oxidant heme and by producing carbon monoxide and biliverdin (promptly reduced to bilirubin).	Bilirubin	229-238	heme oxygenase 1	Homo sapiens	24-28
30784878-5	2019	Development of non-competitive HO-1 inhibitors dates back in 2002 with the discovery of Azalanstat.	azalanstat	88-98	heme oxygenase 1	Homo sapiens	31-35
30883732-0	2019	Crystal structure of a NADPH-cytochrome P450 oxidoreductase (CYPOR) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR upon NADPH/NADP+ binding.	NADP	156-161	heme oxygenase 1	Homo sapiens	72-88
30769048-0	2019	Mangiferin alleviates arsenic induced oxidative lung injury via upregulation of the Nrf2-HO1 axis.	mangiferin	0-10	heme oxygenase 1	Homo sapiens	89-92
30769048-0	2019	Mangiferin alleviates arsenic induced oxidative lung injury via upregulation of the Nrf2-HO1 axis.	Arsenic	22-29	heme oxygenase 1	Homo sapiens	89-92
30883732-1	2019	Heme oxygenase-1 (HMOX1) catalyzes heme degradation utilizing reducing equivalents supplied from NADPH-cytochrome P450 reductase (CYPOR).	Heme	35-39	heme oxygenase 1	Homo sapiens	0-16
30883732-1	2019	Heme oxygenase-1 (HMOX1) catalyzes heme degradation utilizing reducing equivalents supplied from NADPH-cytochrome P450 reductase (CYPOR).	Heme	35-39	heme oxygenase 1	Homo sapiens	18-23
30883732-2	2019	Recently, we determined the complex structure of NADP+ -bound open-conformation stabilized CYPOR and heme-HMOX1, but the resolution was limited to 4.3 A.	NADP	49-54	heme oxygenase 1	Homo sapiens	106-111
30883732-6	2019	As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme.	Heme	71-75	heme oxygenase 1	Homo sapiens	82-87
30883732-6	2019	As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme.	NADP	93-98	heme oxygenase 1	Homo sapiens	82-87
30883732-6	2019	As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme.	Flavin Mononucleotide	32-35	heme oxygenase 1	Homo sapiens	82-87
30883732-6	2019	As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme.	Heme	163-167	heme oxygenase 1	Homo sapiens	82-87
30256411-0	2019	Heme oxygenase-1 reduces the sensitivity to imatinib through nonselective activation of histone deacetylases in chronic myeloid leukemia.	Imatinib Mesylate	44-52	heme oxygenase 1	Homo sapiens	0-16
30594624-0	2019	Nitric oxide protected against NADPH oxidase-derived superoxide generation in vascular endothelium: Critical role for heme oxygenase-1.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	118-134
30594624-2	2019	Nitric oxide (NO), previously viewed as a key regulator of cardiovascular function, is identified to induce expression of heme oxygenase-1 (HO-1), an antioxidant enzyme in blood vessels.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	122-138
30594624-2	2019	Nitric oxide (NO), previously viewed as a key regulator of cardiovascular function, is identified to induce expression of heme oxygenase-1 (HO-1), an antioxidant enzyme in blood vessels.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	140-144
30594624-4	2019	In vascular endothelial cells, NO donor (diethylenetriamine/nitric oxide adduct) significantly attenuated NADPH oxidase-derived O2- generation via a HO-1-dependent mechanism.	diethylenetriamine	41-59	heme oxygenase 1	Homo sapiens	149-153
30594624-4	2019	In vascular endothelial cells, NO donor (diethylenetriamine/nitric oxide adduct) significantly attenuated NADPH oxidase-derived O2- generation via a HO-1-dependent mechanism.	Nitric Oxide	60-72	heme oxygenase 1	Homo sapiens	149-153
30594624-4	2019	In vascular endothelial cells, NO donor (diethylenetriamine/nitric oxide adduct) significantly attenuated NADPH oxidase-derived O2- generation via a HO-1-dependent mechanism.	Superoxides	128-130	heme oxygenase 1	Homo sapiens	149-153
30594624-7	2019	In addition, NO inhibited H2O2-induced endothelial dysfunction through activation of HO-1.	Hydrogen Peroxide	26-30	heme oxygenase 1	Homo sapiens	85-89
30256411-8	2019	These findings related to the inhibitory effects of high HO-1 expression on the reactive oxygen species (ROS) signaling pathway that negatively regulated HDACs.	Reactive Oxygen Species	80-103	heme oxygenase 1	Homo sapiens	57-61
30256411-8	2019	These findings related to the inhibitory effects of high HO-1 expression on the reactive oxygen species (ROS) signaling pathway that negatively regulated HDACs.	Reactive Oxygen Species	105-108	heme oxygenase 1	Homo sapiens	57-61
30256411-9	2019	Increased expression of HO-1 activated HDACs by inhibiting ROS production.	Reactive Oxygen Species	59-62	heme oxygenase 1	Homo sapiens	24-28
31056142-8	2019	Sulforaphane induced activation and nuclear translocation of NRF2 in HUVECs, inducing heme oxygenase 1.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	86-102
30652259-0	2019	Carvacrol Depends on Heme Oxygenase-1 (HO-1) to Exert Antioxidant, Anti-inflammatory, and Mitochondria-Related Protection in the Human Neuroblastoma SH-SY5Y Cells Line Exposed to Hydrogen Peroxide.	carvacrol	0-9	heme oxygenase 1	Homo sapiens	21-37
30652259-0	2019	Carvacrol Depends on Heme Oxygenase-1 (HO-1) to Exert Antioxidant, Anti-inflammatory, and Mitochondria-Related Protection in the Human Neuroblastoma SH-SY5Y Cells Line Exposed to Hydrogen Peroxide.	carvacrol	0-9	heme oxygenase 1	Homo sapiens	39-43
30652259-0	2019	Carvacrol Depends on Heme Oxygenase-1 (HO-1) to Exert Antioxidant, Anti-inflammatory, and Mitochondria-Related Protection in the Human Neuroblastoma SH-SY5Y Cells Line Exposed to Hydrogen Peroxide.	Hydrogen Peroxide	179-196	heme oxygenase 1	Homo sapiens	39-43
30652259-10	2019	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 microM) suppressed the preventive effects caused by CAR regarding mitochondrial function and inflammation.	zinc protoporphyrin	56-78	heme oxygenase 1	Homo sapiens	22-38
30652259-10	2019	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 microM) suppressed the preventive effects caused by CAR regarding mitochondrial function and inflammation.	zinc protoporphyrin	56-78	heme oxygenase 1	Homo sapiens	40-44
30652259-10	2019	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 microM) suppressed the preventive effects caused by CAR regarding mitochondrial function and inflammation.	zinc protoporphyrin	80-87	heme oxygenase 1	Homo sapiens	22-38
30652259-10	2019	The inhibition of the heme oxygenase-1 (HO-1) enzyme by zinc protoporphyrin IX (ZnPP IX, 10 microM) suppressed the preventive effects caused by CAR regarding mitochondrial function and inflammation.	zinc protoporphyrin	80-87	heme oxygenase 1	Homo sapiens	40-44
30652259-11	2019	Thus, it is suggested that CAR caused cytoprotective effects by an HO-1-dependent manner in SH-SY5Y cells exposed to H2O2.	carvacrol	27-30	heme oxygenase 1	Homo sapiens	67-71
30652259-11	2019	Thus, it is suggested that CAR caused cytoprotective effects by an HO-1-dependent manner in SH-SY5Y cells exposed to H2O2.	Hydrogen Peroxide	117-121	heme oxygenase 1	Homo sapiens	67-71
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	Carbon Monoxide	51-66	heme oxygenase 1	Homo sapiens	20-36
30826469-4	2019	Moreover, Nrf2 translocation appeared both in GD 12.5 d and GD 18.5 d. In conclusion, DON-induced ROS accumulation may cause maternal liver damage in the initial stages, but the related stimulation of Nrf2/HO-1 pathway improves the removal of ROS and decreases the level of oxidative stress thereby protecting the liver damage.	ros	243-246	heme oxygenase 1	Homo sapiens	206-210
30826469-3	2019	DON slightly increased the levels of ALT and AST in GD12.5 d instead of GD18.5 d. Oxidative stress and anti-oxidization system were both found to be activated in the experiment which marked by ROS, MDA and GSH increasing, especially on GD12.5 d. The levels of HO-1 were significantly increased by DON exposure at different two time points.	deoxynivalenol	0-3	heme oxygenase 1	Homo sapiens	260-264
30826469-4	2019	Moreover, Nrf2 translocation appeared both in GD 12.5 d and GD 18.5 d. In conclusion, DON-induced ROS accumulation may cause maternal liver damage in the initial stages, but the related stimulation of Nrf2/HO-1 pathway improves the removal of ROS and decreases the level of oxidative stress thereby protecting the liver damage.	deoxynivalenol	86-89	heme oxygenase 1	Homo sapiens	206-210
30826469-4	2019	Moreover, Nrf2 translocation appeared both in GD 12.5 d and GD 18.5 d. In conclusion, DON-induced ROS accumulation may cause maternal liver damage in the initial stages, but the related stimulation of Nrf2/HO-1 pathway improves the removal of ROS and decreases the level of oxidative stress thereby protecting the liver damage.	ros	98-101	heme oxygenase 1	Homo sapiens	206-210
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	Carbon Monoxide	51-66	heme oxygenase 1	Homo sapiens	38-42
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	NADP	137-180	heme oxygenase 1	Homo sapiens	20-36
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	NADP	137-180	heme oxygenase 1	Homo sapiens	38-42
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	NADP	182-187	heme oxygenase 1	Homo sapiens	20-36
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	NADP	182-187	heme oxygenase 1	Homo sapiens	38-42
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	nicotine 1-N-oxide	199-202	heme oxygenase 1	Homo sapiens	20-36
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	nicotine 1-N-oxide	199-202	heme oxygenase 1	Homo sapiens	38-42
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	Reactive Oxygen Species	208-231	heme oxygenase 1	Homo sapiens	20-36
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	Reactive Oxygen Species	208-231	heme oxygenase 1	Homo sapiens	38-42
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	Reactive Oxygen Species	233-236	heme oxygenase 1	Homo sapiens	20-36
30934992-1	2019	The upregulation of heme oxygenase-1 (HO-1) by the carbon monoxide-releasing molecule (CORM)-2 may be mediated through the activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases [Nox] and reactive oxygen species (ROS) generation, which could provide cytoprotection against various cellular injuries.	Reactive Oxygen Species	233-236	heme oxygenase 1	Homo sapiens	38-42
31237164-10	2019	HMOX1 and SOD1 were downregulated after both 24-hour PAH treatments.	Polycyclic Aromatic Hydrocarbons	53-56	heme oxygenase 1	Homo sapiens	0-5
30769116-9	2019	Genetic inhibition of Nrf2 greatly decreased the protective effect of edaravone against cell apoptosis and cytotoxicity induced by Abeta25-35, accompanied by decreases in SOD and HO-1 expression.	Edaravone	70-79	heme oxygenase 1	Homo sapiens	179-183
30196486-10	2019	Treatment with 10 muM BA increased the mRNA levels of all three genes at 1-4 h in DU-145 cells and HMOX1 and GCLC in MEF WT cells.	boric acid	22-24	heme oxygenase 1	Homo sapiens	99-104
30783417-6	2019	Western blot assay showed that allicin could suppress the expression of nuclear factor erythroid 2-related factor 2 (NRF2) and heme oxygenase 1.	allicin	31-38	heme oxygenase 1	Homo sapiens	127-143
30824385-8	2019	Sulfasalazine is known to inhibit nuclear factor kappa-light-chain-enhancer of activated B cells (NFkB) and upregulate heme-oxygenase 1 (HO-1) thus we explored the effect of these transcription factors on sFlt-1 secretion from human cytotrophoblasts.	Sulfasalazine	0-13	heme oxygenase 1	Homo sapiens	119-135
30824385-8	2019	Sulfasalazine is known to inhibit nuclear factor kappa-light-chain-enhancer of activated B cells (NFkB) and upregulate heme-oxygenase 1 (HO-1) thus we explored the effect of these transcription factors on sFlt-1 secretion from human cytotrophoblasts.	Sulfasalazine	0-13	heme oxygenase 1	Homo sapiens	137-141
30881359-0	2019	Plant-Derived Polyphenols Modulate Human Dendritic Cell Metabolism and Immune Function via AMPK-Dependent Induction of Heme Oxygenase-1.	Polyphenols	14-25	heme oxygenase 1	Homo sapiens	119-135
30881359-7	2019	Previously we have reported that both carnosol and curcumin can regulate the maturation and function of human DC through upregulation of the immunomodulatory enzyme, Heme Oxygenase-1 (HO-1).	carnosol	38-46	heme oxygenase 1	Homo sapiens	166-182
30881359-7	2019	Previously we have reported that both carnosol and curcumin can regulate the maturation and function of human DC through upregulation of the immunomodulatory enzyme, Heme Oxygenase-1 (HO-1).	carnosol	38-46	heme oxygenase 1	Homo sapiens	184-188
30881359-7	2019	Previously we have reported that both carnosol and curcumin can regulate the maturation and function of human DC through upregulation of the immunomodulatory enzyme, Heme Oxygenase-1 (HO-1).	Curcumin	51-59	heme oxygenase 1	Homo sapiens	166-182
30881359-7	2019	Previously we have reported that both carnosol and curcumin can regulate the maturation and function of human DC through upregulation of the immunomodulatory enzyme, Heme Oxygenase-1 (HO-1).	Curcumin	51-59	heme oxygenase 1	Homo sapiens	184-188
30881359-8	2019	Here we also demonstrate that the induction of HO-1 by polyphenols in human DC is dependent on their activation of AMPK.	Polyphenols	55-66	heme oxygenase 1	Homo sapiens	47-51
30881359-10	2019	This study therefore describes a novel relationship between metabolic signaling via AMPK and HO-1 induction by carnosol and curcumin in human DC, and characterizes the effects of these polyphenols on DC immunometabolism for the first time.	carnosol	111-119	heme oxygenase 1	Homo sapiens	93-97
30881359-10	2019	This study therefore describes a novel relationship between metabolic signaling via AMPK and HO-1 induction by carnosol and curcumin in human DC, and characterizes the effects of these polyphenols on DC immunometabolism for the first time.	Curcumin	124-132	heme oxygenase 1	Homo sapiens	93-97
30269355-8	2019	Moreover, TQ enhanced the activation of Nrf2/heme oxygenase 1 (HO-1) signaling pathway in H2 O2 -induced ARPE cells.	thymoquinone	10-12	heme oxygenase 1	Homo sapiens	40-61
30269355-8	2019	Moreover, TQ enhanced the activation of Nrf2/heme oxygenase 1 (HO-1) signaling pathway in H2 O2 -induced ARPE cells.	thymoquinone	10-12	heme oxygenase 1	Homo sapiens	63-67
30269355-8	2019	Moreover, TQ enhanced the activation of Nrf2/heme oxygenase 1 (HO-1) signaling pathway in H2 O2 -induced ARPE cells.	Hydrogen Peroxide	90-95	heme oxygenase 1	Homo sapiens	40-61
30270549-8	2019	Furthermore, higenamine elevated the expression levels of p-Akt, heme oxygenase-1 (HO-1) and nuclear factor erythroid 2-related factor 2 (Nrf2).	higenamine	13-23	heme oxygenase 1	Homo sapiens	65-81
30269355-8	2019	Moreover, TQ enhanced the activation of Nrf2/heme oxygenase 1 (HO-1) signaling pathway in H2 O2 -induced ARPE cells.	Hydrogen Peroxide	90-95	heme oxygenase 1	Homo sapiens	63-67
30270549-8	2019	Furthermore, higenamine elevated the expression levels of p-Akt, heme oxygenase-1 (HO-1) and nuclear factor erythroid 2-related factor 2 (Nrf2).	higenamine	13-23	heme oxygenase 1	Homo sapiens	83-87
30270549-10	2019	These findings indicated that higenamine protects neuronal cells against OGD/R-induced injury by regulating the Akt and Nrf2/HO-1-signaling pathways.	higenamine	30-40	heme oxygenase 1	Homo sapiens	125-129
30269355-10	2019	These results suggested that TQ protected ARPE cells from H2 O2 -induced oxidative stress and apoptosis via the Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	58-63	heme oxygenase 1	Homo sapiens	117-121
30604480-6	2019	Furthermore, activation of nuclear factor kappaB (NF-kappaB), which was induced by IL-1beta, was also inhibited by SA through the pathway of nuclear factor-erythroid 2-related factor-2 (Nrf2)/heme oxygenase 1.	sinapinic acid	115-117	heme oxygenase 1	Homo sapiens	192-208
30419276-0	2019	Nepeta angustifolia attenuates responses to vascular inflammation in high glucose-induced human umbilical vein endothelial cells through heme oxygenase-1 induction.	Glucose	74-81	heme oxygenase 1	Homo sapiens	137-153
30709701-0	2019	Oxyresveratrol protects human lens epithelial cells against hydrogen peroxide-induced oxidative stress and apoptosis by activation of Akt/HO-1 pathway.	puag-haad	0-14	heme oxygenase 1	Homo sapiens	138-142
30747216-9	2019	Furthermore, an increase in H2S production enhanced the nuclear accumulation of Nrf2 and expression of its downstream targets, heme oxygenase-1 and superoxide dismutase, as well as HIF-1alpha.	Hydrogen Sulfide	28-31	heme oxygenase 1	Homo sapiens	127-168
30709701-0	2019	Oxyresveratrol protects human lens epithelial cells against hydrogen peroxide-induced oxidative stress and apoptosis by activation of Akt/HO-1 pathway.	Hydrogen Peroxide	60-77	heme oxygenase 1	Homo sapiens	138-142
30709701-9	2019	Oxy increased p-Akt and HO-1 expressions in H2O2-stimulated HLECs.	Hydrogen Peroxide	44-48	heme oxygenase 1	Homo sapiens	24-28
30709701-10	2019	Akt and HO-1 expressions form a regulatory axis and Oxy activated the Akt/HO-1 pathway in H2O2-stimulated HLECs.	Hydrogen Peroxide	90-94	heme oxygenase 1	Homo sapiens	8-12
30709701-10	2019	Akt and HO-1 expressions form a regulatory axis and Oxy activated the Akt/HO-1 pathway in H2O2-stimulated HLECs.	Hydrogen Peroxide	90-94	heme oxygenase 1	Homo sapiens	74-78
30709701-11	2019	Inhibition of the Akt/HO-1 pathway by LY294002 or ZnPP attenuated the effects of Oxy on oxidative stress and apoptosis in H2O2-stimulated HLECs.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	38-46	heme oxygenase 1	Homo sapiens	22-26
30709701-11	2019	Inhibition of the Akt/HO-1 pathway by LY294002 or ZnPP attenuated the effects of Oxy on oxidative stress and apoptosis in H2O2-stimulated HLECs.	zinc protoporphyrin	50-54	heme oxygenase 1	Homo sapiens	22-26
30709701-11	2019	Inhibition of the Akt/HO-1 pathway by LY294002 or ZnPP attenuated the effects of Oxy on oxidative stress and apoptosis in H2O2-stimulated HLECs.	Hydrogen Peroxide	122-126	heme oxygenase 1	Homo sapiens	22-26
30709701-12	2019	In conclusion, Oxy protected H2O2-induced oxidative stress and apoptosis through activating the Akt/HO-1 pathway, suggesting the protective effect of Oxy against H2O2-induced cataract.	Hydrogen Peroxide	29-33	heme oxygenase 1	Homo sapiens	100-104
30709701-12	2019	In conclusion, Oxy protected H2O2-induced oxidative stress and apoptosis through activating the Akt/HO-1 pathway, suggesting the protective effect of Oxy against H2O2-induced cataract.	Hydrogen Peroxide	162-166	heme oxygenase 1	Homo sapiens	100-104
30630055-10	2019	Pretreatment with deferoxamine, an inhibitor of heme synthesis, upregulated BACH1 protein levels and abolished the effect of NO-donors and S1PC on HMOX1 expression.	Deferoxamine	18-30	heme oxygenase 1	Homo sapiens	147-152
29998398-10	2019	The cells were exposed to GAS (25 muM) for 4 h prior to the challenge with PQ at 100 muM for additional 24 h. The silencing of Nrf2 by siRNA or the inhibition of HO-1 by ZnPP IX suppressed the GAS-elicited cytoprotection.	zinc protoporphyrin	170-177	heme oxygenase 1	Homo sapiens	162-166
30813369-0	2019	Anti-Inflammatory Effect of Sulforaphane on LPS-Activated Microglia Potentially through JNK/AP-1/NF-kappaB Inhibition and Nrf2/HO-1 Activation.	sulforaphane	28-40	heme oxygenase 1	Homo sapiens	127-131
30746538-6	2019	PQ-induced DNA fragmentation in lymphocytes, reduction of oxidant scavenging capacity, expression of heme oxygenase 1 and inducible nitric oxide synthase in the lung, and elevation of serum transforming growth factor beta 1 were also inhibited.	Paraquat	0-2	heme oxygenase 1	Homo sapiens	101-153
30783082-2	2019	Caffeic acid phenethyl ester (CAPE), which is a potent inducer of heme oxygenase 1 (HO1), is a central active component of propolis, and the application of propolis improves periodontal status in diabetic patients.	caffeic acid phenethyl ester	0-28	heme oxygenase 1	Homo sapiens	66-82
30783082-2	2019	Caffeic acid phenethyl ester (CAPE), which is a potent inducer of heme oxygenase 1 (HO1), is a central active component of propolis, and the application of propolis improves periodontal status in diabetic patients.	caffeic acid phenethyl ester	0-28	heme oxygenase 1	Homo sapiens	84-87
30783082-2	2019	Caffeic acid phenethyl ester (CAPE), which is a potent inducer of heme oxygenase 1 (HO1), is a central active component of propolis, and the application of propolis improves periodontal status in diabetic patients.	caffeic acid phenethyl ester	30-34	heme oxygenase 1	Homo sapiens	66-82
30783082-2	2019	Caffeic acid phenethyl ester (CAPE), which is a potent inducer of heme oxygenase 1 (HO1), is a central active component of propolis, and the application of propolis improves periodontal status in diabetic patients.	caffeic acid phenethyl ester	30-34	heme oxygenase 1	Homo sapiens	84-87
30605610-3	2019	As one of antioxidant defense systems, heme oxygenase-1 (HO-1) acts as an essential role in tumor development by offering antioxidant bilirubin to protect cancer cells under stress conditions.	Bilirubin	134-143	heme oxygenase 1	Homo sapiens	39-55
30786886-9	2019	Mechanistically, DMO-CAP treatment induced the phosphorylation of p38 mitogen-activated protein kinase (MAPK), JNK MAPK, and ERK MAPK, which led to the activation of Nrf2/heme oxygenase-1 (HO-1) pathway.	Dimethadione	17-20	heme oxygenase 1	Homo sapiens	166-187
30786886-9	2019	Mechanistically, DMO-CAP treatment induced the phosphorylation of p38 mitogen-activated protein kinase (MAPK), JNK MAPK, and ERK MAPK, which led to the activation of Nrf2/heme oxygenase-1 (HO-1) pathway.	Dimethadione	17-20	heme oxygenase 1	Homo sapiens	189-193
30759842-0	2019	Fourfold Filtered Statistical/Computational Approach for the Identification of Imidazole Compounds as HO-1 Inhibitors from Natural Products.	imidazole	79-88	heme oxygenase 1	Homo sapiens	102-106
30759842-3	2019	Imidazole scaffold is normally present in most of the classical HO-1 inhibitors and seems indispensable to the inhibitory activity due to its strong interaction with the Fe(II) of the heme group.	imidazole	0-9	heme oxygenase 1	Homo sapiens	64-68
30759842-3	2019	Imidazole scaffold is normally present in most of the classical HO-1 inhibitors and seems indispensable to the inhibitory activity due to its strong interaction with the Fe(II) of the heme group.	ammonium ferrous sulfate	170-176	heme oxygenase 1	Homo sapiens	64-68
30759842-3	2019	Imidazole scaffold is normally present in most of the classical HO-1 inhibitors and seems indispensable to the inhibitory activity due to its strong interaction with the Fe(II) of the heme group.	Heme	184-188	heme oxygenase 1	Homo sapiens	64-68
30759842-6	2019	Different imidazole-based compounds were suggested by our methodology to be potentially active in inhibiting the HO-1, and the results have been rationalized by the bioactivity of the filtered molecules reported in the literature.	imidazole	10-19	heme oxygenase 1	Homo sapiens	113-117
30685970-8	2019	The results showed that Arg promoted the protein expression of Nrf2, up-regulated expression of the phase II metabolizing enzymes (NQO1 and HO-1), as well as antioxidative enzymes (GPx1, CAT, and SOD2) for alleviating oxidative injury and protected IOECs from LPS-induced apoptosis.	Arginine	24-27	heme oxygenase 1	Homo sapiens	140-144
30605610-5	2019	To establish targeted anticancer therapy based on amplified oxidative stress, we developed molecularly engineered polymer, termed CZP, which incorporates ROS generating CA (cinnamaldehyde) and HO-1 inhibiting ZnPP (zinc protoporphyrin) in its backbone and could form stable micelles in aqueous solutions.	zinc protoporphyrin	209-213	heme oxygenase 1	Homo sapiens	193-197
30605610-6	2019	CZP micelles not only elevated oxidative stress but also suppressed the expression of antioxidant HO-1, leading to apoptotic cell death.	czp	0-3	heme oxygenase 1	Homo sapiens	98-102
30605610-3	2019	As one of antioxidant defense systems, heme oxygenase-1 (HO-1) acts as an essential role in tumor development by offering antioxidant bilirubin to protect cancer cells under stress conditions.	Bilirubin	134-143	heme oxygenase 1	Homo sapiens	57-61
30605610-5	2019	To establish targeted anticancer therapy based on amplified oxidative stress, we developed molecularly engineered polymer, termed CZP, which incorporates ROS generating CA (cinnamaldehyde) and HO-1 inhibiting ZnPP (zinc protoporphyrin) in its backbone and could form stable micelles in aqueous solutions.	czp	130-133	heme oxygenase 1	Homo sapiens	193-197
30804804-7	2019	The cytoprotective effects of HO-1 depend on several cellular mechanisms including the generation of bilirubin, an anti-oxidant molecule, from the degradation of heme; the induction of ferritin, a strong chelator of free iron; and the release of CO, that displays multiple anti-inflammatory and anti-apoptotic actions.	Bilirubin	101-110	heme oxygenase 1	Homo sapiens	30-34
30804804-7	2019	The cytoprotective effects of HO-1 depend on several cellular mechanisms including the generation of bilirubin, an anti-oxidant molecule, from the degradation of heme; the induction of ferritin, a strong chelator of free iron; and the release of CO, that displays multiple anti-inflammatory and anti-apoptotic actions.	Heme	162-166	heme oxygenase 1	Homo sapiens	30-34
30804804-7	2019	The cytoprotective effects of HO-1 depend on several cellular mechanisms including the generation of bilirubin, an anti-oxidant molecule, from the degradation of heme; the induction of ferritin, a strong chelator of free iron; and the release of CO, that displays multiple anti-inflammatory and anti-apoptotic actions.	Iron	221-225	heme oxygenase 1	Homo sapiens	30-34
30324612-1	2019	OBJECTIVES: To evaluate the cytotoxic activity of atractylodin and its potential effects on heme oxygenase (HO)-1 production, STAT1/3 phosporylation and major NF-kappaB protein expression in the cholangiocarcinoma-associated cell line CL-6.	atractylodin	50-62	heme oxygenase 1	Homo sapiens	92-113
30736789-14	2019	CONCLUSIONS: These results indicate that STL or STB may induce GSK3beta-dependent cyclin D1 degradation, and increase HO-1 expression through activating Nrf2 via ROS-dependent p38 activation, which resulted in the decrease of the viability in SW480 cells.	ros	162-165	heme oxygenase 1	Homo sapiens	118-122
30840308-10	2019	Moreover, curcumin also decreased the expression of HIF-1alpha downstream genes, VEGF, HMOX1, ROS and PDGF.	Curcumin	10-18	heme oxygenase 1	Homo sapiens	87-92
30535443-8	2019	Pretreatment with 3-morpholinosydnonimine hydrochloride, an inducer of the HO-1 expression, or overexpression of the HO-1 gene significantly delayed chondrocyte senescence.	linsidomine	18-55	heme oxygenase 1	Homo sapiens	75-79
30736789-12	2019	In addition, STL or STB increased HO-1 expression, and the inhibition of HO-1 attenuated the induction of apoptosis by STL or STB.	stb	20-23	heme oxygenase 1	Homo sapiens	34-38
30736789-13	2019	HO-1 expression by STL or STB resulted from Nrf2 activation through ROS-dependent p38 activation.	ros	68-71	heme oxygenase 1	Homo sapiens	0-4
30815229-0	2019	Correction: 4-Hydroxyestradiol induces mammary epithelial cell transformation through Nrf2-mediated heme oxygenase-1 overexpression.	4-hydroxyestradiol	12-30	heme oxygenase 1	Homo sapiens	100-116
30476559-4	2019	Only in thyrocytes, H2O2 up-regulated GPx activity and expression of HO-1 mRNA.	Hydrogen Peroxide	20-24	heme oxygenase 1	Homo sapiens	69-73
30718683-3	2019	Microarray analysis revealed that exposure of HUVECs to high MGO concentrations significantly changes gene expression, characterized by prominent down-regulation of cell cycle associated genes and up-regulation of heme oxygenase-1 (HO-1).	Pyruvaldehyde	61-64	heme oxygenase 1	Homo sapiens	214-230
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Heme	148-152	heme oxygenase 1	Homo sapiens	12-28
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Heme	148-152	heme oxygenase 1	Homo sapiens	30-34
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Carbon Monoxide	165-180	heme oxygenase 1	Homo sapiens	12-28
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Carbon Monoxide	165-180	heme oxygenase 1	Homo sapiens	30-34
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Carbon Monoxide	182-184	heme oxygenase 1	Homo sapiens	12-28
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Carbon Monoxide	182-184	heme oxygenase 1	Homo sapiens	30-34
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Iron	187-191	heme oxygenase 1	Homo sapiens	12-28
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Iron	187-191	heme oxygenase 1	Homo sapiens	30-34
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Biliverdine	197-207	heme oxygenase 1	Homo sapiens	12-28
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Biliverdine	197-207	heme oxygenase 1	Homo sapiens	30-34
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Biliverdine	209-211	heme oxygenase 1	Homo sapiens	12-28
30580021-1	2019	BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR).	Biliverdine	209-211	heme oxygenase 1	Homo sapiens	30-34
30308911-11	2019	The higher content in PAHs measured in wood and charcoal PMs was likely the reason of the enhanced expression of metabolizing and oxidative stress-related enzymes, like CYP1B1 and HO-1, and the consequent increase in apoptotic cell death.	Promethium	57-60	heme oxygenase 1	Homo sapiens	180-184
30628023-10	2019	High-glucose treatment for 24 h down-regulated the protein expression of redox-specific transcription factors Nrf-2, XBP-1 and NF-kappaB, and subsequently decreased the expression of HO-1, catalase, and SOD-2.	Glucose	5-12	heme oxygenase 1	Homo sapiens	183-197
30529626-5	2019	Importantly, cordycepin treatment down-regulated the expression levels of Nuclear factor erythroid 2-related factor (Nrf2) and a series of downstream genes, such as heme oxygenase-1 (HO-1), to enhance ROS in breast cancer cells exposed to irradiation.	Reactive Oxygen Species	201-204	heme oxygenase 1	Homo sapiens	165-181
30302660-8	2019	Since the prometastatic effects of bioactive phospholipids in vivo were mediated, at least in part, by downregulating HO-1 and iNOS expression in a p38 MAPK-dependent manner, we propose that inhibitors of p38 MAPK or stimulators of HO-1 activity will find application in inhibiting the spread of leukemic cells in response to bioactive phospholipids.	Phospholipids	45-58	heme oxygenase 1	Homo sapiens	118-122
30302660-8	2019	Since the prometastatic effects of bioactive phospholipids in vivo were mediated, at least in part, by downregulating HO-1 and iNOS expression in a p38 MAPK-dependent manner, we propose that inhibitors of p38 MAPK or stimulators of HO-1 activity will find application in inhibiting the spread of leukemic cells in response to bioactive phospholipids.	Phospholipids	45-58	heme oxygenase 1	Homo sapiens	232-236
30302660-0	2019	Bioactive Phospholipids Enhance Migration and Adhesion of Human Leukemic Cells by Inhibiting Heme Oxygenase 1 (HO-1) and Inducible Nitric Oxygenase Synthase (iNOS) in a p38 MAPK-Dependent Manner.	Phospholipids	10-23	heme oxygenase 1	Homo sapiens	93-109
30302660-0	2019	Bioactive Phospholipids Enhance Migration and Adhesion of Human Leukemic Cells by Inhibiting Heme Oxygenase 1 (HO-1) and Inducible Nitric Oxygenase Synthase (iNOS) in a p38 MAPK-Dependent Manner.	Phospholipids	10-23	heme oxygenase 1	Homo sapiens	111-115
30302660-5	2019	We also found that bioactive phospholipids enhanced cell migration and adhesion of leukemic cells by downregulating expression of HO-1 and iNOS in a p38 MAPK-dependent manner but did not affect cell proliferation.	Phospholipids	29-42	heme oxygenase 1	Homo sapiens	130-134
30529626-5	2019	Importantly, cordycepin treatment down-regulated the expression levels of Nuclear factor erythroid 2-related factor (Nrf2) and a series of downstream genes, such as heme oxygenase-1 (HO-1), to enhance ROS in breast cancer cells exposed to irradiation.	Reactive Oxygen Species	201-204	heme oxygenase 1	Homo sapiens	183-187
30529626-6	2019	Together, our observations demonstrate that cordycepin treatment sensitizes breast carcinoma cells toward irradiation via Nrf2/HO-1/ROS axis.	Reactive Oxygen Species	132-135	heme oxygenase 1	Homo sapiens	127-131
30580124-0	2019	heme oxygenase-1 agonist CoPP suppresses influenza virus replication through IRF3-mediated generation of IFN-alpha/beta.	COPP protocol	25-29	heme oxygenase 1	Homo sapiens	0-16
30580124-3	2019	In this study, we aim to confirm the antiviral effect of CoPP (Cobaltic Protoporphyrin IX Chloride), a potent HO-1 inducer on IAV infection and elucidate the possible mechanism of HO-1-mediated host innate immune responses.	COPP protocol	57-61	heme oxygenase 1	Homo sapiens	110-114
30580124-3	2019	In this study, we aim to confirm the antiviral effect of CoPP (Cobaltic Protoporphyrin IX Chloride), a potent HO-1 inducer on IAV infection and elucidate the possible mechanism of HO-1-mediated host innate immune responses.	COPP protocol	57-61	heme oxygenase 1	Homo sapiens	180-184
30580124-3	2019	In this study, we aim to confirm the antiviral effect of CoPP (Cobaltic Protoporphyrin IX Chloride), a potent HO-1 inducer on IAV infection and elucidate the possible mechanism of HO-1-mediated host innate immune responses.	COBALTIC PROTOPORPHYRIN IX CHLORIDE	63-98	heme oxygenase 1	Homo sapiens	110-114
30837406-3	2019	The Nrf2/HO-1 axis counteracts oxidative stress injury by its resistance to inflammation, oxidation, mitochondrial damage and calcium influx, apoptosis, pyroptosis, ferroptosis and autophagy, which provides a theoretical basis for its therapeutic effect on various oxidative stress-relevant diseases in multiple organs (respiratory, cardiovascular, nervous, digestive, urinary and blood systems).	Calcium	126-133	heme oxygenase 1	Homo sapiens	9-13
30696869-5	2019	Biochemical parameters were assayed and showed that the shift from normal glucose (NG; 5.5 mM) to high glucose (HG; 25 mM) promoted cell growth and induced oxidative/inflammatory stress and microglial activation, as evidenced by increased MTT reduction, elevated pro-inflammatory factor secretion (i.e., TNF-alpha and oxygen free radicals), and upregulated expression of stress/inflammatory proteins (i.e., HSP70, HO-1, iNOS, and COX-2).	Glucose	103-110	heme oxygenase 1	Homo sapiens	414-418
30805085-10	2019	The mRNA and protein expression of Nrf2, HO-1, NQO1, and glutathione-S-transferase increased in the As + GSPE group compared with that in the As group (P &lt; 0.05).	Arsenic	100-102	heme oxygenase 1	Homo sapiens	41-45
30683864-7	2019	Collectively, our data indicate that HO-1, by detoxifying heme, blocks p16INK4a expression in macrophages, preventing DNA damage and cellular senescence.	Heme	58-62	heme oxygenase 1	Homo sapiens	37-41
30678050-3	2019	Tin mesoporphyrin (SnMP) is known to inhibit heme oxygenase-1 (HO-1), which has been shown to boost the activation and proliferation of human virus-specific T cells.	tin mesoporphyrin	0-17	heme oxygenase 1	Homo sapiens	45-61
30678050-3	2019	Tin mesoporphyrin (SnMP) is known to inhibit heme oxygenase-1 (HO-1), which has been shown to boost the activation and proliferation of human virus-specific T cells.	tin mesoporphyrin	0-17	heme oxygenase 1	Homo sapiens	63-67
30678050-3	2019	Tin mesoporphyrin (SnMP) is known to inhibit heme oxygenase-1 (HO-1), which has been shown to boost the activation and proliferation of human virus-specific T cells.	tin mesoporphyrin	19-23	heme oxygenase 1	Homo sapiens	45-61
30678050-3	2019	Tin mesoporphyrin (SnMP) is known to inhibit heme oxygenase-1 (HO-1), which has been shown to boost the activation and proliferation of human virus-specific T cells.	tin mesoporphyrin	19-23	heme oxygenase 1	Homo sapiens	63-67
30678050-5	2019	HO-1 inhibition with SnMP increased WT1-specific T-cell frequencies in 13 (26%) of 50 healthy donors.	tin mesoporphyrin	21-25	heme oxygenase 1	Homo sapiens	0-4
30678050-8	2019	In conclusion, pharmacological inhibition of HO-1 activity with SnMP results in more efficient generation of functionally active WT1-specific T cells.	tin mesoporphyrin	64-68	heme oxygenase 1	Homo sapiens	45-49
31679277-0	2019	Nrf2/HO-1 Mediated Protective Activity of Genistein Against Doxorubicin-Induced Cardiac Toxicity.	Genistein	42-51	heme oxygenase 1	Homo sapiens	5-9
31468438-6	2019	Moreover, APW increased the expressions of nuclear Nrf2 and cytosolic HO-1 in H2O2-treated hepatocytes.	Hydrogen Peroxide	78-82	heme oxygenase 1	Homo sapiens	70-74
31468438-7	2019	Interestingly, the treatment of ZnPP, a HO-1 inhibitor abolished the cell viability and intracellular ROS generation induced by APW treatment.	zinc protoporphyrin	32-36	heme oxygenase 1	Homo sapiens	40-44
31468438-7	2019	Interestingly, the treatment of ZnPP, a HO-1 inhibitor abolished the cell viability and intracellular ROS generation induced by APW treatment.	Reactive Oxygen Species	102-105	heme oxygenase 1	Homo sapiens	40-44
30414976-10	2019	Overall, the work reveals that andrographolide through modulation of p53 and HNF4A, regulates miRNAs leading to upregulation of HO-1, glutathione and thioredoxin systems.	andrographolide	31-46	heme oxygenase 1	Homo sapiens	128-132
31679277-14	2019	In conclusion, the potential antioxidant effect of genistein may be because of its modulatory effect on Nrf2/HO-1 signalling pathway and by this means exhibits cardioprotective effects from Dox-induced oxidative injury.	Genistein	51-60	heme oxygenase 1	Homo sapiens	109-113
30621167-0	2019	Protective Effects and Mechanisms of N-Phenethyl Caffeamide from UVA-Induced Skin Damage in Human Epidermal Keratinocytes through Nrf2/HO-1 Regulation.	N-phenethyl caffeamide	37-59	heme oxygenase 1	Homo sapiens	135-139
30529211-9	2019	Also, we demonstrated that BCP"s protective effects against LPS-induced oligodendrocytes toxicity were mediated via the CB2 receptor through different pathways including Nrf2/HO-1/anti-oxidant axis, and PPAR-gamma, at low (0.2 and 1 microM), and high (10-50 microM) concentrations, respectively.	caryophyllene	27-30	heme oxygenase 1	Homo sapiens	175-179
31288720-4	2019	Recent studies revealed that heme oxygenase 1 (HO-1), an enzyme that participates in heme degradation, plays a critical role in the pathogenesis and may regulate autoimmunity.	Heme	29-33	heme oxygenase 1	Homo sapiens	47-51
31032752-11	2019	Treatment with celastrol enhanced the expression of transcription factor Nrf2 and its targets, GCLM and HO-1.	celastrol	15-24	heme oxygenase 1	Homo sapiens	104-108
30128961-7	2019	RESULTS: HO-1 mRNA, protein level, and HO-1 enzyme activity in renal tissue of rats with diabetic nephropathy were significantly increased after treatment with sitagliptin (P &lt; 0.05).	Sitagliptin Phosphate	160-171	heme oxygenase 1	Homo sapiens	39-43
30414976-2	2019	Our earlier studies have demonstrated the ability of andrographolide as well as andrographolide enriched extracts to activate Nrf2/HO-1 pathway through adenosine A2a receptor.	andrographolide	53-68	heme oxygenase 1	Homo sapiens	131-135
30414976-2	2019	Our earlier studies have demonstrated the ability of andrographolide as well as andrographolide enriched extracts to activate Nrf2/HO-1 pathway through adenosine A2a receptor.	andrographolide	80-95	heme oxygenase 1	Homo sapiens	131-135
30414976-7	2019	Downregulation of HNF4A by andrographolide led to decrease in miRNAs regulating Heme oxygenase-1 (miR-377) and glutathione cysteine ligase (miR-433).	andrographolide	27-42	heme oxygenase 1	Homo sapiens	80-96
30256439-4	2019	The excess ROS generation will excite expression of heme oxygenase-1 and suppress CDA expression.	Reactive Oxygen Species	11-14	heme oxygenase 1	Homo sapiens	52-68
30879014-0	2019	Vitamin D Ameliorates Angiotensin II-Induced Human Endothelial Progenitor Cell Injury via the PPAR-gamma/HO-1 Pathway.	Vitamin D	0-9	heme oxygenase 1	Homo sapiens	105-109
30879014-9	2019	These findings also suggest that vitamin D protected EPCs from AngII-induced vascular injury via the activation of the PPAR-gamma/HO-1 signaling pathway.	Vitamin D	33-42	heme oxygenase 1	Homo sapiens	130-134
31679277-0	2019	Nrf2/HO-1 Mediated Protective Activity of Genistein Against Doxorubicin-Induced Cardiac Toxicity.	Doxorubicin	60-71	heme oxygenase 1	Homo sapiens	5-9
31679277-11	2019	Genistein enhanced the Nrf2 and HO-1 expression, which showed protection against oxidative insult induced by Dox.	Genistein	0-9	heme oxygenase 1	Homo sapiens	32-36
31679277-11	2019	Genistein enhanced the Nrf2 and HO-1 expression, which showed protection against oxidative insult induced by Dox.	1-deoxysphinganine	109-112	heme oxygenase 1	Homo sapiens	32-36
30597920-5	2018	FBTA was capable of combating oxidative stress by augmenting messenger RNA (mRNA) and protein levels of both phase I and phase II detoxifying enzymes, especially heme oxygenase 1 (HO-1), by upregulating the nuclear factor erythroid 2-related factor 2 (Nrf2)-mediated pathway in HaCaT cells via the phosphorylation of p38 and extracellular signal-regulated kinase (ERK).	2-(4-((2-Fluoroethyl)amino)phenyl)benzo[d]thiazol-6-ol	0-4	heme oxygenase 1	Homo sapiens	162-178
30444987-7	2019	SIGNIFICANCE: Pretreatment of crocetin and crocetin-loaded NPs provided pronounce protective effect against cyclosporine A-mediated toxicity in HEK-293 cells by nullifying the ROS formation and restored antioxidant network through inhibition of Nrf2 translocation and followed by expression of HO-1.	crocetin	30-38	heme oxygenase 1	Homo sapiens	294-298
30444987-7	2019	SIGNIFICANCE: Pretreatment of crocetin and crocetin-loaded NPs provided pronounce protective effect against cyclosporine A-mediated toxicity in HEK-293 cells by nullifying the ROS formation and restored antioxidant network through inhibition of Nrf2 translocation and followed by expression of HO-1.	crocetin	43-51	heme oxygenase 1	Homo sapiens	294-298
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Heme	37-41	heme oxygenase 1	Homo sapiens	127-143
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Heme	37-41	heme oxygenase 1	Homo sapiens	145-149
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	127-143
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	145-149
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Iron	73-77	heme oxygenase 1	Homo sapiens	127-143
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Iron	73-77	heme oxygenase 1	Homo sapiens	145-149
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Biliverdine	82-92	heme oxygenase 1	Homo sapiens	127-143
30009872-1	2019	Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1).	Biliverdine	82-92	heme oxygenase 1	Homo sapiens	145-149
30009872-4	2019	By converting pro-oxidant heme to the antioxidants, biliverdin and bilirubin, HO-1/biliverdin reductase may help restore a more favorable tissue redox microenvironment.	Heme	26-30	heme oxygenase 1	Homo sapiens	78-82
30009872-4	2019	By converting pro-oxidant heme to the antioxidants, biliverdin and bilirubin, HO-1/biliverdin reductase may help restore a more favorable tissue redox microenvironment.	Bilirubin	67-76	heme oxygenase 1	Homo sapiens	78-82
30009872-7	2019	A comprehensive model of astroglial stress is presented wherein sustained Hmox1 induction promotes oxidative mitochondrial membrane damage, iron sequestration and mitophagy (macroautophagy).	Iron	140-144	heme oxygenase 1	Homo sapiens	74-79
30346043-0	2019	Berberine ameliorates lipopolysaccharide-induced acute lung injury via the PERK-mediated Nrf2/HO-1 signaling axis.	Berberine	0-9	heme oxygenase 1	Homo sapiens	94-98
30346043-12	2019	Therefore, berberine inhibits LPS-induced ALI through the PERK-mediated Nrf2/HO-1 signaling axis.	Berberine	11-20	heme oxygenase 1	Homo sapiens	77-81
30393147-10	2019	Furthermore, pioglitazone increased the expression of PPARgamma target genes such as renal and hepatic PPARgamma1 (Pparg1), hepatic hemoxygenase-1 (Hmox1), and hepatic thioredoxin (TRx).	Pioglitazone	13-25	heme oxygenase 1	Homo sapiens	132-146
30393147-10	2019	Furthermore, pioglitazone increased the expression of PPARgamma target genes such as renal and hepatic PPARgamma1 (Pparg1), hepatic hemoxygenase-1 (Hmox1), and hepatic thioredoxin (TRx).	Pioglitazone	13-25	heme oxygenase 1	Homo sapiens	148-153
30213580-3	2019	Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin.	Carbon Monoxide	90-105	heme oxygenase 1	Homo sapiens	0-16
30213580-3	2019	Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin.	Carbon Monoxide	90-105	heme oxygenase 1	Homo sapiens	18-22
30213580-3	2019	Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin.	Iron	112-116	heme oxygenase 1	Homo sapiens	0-16
30213580-3	2019	Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin.	Iron	112-116	heme oxygenase 1	Homo sapiens	18-22
30213580-3	2019	Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin.	Biliverdine	122-132	heme oxygenase 1	Homo sapiens	0-16
30213580-3	2019	Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin.	Biliverdine	122-132	heme oxygenase 1	Homo sapiens	18-22
30213580-5	2019	Consequently, biological actions of HO-1 are not limited to degradation of a toxic heme released from hemoproteins, but also provide an adaptive cellular response against chronic inflammation and oxidative injury.	Heme	83-87	heme oxygenase 1	Homo sapiens	36-40
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Reactive Oxygen Species	32-55	heme oxygenase 1	Homo sapiens	108-112
30583467-1	2018	Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.	Heme	45-49	heme oxygenase 1	Homo sapiens	0-21
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Reactive Oxygen Species	32-55	heme oxygenase 1	Homo sapiens	171-175
30583467-1	2018	Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.	Biliverdine	55-65	heme oxygenase 1	Homo sapiens	0-21
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Reactive Oxygen Species	57-60	heme oxygenase 1	Homo sapiens	108-112
30583467-1	2018	Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.	Bilirubin	66-75	heme oxygenase 1	Homo sapiens	0-21
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Reactive Oxygen Species	57-60	heme oxygenase 1	Homo sapiens	171-175
30583467-1	2018	Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.	Carbon Monoxide	77-92	heme oxygenase 1	Homo sapiens	0-21
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Iron	142-146	heme oxygenase 1	Homo sapiens	108-112
30583467-1	2018	Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.	Iron	106-110	heme oxygenase 1	Homo sapiens	0-21
30583467-5	2018	The critical role of HO-1 in heme metabolism makes it an important candidate to mediate protective or detrimental effects via ferroptosis induction.	Heme	29-33	heme oxygenase 1	Homo sapiens	21-25
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Iron	142-146	heme oxygenase 1	Homo sapiens	171-175
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Iron	23-27	heme oxygenase 1	Homo sapiens	108-112
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Reactive Oxygen Species	151-154	heme oxygenase 1	Homo sapiens	108-112
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Iron	23-27	heme oxygenase 1	Homo sapiens	171-175
30583467-7	2018	The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator.	Reactive Oxygen Species	151-154	heme oxygenase 1	Homo sapiens	171-175
30577437-1	2018	Heme oxygenase-1 (HO-1), a rate-limiting enzyme involved in the degradation of heme, is induced in response to a wide range of stress conditions.	Heme	79-83	heme oxygenase 1	Homo sapiens	0-16
30619356-0	2018	Heme Drives Susceptibility of Glomerular Endothelium to Complement Overactivation Due to Inefficient Upregulation of Heme Oxygenase-1.	Heme	0-4	heme oxygenase 1	Homo sapiens	117-133
30619356-8	2018	Only HUVEC (Human Umbilical Vein EC) developed adaptation to heme, which was lost after inhibition of HO-1 activity.	Heme	61-65	heme oxygenase 1	Homo sapiens	102-106
30577437-1	2018	Heme oxygenase-1 (HO-1), a rate-limiting enzyme involved in the degradation of heme, is induced in response to a wide range of stress conditions.	Heme	79-83	heme oxygenase 1	Homo sapiens	18-22
30321531-0	2018	A new chalcone derivative, 3-phenyl-1-(2,4,6-tris(methoxymethoxy)phenyl)prop-2-yn-1-one), inhibits phorbol ester-induced metastatic activity of colorectal cancer cells through upregulation of heme oxygenase-1.	Chalcone	6-14	heme oxygenase 1	Homo sapiens	192-208
30647815-8	2018	Results: We found increased levels of ROS and increased expression of ROS-producing enzymes (i.e., p47phox, xanthine oxidase) and decreased antioxidant defense mechanisms (mitochondrial aldehyde dehydrogenase, heme oxygenase-1, and eNOS) in line with elevated inflammatory markers (vascular cell adhesion molecule-1) in the right atrial myocardial tissue and by trend also in serum (sVCAM-1 and CCL5/RANTES).	Reactive Oxygen Species	38-41	heme oxygenase 1	Homo sapiens	210-226
30142309-10	2018	We used zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, to elucidate the relationship between HO-1 expression and cell death in vitro in a hemin injury model.	zinc protoporphyrin	8-27	heme oxygenase 1	Homo sapiens	56-60
30142309-10	2018	We used zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, to elucidate the relationship between HO-1 expression and cell death in vitro in a hemin injury model.	zinc protoporphyrin	8-27	heme oxygenase 1	Homo sapiens	111-115
30142309-10	2018	We used zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, to elucidate the relationship between HO-1 expression and cell death in vitro in a hemin injury model.	zinc protoporphyrin	29-33	heme oxygenase 1	Homo sapiens	56-60
30142309-10	2018	We used zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, to elucidate the relationship between HO-1 expression and cell death in vitro in a hemin injury model.	zinc protoporphyrin	29-33	heme oxygenase 1	Homo sapiens	111-115
30321531-0	2018	A new chalcone derivative, 3-phenyl-1-(2,4,6-tris(methoxymethoxy)phenyl)prop-2-yn-1-one), inhibits phorbol ester-induced metastatic activity of colorectal cancer cells through upregulation of heme oxygenase-1.	3-phenyl-1-(2,4,6-tris(methoxymethoxy)phenyl)prop-2-yn-1-one	27-87	heme oxygenase 1	Homo sapiens	192-208
30321531-0	2018	A new chalcone derivative, 3-phenyl-1-(2,4,6-tris(methoxymethoxy)phenyl)prop-2-yn-1-one), inhibits phorbol ester-induced metastatic activity of colorectal cancer cells through upregulation of heme oxygenase-1.	Phorbol Esters	99-112	heme oxygenase 1	Homo sapiens	192-208
30321531-11	2018	In conclusion, KB-34 inhibits the TPA-stimulated metastatic potential of HT-29 cells by induction of HO-1 and may be a promising anti-cancer agent in chemotherapeutic strategies for CRC.	kb-34	15-20	heme oxygenase 1	Homo sapiens	101-105
30321531-11	2018	In conclusion, KB-34 inhibits the TPA-stimulated metastatic potential of HT-29 cells by induction of HO-1 and may be a promising anti-cancer agent in chemotherapeutic strategies for CRC.	Tetradecanoylphorbol Acetate	34-37	heme oxygenase 1	Homo sapiens	101-105
30563120-10	2018	Our previous studies have documented that bisdemethoxycurcumin (BDMC) induces apoptosis by regulating heme oxygenase (HO)-1 protein expression in activated HSCs.	bisdemethoxycurcumin	42-62	heme oxygenase 1	Homo sapiens	102-123
28793787-7	2018	Constitutive NRF2 activation and subsequent deregulation of iron metabolism have been implicated in cancer development: NRF2-mediated upregulation of the iron storage protein ferritin or heme oxygenase 1 can lead to enhanced proliferation and therapy resistance.	Iron	60-64	heme oxygenase 1	Homo sapiens	187-203
30563120-10	2018	Our previous studies have documented that bisdemethoxycurcumin (BDMC) induces apoptosis by regulating heme oxygenase (HO)-1 protein expression in activated HSCs.	bisdemethoxycurcumin	64-68	heme oxygenase 1	Homo sapiens	102-123
30563120-12	2018	We observed that D2O cotreatment with BDMC significantly decreased cell proliferation compared to treatment with D2O alone, and this effect was accompanied by downregulation of HO-1 and an increase in p53 levels.	Deuterium Oxide	17-20	heme oxygenase 1	Homo sapiens	177-181
30563120-12	2018	We observed that D2O cotreatment with BDMC significantly decreased cell proliferation compared to treatment with D2O alone, and this effect was accompanied by downregulation of HO-1 and an increase in p53 levels.	bisdemethoxycurcumin	38-42	heme oxygenase 1	Homo sapiens	177-181
30159756-1	2018	Doxorubicin (Dox)-induced cardiotoxicity, a limiting factor in the use of Dox to treat cancer, can be mitigated by the mitogenic factor FGF2 in vitro, via a heme oxygenase 1 (HO-1)-dependent pathway.	Doxorubicin	0-11	heme oxygenase 1	Homo sapiens	157-173
30372823-0	2018	Brahma-related gene 1 ameliorates the neuronal apoptosis and oxidative stress induced by oxygen-glucose deprivation/reoxygenation through activation of Nrf2/HO-1 signaling.	oxygen-glucose	89-103	heme oxygenase 1	Homo sapiens	157-161
30548662-0	2018	SIRT3 inhibited the formation of calcium oxalate-induced kidney stones through regulating NRF2/HO-1 signaling pathway.	Calcium Oxalate	33-48	heme oxygenase 1	Homo sapiens	95-99
30159756-1	2018	Doxorubicin (Dox)-induced cardiotoxicity, a limiting factor in the use of Dox to treat cancer, can be mitigated by the mitogenic factor FGF2 in vitro, via a heme oxygenase 1 (HO-1)-dependent pathway.	Doxorubicin	0-11	heme oxygenase 1	Homo sapiens	175-179
30159756-1	2018	Doxorubicin (Dox)-induced cardiotoxicity, a limiting factor in the use of Dox to treat cancer, can be mitigated by the mitogenic factor FGF2 in vitro, via a heme oxygenase 1 (HO-1)-dependent pathway.	Doxorubicin	0-3	heme oxygenase 1	Homo sapiens	157-173
30159756-1	2018	Doxorubicin (Dox)-induced cardiotoxicity, a limiting factor in the use of Dox to treat cancer, can be mitigated by the mitogenic factor FGF2 in vitro, via a heme oxygenase 1 (HO-1)-dependent pathway.	Doxorubicin	0-3	heme oxygenase 1	Homo sapiens	175-179
30159756-1	2018	Doxorubicin (Dox)-induced cardiotoxicity, a limiting factor in the use of Dox to treat cancer, can be mitigated by the mitogenic factor FGF2 in vitro, via a heme oxygenase 1 (HO-1)-dependent pathway.	Doxorubicin	13-16	heme oxygenase 1	Homo sapiens	157-173
30159756-1	2018	Doxorubicin (Dox)-induced cardiotoxicity, a limiting factor in the use of Dox to treat cancer, can be mitigated by the mitogenic factor FGF2 in vitro, via a heme oxygenase 1 (HO-1)-dependent pathway.	Doxorubicin	13-16	heme oxygenase 1	Homo sapiens	175-179
30243774-6	2018	We observe that BBC results in a higher phosphorylation of PKCalpha/beta that is involved in the activation of erythroid 2-related factor 2 (Nrf2) phosphorylation to favor Nrf2 translocation to nucleus at 24 and 48 h. In addition, the results show that BBC also up-regulates both antiviral responses, heme oxygenase-1 (HO-1) expression and cellular IFN response.	Benomyl	16-19	heme oxygenase 1	Homo sapiens	301-317
30243774-6	2018	We observe that BBC results in a higher phosphorylation of PKCalpha/beta that is involved in the activation of erythroid 2-related factor 2 (Nrf2) phosphorylation to favor Nrf2 translocation to nucleus at 24 and 48 h. In addition, the results show that BBC also up-regulates both antiviral responses, heme oxygenase-1 (HO-1) expression and cellular IFN response.	Benomyl	253-256	heme oxygenase 1	Homo sapiens	301-317
30280183-5	2018	The function of protein kinase B (AKT) and heme oxygenase-1 (HO-1) activation on luteolin mediated I/R injury protection was assessed by administration of phosphoinositide-3-kinase/AKT inhibitor LY294002 and HO-1 inhibitor ZNPP.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	195-203	heme oxygenase 1	Homo sapiens	61-65
30238818-0	2018	Role of heme oxygenase-1 and its reaction product, carbon monoxide, in manifestation of breast cancer stem cell-like properties: Notch-1 as a putative target.	Carbon Monoxide	51-66	heme oxygenase 1	Homo sapiens	8-24
30238818-5	2018	Carbon monoxide (CO) is endogenously generated as a consequence of degradation of heme by HO-1.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	90-94
30238818-5	2018	Carbon monoxide (CO) is endogenously generated as a consequence of degradation of heme by HO-1.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	90-94
30272282-6	2018	Furthermore, Sch B enhanced the expression of key antioxidant enzymes, including catalase, heme oxygenase-1, glutathione peroxidase, and superoxide dismutase, and further engaged the nuclear factor-erythroid 2-related factor 2 (Nrf2) signaling pathway by modulating its phosphorylation through activating multiple upstream kinases, including protein kinase B, adenosine monophosphate-activated protein kinase and mitogen-activated protein kinases (MAPKs).	schizandrin B	13-18	heme oxygenase 1	Homo sapiens	91-107
30575934-0	2018	MicroRNA-29a enhances autophagy in podocytes as a protective mechanism against high glucose-induced apoptosis by targeting heme oxygenase-1.	Glucose	84-91	heme oxygenase 1	Homo sapiens	123-139
32186127-7	2018	EXS-induced HO-1 expression was significantly decreased in SnPP (HO-1 inhibitor)- and HO-1 siRNA-treated cells, whereas an increase was found in cobalt protoporphyrin IX (CoPP) (HO-1 inducer)-treated cells.	S-Nitroso-N-propionyl-D,L-penicillamine	59-63	heme oxygenase 1	Homo sapiens	12-16
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Heme	78-82	heme oxygenase 1	Homo sapiens	57-62
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Heme	78-82	heme oxygenase 1	Homo sapiens	96-100
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Iron	134-138	heme oxygenase 1	Homo sapiens	57-62
30272289-11	2018	The results revealed that treatment with TCSGs markedly induced Nrf2 nuclear translocation and upregulated the expression of heme oxygenase-1 (HO-1) in the L02 cells damaged by H2O2.	tcsgs	41-46	heme oxygenase 1	Homo sapiens	125-141
30272289-11	2018	The results revealed that treatment with TCSGs markedly induced Nrf2 nuclear translocation and upregulated the expression of heme oxygenase-1 (HO-1) in the L02 cells damaged by H2O2.	Hydrogen Peroxide	177-181	heme oxygenase 1	Homo sapiens	125-141
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Iron	134-138	heme oxygenase 1	Homo sapiens	78-94
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Iron	134-138	heme oxygenase 1	Homo sapiens	96-100
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Carbon Monoxide	140-155	heme oxygenase 1	Homo sapiens	57-62
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Carbon Monoxide	140-155	heme oxygenase 1	Homo sapiens	78-94
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Carbon Monoxide	140-155	heme oxygenase 1	Homo sapiens	96-100
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Biliverdine	161-171	heme oxygenase 1	Homo sapiens	57-62
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Biliverdine	161-171	heme oxygenase 1	Homo sapiens	78-94
30145824-2	2018	Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities.	Biliverdine	161-171	heme oxygenase 1	Homo sapiens	96-100
32186127-7	2018	EXS-induced HO-1 expression was significantly decreased in SnPP (HO-1 inhibitor)- and HO-1 siRNA-treated cells, whereas an increase was found in cobalt protoporphyrin IX (CoPP) (HO-1 inducer)-treated cells.	S-Nitroso-N-propionyl-D,L-penicillamine	59-63	heme oxygenase 1	Homo sapiens	65-69
30143976-0	2018	Curcumin confers hepatoprotection against AFB1-induced toxicity via activating autophagy and ameliorating inflammation involving Nrf2/HO-1 signaling pathway.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	134-138
32186127-7	2018	EXS-induced HO-1 expression was significantly decreased in SnPP (HO-1 inhibitor)- and HO-1 siRNA-treated cells, whereas an increase was found in cobalt protoporphyrin IX (CoPP) (HO-1 inducer)-treated cells.	S-Nitroso-N-propionyl-D,L-penicillamine	59-63	heme oxygenase 1	Homo sapiens	65-69
30143976-0	2018	Curcumin confers hepatoprotection against AFB1-induced toxicity via activating autophagy and ameliorating inflammation involving Nrf2/HO-1 signaling pathway.	Aflatoxin B1	42-46	heme oxygenase 1	Homo sapiens	134-138
32186127-7	2018	EXS-induced HO-1 expression was significantly decreased in SnPP (HO-1 inhibitor)- and HO-1 siRNA-treated cells, whereas an increase was found in cobalt protoporphyrin IX (CoPP) (HO-1 inducer)-treated cells.	S-Nitroso-N-propionyl-D,L-penicillamine	59-63	heme oxygenase 1	Homo sapiens	65-69
30143976-9	2018	Moreover, curcumin treatment significantly (p &lt; 0.05) elevated AFB1-induced decrease in Nrf2 and HO-1 mRNA and protein expression level.	Curcumin	10-18	heme oxygenase 1	Homo sapiens	100-104
32186127-8	2018	In addition, pretreatment with EXS increased HO-1 and Nrf-2 expression under TNF-alpha stimulation with or without N-acetyl-L-cysteine.	(2R)-2,4-dihydroxy-N-[2-(7-hydroxy-1H-benzimidazol-2-yl)ethyl]-3,3-dimethylbutanamide	31-34	heme oxygenase 1	Homo sapiens	45-49
30382449-4	2018	In addition, we revealed that PFOS exposure caused marked activation of Nrf2 pathway and the expression of Nrf2 transcription target heme oxygenase-1.	perfluorooctane sulfonic acid	30-34	heme oxygenase 1	Homo sapiens	133-149
30439604-0	2018	Celastrol antagonizes high glucose-evoked podocyte injury, inflammation and insulin resistance by restoring the HO-1-mediated autophagy pathway.	celastrol	0-9	heme oxygenase 1	Homo sapiens	112-116
30439604-11	2018	Importantly, celastrol enhanced heme oxygenase-1 (HO-1) expression in HG-stimulated podocytes.	celastrol	13-22	heme oxygenase 1	Homo sapiens	32-48
30439604-11	2018	Importantly, celastrol enhanced heme oxygenase-1 (HO-1) expression in HG-stimulated podocytes.	celastrol	13-22	heme oxygenase 1	Homo sapiens	50-54
30439604-12	2018	Notably, HO-1 cessation depressed autophagy pathway activation and subsequently blunted beneficial effects of celastrol on HG-exposed podocytes.	celastrol	110-119	heme oxygenase 1	Homo sapiens	9-13
30439604-13	2018	These finding suggest that celastrol may protect against HG-induced podocyte injury, inflammation and insulin resistance by restoring HO-1-mediated autophagy pathway, implying a promising therapeutic strategy against DN.	celastrol	27-36	heme oxygenase 1	Homo sapiens	134-138
30515391-8	2018	Our results were further confirmed by specific HO-1 gene knockdown studies which clearly demonstrated that HO-1 induction indeed played a key role in SAC mediated inhibition of apoptosis and ROS production in HepG2 cells, thus suggesting a hepatoprotective role of SAC in combating oxidative stress mediated liver diseases.	Reactive Oxygen Species	191-194	heme oxygenase 1	Homo sapiens	107-111
29782798-5	2018	Moreover, in primary pan-microglial marker (CD11b)-positive cells, the major producers of inflammatory mediators in the brain, DA and its derivatives significantly diminish inflammation and oxidative stress triggered by lipopolysaccharides and Abeta through the reduced induction of inflammatory mediators as well as upregulated expression of heme oxygenase-1, the enzyme responsible for production of antioxidants.	Dopamine	127-129	heme oxygenase 1	Homo sapiens	343-359
30248308-3	2018	In this paper, we investigated the role of HO-1 activation in NTP-induced apoptosis in A549 cells.	ntp	62-65	heme oxygenase 1	Homo sapiens	43-47
30248308-5	2018	NTP exposure induced HO-1 expression in a dose- and time-dependent manner via activating the translocation of Nuclear factor (erythroid-derived 2)-like 2 (Nrf2) from cytoplasm to nucleus.	ntp	0-3	heme oxygenase 1	Homo sapiens	21-25
30248308-6	2018	Furthermore, inhibiting HO-1 activation with its specific inhibitor, ZnPP, increased "killing" effect of NTP.	zinc protoporphyrin	69-73	heme oxygenase 1	Homo sapiens	24-28
30248308-6	2018	Furthermore, inhibiting HO-1 activation with its specific inhibitor, ZnPP, increased "killing" effect of NTP.	ntp	105-108	heme oxygenase 1	Homo sapiens	24-28
30248308-7	2018	Knocking down HO-1 or Nrf2 with the special siRNA also led to elevated ROS level and enhanced NTP-induced cell death.	Reactive Oxygen Species	71-74	heme oxygenase 1	Homo sapiens	14-18
30248308-7	2018	Knocking down HO-1 or Nrf2 with the special siRNA also led to elevated ROS level and enhanced NTP-induced cell death.	ntp	94-97	heme oxygenase 1	Homo sapiens	14-18
30248308-8	2018	In addition, the c-JUN N-terminal kinase (JNK) signaling pathway was shown to be involved in NTP-induced HO-1 expression.	ntp	93-96	heme oxygenase 1	Homo sapiens	105-109
30248308-10	2018	These findings revealed that HO-1 could be considered as a potential target to improve the effect of NTP in cancer therapy.	ntp	101-104	heme oxygenase 1	Homo sapiens	29-33
30428359-4	2018	HO-1 mitigates TB pathophysiology by diminishing myeloid cell-mediated oxidative damage caused by reactive oxygen and/or nitrogen intermediates, which control granulocytic karyorrhexis to generate a zonal HO-1 response.	Oxygen	107-113	heme oxygenase 1	Homo sapiens	0-4
30419705-8	2018	In all groups ROS levels were detected after exposed to ZnO-NPs for 4 hours, the protein expression of HO-1 was detected after exposed to ZnO-NPs for 24 hours.	Zinc Oxide	138-141	heme oxygenase 1	Homo sapiens	103-107
30419705-10	2018	HO-1 expression in ZnPPIx pretreatment group decreased compared with ZnO-NPs group (1.05+-0.05 vs. 1.12+-0.01, P&lt;0.05), meanwhile ROS level enhanced (62 683.95+-2 589.59 vs. 53 654.53+-2 229.01, P&lt;0.05).	zinc protoporphyrin	19-25	heme oxygenase 1	Homo sapiens	0-4
30419705-10	2018	HO-1 expression in ZnPPIx pretreatment group decreased compared with ZnO-NPs group (1.05+-0.05 vs. 1.12+-0.01, P&lt;0.05), meanwhile ROS level enhanced (62 683.95+-2 589.59 vs. 53 654.53+-2 229.01, P&lt;0.05).	Zinc Oxide	69-72	heme oxygenase 1	Homo sapiens	0-4
30419705-10	2018	HO-1 expression in ZnPPIx pretreatment group decreased compared with ZnO-NPs group (1.05+-0.05 vs. 1.12+-0.01, P&lt;0.05), meanwhile ROS level enhanced (62 683.95+-2 589.59 vs. 53 654.53+-2 229.01, P&lt;0.05).	Reactive Oxygen Species	133-136	heme oxygenase 1	Homo sapiens	0-4
30419705-11	2018	However, CoPPIx pretreatment had higher HO-1 level and lower level of ROS compared with ZnO-NPs group (HO-1: 1.74+-0.11 vs. 0.22+-0.03, P&lt;0.05; ROS: 32 845.04+-993.48 vs. 53 654.53+-2 229.01, P&lt;0.05).	coppix	9-15	heme oxygenase 1	Homo sapiens	40-44
30419705-11	2018	However, CoPPIx pretreatment had higher HO-1 level and lower level of ROS compared with ZnO-NPs group (HO-1: 1.74+-0.11 vs. 0.22+-0.03, P&lt;0.05; ROS: 32 845.04+-993.48 vs. 53 654.53+-2 229.01, P&lt;0.05).	coppix	9-15	heme oxygenase 1	Homo sapiens	103-107
30419705-13	2018	HO-1 regulated ZnO-NPs-induced oxidative stress.	Zinc Oxide	15-18	heme oxygenase 1	Homo sapiens	0-4
30354231-0	2018	Intravenous Heme Arginate Induces HO-1 (Heme Oxygenase-1) in the Human Heart.	heme arginate	12-25	heme oxygenase 1	Homo sapiens	34-38
30354231-0	2018	Intravenous Heme Arginate Induces HO-1 (Heme Oxygenase-1) in the Human Heart.	heme arginate	12-25	heme oxygenase 1	Homo sapiens	40-56
30354231-3	2018	The current trial was designed to assess the pharmacological tissue induction of HO-1 in the human heart with heme arginate in vivo.	heme arginate	110-123	heme oxygenase 1	Homo sapiens	81-85
30354231-11	2018	Surgery and heme arginate infusion significantly increased HO-1 mRNA concentration in peripheral blood mononuclear cells ( P&lt;0.001).	Heme	12-16	heme oxygenase 1	Homo sapiens	59-63
30354231-11	2018	Surgery and heme arginate infusion significantly increased HO-1 mRNA concentration in peripheral blood mononuclear cells ( P&lt;0.001).	L-argininate	17-25	heme oxygenase 1	Homo sapiens	59-63
30354231-14	2018	Conclusions- Myocardial HO-1 mRNA and protein can be dose-dependently induced by heme arginate.	heme arginate	81-94	heme oxygenase 1	Homo sapiens	24-28
30515391-0	2018	S-Allyl Cysteine Alleviates Hydrogen Peroxide Induced Oxidative Injury and Apoptosis through Upregulation of Akt/Nrf-2/HO-1 Signaling Pathway in HepG2 Cells.	S-allylcysteine	0-16	heme oxygenase 1	Homo sapiens	119-123
30268863-13	2018	p38MAPK, JNK and HO-1 were activated after PDT treatment and the activation were reversed by adding ROS scavenger NAC.	Reactive Oxygen Species	100-103	heme oxygenase 1	Homo sapiens	17-21
30428359-4	2018	HO-1 mitigates TB pathophysiology by diminishing myeloid cell-mediated oxidative damage caused by reactive oxygen and/or nitrogen intermediates, which control granulocytic karyorrhexis to generate a zonal HO-1 response.	Nitrogen	121-129	heme oxygenase 1	Homo sapiens	0-4
30419705-0	2018	[The role of heme oxygenase-1 on oxidative stress injury induced by zinc oxide nanoparticles in human umbilical vein endothelial cells line EA.hy926 cells].	Zinc Oxide	68-78	heme oxygenase 1	Homo sapiens	13-29
30419705-1	2018	Objective: To explore the effect of heme oxygenase-1 (HO-1) on level of reactive oxygen species (ROS) induced by zinc oxide nanoparticles (ZnO-NPs) in Human umbilical vein endothelial cells line EA.hy926.	Reactive Oxygen Species	72-95	heme oxygenase 1	Homo sapiens	36-52
30419705-1	2018	Objective: To explore the effect of heme oxygenase-1 (HO-1) on level of reactive oxygen species (ROS) induced by zinc oxide nanoparticles (ZnO-NPs) in Human umbilical vein endothelial cells line EA.hy926.	Reactive Oxygen Species	72-95	heme oxygenase 1	Homo sapiens	54-58
30419705-1	2018	Objective: To explore the effect of heme oxygenase-1 (HO-1) on level of reactive oxygen species (ROS) induced by zinc oxide nanoparticles (ZnO-NPs) in Human umbilical vein endothelial cells line EA.hy926.	Reactive Oxygen Species	97-100	heme oxygenase 1	Homo sapiens	36-52
30419705-1	2018	Objective: To explore the effect of heme oxygenase-1 (HO-1) on level of reactive oxygen species (ROS) induced by zinc oxide nanoparticles (ZnO-NPs) in Human umbilical vein endothelial cells line EA.hy926.	Reactive Oxygen Species	97-100	heme oxygenase 1	Homo sapiens	54-58
30419705-1	2018	Objective: To explore the effect of heme oxygenase-1 (HO-1) on level of reactive oxygen species (ROS) induced by zinc oxide nanoparticles (ZnO-NPs) in Human umbilical vein endothelial cells line EA.hy926.	Zinc Oxide	113-123	heme oxygenase 1	Homo sapiens	36-52
30419705-1	2018	Objective: To explore the effect of heme oxygenase-1 (HO-1) on level of reactive oxygen species (ROS) induced by zinc oxide nanoparticles (ZnO-NPs) in Human umbilical vein endothelial cells line EA.hy926.	Zinc Oxide	113-123	heme oxygenase 1	Homo sapiens	54-58
30419705-3	2018	The ROS level, reflected by mean fluorescence intensity (MFI), was examined by flow cytometer after 4 hours exposure, the protein expression of HO-1 which was determined by Western Blot after exposed to ZnO-NPs for 24 hours.	Zinc Oxide	203-206	heme oxygenase 1	Homo sapiens	144-148
30419705-6	2018	15 mg/L ZnO-NPs was chosen to conduct the experiment of HO-1 activation and inhibition.	Zinc Oxide	8-11	heme oxygenase 1	Homo sapiens	56-60
30419705-8	2018	In all groups ROS levels were detected after exposed to ZnO-NPs for 4 hours, the protein expression of HO-1 was detected after exposed to ZnO-NPs for 24 hours.	Zinc Oxide	56-59	heme oxygenase 1	Homo sapiens	103-107
30257325-7	2018	Furthermore, eriodictyol pretreatment inhibited IkappaBalpha degradation and the level of p-p65, and enhanced the up-regulation of nuclear factor (erythroid-derived 2)-like 2 (Nrf2) and heme oxygenase 1 (HO-1) in IL-1beta-stimulated chondrocytes.	eriodictyol	13-24	heme oxygenase 1	Homo sapiens	186-202
30257325-7	2018	Furthermore, eriodictyol pretreatment inhibited IkappaBalpha degradation and the level of p-p65, and enhanced the up-regulation of nuclear factor (erythroid-derived 2)-like 2 (Nrf2) and heme oxygenase 1 (HO-1) in IL-1beta-stimulated chondrocytes.	eriodictyol	13-24	heme oxygenase 1	Homo sapiens	204-208
30216645-0	2018	Heme oxygenase-1 induction mediates chemoresistance of breast cancer cells to pharmorubicin by promoting autophagy via PI3K/Akt pathway.	Epirubicin	78-91	heme oxygenase 1	Homo sapiens	0-16
30216645-8	2018	RESULTS: After being treated with pharmorubicin, the expression of HO-1 and autophagy related proteins was significantly enhanced, but the cell survival ratio in the two cell lines decreased.	Epirubicin	34-47	heme oxygenase 1	Homo sapiens	67-71
30216645-10	2018	When pharmorubicin-resistant cells were transfected with si-HO-1, the cell survival decreased and the protein expression of HO-1, autophagic proteins (LC3-II/LC3-I and Beclin-1) as well as autophagy were all down-regulated, while in pharmorubicin-resistant cells transfected with pcDNA3.1-HO-1, the results were reverse.	Epirubicin	5-18	heme oxygenase 1	Homo sapiens	60-64
30216645-10	2018	When pharmorubicin-resistant cells were transfected with si-HO-1, the cell survival decreased and the protein expression of HO-1, autophagic proteins (LC3-II/LC3-I and Beclin-1) as well as autophagy were all down-regulated, while in pharmorubicin-resistant cells transfected with pcDNA3.1-HO-1, the results were reverse.	Epirubicin	5-18	heme oxygenase 1	Homo sapiens	124-128
30216645-10	2018	When pharmorubicin-resistant cells were transfected with si-HO-1, the cell survival decreased and the protein expression of HO-1, autophagic proteins (LC3-II/LC3-I and Beclin-1) as well as autophagy were all down-regulated, while in pharmorubicin-resistant cells transfected with pcDNA3.1-HO-1, the results were reverse.	Epirubicin	5-18	heme oxygenase 1	Homo sapiens	124-128
30216645-10	2018	When pharmorubicin-resistant cells were transfected with si-HO-1, the cell survival decreased and the protein expression of HO-1, autophagic proteins (LC3-II/LC3-I and Beclin-1) as well as autophagy were all down-regulated, while in pharmorubicin-resistant cells transfected with pcDNA3.1-HO-1, the results were reverse.	Epirubicin	233-246	heme oxygenase 1	Homo sapiens	60-64
30216645-12	2018	CONCLUSION: It was proved that HO-1 induction mediated chemoresistance of pharmorubicin in breast cancer cells by promoting autophagy via PI3K/Akt pathway.	Epirubicin	74-87	heme oxygenase 1	Homo sapiens	31-35
29707997-10	2018	Linear regression analysis demonstrated that HO-1 was the independent predictor of AKI demonstrated by elevated creatinine among GI and GII.	Creatinine	112-122	heme oxygenase 1	Homo sapiens	45-49
29707997-12	2018	HO-1 is a promising target for prevention and/or treatment of cisplatin-induced nephrotoxicity.	Cisplatin	62-71	heme oxygenase 1	Homo sapiens	0-4
30397576-2	2018	Here, we tested the ability of different isoxazoline-based electrophiles to up-regulate Nrf2/HO-1.	Isoxazoline	41-52	heme oxygenase 1	Homo sapiens	93-97
30367621-0	2018	Sorafenib and docosahexaenoic acid act in synergy to suppress cancer cell viability: a role of heme oxygenase 1.	Sorafenib	0-9	heme oxygenase 1	Homo sapiens	95-111
30367621-0	2018	Sorafenib and docosahexaenoic acid act in synergy to suppress cancer cell viability: a role of heme oxygenase 1.	Docosahexaenoic Acids	14-34	heme oxygenase 1	Homo sapiens	95-111
30367621-3	2018	We recently reported that DHA induces HO-1 gene transcription in human cancer cells by augmenting the degradation of Bach1 protein, which functions as a negative regulator of HO-1.	Docosahexaenoic Acids	26-29	heme oxygenase 1	Homo sapiens	38-42
30367621-3	2018	We recently reported that DHA induces HO-1 gene transcription in human cancer cells by augmenting the degradation of Bach1 protein, which functions as a negative regulator of HO-1.	Docosahexaenoic Acids	26-29	heme oxygenase 1	Homo sapiens	175-179
30206627-7	2018	Moreover, the combination treatments reduced reactive oxygen species in cells and increased the expression of Nrf2 and HO-1, which are cellular antioxidant proteins.	Reactive Oxygen Species	45-68	heme oxygenase 1	Homo sapiens	119-123
30367621-4	2018	Since the degradation of Bach1 protein relies on protein phosphorylation, we hypothesized that DHA-induced HO-1 gene transcription could be attenuated by kinase inhibitors, resulting in an enhanced cytotoxicity.	Docosahexaenoic Acids	95-98	heme oxygenase 1	Homo sapiens	107-111
30367621-11	2018	Consequently, DHA-induced HO-1 gene transcription was reversed by Sorafenib as evidenced by western blot and reporter gene analysis.	Docosahexaenoic Acids	14-17	heme oxygenase 1	Homo sapiens	26-30
30367621-11	2018	Consequently, DHA-induced HO-1 gene transcription was reversed by Sorafenib as evidenced by western blot and reporter gene analysis.	Sorafenib	66-75	heme oxygenase 1	Homo sapiens	26-30
30367621-14	2018	CONCLUSIONS: We demonstrate that sorafenib attenuates DHA-induced HO-1 expression and acts in synergy with DHA to suppress cancer cell viability and tumor growth.	Sorafenib	33-42	heme oxygenase 1	Homo sapiens	66-70
30367621-14	2018	CONCLUSIONS: We demonstrate that sorafenib attenuates DHA-induced HO-1 expression and acts in synergy with DHA to suppress cancer cell viability and tumor growth.	Docosahexaenoic Acids	54-57	heme oxygenase 1	Homo sapiens	66-70
30416532-5	2018	Additionally, exposure of bone marrow stromal cells (HS-5) to NAC increased adiponectin, PPARgamma, HO-1, and SIRT-1 and increased beta-oxidation markers such as PPARalpha and PPARdelta mRNA levels.	Acetylcysteine	62-65	heme oxygenase 1	Homo sapiens	100-104
30397576-3	2018	The potency of activation is dependent on the leaving group at the 3-position of the isoxazoline nucleus, and an additional ring on the molecule limits the Nrf2/HO-1 activating properties.	Isoxazoline	85-96	heme oxygenase 1	Homo sapiens	161-165
30144404-7	2018	Glutamine deprivation or GLS1 inhibition also stimulated the production of reactive oxygen species and this was associated with a marked decline in heme oxygenase-1 (HO-1) expression.	Glutamine	0-9	heme oxygenase 1	Homo sapiens	148-164
30105448-13	2018	The induction of HO-1 might have be a promising approach for the treatment of psoriasis through antioxidant ability, immunomodulatory role as well as its role in heme synthesis.	Heme	162-166	heme oxygenase 1	Homo sapiens	17-21
30261468-0	2018	Targeting heme Oxygenase-1 with hybrid compounds to overcome Imatinib resistance in chronic myeloid leukemia cell lines.	Imatinib Mesylate	61-69	heme oxygenase 1	Homo sapiens	10-26
30261468-4	2018	With this in mind, in this study, we designed and synthesized the first series of hybrid compounds obtained by combining the structures of IM, as BCR-ABL inhibitor, with imidazole-based HO-1 inhibitors.	imidazole	170-179	heme oxygenase 1	Homo sapiens	186-190
30349652-2	2018	The cytoprotective enzyme heme oxygenase-1 (HO-1) has been shown to mediate anti-proliferative and anti-migratory effects in VSMC.	vsmc	125-129	heme oxygenase 1	Homo sapiens	26-42
30349652-2	2018	The cytoprotective enzyme heme oxygenase-1 (HO-1) has been shown to mediate anti-proliferative and anti-migratory effects in VSMC.	vsmc	125-129	heme oxygenase 1	Homo sapiens	44-48
30349652-3	2018	This study investigates the effect of cannabidiol (CBD), a non-psychoactive cannabinoid, on HO-1 expression and disease-associated functions of human umbilical artery smooth muscle cells (HUASMC).	Cannabidiol	38-49	heme oxygenase 1	Homo sapiens	92-96
30349652-3	2018	This study investigates the effect of cannabidiol (CBD), a non-psychoactive cannabinoid, on HO-1 expression and disease-associated functions of human umbilical artery smooth muscle cells (HUASMC).	Cannabidiol	51-54	heme oxygenase 1	Homo sapiens	92-96
30349652-6	2018	Instead, the CBD-mediated increase in HO-1 protein was reversed by the glutathione precursor N-acetylcysteine, indicating the participation of reactive oxygen species (ROS) signaling; this was confirmed by flow cytometry-based ROS detection.	Glutathione	71-82	heme oxygenase 1	Homo sapiens	38-42
30349652-6	2018	Instead, the CBD-mediated increase in HO-1 protein was reversed by the glutathione precursor N-acetylcysteine, indicating the participation of reactive oxygen species (ROS) signaling; this was confirmed by flow cytometry-based ROS detection.	Acetylcysteine	93-109	heme oxygenase 1	Homo sapiens	38-42
30349652-6	2018	Instead, the CBD-mediated increase in HO-1 protein was reversed by the glutathione precursor N-acetylcysteine, indicating the participation of reactive oxygen species (ROS) signaling; this was confirmed by flow cytometry-based ROS detection.	Reactive Oxygen Species	143-166	heme oxygenase 1	Homo sapiens	38-42
30349652-6	2018	Instead, the CBD-mediated increase in HO-1 protein was reversed by the glutathione precursor N-acetylcysteine, indicating the participation of reactive oxygen species (ROS) signaling; this was confirmed by flow cytometry-based ROS detection.	Reactive Oxygen Species	168-171	heme oxygenase 1	Homo sapiens	38-42
30349652-6	2018	Instead, the CBD-mediated increase in HO-1 protein was reversed by the glutathione precursor N-acetylcysteine, indicating the participation of reactive oxygen species (ROS) signaling; this was confirmed by flow cytometry-based ROS detection.	Reactive Oxygen Species	227-230	heme oxygenase 1	Homo sapiens	38-42
30349652-10	2018	Collectively, this work provides the first indication of CBD-mediated enhancement of HO-1 in VSMC and potential protective effects against aberrant VSMC proliferation and migration.	Cannabidiol	57-60	heme oxygenase 1	Homo sapiens	85-89
30144404-7	2018	Glutamine deprivation or GLS1 inhibition also stimulated the production of reactive oxygen species and this was associated with a marked decline in heme oxygenase-1 (HO-1) expression.	Glutamine	0-9	heme oxygenase 1	Homo sapiens	166-170
30144404-8	2018	GLS1 inhibition also sensitized ECs to the cytotoxic effect of hydrogen peroxide and this was prevented by the overexpression of HO-1.	Hydrogen Peroxide	63-80	heme oxygenase 1	Homo sapiens	129-133
30088830-1	2018	BACKGROUND AND PURPOSE: Haem oxygenase-1 (HO-1) is induced by thiazolidinediones including rosiglitazone and exerts anti-inflammatory effects in various models.	Thiazolidinediones	62-80	heme oxygenase 1	Homo sapiens	24-40
30088830-0	2018	Haem oxygenase-1 up-regulation by rosiglitazone via ROS-dependent Nrf2-antioxidant response elements axis or PPARgamma attenuates LPS-mediated lung inflammation.	Rosiglitazone	34-47	heme oxygenase 1	Homo sapiens	0-16
30088830-1	2018	BACKGROUND AND PURPOSE: Haem oxygenase-1 (HO-1) is induced by thiazolidinediones including rosiglitazone and exerts anti-inflammatory effects in various models.	Thiazolidinediones	62-80	heme oxygenase 1	Homo sapiens	42-46
30088830-0	2018	Haem oxygenase-1 up-regulation by rosiglitazone via ROS-dependent Nrf2-antioxidant response elements axis or PPARgamma attenuates LPS-mediated lung inflammation.	Rosiglitazone	52-55	heme oxygenase 1	Homo sapiens	0-16
30088830-1	2018	BACKGROUND AND PURPOSE: Haem oxygenase-1 (HO-1) is induced by thiazolidinediones including rosiglitazone and exerts anti-inflammatory effects in various models.	Rosiglitazone	91-104	heme oxygenase 1	Homo sapiens	24-40
30088830-1	2018	BACKGROUND AND PURPOSE: Haem oxygenase-1 (HO-1) is induced by thiazolidinediones including rosiglitazone and exerts anti-inflammatory effects in various models.	Rosiglitazone	91-104	heme oxygenase 1	Homo sapiens	42-46
30088830-2	2018	However, the molecular mechanisms underlying rosiglitazone-induced HO-1 expression remain largely unknown in human pulmonary alveolar epithelial cells (HPAEpiCs).	Rosiglitazone	45-58	heme oxygenase 1	Homo sapiens	67-71
30085341-0	2018	Cyclooxygenase-2-mediated upregulation of heme oxygenase 1 mitigates the toxicity of deuterium-tritium fusion radiation.	deuterium-tritium	85-102	heme oxygenase 1	Homo sapiens	42-58
29748730-9	2018	The expression of Nrf2 and HO-1 was up-regulated by the treatment of corynoline.	corynoline	69-79	heme oxygenase 1	Homo sapiens	27-31
30085341-6	2018	Pretreatment with the HO-1 inhibitor, protoporphyrin IX zinc (II), exacerbated double strand break formation following exposure to fusion radiation.	protoporphyrin IX	38-55	heme oxygenase 1	Homo sapiens	22-26
30085341-7	2018	The expression of cyclooxygenase-2 (COX-2) contributed to the upregulation of HO-1, as demonstrated by the result that its inhibitor, NS-398, inhibited the induction of HO-1 in irradiated cells.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	134-140	heme oxygenase 1	Homo sapiens	78-82
30085341-7	2018	The expression of cyclooxygenase-2 (COX-2) contributed to the upregulation of HO-1, as demonstrated by the result that its inhibitor, NS-398, inhibited the induction of HO-1 in irradiated cells.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	134-140	heme oxygenase 1	Homo sapiens	169-173
29959986-6	2018	Long-term iron exposure resulted in iron accumulation, cytosolic ROS formation and increased heme oxygenase 1 (HMOX-1) mRNA expression (all p &lt; 0.001).	Iron	10-14	heme oxygenase 1	Homo sapiens	93-109
29797346-0	2018	Hemin provides protection against lead neurotoxicity through heme oxygenase 1/carbon monoxide activation.	Hemin	0-5	heme oxygenase 1	Homo sapiens	61-77
29797346-3	2018	In this study, we applied hemin, the substrate and a well-known inducer of HO-1, to investigate the possible role of HO-1 in protecting against Pb neurotoxicity.	Hemin	26-31	heme oxygenase 1	Homo sapiens	75-79
29797346-3	2018	In this study, we applied hemin, the substrate and a well-known inducer of HO-1, to investigate the possible role of HO-1 in protecting against Pb neurotoxicity.	Lead	144-146	heme oxygenase 1	Homo sapiens	117-121
29797346-6	2018	However, knocking down HO-1 could significantly abolish the cytoprotective action of hemin against Pb toxicity, confirming HO-1 contributed to the protection.	Hemin	85-90	heme oxygenase 1	Homo sapiens	23-27
29797346-6	2018	However, knocking down HO-1 could significantly abolish the cytoprotective action of hemin against Pb toxicity, confirming HO-1 contributed to the protection.	Hemin	85-90	heme oxygenase 1	Homo sapiens	123-127
29797346-6	2018	However, knocking down HO-1 could significantly abolish the cytoprotective action of hemin against Pb toxicity, confirming HO-1 contributed to the protection.	Lead	99-101	heme oxygenase 1	Homo sapiens	23-27
29797346-7	2018	Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells.	Carbon Monoxide	40-55	heme oxygenase 1	Homo sapiens	13-17
29797346-7	2018	Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells.	Carbon Monoxide	40-55	heme oxygenase 1	Homo sapiens	123-127
29797346-7	2018	Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells.	Hemin	150-155	heme oxygenase 1	Homo sapiens	13-17
29797346-7	2018	Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells.	Hemin	150-155	heme oxygenase 1	Homo sapiens	123-127
29797346-7	2018	Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells.	Lead	174-176	heme oxygenase 1	Homo sapiens	13-17
29797346-7	2018	Finally, the HO-1-derived production of carbon monoxide, but not of bilirubin or Fe2+ , mediated the protective effects of HO-1 activation induced by hemin treatment against Pb-induced cell death and oxidative stress in SHSY5Y cells.	Lead	174-176	heme oxygenase 1	Homo sapiens	123-127
29797346-8	2018	Overall, this study showed that hemin provided protection against Pb neurotoxicity by HO-1/carbon monoxide activation.	Hemin	32-37	heme oxygenase 1	Homo sapiens	86-90
29797346-8	2018	Overall, this study showed that hemin provided protection against Pb neurotoxicity by HO-1/carbon monoxide activation.	Lead	66-68	heme oxygenase 1	Homo sapiens	86-90
30216854-7	2018	We found that RS9 protected ARPE-19 cells against NaIO3-induced oxidative damage, and that the protective effects of RS9 were inhibited by co-treatment with zinc protoporphyrin, an HO-1 inhibitor.	zinc protoporphyrin	157-176	heme oxygenase 1	Homo sapiens	181-185
29882686-10	2018	ZnO and CuO nanoparticles displayed severe cytotoxicity and enhanced gene expression of heme oxygenase-1 (HO-1) and interleukin-8 (IL-8).	Zinc Oxide	0-3	heme oxygenase 1	Homo sapiens	88-104
29882686-10	2018	ZnO and CuO nanoparticles displayed severe cytotoxicity and enhanced gene expression of heme oxygenase-1 (HO-1) and interleukin-8 (IL-8).	Zinc Oxide	0-3	heme oxygenase 1	Homo sapiens	106-110
29882686-14	2018	The enhancement of HO-1, IL-8, and MT2A gene expressions was related to the cytotoxic activity of metal oxide nanoparticles.	metal oxide	98-109	heme oxygenase 1	Homo sapiens	19-23
30040983-0	2018	Heme Oxygenase-1 protects astroglia against manganese-induced oxidative injury by regulating mitochondrial quality control.	Manganese	44-53	heme oxygenase 1	Homo sapiens	0-16
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Heme	69-73	heme oxygenase 1	Homo sapiens	0-16
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Heme	69-73	heme oxygenase 1	Homo sapiens	18-22
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Iron	91-95	heme oxygenase 1	Homo sapiens	0-16
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Iron	91-95	heme oxygenase 1	Homo sapiens	18-22
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Carbon Monoxide	97-112	heme oxygenase 1	Homo sapiens	0-16
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Carbon Monoxide	97-112	heme oxygenase 1	Homo sapiens	18-22
30214615-7	2018	The present study demonstrated a positive correlation between 8-OHdG and HO-1 levels (P=0.012).	8-ohdg	62-68	heme oxygenase 1	Homo sapiens	73-77
29530745-1	2018	OBJECTIVE: The aim of this study was to investigate how maternal cell-free fetal hemoglobin and heme impact the scavenger enzyme systems Hemopexin and Heme Oxygenase-1 in patients with preeclampsia (PE).	Heme	96-100	heme oxygenase 1	Homo sapiens	151-167
29530745-10	2018	CONCLUSIONS: Increased maternal plasma levels of heme and HbF in PE are associated with decreased HO-1 and hemopexin protein levels as well as reduced hemopexin activity.	Heme	49-53	heme oxygenase 1	Homo sapiens	98-102
30031050-7	2018	In Drp1 knock out cells, HO-1 levels were low compared to wild type cells, both in untreated controls as well as after BH3I-1 exposure, demonstrating that Drp1 is at least in part required for determining basal and inducible HO-1 levels.	BH3I-1	119-125	heme oxygenase 1	Homo sapiens	25-29
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Biliverdine	118-128	heme oxygenase 1	Homo sapiens	0-16
29959986-6	2018	Long-term iron exposure resulted in iron accumulation, cytosolic ROS formation and increased heme oxygenase 1 (HMOX-1) mRNA expression (all p &lt; 0.001).	Iron	10-14	heme oxygenase 1	Homo sapiens	111-117
30040983-1	2018	Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways.	Biliverdine	118-128	heme oxygenase 1	Homo sapiens	18-22
30327711-12	2018	Treatment of cultured human artery endothelial cells with curcumin induced the HO-1 expression through the activation of nuclear factor-E2-related factor 2 (Nrf2) and an antioxidant responsive element via the p38 MAPK signalling pathway.	Curcumin	58-66	heme oxygenase 1	Homo sapiens	79-83
30040983-4	2018	HO-1 exerted a protective effect against Mn2+ injury.	Manganese(2+)	41-45	heme oxygenase 1	Homo sapiens	0-4
30040983-5	2018	In fact, HO-1 decreased both intracellular and mitochondrial reactive oxygen species as well as the appearance of apoptotic features.	Reactive Oxygen Species	61-84	heme oxygenase 1	Homo sapiens	9-13
30040983-6	2018	Considering that Mn2+ induces mitochondrial damage and a defective MQC has been implicated in neurodegenerative diseases, we hypothesized that HO-1 could mediate cytoprotection by regulating the MQC processes.	Manganese(2+)	17-21	heme oxygenase 1	Homo sapiens	143-147
30040983-8	2018	Altogether, our data demonstrate a pro-survival function for HO-1 in Mn2+-induced apoptosis that involves the preservation of a proper MQC.	Manganese(2+)	69-73	heme oxygenase 1	Homo sapiens	61-65
30055129-8	2018	All of our data confirmed that oxidative stress-mediated mitochondrial apoptosis (especially the Nrf-2/HO-1 pathway) is responsible for 5h2c-induced HCC damage.	5h2c	136-140	heme oxygenase 1	Homo sapiens	103-107
30956868-4	2019	The treatment with chebulic acid attenuated cell death in t-BHP-induced HepG2 liver cells and increased intracellular glutathione content, upregulated the activity of heme oxygenase-1, and also increased the translocation of Nrf2 into the nucleus and Nrf2 target gene expression in a dose-dependent manner.	chebulic acid	19-32	heme oxygenase 1	Homo sapiens	167-183
30053409-0	2018	Hydroxytyrosol butyrate inhibits 6-OHDA-induced apoptosis through activation of the Nrf2/HO-1 axis in SH-SY5Y cells.	2-(3,4-Dihydroxyphenyl)ethyl butyrate	0-23	heme oxygenase 1	Homo sapiens	89-93
30218018-6	2018	We validated genes belonging to these pathways, such as HSPA5, SEC61B, G6PD, HMOX1 and PDE3B to be cooperatively modulated by the OPCs-curcumin combination.	Curcumin	135-143	heme oxygenase 1	Homo sapiens	77-82
30327713-0	2018	Heme Oxygenase-1 May Affect Cell Signalling via Modulation of Ganglioside Composition.	Gangliosides	62-73	heme oxygenase 1	Homo sapiens	0-16
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Heme	56-60	heme oxygenase 1	Homo sapiens	0-16
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Heme	56-60	heme oxygenase 1	Homo sapiens	18-23
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	0-16
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	18-23
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Iron	81-85	heme oxygenase 1	Homo sapiens	0-16
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Iron	81-85	heme oxygenase 1	Homo sapiens	18-23
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	0-16
30327713-1	2018	Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	18-23
30327713-4	2018	The aim of this study was to assess the possible role of Hmox1 in ganglioside metabolism in relation to oxidative stress.	Gangliosides	66-77	heme oxygenase 1	Homo sapiens	57-62
30327713-6	2018	To elucidate the possible underlying mechanisms between Hmox1 and ganglioside metabolism, hepatoblastoma HepG2 and neuroblastoma SH-SY5Y cell lines were used for in vitro experiments.	Gangliosides	66-77	heme oxygenase 1	Homo sapiens	56-61
30258436-1	2018	Heme Oxygenase 1 (HMOX1) is an enzyme that catalyzes the reaction that degrades the heme group contained in several important proteins, such as hemoglobin, myoglobin, and cytochrome p450.	Heme	84-88	heme oxygenase 1	Homo sapiens	0-16
30258436-1	2018	Heme Oxygenase 1 (HMOX1) is an enzyme that catalyzes the reaction that degrades the heme group contained in several important proteins, such as hemoglobin, myoglobin, and cytochrome p450.	Heme	84-88	heme oxygenase 1	Homo sapiens	18-23
30258436-2	2018	The enzymatic reaction catalyzed by HMOX1 generates Fe2+, biliverdin and CO.	ammonium ferrous sulfate	52-56	heme oxygenase 1	Homo sapiens	36-41
30258436-2	2018	The enzymatic reaction catalyzed by HMOX1 generates Fe2+, biliverdin and CO.	Biliverdine	58-68	heme oxygenase 1	Homo sapiens	36-41
30258436-2	2018	The enzymatic reaction catalyzed by HMOX1 generates Fe2+, biliverdin and CO.	Carbon Monoxide	73-75	heme oxygenase 1	Homo sapiens	36-41
30053409-0	2018	Hydroxytyrosol butyrate inhibits 6-OHDA-induced apoptosis through activation of the Nrf2/HO-1 axis in SH-SY5Y cells.	Oxidopamine	33-39	heme oxygenase 1	Homo sapiens	89-93
30053409-4	2018	HT-B also induced the protein expression of the transcription factor, NF-E2-related factor-2 (Nrf2) and its transcriptional activation, resulting in the up-regulated expression of heme oxygenase-1 (HO-1), which conferred neuroprotection against 6-OHDA-induced oxidative damage.	Oxidopamine	245-251	heme oxygenase 1	Homo sapiens	180-196
30053409-4	2018	HT-B also induced the protein expression of the transcription factor, NF-E2-related factor-2 (Nrf2) and its transcriptional activation, resulting in the up-regulated expression of heme oxygenase-1 (HO-1), which conferred neuroprotection against 6-OHDA-induced oxidative damage.	Oxidopamine	245-251	heme oxygenase 1	Homo sapiens	198-202
29761622-4	2018	HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron.	Heme	47-51	heme oxygenase 1	Homo sapiens	0-5
29671417-5	2018	Furthermore, pretreatment with cyanidin greatly promoted the translocation of the Nrf2 protein from the cytoplasm to the nucleus; upregulating cytoprotective enzymes, including HO-1, NQO-1 and GCLC; and increased the activity of SOD enzymes.	cyanidin	31-39	heme oxygenase 1	Homo sapiens	177-181
29913410-10	2018	Notably, IA increased the antioxidant enzyme heme oxygenase-1 (HO-1) expression and this effect was reversed by HO-1 inhibitor zinc protoporphyrin (ZnPP) leading to reduction of the neuroprotective effect of IA against Abeta-induced neurotoxicity.	zinc protoporphyrin	127-146	heme oxygenase 1	Homo sapiens	45-61
29913410-10	2018	Notably, IA increased the antioxidant enzyme heme oxygenase-1 (HO-1) expression and this effect was reversed by HO-1 inhibitor zinc protoporphyrin (ZnPP) leading to reduction of the neuroprotective effect of IA against Abeta-induced neurotoxicity.	zinc protoporphyrin	148-152	heme oxygenase 1	Homo sapiens	45-61
29947925-3	2018	Nuclear factor erythroid-derived 2-like 2 (NFE2L2 or Nrf-2) is essential for the antioxidant responsive element (ARE)-mediated induction of endogenous antioxidant enzymes such as heme oxygenase 1 (HO-1) and glutamate-cysteine ligase [GCL, the rate-limiting enzyme in the synthesis of glutathione (GSH)].	Glutathione	284-295	heme oxygenase 1	Homo sapiens	179-195
29947925-3	2018	Nuclear factor erythroid-derived 2-like 2 (NFE2L2 or Nrf-2) is essential for the antioxidant responsive element (ARE)-mediated induction of endogenous antioxidant enzymes such as heme oxygenase 1 (HO-1) and glutamate-cysteine ligase [GCL, the rate-limiting enzyme in the synthesis of glutathione (GSH)].	Glutathione	284-295	heme oxygenase 1	Homo sapiens	197-201
29947925-3	2018	Nuclear factor erythroid-derived 2-like 2 (NFE2L2 or Nrf-2) is essential for the antioxidant responsive element (ARE)-mediated induction of endogenous antioxidant enzymes such as heme oxygenase 1 (HO-1) and glutamate-cysteine ligase [GCL, the rate-limiting enzyme in the synthesis of glutathione (GSH)].	Glutathione	297-300	heme oxygenase 1	Homo sapiens	179-195
29947925-3	2018	Nuclear factor erythroid-derived 2-like 2 (NFE2L2 or Nrf-2) is essential for the antioxidant responsive element (ARE)-mediated induction of endogenous antioxidant enzymes such as heme oxygenase 1 (HO-1) and glutamate-cysteine ligase [GCL, the rate-limiting enzyme in the synthesis of glutathione (GSH)].	Glutathione	297-300	heme oxygenase 1	Homo sapiens	197-201
29066411-5	2018	Additionally, GA induced phosphorylated activation of extracellular regulated kinase (ERK), and ERK inhibitor PD98059 partially decreased GA-induced hepatoprotection, and downregulated the increased protein expressions of Nrf2, GCLC and HO-1 induced by GA.	Gallic Acid	14-16	heme oxygenase 1	Homo sapiens	237-241
29066411-5	2018	Additionally, GA induced phosphorylated activation of extracellular regulated kinase (ERK), and ERK inhibitor PD98059 partially decreased GA-induced hepatoprotection, and downregulated the increased protein expressions of Nrf2, GCLC and HO-1 induced by GA.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	110-117	heme oxygenase 1	Homo sapiens	237-241
30186615-9	2018	Results: Pretreatment with low-dose (1 and 5 muM) CAM for 72 h inhibited H2O2-induced reductions of GPx-1, GR, SOD, CAT and HO-1 activities, and mRNA expressions of GPx-1 and HO-1, and improved the GSH/GSSG ratio.	Hydrogen Peroxide	73-77	heme oxygenase 1	Homo sapiens	124-128
30186615-9	2018	Results: Pretreatment with low-dose (1 and 5 muM) CAM for 72 h inhibited H2O2-induced reductions of GPx-1, GR, SOD, CAT and HO-1 activities, and mRNA expressions of GPx-1 and HO-1, and improved the GSH/GSSG ratio.	Hydrogen Peroxide	73-77	heme oxygenase 1	Homo sapiens	175-179
29761622-4	2018	HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	0-5
29761622-4	2018	HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron.	Carbon Monoxide	81-83	heme oxygenase 1	Homo sapiens	0-5
29761622-4	2018	HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron.	Biliverdine	86-96	heme oxygenase 1	Homo sapiens	0-5
29761622-4	2018	HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron.	Iron	112-116	heme oxygenase 1	Homo sapiens	0-5
29974998-6	2018	Moreover, the expression of HO-1, a functional modulator of Tregs, was decreased in vitiligo Tregs, and the concentrations of HO-1 metabolites, including bilirubin, CoHb and iron, were correspondingly decreased in serum of vitiligo patients.	Bilirubin	154-163	heme oxygenase 1	Homo sapiens	126-130
29974998-6	2018	Moreover, the expression of HO-1, a functional modulator of Tregs, was decreased in vitiligo Tregs, and the concentrations of HO-1 metabolites, including bilirubin, CoHb and iron, were correspondingly decreased in serum of vitiligo patients.	Iron	174-178	heme oxygenase 1	Homo sapiens	28-32
30015902-7	2018	Furthermore, spilanthol significantly suppressed the phosphorylation of c-Jun N-terminal kinase (JNK), while pretreatment with spilanthol enhanced heme oxygenase (HO)-1 protein expression by western blotting.	N-isobutyl-2E-decenamide	127-137	heme oxygenase 1	Homo sapiens	147-168
29278009-1	2018	BACKGROUND: Heme oxygenase (HO)-1 is a heme-degrading enzyme highly expressed in monocyte/macrophage, serum levels of which may be promising biomarker for adult-onset Still"s disease (AOSD).	Heme	39-43	heme oxygenase 1	Homo sapiens	12-33
30302047-7	2018	More recent studies also suggest a role of ROS-induced downregulation of Heme Oxygenase (HO)1-targeting micro RNAs and upregulation of HO1 for ammonia-induced proliferation inhibition in cultured astrocytes.	Ammonia	143-150	heme oxygenase 1	Homo sapiens	135-138
30015902-0	2018	Spilanthol inhibits TNF-alpha-induced ICAM-1 expression and pro-inflammatory responses by inducing heme oxygenase-1 expression and suppressing pJNK in HaCaT keratinocytes.	N-isobutyl-2E-decenamide	0-10	heme oxygenase 1	Homo sapiens	99-115
30122195-4	2018	l-Arg deprivation markedly increased the mRNA expression of heat shock protein 70 and heme-oxygenase-1 under HS conditions.	Arginine	0-5	heme oxygenase 1	Homo sapiens	86-102
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Heme	75-79	heme oxygenase 1	Homo sapiens	24-40
30041041-10	2018	Notably, activation of HO-1 gene expression further increased the levels of EETs, suggesting that the antioxidant HO-1 system protects EETs from degradation by ROS.	ros	160-163	heme oxygenase 1	Homo sapiens	23-27
30041041-10	2018	Notably, activation of HO-1 gene expression further increased the levels of EETs, suggesting that the antioxidant HO-1 system protects EETs from degradation by ROS.	ros	160-163	heme oxygenase 1	Homo sapiens	114-118
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Heme	75-79	heme oxygenase 1	Homo sapiens	42-46
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	24-40
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	42-46
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	24-40
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	42-46
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Iron	125-129	heme oxygenase 1	Homo sapiens	24-40
30354985-1	2018	Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Iron	125-129	heme oxygenase 1	Homo sapiens	42-46
30159112-9	2018	Trx, nuclear Nrf2 protein, and HO-1 protein were also negatively correlated with the percent of time that SaO2 was less than 90% (TSat90).	sao2	106-110	heme oxygenase 1	Homo sapiens	31-35
29969714-5	2018	We find that, in combination with 2.5 microM sulforaphane, dtBHQ markedly enhances ARE-regulated gene expression, including expression of the cytoprotective proteins aldo-keto reductase family 1 member C1 (AKR1C1) and heme oxygenase-1 (HO-1).	2,5-di-tert-butylhydroquinone	59-64	heme oxygenase 1	Homo sapiens	218-234
29753693-7	2018	The combination of ALA 600 mg and sodium ferrous citrate (SFC) 942 mg upregulated HO-1 in PBMC at 8 h after administration while sole administration of ALA or SFC was unable to induce HO-1.	5-amino levulinic acid	19-22	heme oxygenase 1	Homo sapiens	82-86
29753693-7	2018	The combination of ALA 600 mg and sodium ferrous citrate (SFC) 942 mg upregulated HO-1 in PBMC at 8 h after administration while sole administration of ALA or SFC was unable to induce HO-1.	Ferromia	34-56	heme oxygenase 1	Homo sapiens	82-86
29753693-7	2018	The combination of ALA 600 mg and sodium ferrous citrate (SFC) 942 mg upregulated HO-1 in PBMC at 8 h after administration while sole administration of ALA or SFC was unable to induce HO-1.	SFC	58-61	heme oxygenase 1	Homo sapiens	82-86
29753693-8	2018	HO-1 in blood myeloid and plasmacytoid dendritic cells was also upregulated with ALA+SFC.	ala+sfc	81-88	heme oxygenase 1	Homo sapiens	0-4
29993075-0	2018	Targeting heme oxygenase-1 by quercetin ameliorates alcohol-induced acute liver injury via inhibiting NLRP3 inflammasome activation.	Quercetin	30-39	heme oxygenase 1	Homo sapiens	10-26
29993075-0	2018	Targeting heme oxygenase-1 by quercetin ameliorates alcohol-induced acute liver injury via inhibiting NLRP3 inflammasome activation.	Alcohols	52-59	heme oxygenase 1	Homo sapiens	10-26
29993075-7	2018	Moreover, this protective effect of quercetin could be diminished when combined with the HO-1 inhibitor ZnppIX which demonstrated a critical role of HO-1 in quercetin"s hepatoprotection.	Quercetin	36-45	heme oxygenase 1	Homo sapiens	149-153
29993075-7	2018	Moreover, this protective effect of quercetin could be diminished when combined with the HO-1 inhibitor ZnppIX which demonstrated a critical role of HO-1 in quercetin"s hepatoprotection.	zinc protoporphyrin	104-110	heme oxygenase 1	Homo sapiens	89-93
29993075-7	2018	Moreover, this protective effect of quercetin could be diminished when combined with the HO-1 inhibitor ZnppIX which demonstrated a critical role of HO-1 in quercetin"s hepatoprotection.	zinc protoporphyrin	104-110	heme oxygenase 1	Homo sapiens	149-153
29993075-7	2018	Moreover, this protective effect of quercetin could be diminished when combined with the HO-1 inhibitor ZnppIX which demonstrated a critical role of HO-1 in quercetin"s hepatoprotection.	Quercetin	157-166	heme oxygenase 1	Homo sapiens	89-93
29993075-7	2018	Moreover, this protective effect of quercetin could be diminished when combined with the HO-1 inhibitor ZnppIX which demonstrated a critical role of HO-1 in quercetin"s hepatoprotection.	Quercetin	157-166	heme oxygenase 1	Homo sapiens	149-153
29993075-8	2018	The underlying mechanism of quercetin"s benefit on the liver may be explained by its anti-oxidant properties and inhibitory effect on the ROS/NF-kappaB/NLRP3 inflammasome/IL-1beta and IL-18 pathway by inducing HO-1.	Quercetin	28-37	heme oxygenase 1	Homo sapiens	210-214
29993075-10	2018	In conclusion, quercetin can preserve the function of the liver in acute alcoholic injury by upregulating the expression of IL-10 and HO-1 and thus inhibiting NLRP3 inflammasome activation and inflammatory factor secretion.	Quercetin	15-24	heme oxygenase 1	Homo sapiens	134-138
29777873-4	2018	Moreover, cinnamaldehyde inhibited the phosphorylation of p38, JNK and p65 NF-kappaB and increased heme oxygenase-1 (HO-1) activity.	cinnamaldehyde	10-24	heme oxygenase 1	Homo sapiens	99-115
29777873-4	2018	Moreover, cinnamaldehyde inhibited the phosphorylation of p38, JNK and p65 NF-kappaB and increased heme oxygenase-1 (HO-1) activity.	cinnamaldehyde	10-24	heme oxygenase 1	Homo sapiens	117-121
29777873-7	2018	Thus, results indicated that cinnamaldehyde antagonized the ox-LDL-induced VSMCs proliferation, migration, inflammation and foam cell formation through regulation of HO-1, MMP-2, LOX-1 and blockage of cell cycle, and - suppression of p38, JNK/MAPK and NF-kappaB signaling pathways.	cinnamaldehyde	29-43	heme oxygenase 1	Homo sapiens	166-170
30153269-7	2018	These data suggest that the HO-1-derived metabolites, CO and bilirubin, elevate astrocytic mitochondrial function via a HIF-1alpha/ERRalpha circuit coupled with L-type Ca2+ channel activation and PGC-1alpha-mediated oxygen consumption.	Carbon Monoxide	54-56	heme oxygenase 1	Homo sapiens	28-32
30153269-7	2018	These data suggest that the HO-1-derived metabolites, CO and bilirubin, elevate astrocytic mitochondrial function via a HIF-1alpha/ERRalpha circuit coupled with L-type Ca2+ channel activation and PGC-1alpha-mediated oxygen consumption.	Bilirubin	61-70	heme oxygenase 1	Homo sapiens	28-32
30153269-7	2018	These data suggest that the HO-1-derived metabolites, CO and bilirubin, elevate astrocytic mitochondrial function via a HIF-1alpha/ERRalpha circuit coupled with L-type Ca2+ channel activation and PGC-1alpha-mediated oxygen consumption.	Oxygen	216-222	heme oxygenase 1	Homo sapiens	28-32
30061089-4	2018	In this study, we found that increased expression of Mkp-1, Nrf2, and heme oxygenase 1 (Ho-1) was correlated in colonic tissues in patients with ulcerative colitis and Crohn"s disease, as well as wild-type mice with colitis induced by dextran sodium sulfate (DSS).	dextran sodium sulfate	235-257	heme oxygenase 1	Homo sapiens	70-86
30061089-4	2018	In this study, we found that increased expression of Mkp-1, Nrf2, and heme oxygenase 1 (Ho-1) was correlated in colonic tissues in patients with ulcerative colitis and Crohn"s disease, as well as wild-type mice with colitis induced by dextran sodium sulfate (DSS).	dextran sodium sulfate	235-257	heme oxygenase 1	Homo sapiens	88-92
30061089-4	2018	In this study, we found that increased expression of Mkp-1, Nrf2, and heme oxygenase 1 (Ho-1) was correlated in colonic tissues in patients with ulcerative colitis and Crohn"s disease, as well as wild-type mice with colitis induced by dextran sodium sulfate (DSS).	dss	259-262	heme oxygenase 1	Homo sapiens	70-86
30061089-4	2018	In this study, we found that increased expression of Mkp-1, Nrf2, and heme oxygenase 1 (Ho-1) was correlated in colonic tissues in patients with ulcerative colitis and Crohn"s disease, as well as wild-type mice with colitis induced by dextran sodium sulfate (DSS).	dss	259-262	heme oxygenase 1	Homo sapiens	88-92
29753693-0	2018	Oral administration of 5-aminolevulinic acid induces heme oxygenase-1 expression in peripheral blood mononuclear cells of healthy human subjects in combination with ferrous iron.	5-amino levulinic acid	23-44	heme oxygenase 1	Homo sapiens	53-69
29753693-2	2018	The aim of this study is to determine whether the combination of 5-aminolevulinic acid (ALA) and iron induces HO-1 expression in healthy human peripheral blood mononuclear cells (PBMC).	5-amino levulinic acid	65-86	heme oxygenase 1	Homo sapiens	110-114
29753693-2	2018	The aim of this study is to determine whether the combination of 5-aminolevulinic acid (ALA) and iron induces HO-1 expression in healthy human peripheral blood mononuclear cells (PBMC).	5-amino levulinic acid	88-91	heme oxygenase 1	Homo sapiens	110-114
29753693-2	2018	The aim of this study is to determine whether the combination of 5-aminolevulinic acid (ALA) and iron induces HO-1 expression in healthy human peripheral blood mononuclear cells (PBMC).	Iron	97-101	heme oxygenase 1	Homo sapiens	110-114
29753693-5	2018	Study B aimed to examine HO-1 dose dependency at 150, 300, and 600 mg of ALA and the need for iron supplementation.	5-amino levulinic acid	73-76	heme oxygenase 1	Homo sapiens	25-29
29753693-6	2018	Study C aimed to investigate HO-1 changes during a three-day, repetitive administration of ALA and iron.	5-amino levulinic acid	91-94	heme oxygenase 1	Homo sapiens	29-33
29753693-6	2018	Study C aimed to investigate HO-1 changes during a three-day, repetitive administration of ALA and iron.	Iron	99-103	heme oxygenase 1	Homo sapiens	29-33
30092096-11	2018	The mRNA levels of heme oxygenase-1 and superoxide dismutase-1 and ROS levels were significantly increased in HGFs after 72 h of exposure to 50 mM glucose concentration.	Glucose	147-154	heme oxygenase 1	Homo sapiens	19-35
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Heme	89-93	heme oxygenase 1	Homo sapiens	6-22
30096430-0	2018	WITHDRAWN: Paeoniflorin attenuates LPS-induced inflammation in nucleus pulposus cells via Nrf-2/HO-1/HMGB1/NF-kappaB pathway.	peoniflorin	11-23	heme oxygenase 1	Homo sapiens	96-100
29961319-6	2018	Further investigations showed that PSB significantly enhanced Nrf2 expression and nuclear accumulation, improved ARE promoter activity and up-regulated expression of HO-1 and GCLC.	pinostrobin	35-38	heme oxygenase 1	Homo sapiens	166-170
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Heme	89-93	heme oxygenase 1	Homo sapiens	24-28
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Carbon Monoxide	106-108	heme oxygenase 1	Homo sapiens	6-22
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Carbon Monoxide	106-108	heme oxygenase 1	Homo sapiens	24-28
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Biliverdine	110-120	heme oxygenase 1	Homo sapiens	6-22
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Biliverdine	110-120	heme oxygenase 1	Homo sapiens	24-28
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Iron	126-130	heme oxygenase 1	Homo sapiens	6-22
30159103-1	2018	Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron.	Iron	126-130	heme oxygenase 1	Homo sapiens	24-28
30186543-4	2018	We found that the antioxidant cinnamaldehyde activated the NRF2/HMOX1 pathway.	cinnamaldehyde	30-44	heme oxygenase 1	Homo sapiens	64-69
29969038-6	2018	Moreover, metformin alleviated LPS-induced NF-kappaB phosphorylation, promoted Nrf2 nuclear translocation, and increased the expression of the antioxidative genes (HO-1 and NQO-1), leading to reduced intestinal ROS content.	Metformin	10-19	heme oxygenase 1	Homo sapiens	164-168
29730426-6	2018	Mechanism studies demonstrated that isorhamnetin pretreatment remarkably abolished H/R-induced downregulation of Nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expressions and upregulation of NADPH oxidase-2/4 (NOX-2/4) expressions in cardiomyocytes.	r	85-86	heme oxygenase 1	Homo sapiens	168-184
29730426-6	2018	Mechanism studies demonstrated that isorhamnetin pretreatment remarkably abolished H/R-induced downregulation of Nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expressions and upregulation of NADPH oxidase-2/4 (NOX-2/4) expressions in cardiomyocytes.	r	85-86	heme oxygenase 1	Homo sapiens	186-190
29730426-6	2018	Mechanism studies demonstrated that isorhamnetin pretreatment remarkably abolished H/R-induced downregulation of Nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expressions and upregulation of NADPH oxidase-2/4 (NOX-2/4) expressions in cardiomyocytes.	3-methylquercetin	36-48	heme oxygenase 1	Homo sapiens	168-184
29730426-6	2018	Mechanism studies demonstrated that isorhamnetin pretreatment remarkably abolished H/R-induced downregulation of Nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expressions and upregulation of NADPH oxidase-2/4 (NOX-2/4) expressions in cardiomyocytes.	3-methylquercetin	36-48	heme oxygenase 1	Homo sapiens	186-190
29730426-7	2018	However, SIRT1 inhibition (Sirtinol) not only inhibited isorhamnetin-induced Nrf2/HO-1 upregulation and NOX-2/4 downregulation, but also alleviated its anti-apoptotic effects.	sirtinol	27-35	heme oxygenase 1	Homo sapiens	82-86
29730426-7	2018	However, SIRT1 inhibition (Sirtinol) not only inhibited isorhamnetin-induced Nrf2/HO-1 upregulation and NOX-2/4 downregulation, but also alleviated its anti-apoptotic effects.	3-methylquercetin	56-68	heme oxygenase 1	Homo sapiens	82-86
29730426-8	2018	Taken together, these data indicate that isorhamnetin can exhibit positive effect on H/R-induced injure by attenuating apoptosis and oxidative stress in H9c2 cardiomyocytes, which is partly attributable to the upregulation of SIRT1 and Nrf2/HO-1-mediated antioxidant signaling pathway.	3-methylquercetin	41-53	heme oxygenase 1	Homo sapiens	241-245
29730426-8	2018	Taken together, these data indicate that isorhamnetin can exhibit positive effect on H/R-induced injure by attenuating apoptosis and oxidative stress in H9c2 cardiomyocytes, which is partly attributable to the upregulation of SIRT1 and Nrf2/HO-1-mediated antioxidant signaling pathway.	r	87-88	heme oxygenase 1	Homo sapiens	241-245
29679944-0	2018	Epigallocatechin-3-gallate attenuates microcystin-LR-induced apoptosis in human umbilical vein endothelial cells through activation of the NRF2/HO-1 pathway.	epigallocatechin gallate	0-26	heme oxygenase 1	Homo sapiens	144-148
29698685-0	2018	Effect of hemin, baicalein and heme oxygenase-1 (HO-1) enzyme activity inhibitors on Cd-induced accumulation of HO-1, HSPs and aggresome-like structures in Xenopus kidney epithelial cells.	Cadmium	85-87	heme oxygenase 1	Homo sapiens	31-47
29698685-0	2018	Effect of hemin, baicalein and heme oxygenase-1 (HO-1) enzyme activity inhibitors on Cd-induced accumulation of HO-1, HSPs and aggresome-like structures in Xenopus kidney epithelial cells.	Cadmium	85-87	heme oxygenase 1	Homo sapiens	49-53
29698685-0	2018	Effect of hemin, baicalein and heme oxygenase-1 (HO-1) enzyme activity inhibitors on Cd-induced accumulation of HO-1, HSPs and aggresome-like structures in Xenopus kidney epithelial cells.	Cadmium	85-87	heme oxygenase 1	Homo sapiens	112-116
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Heme	40-44	heme oxygenase 1	Homo sapiens	58-62
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Iron	117-121	heme oxygenase 1	Homo sapiens	40-56
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Iron	117-121	heme oxygenase 1	Homo sapiens	58-62
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Biliverdine	126-136	heme oxygenase 1	Homo sapiens	40-56
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Biliverdine	126-136	heme oxygenase 1	Homo sapiens	58-62
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Cadmium Chloride	213-218	heme oxygenase 1	Homo sapiens	40-56
29698685-3	2018	In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2.	Cadmium Chloride	213-218	heme oxygenase 1	Homo sapiens	58-62
29698685-4	2018	In the present study, CdCl2 treatment of A6 kidney epithelial cells, derived from the frog, Xenopus laevis, induced the accumulation of HO-1, heat shock protein 70 (HSP70) and HSP30 as well as an increase in the production of aggregated protein and aggresome-like structures.	Cadmium Chloride	22-27	heme oxygenase 1	Homo sapiens	136-140
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	S-Nitroso-N-propionyl-D,L-penicillamine	80-84	heme oxygenase 1	Homo sapiens	38-42
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	S-Nitroso-N-propionyl-D,L-penicillamine	80-84	heme oxygenase 1	Homo sapiens	200-204
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	zinc protoporphyrin	90-109	heme oxygenase 1	Homo sapiens	38-42
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	zinc protoporphyrin	90-109	heme oxygenase 1	Homo sapiens	200-204
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	zinc protoporphyrin	111-115	heme oxygenase 1	Homo sapiens	38-42
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	Cadmium Chloride	127-132	heme oxygenase 1	Homo sapiens	38-42
29698685-5	2018	Treatment of cells with inhibitors of HO-1 enzyme activity, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced CdCl2-induced actin cytoskeletal disorganization and the accumulation of HO-1, HSP70, aggregated protein and aggresome-like structures.	Cadmium Chloride	127-132	heme oxygenase 1	Homo sapiens	200-204
29698685-9	2018	These results suggest that HO-1-mediated protection against CdCl2 toxicity includes the maintenance of actin cytoskeletal and microtubular structure and the suppression of aggregated protein and aggresome-like structures.	Cadmium Chloride	60-65	heme oxygenase 1	Homo sapiens	27-31
29960846-4	2018	Treatment of Hep3B with BPA increased the levels of nitrous oxide, a metabolite of nitric oxide and activated Nrf2 by nitrosylation of Keap1, leading to the induction of heme oxygenase-1 (HO-1) and UGT2B1 mRNAs.	bisphenol A	24-27	heme oxygenase 1	Homo sapiens	170-186
29960846-4	2018	Treatment of Hep3B with BPA increased the levels of nitrous oxide, a metabolite of nitric oxide and activated Nrf2 by nitrosylation of Keap1, leading to the induction of heme oxygenase-1 (HO-1) and UGT2B1 mRNAs.	Nitrous Oxide	52-65	heme oxygenase 1	Homo sapiens	170-186
29679944-8	2018	Our findings indicate that EGCG treatment protects against MC-LR-mediated HUVEC apoptosis via activation of NRF2/HO-1 signaling.	epigallocatechin gallate	27-31	heme oxygenase 1	Homo sapiens	113-117
29679944-8	2018	Our findings indicate that EGCG treatment protects against MC-LR-mediated HUVEC apoptosis via activation of NRF2/HO-1 signaling.	cyanoginosin LR	59-64	heme oxygenase 1	Homo sapiens	113-117
29679944-7	2018	EGCG induced NRF2/HO-1 expression and activation in MC-LR treated HUVECs, while downregulation of NRF2/HO-1 by specific siRNAs revealed that NRF2/HO-1 signaling was involved in EGCG attenuation of MC-LR-induced HUVEC apoptosis.	epigallocatechin gallate	0-4	heme oxygenase 1	Homo sapiens	18-22
29679944-7	2018	EGCG induced NRF2/HO-1 expression and activation in MC-LR treated HUVECs, while downregulation of NRF2/HO-1 by specific siRNAs revealed that NRF2/HO-1 signaling was involved in EGCG attenuation of MC-LR-induced HUVEC apoptosis.	cyanoginosin LR	52-57	heme oxygenase 1	Homo sapiens	18-22
29753142-0	2018	Heme Oxygenase-1 inhibits spring viremia of carp virus replication through carbon monoxide mediated cyclic GMP/Protein kinase G signaling pathway.	Carbon Monoxide	75-90	heme oxygenase 1	Homo sapiens	0-16
29753142-0	2018	Heme Oxygenase-1 inhibits spring viremia of carp virus replication through carbon monoxide mediated cyclic GMP/Protein kinase G signaling pathway.	Cyclic GMP	100-110	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Heme	69-73	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Heme	69-73	heme oxygenase 1	Homo sapiens	18-22
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Carbon Monoxide	85-100	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Carbon Monoxide	85-100	heme oxygenase 1	Homo sapiens	18-22
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Carbon Monoxide	102-104	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Carbon Monoxide	102-104	heme oxygenase 1	Homo sapiens	18-22
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Biliverdine	107-117	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Biliverdine	107-117	heme oxygenase 1	Homo sapiens	18-22
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Iron	130-134	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	Iron	130-134	heme oxygenase 1	Homo sapiens	18-22
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	ammonium ferrous sulfate	136-140	heme oxygenase 1	Homo sapiens	0-16
29753142-3	2018	Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties.	ammonium ferrous sulfate	136-140	heme oxygenase 1	Homo sapiens	18-22
29753142-6	2018	The elevated expression of HO-1 was induced upon cobalt protoporphyrin (CoPP) treatment in EPC cells without affecting cell viability and thus inhibited SVCV replication in a dose dependent manner.	cobaltiprotoporphyrin	49-70	heme oxygenase 1	Homo sapiens	27-31
29753142-6	2018	The elevated expression of HO-1 was induced upon cobalt protoporphyrin (CoPP) treatment in EPC cells without affecting cell viability and thus inhibited SVCV replication in a dose dependent manner.	cobaltiprotoporphyrin	72-76	heme oxygenase 1	Homo sapiens	27-31
29753142-8	2018	Thereby, the antiviral activity of ROS/Nrf2/HO-1 axis was confirmed in EPC cells.	ros	35-38	heme oxygenase 1	Homo sapiens	44-48
29753142-10	2018	Collectively, these findings suggest potential drug or therapy that induced the Nrf2/HO-1/CO/cGMP/PKG signaling pathway as a promising strategy for treating SVC.	Cyclic GMP	93-97	heme oxygenase 1	Homo sapiens	85-92
29939160-4	2018	Noncanonical ferroptosis induction is characterized by an increase in intracellular labile Fe(II) upon excessive activation of heme oxygenase-1, which is sufficient to induce ferroptosis.	ammonium ferrous sulfate	91-97	heme oxygenase 1	Homo sapiens	127-143
29906742-10	2018	The expression of Nrf2 and HO-1 were dose-dependently up-regulated by the treatment of xanthohumol.	xanthohumol	87-98	heme oxygenase 1	Homo sapiens	27-31
29909234-6	2018	Additionally, the Puerarin treatment also significantly enhanced (P &lt; 0.001) the mRNA expressions levels of the anti-oxidant enzymes such as Nrf2, HO-1 and SOD2.	puerarin	18-26	heme oxygenase 1	Homo sapiens	150-154
31949812-0	2018	Overexpression of miR-153 promotes oxidative stress in MPP+-induced PD model by negatively regulating the Nrf2/HO-1 signaling pathway.	1-(4-methoxyphenyl)pyridinium	55-59	heme oxygenase 1	Homo sapiens	111-115
31949812-10	2018	Finally, it was observed that miR-153 could suppress the Nrf2/HO-1 signaling pathway in MPP+-treated SH-SY5Y cells.	1-(4-methoxyphenyl)pyridinium	88-91	heme oxygenase 1	Homo sapiens	62-66
30106049-8	2018	Compared with the control group, the expression of NFE2L2 and HMOX1 was significantly increased in the genistein + rotenone group.	Genistein	103-112	heme oxygenase 1	Homo sapiens	62-67
29473125-0	2018	Sulforaphane Attenuated the Pro-Inflammatory State Induced by Hydrogen Peroxide in SH-SY5Y Cells Through the Nrf2/HO-1 Signaling Pathway.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	114-118
29473125-0	2018	Sulforaphane Attenuated the Pro-Inflammatory State Induced by Hydrogen Peroxide in SH-SY5Y Cells Through the Nrf2/HO-1 Signaling Pathway.	Hydrogen Peroxide	62-79	heme oxygenase 1	Homo sapiens	114-118
29473125-8	2018	Therefore, SFN exerted an anti-inflammatory effect in H2O2-challenged SH-SY5Y cells by a mechanism dependent on the Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	54-58	heme oxygenase 1	Homo sapiens	121-125
30106049-8	2018	Compared with the control group, the expression of NFE2L2 and HMOX1 was significantly increased in the genistein + rotenone group.	Rotenone	115-123	heme oxygenase 1	Homo sapiens	62-67
30187882-5	2018	In HepG2 cells, treatment with triptolide significantly inhibited the cell growth, resulting in a cell viability as low as 72.83% at 24 h; triptolide also induced obvious cell apoptosis and cell nucleus deformation, causing an apoptosis rate of 43.1% in the cells at 24 h. Triptolide significantly reduced the expressions of Nrf2 and HO-1 proteins related with the oxidative stress pathway.	triptolide	31-41	heme oxygenase 1	Homo sapiens	334-338
29732634-4	2018	Well-known pathways such as Pl3K/Akt/Bcl-2 pathway, Nrf2/HO-1 pathway, and MAPK signaling pathway help berberine to protect neurons through antiapoptotic, antioxidative, and anti-inflammatory activities.	Berberine	103-112	heme oxygenase 1	Homo sapiens	57-61
30060630-16	2018	Moreover, the expression of HO-1 and NQO-1 increased significantly in the CTP group.	Cytidine Triphosphate	74-77	heme oxygenase 1	Homo sapiens	28-32
30084803-0	2018	Pyridoxine exerts antioxidant effects in cell model of Alzheimer"s disease via the Nrf-2/HO-1 pathway.	Pyridoxine	0-10	heme oxygenase 1	Homo sapiens	89-93
30084803-5	2018	The results obtained revealed that pyridoxine exerted a protective potential against AD, attenuated ROS levels, decreased the expressions of cytoplasmic Nrf2, and upregulated whole-cell HO-1 expression.	Pyridoxine	35-45	heme oxygenase 1	Homo sapiens	186-190
30084803-6	2018	These results suggest that the anti-AD effect of pyridoxine may be attributed to its anti-oxidant property elicited via stimulation of the Nrf2/HO-1 pathway.	Pyridoxine	49-59	heme oxygenase 1	Homo sapiens	144-148
30187882-5	2018	In HepG2 cells, treatment with triptolide significantly inhibited the cell growth, resulting in a cell viability as low as 72.83% at 24 h; triptolide also induced obvious cell apoptosis and cell nucleus deformation, causing an apoptosis rate of 43.1% in the cells at 24 h. Triptolide significantly reduced the expressions of Nrf2 and HO-1 proteins related with the oxidative stress pathway.	triptolide	139-149	heme oxygenase 1	Homo sapiens	334-338
29678719-0	2018	Carnosic acid attenuates cartilage degeneration through induction of heme oxygenase-1 in human articular chondrocytes.	salvin	0-13	heme oxygenase 1	Homo sapiens	69-85
30048241-4	2018	METHODS AND RESULTS: Upregulation of HO-1 by Hemin or adenovirus infection reversed H2O2-induced senescence in human umbilical vein endothelial cells (HUVECs); whereas depletion of HO-1 by siRNA or HO-1 inhibitor protoporphyrin IX zinc (II) (ZnPP) triggered HUVEC senescence.	Hydrogen Peroxide	84-88	heme oxygenase 1	Homo sapiens	37-41
30048241-4	2018	METHODS AND RESULTS: Upregulation of HO-1 by Hemin or adenovirus infection reversed H2O2-induced senescence in human umbilical vein endothelial cells (HUVECs); whereas depletion of HO-1 by siRNA or HO-1 inhibitor protoporphyrin IX zinc (II) (ZnPP) triggered HUVEC senescence.	protoporphyrin IX	213-230	heme oxygenase 1	Homo sapiens	37-41
30048241-4	2018	METHODS AND RESULTS: Upregulation of HO-1 by Hemin or adenovirus infection reversed H2O2-induced senescence in human umbilical vein endothelial cells (HUVECs); whereas depletion of HO-1 by siRNA or HO-1 inhibitor protoporphyrin IX zinc (II) (ZnPP) triggered HUVEC senescence.	zinc protoporphyrin	242-246	heme oxygenase 1	Homo sapiens	37-41
30048241-5	2018	Mechanistically, overexpression of HO-1 enhanced the interaction between HO-1 and endothelial nitric oxide synthase (eNOS), and promoted the interaction between eNOS and its upstream kinase Akt, thus resulting in an enhancement of eNOS phosphorylation at Ser1177 and a subsequent increase of nitric oxide (NO) production.	Nitric Oxide	94-106	heme oxygenase 1	Homo sapiens	35-39
30048241-5	2018	Mechanistically, overexpression of HO-1 enhanced the interaction between HO-1 and endothelial nitric oxide synthase (eNOS), and promoted the interaction between eNOS and its upstream kinase Akt, thus resulting in an enhancement of eNOS phosphorylation at Ser1177 and a subsequent increase of nitric oxide (NO) production.	Nitric Oxide	94-106	heme oxygenase 1	Homo sapiens	73-77
30048241-6	2018	Moreover, HO-1 induction prevented the decrease of eNOS dimer/monomer ratio stimulated by H2O2 via its antioxidant properties.	Hydrogen Peroxide	90-94	heme oxygenase 1	Homo sapiens	10-14
29980703-3	2018	The plant-derived polyphenols, carnosol and curcumin, have been identified as candidate HO-1 inducers however there has been little investigation into their effects on human immune cells.	Polyphenols	18-29	heme oxygenase 1	Homo sapiens	88-92
29980703-3	2018	The plant-derived polyphenols, carnosol and curcumin, have been identified as candidate HO-1 inducers however there has been little investigation into their effects on human immune cells.	carnosol	31-39	heme oxygenase 1	Homo sapiens	88-92
29980703-3	2018	The plant-derived polyphenols, carnosol and curcumin, have been identified as candidate HO-1 inducers however there has been little investigation into their effects on human immune cells.	Curcumin	44-52	heme oxygenase 1	Homo sapiens	88-92
30097118-10	2018	Hypericin reduced HO-1 and NS5A in a time- and dose- dependent manner.	hypericin	0-9	heme oxygenase 1	Homo sapiens	18-22
30097118-11	2018	Chidamide, but not 5-Aza-dc, restored hypericin-induced reduction in HCV NS3 expression and reversed HO-1 expression in Ava5 cells.	N-(2-amino-5-fluorobenzyl)-4-(N-(pyridine-3-acrylyl)aminomethyl)benzamide	0-9	heme oxygenase 1	Homo sapiens	101-105
30097118-12	2018	LY294002 inhibited HCV replication via HO-1 down-regulation.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	0-8	heme oxygenase 1	Homo sapiens	39-43
30097118-15	2018	CONCLUSION: In conclusion, hypericin inhibits HCV replication via down-regulation of HO-1 expression and deacetylation.	hypericin	27-36	heme oxygenase 1	Homo sapiens	85-89
29792861-7	2018	Conversely, Akt-mTORC1 inhibitors (RAD001 and LY294002) reduced NLGN3-induced HO1, NOQ1 and GCLC mRNA expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	46-54	heme oxygenase 1	Homo sapiens	78-81
29678719-5	2018	Among the signaling pathways that control cellular protective mechanisms against oxygen radical damage is heme oxygenase-1 (HO-1).	Oxygen	81-87	heme oxygenase 1	Homo sapiens	106-122
29678719-5	2018	Among the signaling pathways that control cellular protective mechanisms against oxygen radical damage is heme oxygenase-1 (HO-1).	Oxygen	81-87	heme oxygenase 1	Homo sapiens	124-128
29678719-8	2018	Carnosic acid (CA), a natural diterpene with oxidant activity, is prevents cartilage degeneration though induction of HO-1.	salvin	0-13	heme oxygenase 1	Homo sapiens	118-122
29452096-1	2018	Heme oxygenase (HO)-1, the inducible isoform of the heme-degrading enzyme HO, plays a critical role in inflammation and iron homeostasis.	Heme	52-56	heme oxygenase 1	Homo sapiens	0-21
30057686-0	2018	Flutamide Induces Hepatic Cell Death and Mitochondrial Dysfunction via Inhibition of Nrf2-Mediated Heme Oxygenase-1.	Flutamide	0-9	heme oxygenase 1	Homo sapiens	99-115
30057686-4	2018	This study was designed to delineate the role of Nrf2/HO-1 in flutamide-induced hepatic cell injury.	Flutamide	62-71	heme oxygenase 1	Homo sapiens	54-58
30057686-6	2018	The protein expression of Nrf2 and HO-1 was induced by flutamide at 12.5 muM but was downregulated by higher concentrations of flutamide.	Flutamide	55-64	heme oxygenase 1	Homo sapiens	35-39
30057686-6	2018	The protein expression of Nrf2 and HO-1 was induced by flutamide at 12.5 muM but was downregulated by higher concentrations of flutamide.	Flutamide	127-136	heme oxygenase 1	Homo sapiens	35-39
30057686-7	2018	Silencing either Nrf2 or HO-1 was found to aggravate flutamide-induced hydrogen peroxide accumulation and mitochondrial dysfunction as well as inhibition of the Nrf2 pathway.	Flutamide	53-62	heme oxygenase 1	Homo sapiens	25-29
30057686-7	2018	Silencing either Nrf2 or HO-1 was found to aggravate flutamide-induced hydrogen peroxide accumulation and mitochondrial dysfunction as well as inhibition of the Nrf2 pathway.	Hydrogen Peroxide	71-88	heme oxygenase 1	Homo sapiens	25-29
30057686-8	2018	Moreover, preinduction of HO-1 by Copp significantly attenuated flutamide-induced oxidative stress and mitochondrial dysfunction, while inhibition of HO-1 by Snpp aggravated these deleterious effects.	COPP protocol	34-38	heme oxygenase 1	Homo sapiens	26-30
30057686-8	2018	Moreover, preinduction of HO-1 by Copp significantly attenuated flutamide-induced oxidative stress and mitochondrial dysfunction, while inhibition of HO-1 by Snpp aggravated these deleterious effects.	Flutamide	64-73	heme oxygenase 1	Homo sapiens	26-30
30057686-9	2018	These findings suggest that flutamide-induced hepatic cell death and mitochondrial dysfunction is assoicated with inhibition of Nrf2-mediated HO-1.	Flutamide	28-37	heme oxygenase 1	Homo sapiens	142-146
30057686-10	2018	Pharmacologic intervention of Nrf2/HO-1 may provide a promising therapeutic approach in flutamide-induced liver injury.	Flutamide	88-97	heme oxygenase 1	Homo sapiens	35-39
29452096-1	2018	Heme oxygenase (HO)-1, the inducible isoform of the heme-degrading enzyme HO, plays a critical role in inflammation and iron homeostasis.	Iron	120-124	heme oxygenase 1	Homo sapiens	0-21
29656184-0	2018	Ropivacaine regulates the expression and function of heme oxygenase-1.	Ropivacaine	0-11	heme oxygenase 1	Homo sapiens	53-69
29582209-7	2018	Increased ROS levels were also observed, possibly attributed to the weakened anti-oxidative response evidenced by the underexpression of the Nrf2-regulated genes encoding HO-1 and NQO1.	Reactive Oxygen Species	10-13	heme oxygenase 1	Homo sapiens	171-175
29656184-4	2018	In the current study, our results indicated that ropivacaine treatment caused a significant induction of heme oxygenase-1 (HO-1) at both the mRNA and protein levels in human SHSY5Y cells.	Ropivacaine	49-60	heme oxygenase 1	Homo sapiens	105-121
29656184-6	2018	Additionally, ropivacaine treatment enhanced HO-1 activity in a dose-dependent manner.	Ropivacaine	14-25	heme oxygenase 1	Homo sapiens	45-49
29656184-4	2018	In the current study, our results indicated that ropivacaine treatment caused a significant induction of heme oxygenase-1 (HO-1) at both the mRNA and protein levels in human SHSY5Y cells.	Ropivacaine	49-60	heme oxygenase 1	Homo sapiens	123-127
29656184-8	2018	Blockage of p38 phosphorylation with its specific inhibitor SB203580 or by transfection with p38 siRNA restrained ropivacaine-stimulated HO-1 expression.	SB 203580	60-68	heme oxygenase 1	Homo sapiens	137-141
29656184-8	2018	Blockage of p38 phosphorylation with its specific inhibitor SB203580 or by transfection with p38 siRNA restrained ropivacaine-stimulated HO-1 expression.	Ropivacaine	114-125	heme oxygenase 1	Homo sapiens	137-141
29656184-10	2018	Silencing of Nrf2 abolished ropivacaine-induced HO-1 expression.	Ropivacaine	28-39	heme oxygenase 1	Homo sapiens	48-52
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Ropivacaine	60-71	heme oxygenase 1	Homo sapiens	37-41
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Ropivacaine	60-71	heme oxygenase 1	Homo sapiens	237-241
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Reactive Oxygen Species	94-117	heme oxygenase 1	Homo sapiens	37-41
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Reactive Oxygen Species	119-122	heme oxygenase 1	Homo sapiens	37-41
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Glutathione	145-156	heme oxygenase 1	Homo sapiens	37-41
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Glutathione	158-161	heme oxygenase 1	Homo sapiens	37-41
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Ropivacaine	245-256	heme oxygenase 1	Homo sapiens	37-41
29656184-11	2018	Notably, we found that inhibition of HO-1 activity promoted ropivacaine-induced production of reactive oxygen species (ROS), deletion of reduced glutathione (GSH), and release of lactate dehydrogenase (LDH), suggesting that induction of HO-1 by ropivacaine acted as a compensatory survival response against ropivacaine.	Ropivacaine	245-256	heme oxygenase 1	Homo sapiens	37-41
29656184-5	2018	Levels of HO-1 mRNA and protein peaked at 1 h and 18 h, respectively, in response to ropivacaine treatment.	Ropivacaine	85-96	heme oxygenase 1	Homo sapiens	10-14
29758489-8	2018	Furthermore, fisetin significantly increased the effects of the protective antioxidant pathway by promoting the expression of nuclear factor erythroid-2-related factor-2 and heme oxygenase 1.	fisetin	13-20	heme oxygenase 1	Homo sapiens	174-190
29693710-3	2018	HO-1, by regulating intracellular levels of pro-oxidant heme, or by other benefits of its by-products such as carbon monoxide (CO) and biliverdin (BV) had become an important candidate protein to be up-regulated to combat diverse stressful events.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	0-4
29896252-4	2018	HSCs-T6 were incubated with different concentrations of hemin (HO-1 chemical inducer) and Znpp-IX (HO-1 chemical inhibitor) for 12, 24 and 48 h. Cell viability was determined using an MTT assay.	Hemin	56-61	heme oxygenase 1	Homo sapiens	63-67
29896252-4	2018	HSCs-T6 were incubated with different concentrations of hemin (HO-1 chemical inducer) and Znpp-IX (HO-1 chemical inhibitor) for 12, 24 and 48 h. Cell viability was determined using an MTT assay.	zinc protoporphyrin	90-97	heme oxygenase 1	Homo sapiens	99-103
29751106-6	2018	Curcumin significantly induced HMOX1 in single cell type models and co-cultures.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	31-36
29693114-0	2018	Human circular RNA-0054633 regulates high glucose-induced vascular endothelial cell dysfunction through the microRNA-218/roundabout 1 and microRNA-218/heme oxygenase-1 axes.	Glucose	42-49	heme oxygenase 1	Homo sapiens	138-167
29693114-9	2018	It was also demonstrated that downregulating the expression of miR-218 inhibited the high glucose-induced endothelial cell dysfunction by promoting the expression of ROBO1 and HO-1.	Glucose	90-97	heme oxygenase 1	Homo sapiens	176-180
29693710-3	2018	HO-1, by regulating intracellular levels of pro-oxidant heme, or by other benefits of its by-products such as carbon monoxide (CO) and biliverdin (BV) had become an important candidate protein to be up-regulated to combat diverse stressful events.	Carbon Monoxide	127-129	heme oxygenase 1	Homo sapiens	0-4
29693710-3	2018	HO-1, by regulating intracellular levels of pro-oxidant heme, or by other benefits of its by-products such as carbon monoxide (CO) and biliverdin (BV) had become an important candidate protein to be up-regulated to combat diverse stressful events.	Biliverdine	135-145	heme oxygenase 1	Homo sapiens	0-4
29693710-3	2018	HO-1, by regulating intracellular levels of pro-oxidant heme, or by other benefits of its by-products such as carbon monoxide (CO) and biliverdin (BV) had become an important candidate protein to be up-regulated to combat diverse stressful events.	Biliverdine	147-149	heme oxygenase 1	Homo sapiens	0-4
29498764-8	2018	Moreover, we showed that both in animal model and in human liver, frequent hemin infusions generate a chronic inflammatory hepatic disease which induces HO1 remotely to hemin treatment and maintains a high ALAS1 level responsible for recurrence.	Hemin	75-80	heme oxygenase 1	Homo sapiens	153-156
29498764-8	2018	Moreover, we showed that both in animal model and in human liver, frequent hemin infusions generate a chronic inflammatory hepatic disease which induces HO1 remotely to hemin treatment and maintains a high ALAS1 level responsible for recurrence.	Hemin	169-174	heme oxygenase 1	Homo sapiens	153-156
29704670-7	2018	The expression of Nrf2 and HO-1 were up-regulated by treatment of isorhamnetin.	3-methylquercetin	66-78	heme oxygenase 1	Homo sapiens	27-31
29951371-6	2018	In addition, endogenous miR-494 inhibition in undifferentiated cells impairs HO-1 induction in response to exposure to 500 microM H2O2, reducing the number of viable cells.	Hydrogen Peroxide	130-134	heme oxygenase 1	Homo sapiens	77-81
29997086-8	2018	CONCLUSION: Agmatine inhibits LPS-induced activation and dysfunction of HUVECs by modulating NF-kappaB and MAPK signal pathways to down-regulate the expressions of adhesion molecules and chemokines and by up-regulating the expression of HO-1 to reduce ROS production.	Agmatine	12-20	heme oxygenase 1	Homo sapiens	237-241
29997086-7	2018	Agmatine significantly up-regulated the mRNA expression of HO-1 (P&lt;0.05), inhibited LPS-induced phosphorylation of p38, ERK, nuclear p65 and cytoplasmic IkappaBalpha, and up-regulated the protein expression of cytoplasmic IkappaBalpha.	Agmatine	0-8	heme oxygenase 1	Homo sapiens	59-63
29921869-9	2018	Iron deposition associated with oxidative injury as indicated by heme oxygenase-1 abundance.	Iron	0-4	heme oxygenase 1	Homo sapiens	65-81
29951371-7	2018	The analysis of Bach1 expression did not reveal any significant modifications in any experimental conditions tested, proving that the impairment of HO-1 induction observed in cells treated with miR-494 inhibitor and exposed to H2O2 is independent from Bach1.	Hydrogen Peroxide	227-231	heme oxygenase 1	Homo sapiens	148-152
29704732-4	2018	Furthermore, paeonol treatment resulted in the increase of Nrf2 nuclear translocation, the increase of NQO-1 and HO-1 expression, and the suppression of NF-kappaB p65 nuclear translocation.	paeonol	13-20	heme oxygenase 1	Homo sapiens	113-117
29874784-8	2018	In addition, EESS increased not only expression, but also phosphorylation of nuclear factor-erythroid 2 related factor 2 (Nrf2), and promoted the expression of heme oxygenase-1 (HO-1), a critical target enzyme of Nrf2, but decreased the expression of kelch-like ECH-associated protein-1; however, the inhibition of HO-1 activity by zinc protoporphyrin abolished the antioxidant potential induced by EESS against H2O2-mediated oxidative stress.	zinc protoporphyrin	332-351	heme oxygenase 1	Homo sapiens	160-176
29874784-8	2018	In addition, EESS increased not only expression, but also phosphorylation of nuclear factor-erythroid 2 related factor 2 (Nrf2), and promoted the expression of heme oxygenase-1 (HO-1), a critical target enzyme of Nrf2, but decreased the expression of kelch-like ECH-associated protein-1; however, the inhibition of HO-1 activity by zinc protoporphyrin abolished the antioxidant potential induced by EESS against H2O2-mediated oxidative stress.	zinc protoporphyrin	332-351	heme oxygenase 1	Homo sapiens	178-182
29874784-8	2018	In addition, EESS increased not only expression, but also phosphorylation of nuclear factor-erythroid 2 related factor 2 (Nrf2), and promoted the expression of heme oxygenase-1 (HO-1), a critical target enzyme of Nrf2, but decreased the expression of kelch-like ECH-associated protein-1; however, the inhibition of HO-1 activity by zinc protoporphyrin abolished the antioxidant potential induced by EESS against H2O2-mediated oxidative stress.	Hydrogen Peroxide	412-416	heme oxygenase 1	Homo sapiens	160-176
29874784-8	2018	In addition, EESS increased not only expression, but also phosphorylation of nuclear factor-erythroid 2 related factor 2 (Nrf2), and promoted the expression of heme oxygenase-1 (HO-1), a critical target enzyme of Nrf2, but decreased the expression of kelch-like ECH-associated protein-1; however, the inhibition of HO-1 activity by zinc protoporphyrin abolished the antioxidant potential induced by EESS against H2O2-mediated oxidative stress.	Hydrogen Peroxide	412-416	heme oxygenase 1	Homo sapiens	178-182
29626606-6	2018	Moreover, curcumin markedly enhanced the translocation of Nrf2 from the cytoplasm to the nucleus, proved by the results of western blot and immunofluorescence, subsequently increased the expression of downstream factors such as heme oxygenase 1 (HO1) and NAD(P)H: quinone oxidoreductase 1 (NQO1) and prevented the decline of antioxidant enzyme activities.	Curcumin	10-18	heme oxygenase 1	Homo sapiens	228-244
29626606-6	2018	Moreover, curcumin markedly enhanced the translocation of Nrf2 from the cytoplasm to the nucleus, proved by the results of western blot and immunofluorescence, subsequently increased the expression of downstream factors such as heme oxygenase 1 (HO1) and NAD(P)H: quinone oxidoreductase 1 (NQO1) and prevented the decline of antioxidant enzyme activities.	Curcumin	10-18	heme oxygenase 1	Homo sapiens	246-249
29704732-5	2018	However, pretreatment with NAM (inhibitor of SIRT1) not only inhibited the effect of paeonol on reducing nuclear translocation of NF-kappaBp65, but also inhibited the effect of paeonol on promoting the expression of nuclear Nrf2, NQO1 and HO-1.	paeonol	85-92	heme oxygenase 1	Homo sapiens	239-243
29704732-5	2018	However, pretreatment with NAM (inhibitor of SIRT1) not only inhibited the effect of paeonol on reducing nuclear translocation of NF-kappaBp65, but also inhibited the effect of paeonol on promoting the expression of nuclear Nrf2, NQO1 and HO-1.	paeonol	177-184	heme oxygenase 1	Homo sapiens	239-243
29477863-7	2018	These divergences in ROS production seem to be correlated with the different extension of intracellular signaling pathways activation and, by consequence, with distinct transcription kinetics of genes such as HMOX1, IL8, IL1B and CD86.	Reactive Oxygen Species	21-24	heme oxygenase 1	Homo sapiens	209-214
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Heme	96-100	heme oxygenase 1	Homo sapiens	0-16
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Heme	96-100	heme oxygenase 1	Homo sapiens	18-22
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Biliverdine	106-116	heme oxygenase 1	Homo sapiens	0-16
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Biliverdine	106-116	heme oxygenase 1	Homo sapiens	18-22
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Iron	123-127	heme oxygenase 1	Homo sapiens	0-16
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Iron	123-127	heme oxygenase 1	Homo sapiens	18-22
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Carbon Monoxide	133-148	heme oxygenase 1	Homo sapiens	0-16
29772541-2	2018	Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide.	Carbon Monoxide	133-148	heme oxygenase 1	Homo sapiens	18-22
29532858-8	2018	All of the results indicated that hydrogen decreased the levels of reactive oxygen species, 8-iso-prostaglandin F2alpha and malondialdehyde, and promoted the UVB exposure-induced expression of PI3K, Akt, Nrf2 and heme oxygenase-1 in HaCaT cells.	Hydrogen	34-42	heme oxygenase 1	Homo sapiens	213-229
29532858-10	2018	Therefore, hydrogen effectively protects cells from UVB radiation-induced oxidative stress by inhibiting Nrf2/HO-1 activation through the PI3K/Akt signaling pathway.	Hydrogen	11-19	heme oxygenase 1	Homo sapiens	110-114
29194609-10	2018	Based on gene expression data of withaferin-A and salbutamol, we identified HMOX1 and STC1 as being strongly differentially expressed .	withaferin A	33-45	heme oxygenase 1	Homo sapiens	76-81
29194609-10	2018	Based on gene expression data of withaferin-A and salbutamol, we identified HMOX1 and STC1 as being strongly differentially expressed .	Albuterol	50-60	heme oxygenase 1	Homo sapiens	76-81
29668263-7	2018	In addition, ALA treatment inhibited reactive oxygen species generation induced by Abeta25-35 through the enhancement of the nuclear factor-erythroid 2-related factor-2 (Nrf-2) protein levels and subsequent induction of heme-oxygenase-1 (HO-1) expression in C6 glial cells dose- and time-dependently.	alpha-Linolenic Acid	13-16	heme oxygenase 1	Homo sapiens	220-236
29783634-0	2018	Novel Structural Insight into Inhibitors of Heme Oxygenase-1 (HO-1) by New Imidazole-Based Compounds: Biochemical and In Vitro Anticancer Activity Evaluation.	imidazole	75-84	heme oxygenase 1	Homo sapiens	44-60
29783634-0	2018	Novel Structural Insight into Inhibitors of Heme Oxygenase-1 (HO-1) by New Imidazole-Based Compounds: Biochemical and In Vitro Anticancer Activity Evaluation.	imidazole	75-84	heme oxygenase 1	Homo sapiens	62-66
29783634-1	2018	In this paper, the design, synthesis, and molecular modeling of a new azole-based HO-1 inhibitors was reported, using compound 1 as a lead compound, in which an imidazole moiety is linked to a hydrophobic group by means of an ethanolic spacer.	Azoles	70-75	heme oxygenase 1	Homo sapiens	82-86
29783634-1	2018	In this paper, the design, synthesis, and molecular modeling of a new azole-based HO-1 inhibitors was reported, using compound 1 as a lead compound, in which an imidazole moiety is linked to a hydrophobic group by means of an ethanolic spacer.	imidazole	161-170	heme oxygenase 1	Homo sapiens	82-86
29783634-4	2018	Molecular modeling studies confirmed a consolidated binding mode in which the nitrogen of the imidazolyl moiety coordinated the heme ferrous iron, meanwhile the hydrophobic groups were located in the western region of HO-1 binding pocket.	Nitrogen	78-86	heme oxygenase 1	Homo sapiens	218-222
29783634-4	2018	Molecular modeling studies confirmed a consolidated binding mode in which the nitrogen of the imidazolyl moiety coordinated the heme ferrous iron, meanwhile the hydrophobic groups were located in the western region of HO-1 binding pocket.	imidazolyl	94-104	heme oxygenase 1	Homo sapiens	218-222
29783634-4	2018	Molecular modeling studies confirmed a consolidated binding mode in which the nitrogen of the imidazolyl moiety coordinated the heme ferrous iron, meanwhile the hydrophobic groups were located in the western region of HO-1 binding pocket.	Heme	128-132	heme oxygenase 1	Homo sapiens	218-222
29783634-4	2018	Molecular modeling studies confirmed a consolidated binding mode in which the nitrogen of the imidazolyl moiety coordinated the heme ferrous iron, meanwhile the hydrophobic groups were located in the western region of HO-1 binding pocket.	Iron	141-145	heme oxygenase 1	Homo sapiens	218-222
29668263-7	2018	In addition, ALA treatment inhibited reactive oxygen species generation induced by Abeta25-35 through the enhancement of the nuclear factor-erythroid 2-related factor-2 (Nrf-2) protein levels and subsequent induction of heme-oxygenase-1 (HO-1) expression in C6 glial cells dose- and time-dependently.	alpha-Linolenic Acid	13-16	heme oxygenase 1	Homo sapiens	238-242
29668263-9	2018	In conclusion, effects of ALA on Abeta degradation were shown to be mediated through inhibition of inflammatory responses and activation of antioxidative system, Nrf-2/HO-1 signaling pathway, in C6 glial cells.	alpha-Linolenic Acid	26-29	heme oxygenase 1	Homo sapiens	168-172
29491190-9	2018	Results: Our results demonstrate that pre-treatment and post-treatment with glutamine promoted melanocyte viability, increased levels of superoxide dismutase, glutathione-S-transferase and bcl-2, decreased levels of reactive oxygen species, malondialdehyde, bax and caspase-3, and enhanced nuclear factor-E2-related factor 2, heme oxygenase-1, and heat shock protein 70 expression in a dose dependent manner.	Glutamine	76-85	heme oxygenase 1	Homo sapiens	298-342
29461260-5	2018	Heme may increase host susceptibility to infections by inducing heme oxygenase 1 (HO-1) in immature neutrophils, thereby inhibiting oxidative burst required for clearance of engulfed bacteria.	Heme	0-4	heme oxygenase 1	Homo sapiens	64-80
29461260-5	2018	Heme may increase host susceptibility to infections by inducing heme oxygenase 1 (HO-1) in immature neutrophils, thereby inhibiting oxidative burst required for clearance of engulfed bacteria.	Heme	0-4	heme oxygenase 1	Homo sapiens	82-86
29644357-5	2018	Furthermore, MH suppressed the Nrf2-dependent antioxidant enzyme expression (superoxide dismutase (SOD), catalase and heme oxygenase-1) and the activity of SOD, catalase, glutathione peroxidase and glutathione reductase.	mh	13-15	heme oxygenase 1	Homo sapiens	118-134
28989083-14	2018	Furthermore, hNSCs co-treated with resveratrol were significantly rescued from Abeta-induced oxidative stress, which correlated with reversal of the Abeta-induced mRNA decrease in oxidative defense genes (SOD-1, NRF2, Gpx1, Catalase, GSH and HO-1).	Resveratrol	35-46	heme oxygenase 1	Homo sapiens	242-246
29356228-0	2018	Curcuma sp.-derived dehydrocurdione induces heme oxygenase-1 through a Michael reaction between its alpha, beta-unsaturated carbonyl and Keap1.	curcuma sp.	0-11	heme oxygenase 1	Homo sapiens	44-60
29356228-0	2018	Curcuma sp.-derived dehydrocurdione induces heme oxygenase-1 through a Michael reaction between its alpha, beta-unsaturated carbonyl and Keap1.	dehydrocurdione	20-35	heme oxygenase 1	Homo sapiens	44-60
29356228-1	2018	To elucidate the anti-inflammatory mechanism of Curcuma sp., we investigated whether dehydrocurdione, a sesquiterpene contained in Curcuma sp., induces heme oxygenase (HO)-1, an antioxidative enzyme, in RAW 264.7 macrophages.	dehydrocurdione	85-100	heme oxygenase 1	Homo sapiens	152-173
29288927-9	2018	Moreover, ZYZ-803 upregulated the endogenous antioxidants, glutathione peroxidase (GPx) and heme oxygenase 1 (HO-1).	zyz-803	10-17	heme oxygenase 1	Homo sapiens	92-108
29525432-0	2018	Marliolide inhibits skin carcinogenesis by activating NRF2/ARE to induce heme oxygenase-1.	marliolide	0-10	heme oxygenase 1	Homo sapiens	73-89
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Heme	63-67	heme oxygenase 1	Homo sapiens	0-16
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Heme	63-67	heme oxygenase 1	Homo sapiens	18-22
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	0-16
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	18-22
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Carbon Monoxide	126-128	heme oxygenase 1	Homo sapiens	0-16
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Carbon Monoxide	126-128	heme oxygenase 1	Homo sapiens	18-22
29568961-10	2018	Furthermore, pretreatment with diosmetin elevated mRNA and protein expression levels of Nrf2, HO-1 and NQO1.	diosmetin	31-40	heme oxygenase 1	Homo sapiens	94-98
29568961-11	2018	The present study is the first, to the best of our knowledge, to demonstrate that activation of the Nrf2/NQO1-HO-1 signaling pathway maybe involved in the cytoprotective effects of diosmetin against oxidative stress.	diosmetin	181-190	heme oxygenase 1	Homo sapiens	110-114
29796178-0	2018	SB202190 inhibits endothelial cell apoptosis via induction of autophagy and heme oxygenase-1.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	0-8	heme oxygenase 1	Homo sapiens	76-92
29796178-2	2018	The present study therefore investigates the impact of the p38 MAPK inhibitor SB202190 on the expression of the cytoprotective enzyme heme oxygenase-1 (HO-1) as well as metabolic activity, apoptosis and autophagy of endothelial cells.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	78-86	heme oxygenase 1	Homo sapiens	134-150
29796178-2	2018	The present study therefore investigates the impact of the p38 MAPK inhibitor SB202190 on the expression of the cytoprotective enzyme heme oxygenase-1 (HO-1) as well as metabolic activity, apoptosis and autophagy of endothelial cells.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	78-86	heme oxygenase 1	Homo sapiens	152-156
29796178-4	2018	Induction of HO-1 protein expression was mimicked by SB203580, another p38 MAPK inhibitor, but not by SB202474, an inactive structural analogue of p38 MAPK inhibitors.	SB 203580	53-61	heme oxygenase 1	Homo sapiens	13-17
29796178-5	2018	HO-1 induction by both SB202190 and SB203580 was also demonstrated by analysis of mRNA expression.	SB 203580	36-44	heme oxygenase 1	Homo sapiens	0-4
29796178-7	2018	Treatment of cells with tin protoporphyrin IX (SnPPIX), a well-characterised HO-1 enzymatic inhibitor, or HO-1 siRNA left SB202190-modulated metabolic activity and autophagy virtually unaltered but caused a significant reversal of the anti-apoptotic action of SB202190.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	122-130	heme oxygenase 1	Homo sapiens	106-110
29796178-8	2018	Conversely, however, HO-1 expression by SB202190 became completely suppressed by the autophagy inhibitor bafilomycin A1.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	40-48	heme oxygenase 1	Homo sapiens	21-25
29796178-8	2018	Conversely, however, HO-1 expression by SB202190 became completely suppressed by the autophagy inhibitor bafilomycin A1.	bafilomycin	105-116	heme oxygenase 1	Homo sapiens	21-25
29796178-10	2018	Collectively, this work demonstrates SB202190 to confer upstream induction of autophagy followed by HO-1 induction resulting in potential protective effects against apoptosis.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	37-45	heme oxygenase 1	Homo sapiens	100-104
29796178-11	2018	On the other hand, our data oppose HO-1 to contribute to SB202190-mediated increases in metabolic activity and autophagy, respectively.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	57-65	heme oxygenase 1	Homo sapiens	35-39
29241092-5	2018	In addition, trehalose increased nuclear translocation of nuclear factor (erythroid-derived 2)-like 2 (Nrf2) in a p62-dependent manner and enhance expression of its downstream antioxidant factors, heme oxygenase-1 (Ho-1) and nicotinamide adenine dinucleotide phosphate quinone dehydrogenase 1 (Nqo1).	Trehalose	13-22	heme oxygenase 1	Homo sapiens	197-213
29854096-5	2018	The effects of cafestol on mitogen-activated protein kinases (MAPK), heme oxygenase-1 (HO-1), and sirtuin 1 (Sirt1) signaling pathways were examined using Western blotting and specific inhibitors.	cafestol	15-23	heme oxygenase 1	Homo sapiens	69-85
29854096-8	2018	By contrast, cafestol upregulated cyclic-strain-induced HO-1 and Sirt1 expression.	cafestol	13-21	heme oxygenase 1	Homo sapiens	56-60
29854096-10	2018	This is the first study to report that cafestol inhibited cyclic-strain-induced inflammatory molecule secretion, possibly through the activation of HO-1 and Sirt1 in endothelial cells.	cafestol	39-47	heme oxygenase 1	Homo sapiens	148-152
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	ammonium ferrous sulfate	144-148	heme oxygenase 1	Homo sapiens	0-16
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	ammonium ferrous sulfate	144-148	heme oxygenase 1	Homo sapiens	18-22
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Biliverdine	155-165	heme oxygenase 1	Homo sapiens	0-16
29525432-1	2018	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin.	Biliverdine	155-165	heme oxygenase 1	Homo sapiens	18-22
29525432-3	2018	In the present study, we identified marliolide as a novel inducer of HO-1 in human normal keratinocyte HaCaT cells.	marliolide	36-46	heme oxygenase 1	Homo sapiens	69-73
29525432-4	2018	Mechanism-based studies demonstrated that the induction of HO-1 by marliolide occurred through activation of NRF2/ARE via direct binding of marliolide to KEAP1.	marliolide	67-77	heme oxygenase 1	Homo sapiens	59-63
29525432-4	2018	Mechanism-based studies demonstrated that the induction of HO-1 by marliolide occurred through activation of NRF2/ARE via direct binding of marliolide to KEAP1.	marliolide	140-150	heme oxygenase 1	Homo sapiens	59-63
29525432-5	2018	Structure-activity relationship revealed chemical moieties of marliolide critical for induction of HO-1, which renders a support for Michael reaction as a potential mechanism of action.	marliolide	62-72	heme oxygenase 1	Homo sapiens	99-103
29679467-7	2018	We also showed that nuclear factor (erythroid-derived 2)-like 2 (Nrf2)/heme oxygenase 1 (HO-1) and nuclear factor kappa B (NF-kappaB) signaling was critical for the salidroside-mediated beneficial regulation.	rhodioloside	165-176	heme oxygenase 1	Homo sapiens	71-87
29674687-3	2018	In human arterial and venous endothelial cells (EC), and in contrast to ibuprofen and naproxen, celecoxib induced the protective protein heme oxygenase-1 (HO-1).	Celecoxib	96-105	heme oxygenase 1	Homo sapiens	137-153
29674687-3	2018	In human arterial and venous endothelial cells (EC), and in contrast to ibuprofen and naproxen, celecoxib induced the protective protein heme oxygenase-1 (HO-1).	Celecoxib	96-105	heme oxygenase 1	Homo sapiens	155-159
29674687-4	2018	Celecoxib derivative 2,5-dimethyl-celecoxib (DMC) which lacks COX-2 inhibition also upregulated HO-1, implicating a COX-2-independent mechanism.	Celecoxib	0-9	heme oxygenase 1	Homo sapiens	96-100
29674687-4	2018	Celecoxib derivative 2,5-dimethyl-celecoxib (DMC) which lacks COX-2 inhibition also upregulated HO-1, implicating a COX-2-independent mechanism.	2,5-dimethylcelecoxib	21-43	heme oxygenase 1	Homo sapiens	96-100
29674687-4	2018	Celecoxib derivative 2,5-dimethyl-celecoxib (DMC) which lacks COX-2 inhibition also upregulated HO-1, implicating a COX-2-independent mechanism.	2,5-dimethylcelecoxib	45-48	heme oxygenase 1	Homo sapiens	96-100
29674687-9	2018	This attenuated VCAM-1 upregulation via induction of HO-1, a response reproduced by DMC but not ibuprofen or naproxen.	2,5-dimethylcelecoxib	84-87	heme oxygenase 1	Homo sapiens	53-57
29765448-8	2018	Moreover, it was demonstrated that HO-1 overexpression significantly inhibited the hypoxia-promoted STAT3 phosphorylation (Tyr 705).	Tyrosine	123-126	heme oxygenase 1	Homo sapiens	35-39
29543451-4	2018	With the exception of DeltaNOD, the presence of an intact catechol structure was obligatory for the inhibition of VCAM-1 and the induction of HO-1 expression.	catechol	58-66	heme oxygenase 1	Homo sapiens	142-146
29524413-0	2018	Heme oxygenase-1/carbon monoxide axis suppresses transforming growth factor-beta1-induced growth inhibition by increasing ERK1/2-mediated phosphorylation of Smad3 at Thr-179 in human hepatocellular carcinoma cell lines.	Carbon Monoxide	17-32	heme oxygenase 1	Homo sapiens	0-16
29524413-0	2018	Heme oxygenase-1/carbon monoxide axis suppresses transforming growth factor-beta1-induced growth inhibition by increasing ERK1/2-mediated phosphorylation of Smad3 at Thr-179 in human hepatocellular carcinoma cell lines.	Threonine	166-169	heme oxygenase 1	Homo sapiens	0-16
29524413-4	2018	Moreover, TGF-beta1-induced cell cycle arrest and up-regulation of cyclin-dependent kinase inhibitors in HCC cell lines were significantly attenuated by overexpression of HO-1 or treatment with tricarbonyldichlororuthenium(II) dimer ([Ru(CO)3Cl2]2, suggesting an inhibitory role of the HO-1/CO axis in TGF-beta signaling to growth inhibition in HCC cell lines.	tricarbonyldichlororuthenium(ii	194-225	heme oxygenase 1	Homo sapiens	286-290
29524413-4	2018	Moreover, TGF-beta1-induced cell cycle arrest and up-regulation of cyclin-dependent kinase inhibitors in HCC cell lines were significantly attenuated by overexpression of HO-1 or treatment with tricarbonyldichlororuthenium(II) dimer ([Ru(CO)3Cl2]2, suggesting an inhibitory role of the HO-1/CO axis in TGF-beta signaling to growth inhibition in HCC cell lines.	[ru(co)3cl2	234-245	heme oxygenase 1	Homo sapiens	171-175
29524413-6	2018	Additional experiments revealed that HO-1/CO axis selectively induces phosphorylation of Smad3 at Thr-179 residue in the linker region through activation of extracellular signal-activated kinase (ERK) 1/2.	Threonine	98-101	heme oxygenase 1	Homo sapiens	37-44
29524413-7	2018	Transfection with a phospho-deficient Smad3 (T179A) mutant or treatment with FR180204, a specific inhibitor for ERK1/2, significantly reversed the inhibitory effects of HO-1 and [Ru(CO)3Cl2]2 on cell cycle arrest induced by TGF-beta1.	FR 180204	77-85	heme oxygenase 1	Homo sapiens	169-173
29524413-8	2018	These findings for the first time demonstrate that HO-1/CO axis confer resistance of HCC cells to TGF-beta growth inhibitory signal by increasing Smad3 phosphorylation at Thr-179 via ERK1/2 pathway.	Threonine	171-174	heme oxygenase 1	Homo sapiens	51-55
29652826-0	2018	Cardiovascular Mechanisms of Action of Anthocyanins May Be Associated with the Impact of Microbial Metabolites on Heme Oxygenase-1 in Vascular Smooth Muscle Cells.	Anthocyanins	39-51	heme oxygenase 1	Homo sapiens	114-130
29652826-2	2018	We aimed to explore the effects of microbial metabolites common to anthocyanins and other flavonoids on vascular smooth muscle heme oxygenase-1 (HO-1) expression.	Anthocyanins	67-79	heme oxygenase 1	Homo sapiens	127-143
29652826-2	2018	We aimed to explore the effects of microbial metabolites common to anthocyanins and other flavonoids on vascular smooth muscle heme oxygenase-1 (HO-1) expression.	Anthocyanins	67-79	heme oxygenase 1	Homo sapiens	145-149
29652826-2	2018	We aimed to explore the effects of microbial metabolites common to anthocyanins and other flavonoids on vascular smooth muscle heme oxygenase-1 (HO-1) expression.	Flavonoids	90-100	heme oxygenase 1	Homo sapiens	127-143
29652826-2	2018	We aimed to explore the effects of microbial metabolites common to anthocyanins and other flavonoids on vascular smooth muscle heme oxygenase-1 (HO-1) expression.	Flavonoids	90-100	heme oxygenase 1	Homo sapiens	145-149
29652826-5	2018	The present study demonstrates that phenolic metabolites of anthocyanins differentially affect HO-1 activity, often having additive, synergistic or nullifying effects.	Anthocyanins	60-72	heme oxygenase 1	Homo sapiens	95-99
29437594-2	2018	Patrolling monocytes, which normally scavenge damaged cells and debris from the vasculature, express higher levels of anti-inflammatory heme oxygenase 1 (HO-1), a heme degrading enzyme.	Heme	136-140	heme oxygenase 1	Homo sapiens	154-158
29437594-4	2018	We found that a mean 37% of patrolling monocytes from SCD patients express very high levels of HO-1 (HO-1hi) vs 6% in healthy controls and demonstrated that HO-1hi expression was dependent on uptake of heme-exposed endothelium.	Heme	202-206	heme oxygenase 1	Homo sapiens	95-99
29437594-4	2018	We found that a mean 37% of patrolling monocytes from SCD patients express very high levels of HO-1 (HO-1hi) vs 6% in healthy controls and demonstrated that HO-1hi expression was dependent on uptake of heme-exposed endothelium.	Heme	202-206	heme oxygenase 1	Homo sapiens	101-107
29437594-4	2018	We found that a mean 37% of patrolling monocytes from SCD patients express very high levels of HO-1 (HO-1hi) vs 6% in healthy controls and demonstrated that HO-1hi expression was dependent on uptake of heme-exposed endothelium.	Heme	202-206	heme oxygenase 1	Homo sapiens	157-163
29765448-9	2018	Conclusions: HO-1 was overexpressed in PE placenta, in association with reduced STAT3 phosphorylation (Tyr 705).	Tyrosine	103-106	heme oxygenase 1	Homo sapiens	13-17
29765448-11	2018	Thus, we speculate that overexpressed HO-1 might contribute to the reduced STAT3 phosphorylation (Tyr 705) and the pathogenesis of preeclampsia.	Tyrosine	98-101	heme oxygenase 1	Homo sapiens	38-42
29471244-0	2018	Two sesquiterpene aminoquinones protect against oxidative injury in HaCaT keratinocytes via activation of AMPKalpha/ERK-Nrf2/ARE/HO-1 signaling.	sesquiterpene aminoquinones	4-31	heme oxygenase 1	Homo sapiens	129-133
29191105-3	2018	Curcumin dose-dependently inhibited TCDD-induced expression of phase I enzyme cytochrome P450 1A1 (CYP1A1) and phase II enzymes NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase 1 (HO-1) but not tert-butyl hydroquinone-induced NQO1 and HO-1, suggesting that curcumin inhibited only AhR pathway, but not Nrf2 one directly.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	172-188
29191105-3	2018	Curcumin dose-dependently inhibited TCDD-induced expression of phase I enzyme cytochrome P450 1A1 (CYP1A1) and phase II enzymes NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase 1 (HO-1) but not tert-butyl hydroquinone-induced NQO1 and HO-1, suggesting that curcumin inhibited only AhR pathway, but not Nrf2 one directly.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	190-194
29191105-3	2018	Curcumin dose-dependently inhibited TCDD-induced expression of phase I enzyme cytochrome P450 1A1 (CYP1A1) and phase II enzymes NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase 1 (HO-1) but not tert-butyl hydroquinone-induced NQO1 and HO-1, suggesting that curcumin inhibited only AhR pathway, but not Nrf2 one directly.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	245-249
29191105-3	2018	Curcumin dose-dependently inhibited TCDD-induced expression of phase I enzyme cytochrome P450 1A1 (CYP1A1) and phase II enzymes NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase 1 (HO-1) but not tert-butyl hydroquinone-induced NQO1 and HO-1, suggesting that curcumin inhibited only AhR pathway, but not Nrf2 one directly.	Polychlorinated Dibenzodioxins	36-40	heme oxygenase 1	Homo sapiens	172-188
29191105-3	2018	Curcumin dose-dependently inhibited TCDD-induced expression of phase I enzyme cytochrome P450 1A1 (CYP1A1) and phase II enzymes NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase 1 (HO-1) but not tert-butyl hydroquinone-induced NQO1 and HO-1, suggesting that curcumin inhibited only AhR pathway, but not Nrf2 one directly.	Polychlorinated Dibenzodioxins	36-40	heme oxygenase 1	Homo sapiens	190-194
29191105-3	2018	Curcumin dose-dependently inhibited TCDD-induced expression of phase I enzyme cytochrome P450 1A1 (CYP1A1) and phase II enzymes NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase 1 (HO-1) but not tert-butyl hydroquinone-induced NQO1 and HO-1, suggesting that curcumin inhibited only AhR pathway, but not Nrf2 one directly.	Polychlorinated Dibenzodioxins	36-40	heme oxygenase 1	Homo sapiens	245-249
29471244-11	2018	SIGNIFICANCE: DAs provided cytoprotective effects against H2O2-induced cytotoxicity by activation of the Nrf2/ARE/HO-1 pathway via phosphorylation of AMPKalpha and ERK.	Hydrogen Peroxide	58-62	heme oxygenase 1	Homo sapiens	114-118
29421327-1	2018	Our previous study has shown heme oxygenase-1 (HO-1) protects human lens epithelial cells (LECs) against H2O2-induced oxidative stress and apoptosis.	Hydrogen Peroxide	105-109	heme oxygenase 1	Homo sapiens	29-45
29351417-9	2018	Zn2+ also regulated inflammation-related key molecules such as heme oxygenase-1, selectin L, IL-10, and platelet endothelial cell adhesion molecule 1, as well as vascular tone-related prostaglandin I2 synthase and nitric oxide synthase-3.	Zinc	0-4	heme oxygenase 1	Homo sapiens	63-79
29339440-4	2018	Single-cell RNA sequencing analysis, tumor microarray, and clinical survival data from breast cancer patients were used to support the clinical relevance of our observations.Results: We demonstrate that SnMP inhibits immune suppression of chemotherapy-elicited CD8+ T cells by targeting myeloid HO-1 activity in the tumor microenvironment.	tin mesoporphyrin	203-207	heme oxygenase 1	Homo sapiens	295-299
29421327-1	2018	Our previous study has shown heme oxygenase-1 (HO-1) protects human lens epithelial cells (LECs) against H2O2-induced oxidative stress and apoptosis.	Hydrogen Peroxide	105-109	heme oxygenase 1	Homo sapiens	47-51
29436680-16	2018	Overall, these data indicated that curcumin activates the Nrf2-ARE signaling pathway and upregulates HO-1 expression, which mediates SR-BI and ABCA1 expression and thereby increases cholesterol efflux.	Cholesterol	182-193	heme oxygenase 1	Homo sapiens	101-105
29302043-3	2018	Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe).	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
29302043-3	2018	Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe).	Bilirubin	108-117	heme oxygenase 1	Homo sapiens	0-16
29302043-3	2018	Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe).	Carbon Monoxide	119-134	heme oxygenase 1	Homo sapiens	0-16
29302043-3	2018	Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe).	Carbon Monoxide	136-138	heme oxygenase 1	Homo sapiens	0-16
29302043-3	2018	Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe).	Iron	149-153	heme oxygenase 1	Homo sapiens	0-16
29302043-3	2018	Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe).	Iron	155-157	heme oxygenase 1	Homo sapiens	0-16
29436680-0	2018	Curcumin increases cholesterol efflux via heme oxygenase-1-mediated ABCA1 and SR-BI expression in macrophages.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	42-58
29436680-0	2018	Curcumin increases cholesterol efflux via heme oxygenase-1-mediated ABCA1 and SR-BI expression in macrophages.	Cholesterol	19-30	heme oxygenase 1	Homo sapiens	42-58
29436680-9	2018	Additionally, curcumin significantly upregulated HO-1 expression.	Curcumin	14-22	heme oxygenase 1	Homo sapiens	49-53
29436680-10	2018	The HO-1 inhibitor (zinc protoporphyrin) partly blocked this effect.	zinc protoporphyrin	20-39	heme oxygenase 1	Homo sapiens	4-8
29436680-12	2018	HO-1 small interfering (si)RNA partly abolished the increased SR-BI and ABCA1 expression induced by curcumin.	Curcumin	100-108	heme oxygenase 1	Homo sapiens	0-4
29436680-14	2018	Nrf2 siRNA successfully inhibited the curcumin-induced HO-1 expression.	Curcumin	38-46	heme oxygenase 1	Homo sapiens	55-59
29436680-16	2018	Overall, these data indicated that curcumin activates the Nrf2-ARE signaling pathway and upregulates HO-1 expression, which mediates SR-BI and ABCA1 expression and thereby increases cholesterol efflux.	Curcumin	35-43	heme oxygenase 1	Homo sapiens	101-105
29411263-0	2018	Naringenin Exerts Anti-inflammatory Effects in Paraquat-Treated SH-SY5Y Cells Through a Mechanism Associated with the Nrf2/HO-1 Axis.	naringenin	0-10	heme oxygenase 1	Homo sapiens	123-127
28456938-6	2018	Additionally, resveratrol prevented the LPS-induced increase in the intracellular reactive oxygen species (ROS) as well as the decrease in glutathione (GSH) levels and in glutamate cysteine ligase (GCL) activity, through Nrf2/HO-1 signaling pathways.	Resveratrol	14-25	heme oxygenase 1	Homo sapiens	226-230
28456938-4	2018	In this sense, we have demonstrated that resveratrol has a protective effect on oligodendroglial functionality against lipopolysaccharide (LPS)-mediated cytotoxicity and that its glioprotective mechanism involves the nuclear factor erythroid 2-related factor 2 (Nrf2) and HO-1 pathways.	Resveratrol	41-52	heme oxygenase 1	Homo sapiens	272-276
28497200-7	2018	Furthermore, BTZ significantly induced heme oxygenase-1 as a result of increased oxidative stress and such overexpression was prevented by concomitant treatment with ALA.	Bortezomib	13-16	heme oxygenase 1	Homo sapiens	39-55
28497200-7	2018	Furthermore, BTZ significantly induced heme oxygenase-1 as a result of increased oxidative stress and such overexpression was prevented by concomitant treatment with ALA.	ala	166-169	heme oxygenase 1	Homo sapiens	39-55
29411263-0	2018	Naringenin Exerts Anti-inflammatory Effects in Paraquat-Treated SH-SY5Y Cells Through a Mechanism Associated with the Nrf2/HO-1 Axis.	Paraquat	47-55	heme oxygenase 1	Homo sapiens	123-127
29411263-2	2018	NGN is a potent inducer of the nuclear factor erythroid 2-related factor 2 (Nrf2) and upregulates the expression of heme oxygenase-1 (HO-1), an enzyme exhibiting both antioxidant and anti-inflammatory effects.	naringenin	0-3	heme oxygenase 1	Homo sapiens	116-132
29411263-2	2018	NGN is a potent inducer of the nuclear factor erythroid 2-related factor 2 (Nrf2) and upregulates the expression of heme oxygenase-1 (HO-1), an enzyme exhibiting both antioxidant and anti-inflammatory effects.	naringenin	0-3	heme oxygenase 1	Homo sapiens	134-138
29411263-9	2018	The anti-apoptotic and anti-inflammatory effects promoted by NGN were abolished by ZnPP IX (a specific inhibitor of HO-1) or by knockdown of Nrf2 by small interfering RNA (siRNA).	naringenin	61-64	heme oxygenase 1	Homo sapiens	116-120
29411263-9	2018	The anti-apoptotic and anti-inflammatory effects promoted by NGN were abolished by ZnPP IX (a specific inhibitor of HO-1) or by knockdown of Nrf2 by small interfering RNA (siRNA).	zinc protoporphyrin	83-90	heme oxygenase 1	Homo sapiens	116-120
29411263-10	2018	Therefore, NGN induced anti-inflammatory effects in PQ-treated SH-SY5Y cells by a mechanism associated with the Nrf2/HO-1 signaling pathway.	naringenin	11-14	heme oxygenase 1	Homo sapiens	117-121
29526395-0	2018	Up-regulation of HO-1 by Nrf2 activation protects against palmitic acid-induced ROS increase in human neuroblastoma BE(2)-M17 cells.	Palmitic Acid	58-71	heme oxygenase 1	Homo sapiens	17-21
29526395-10	2018	Therefore, our results suggest that up-regulation of HO-1 in PA-treated neurons is a compensatory response to ROS increase and that increasing HO-1 expression by Nrf2 activation can prevent the process of ROS production in PA-treated neurons.	Reactive Oxygen Species	110-113	heme oxygenase 1	Homo sapiens	53-57
29411263-10	2018	Therefore, NGN induced anti-inflammatory effects in PQ-treated SH-SY5Y cells by a mechanism associated with the Nrf2/HO-1 signaling pathway.	Paraquat	52-54	heme oxygenase 1	Homo sapiens	117-121
29526395-10	2018	Therefore, our results suggest that up-regulation of HO-1 in PA-treated neurons is a compensatory response to ROS increase and that increasing HO-1 expression by Nrf2 activation can prevent the process of ROS production in PA-treated neurons.	Reactive Oxygen Species	205-208	heme oxygenase 1	Homo sapiens	53-57
29526395-0	2018	Up-regulation of HO-1 by Nrf2 activation protects against palmitic acid-induced ROS increase in human neuroblastoma BE(2)-M17 cells.	Beryllium	116-118	heme oxygenase 1	Homo sapiens	17-21
29743974-0	2018	Simvastatin Treatment Upregulates HO-1 in Patients with Abdominal Aortic Aneurysm but Independently of Nrf2.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	34-38
29526395-2	2018	Extracellular signal regulated kinase (ERK)/nuclear factor erythroid-2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) is a ROS response pathway.	Reactive Oxygen Species	124-127	heme oxygenase 1	Homo sapiens	95-111
29526395-2	2018	Extracellular signal regulated kinase (ERK)/nuclear factor erythroid-2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) is a ROS response pathway.	Reactive Oxygen Species	124-127	heme oxygenase 1	Homo sapiens	113-117
29526395-4	2018	We hypothesized that the up-regulation of HO-1 is compensatory for response to fatty acid-induced oxidative stress but not enough to reduce ROS levels.	Fatty Acids	79-89	heme oxygenase 1	Homo sapiens	42-46
29526395-5	2018	We evaluated the anti-ROS effect of HO-1 and the involved pathway in palmitic acid (PA)-treated human neuroblastoma BE(2)-M17 cells.	Reactive Oxygen Species	22-25	heme oxygenase 1	Homo sapiens	36-40
29526395-5	2018	We evaluated the anti-ROS effect of HO-1 and the involved pathway in palmitic acid (PA)-treated human neuroblastoma BE(2)-M17 cells.	Palmitic Acid	84-86	heme oxygenase 1	Homo sapiens	36-40
29526395-5	2018	We evaluated the anti-ROS effect of HO-1 and the involved pathway in palmitic acid (PA)-treated human neuroblastoma BE(2)-M17 cells.	Beryllium	116-118	heme oxygenase 1	Homo sapiens	36-40
29526395-6	2018	As expected, PA-induced ROS increase was accompanied by activation of the ERK-Nrf2-HO-1 pathway, as demonstrated by an increase in ERK phosphorylation, Nrf2 phosphorylation and nuclear accumulation, and HO-1 expression at the mRNA and protein levels, in a PA-dose-dependent manner.	Palmitic Acid	13-15	heme oxygenase 1	Homo sapiens	83-87
29526395-6	2018	As expected, PA-induced ROS increase was accompanied by activation of the ERK-Nrf2-HO-1 pathway, as demonstrated by an increase in ERK phosphorylation, Nrf2 phosphorylation and nuclear accumulation, and HO-1 expression at the mRNA and protein levels, in a PA-dose-dependent manner.	Palmitic Acid	13-15	heme oxygenase 1	Homo sapiens	203-207
29526395-6	2018	As expected, PA-induced ROS increase was accompanied by activation of the ERK-Nrf2-HO-1 pathway, as demonstrated by an increase in ERK phosphorylation, Nrf2 phosphorylation and nuclear accumulation, and HO-1 expression at the mRNA and protein levels, in a PA-dose-dependent manner.	Palmitic Acid	256-258	heme oxygenase 1	Homo sapiens	83-87
29526395-7	2018	In contrast, administration of the ROS scavenger NAC significantly reduced the levels of PA-regulated ROS and HO-1 protein.	Reactive Oxygen Species	35-38	heme oxygenase 1	Homo sapiens	110-114
29526395-7	2018	In contrast, administration of the ROS scavenger NAC significantly reduced the levels of PA-regulated ROS and HO-1 protein.	Palmitic Acid	89-91	heme oxygenase 1	Homo sapiens	110-114
29526395-8	2018	However, the ERK inhibitor U0126 not only reversed the activating effect of PA on the ERK-Nrf2-HO-1 pathway but also aggravated PA-induced ROS.	U 0126	27-32	heme oxygenase 1	Homo sapiens	95-99
29526395-8	2018	However, the ERK inhibitor U0126 not only reversed the activating effect of PA on the ERK-Nrf2-HO-1 pathway but also aggravated PA-induced ROS.	Palmitic Acid	76-78	heme oxygenase 1	Homo sapiens	95-99
29526395-9	2018	Furthermore, the Nrf2-specific activator NK-252 significantly increased PA-up-regulated HO-1 protein and alleviated PA-induced ROS.	Palmitic Acid	72-74	heme oxygenase 1	Homo sapiens	88-92
29526395-10	2018	Therefore, our results suggest that up-regulation of HO-1 in PA-treated neurons is a compensatory response to ROS increase and that increasing HO-1 expression by Nrf2 activation can prevent the process of ROS production in PA-treated neurons.	Palmitic Acid	61-63	heme oxygenase 1	Homo sapiens	53-57
29526395-10	2018	Therefore, our results suggest that up-regulation of HO-1 in PA-treated neurons is a compensatory response to ROS increase and that increasing HO-1 expression by Nrf2 activation can prevent the process of ROS production in PA-treated neurons.	Reactive Oxygen Species	205-208	heme oxygenase 1	Homo sapiens	143-147
29526395-10	2018	Therefore, our results suggest that up-regulation of HO-1 in PA-treated neurons is a compensatory response to ROS increase and that increasing HO-1 expression by Nrf2 activation can prevent the process of ROS production in PA-treated neurons.	Palmitic Acid	223-225	heme oxygenase 1	Homo sapiens	53-57
29526395-10	2018	Therefore, our results suggest that up-regulation of HO-1 in PA-treated neurons is a compensatory response to ROS increase and that increasing HO-1 expression by Nrf2 activation can prevent the process of ROS production in PA-treated neurons.	Palmitic Acid	223-225	heme oxygenase 1	Homo sapiens	143-147
29425821-0	2018	MMP9 is involved in HO-1-mediated upregulation of apical junctional complex in Caco-2 cells under oxygen-glucose deprivation.	oxygen-glucose	98-112	heme oxygenase 1	Homo sapiens	20-24
29425821-2	2018	This study was the first to explore the expression of apical junctional complex (AJC) induced by heme oxygenase-1 (HO-1) in Caco-2 cells in oxygen-glucose deprivation (OGD) models.	oxygen-glucose	140-154	heme oxygenase 1	Homo sapiens	97-113
29425821-2	2018	This study was the first to explore the expression of apical junctional complex (AJC) induced by heme oxygenase-1 (HO-1) in Caco-2 cells in oxygen-glucose deprivation (OGD) models.	oxygen-glucose	140-154	heme oxygenase 1	Homo sapiens	115-119
29454190-0	2018	Potholing of the hydrophobic heme oxygenase-1 western region for the search of potent and selective imidazole-based inhibitors.	imidazole	100-109	heme oxygenase 1	Homo sapiens	29-45
29743974-6	2018	Simvastatin treatment increased HO-1 protein level in AAA, both in endothelial cells (ECs) and in smooth muscle cells (SMCs), but increased Nrf2 localization was restricted only to vasa vasorum.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	32-36
29743974-8	2018	In vitro studies showed that simvastatin raises HO-1 protein level slightly in ECs and to much higher extent in SMCs, which is not related to Nrf2/ARE activation, although HMOX1 expression is upregulated by simvastatin in both cell types.	Simvastatin	29-40	heme oxygenase 1	Homo sapiens	48-52
29743974-8	2018	In vitro studies showed that simvastatin raises HO-1 protein level slightly in ECs and to much higher extent in SMCs, which is not related to Nrf2/ARE activation, although HMOX1 expression is upregulated by simvastatin in both cell types.	Simvastatin	207-218	heme oxygenase 1	Homo sapiens	172-177
29743974-9	2018	In conclusion, simvastatin-induced modulation of HO-1 level in ECs and SMCs in vitro is not related to Nrf2/ARE activity.	Simvastatin	15-26	heme oxygenase 1	Homo sapiens	49-53
29355553-6	2018	Reb-A treatment induced nuclear factor erythroid-derived 2-like 2 (Nrf2) activation and antioxidant response element activity, as well as the expression of heme oxygenase-1 (HO-1) and NAD(P)H quinone oxidoreductase 1 (NQO1).	rebaudioside A	0-5	heme oxygenase 1	Homo sapiens	156-172
29619425-1	2018	Background: Heme oxygenase-1 (HO-1) is a protein secreted by immune cells as a part of immune response mechanism.HO-1 can be induced by variety agents that causingoxidative stress, such as exposure to 100% oxygenat2,4 ATA pressure.It plays a vital role in maintaining cellular homeostasis.This study was conducted to identify the effect of hyperbaric oxygen exposure in cultured ofPBMCthat infected by HIV-1.	Oxygen	17-23	heme oxygenase 1	Homo sapiens	30-34
29619425-1	2018	Background: Heme oxygenase-1 (HO-1) is a protein secreted by immune cells as a part of immune response mechanism.HO-1 can be induced by variety agents that causingoxidative stress, such as exposure to 100% oxygenat2,4 ATA pressure.It plays a vital role in maintaining cellular homeostasis.This study was conducted to identify the effect of hyperbaric oxygen exposure in cultured ofPBMCthat infected by HIV-1.	Oxygen	17-23	heme oxygenase 1	Homo sapiens	113-117
29274359-8	2018	The ferroptotic process induced by hHO-1 overexpression further indicated that HO-1 is a key mediator of BAY-induced ferroptosis that operates through cellular redox regulation and iron accumulation.	Iron	181-185	heme oxygenase 1	Homo sapiens	35-40
29165873-8	2018	Concomitantly, the HO-1 byproduct CO and the cGMP analogue 8-bromoguanosine 3",5"-cyclic monophosphate (8-Br-cGMP) increased MKP-5 expression, and pretreatment with CO and 8-Br-cGMP inhibited hypoxia-induced HIF-1alpha and ET-1 expression.	8-bromoguanosino-3',5'-cyclic monophosphorothioate	104-113	heme oxygenase 1	Homo sapiens	19-23
29165873-0	2018	Andrographolide inhibits hypoxia-induced hypoxia-inducible factor 1alpha and endothelin 1 expression through the heme oxygenase 1/CO/cGMP/MKP-5 pathways in EA.hy926 cells.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	113-129
29165873-8	2018	Concomitantly, the HO-1 byproduct CO and the cGMP analogue 8-bromoguanosine 3",5"-cyclic monophosphate (8-Br-cGMP) increased MKP-5 expression, and pretreatment with CO and 8-Br-cGMP inhibited hypoxia-induced HIF-1alpha and ET-1 expression.	Carbon Monoxide	34-36	heme oxygenase 1	Homo sapiens	19-23
29165873-7	2018	Andrographolide enhanced HO-1 and MKP-5 expression and cellular cGMP content in addition to inhibiting hypoxia-induced ROS generation.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	25-29
29165873-8	2018	Concomitantly, the HO-1 byproduct CO and the cGMP analogue 8-bromoguanosine 3",5"-cyclic monophosphate (8-Br-cGMP) increased MKP-5 expression, and pretreatment with CO and 8-Br-cGMP inhibited hypoxia-induced HIF-1alpha and ET-1 expression.	8-bromoguanosino-3',5'-cyclic monophosphorothioate	172-181	heme oxygenase 1	Homo sapiens	19-23
29165873-9	2018	Transfection of HO-1 siRNA or pretreatment with the HO-1 inhibitor ZnPP-9 or 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one, a specific inhibitor of soluble guanylate cyclase, reduced andrographolide-induced MKP-5 expression.	zinc protoporphyrin	67-73	heme oxygenase 1	Homo sapiens	52-56
29165873-11	2018	The inhibition of hypoxia-induced HIF-1alpha and ET-1 expression by andrographolide is likely associated with HO-1/CO/cGMP/MKP-5 pathways, which is involved in inhibiting hypoxia-induced p38 MAPK activation.	andrographolide	68-83	heme oxygenase 1	Homo sapiens	110-117
29165873-11	2018	The inhibition of hypoxia-induced HIF-1alpha and ET-1 expression by andrographolide is likely associated with HO-1/CO/cGMP/MKP-5 pathways, which is involved in inhibiting hypoxia-induced p38 MAPK activation.	Cyclic GMP	118-122	heme oxygenase 1	Homo sapiens	110-117
29317217-0	2018	Crucial role of HO-1/IRF4-dependent apoptosis induced by panobinostat and lenalidomide in multiple myeloma.	Panobinostat	57-69	heme oxygenase 1	Homo sapiens	16-20
29168081-0	2018	High Glucose Stimulates Expression of MFHAS1 to Mitigate Inflammation via Akt/HO-1 Pathway in Human Umbilical Vein Endothelial Cells.	Glucose	5-12	heme oxygenase 1	Homo sapiens	78-82
29168081-6	2018	Our results indicated that MFHAS1 deadened high-glucose induced inflammation by activating AKT/HO-1 pathway, suggesting that MFHAS1 may act as a new therapeutic target of diabetes mellitus.	high-glucose	43-55	heme oxygenase 1	Homo sapiens	95-99
29470442-9	2018	Induction of HO-1 induced by Pc was suppressed by Go6976, a selective inhibitor of PKC alpha/beta II.	Go 6976	50-56	heme oxygenase 1	Homo sapiens	13-17
29317217-8	2018	Adding Z-DEVD-FMK, a caspase-3 inhibitor, abolished the HO-1/IRF4 reduction by panobinostat alone or in combination with lenalidomide, suggesting that caspase-3-mediated HO-1/IRF4/MYC degradation occurred.	Lenalidomide	121-133	heme oxygenase 1	Homo sapiens	170-174
29317217-10	2018	LBH589 and lenalidomide exerted synergistic effects, and LBH589 reversed the efficacy of lenalidomide on the resistance of CD138+ primary MM cells, in part due to simultaneous suppression of HO-1, IRF4 and MYC.	Panobinostat	57-63	heme oxygenase 1	Homo sapiens	191-195
29317217-10	2018	LBH589 and lenalidomide exerted synergistic effects, and LBH589 reversed the efficacy of lenalidomide on the resistance of CD138+ primary MM cells, in part due to simultaneous suppression of HO-1, IRF4 and MYC.	Lenalidomide	89-101	heme oxygenase 1	Homo sapiens	191-195
29094331-0	2018	Pterostilbene protects against uraemia serum-induced endothelial cell damage via activation of Keap1/Nrf2/HO-1 signaling.	pterostilbene	0-13	heme oxygenase 1	Homo sapiens	106-110
29094331-9	2018	Collectively, our study demonstrated that PT is effective in reducing US-evoked endothelial cell dysfunction via suppression of oxidative/nitrative stress and inflammatory response, which at least partly depended on Keap1/Nrf2/HO-1 signaling pathway.	pterostilbene	42-44	heme oxygenase 1	Homo sapiens	227-231
28861811-7	2018	Furthermore, neurotoxicity of lopinavir was blocked by pharmacological augmentation of the endogenous antioxidant heme oxygenase-1 (HO-1), expanding our previous finding that protease inhibitor-induced neurotoxicity was mediated by oxidative stress.	Lopinavir	30-39	heme oxygenase 1	Homo sapiens	114-130
29278300-6	2018	Pretreatment with the phenolic acids for 18 h results in a significant upregulation of the Nrf2-regulated antioxidant response proteins heme oxygenase 1 (HO-1) and glutamate-cysteine ligase modifier subunit (GCLM), following 6 h exposure to 2.5 mum H2 O2 .	phenolic acid	22-36	heme oxygenase 1	Homo sapiens	136-152
29278300-6	2018	Pretreatment with the phenolic acids for 18 h results in a significant upregulation of the Nrf2-regulated antioxidant response proteins heme oxygenase 1 (HO-1) and glutamate-cysteine ligase modifier subunit (GCLM), following 6 h exposure to 2.5 mum H2 O2 .	phenolic acid	22-36	heme oxygenase 1	Homo sapiens	154-158
29278300-6	2018	Pretreatment with the phenolic acids for 18 h results in a significant upregulation of the Nrf2-regulated antioxidant response proteins heme oxygenase 1 (HO-1) and glutamate-cysteine ligase modifier subunit (GCLM), following 6 h exposure to 2.5 mum H2 O2 .	Hydrogen Peroxide	249-254	heme oxygenase 1	Homo sapiens	136-152
29278300-6	2018	Pretreatment with the phenolic acids for 18 h results in a significant upregulation of the Nrf2-regulated antioxidant response proteins heme oxygenase 1 (HO-1) and glutamate-cysteine ligase modifier subunit (GCLM), following 6 h exposure to 2.5 mum H2 O2 .	Hydrogen Peroxide	249-254	heme oxygenase 1	Homo sapiens	154-158
29307774-7	2018	5-aminolevulinate synthase 1 (ALAS1), Ferrochelatase (FECH), hemeoxygenase 1 (HO-1) and ATP binding cassette subfamily G member 2 (ABCG2)) which affect production of PpIX was assessed.	protoporphyrin IX	166-170	heme oxygenase 1	Homo sapiens	61-82
29317217-0	2018	Crucial role of HO-1/IRF4-dependent apoptosis induced by panobinostat and lenalidomide in multiple myeloma.	Lenalidomide	74-86	heme oxygenase 1	Homo sapiens	16-20
29317217-7	2018	Herein, panobinostat induced acetylation of histone H3K9 and activation of caspase-3 in MM cells, being inversely correlated with the reduction of HO-1/IRF4/MYC protein levels.	Panobinostat	8-20	heme oxygenase 1	Homo sapiens	147-151
29317217-8	2018	Adding Z-DEVD-FMK, a caspase-3 inhibitor, abolished the HO-1/IRF4 reduction by panobinostat alone or in combination with lenalidomide, suggesting that caspase-3-mediated HO-1/IRF4/MYC degradation occurred.	benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone	7-17	heme oxygenase 1	Homo sapiens	56-60
29317217-8	2018	Adding Z-DEVD-FMK, a caspase-3 inhibitor, abolished the HO-1/IRF4 reduction by panobinostat alone or in combination with lenalidomide, suggesting that caspase-3-mediated HO-1/IRF4/MYC degradation occurred.	benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone	7-17	heme oxygenase 1	Homo sapiens	170-174
29317217-8	2018	Adding Z-DEVD-FMK, a caspase-3 inhibitor, abolished the HO-1/IRF4 reduction by panobinostat alone or in combination with lenalidomide, suggesting that caspase-3-mediated HO-1/IRF4/MYC degradation occurred.	Panobinostat	79-91	heme oxygenase 1	Homo sapiens	56-60
29317217-8	2018	Adding Z-DEVD-FMK, a caspase-3 inhibitor, abolished the HO-1/IRF4 reduction by panobinostat alone or in combination with lenalidomide, suggesting that caspase-3-mediated HO-1/IRF4/MYC degradation occurred.	Panobinostat	79-91	heme oxygenase 1	Homo sapiens	170-174
29317217-8	2018	Adding Z-DEVD-FMK, a caspase-3 inhibitor, abolished the HO-1/IRF4 reduction by panobinostat alone or in combination with lenalidomide, suggesting that caspase-3-mediated HO-1/IRF4/MYC degradation occurred.	Lenalidomide	121-133	heme oxygenase 1	Homo sapiens	56-60
28683566-6	2018	Overexpression of miR-92a suppresses expression of heme oxygenase-1 (HO-1), a critical cytoprotective enzyme, whereas inhibition of miR-92a increases HO-1 expression in human umbilical vein ECs (HUVECs) and db/db mouse aortas.	mir-92a	18-25	heme oxygenase 1	Homo sapiens	69-73
29381356-0	2018	Astaxanthin Induces the Nrf2/HO-1 Antioxidant Pathway in Human Umbilical Vein Endothelial Cells by Generating Trace Amounts of ROS.	astaxanthine	0-11	heme oxygenase 1	Homo sapiens	29-33
29381356-5	2018	In addition, astaxanthin increased the mRNA levels of phase II enzymes HO-1 and also promoted GSH-Px enzyme activity.	astaxanthine	13-24	heme oxygenase 1	Homo sapiens	71-75
29381356-7	2018	Knockdown of Nrf-2 by small interfering RNA inhibited HO-1 mRNA expression by 60%, indicating that the Nrf-2/ARE signaling pathway is activated by astaxanthin.	astaxanthine	147-158	heme oxygenase 1	Homo sapiens	54-58
29381356-8	2018	Our results suggest that astaxanthin activates the Nrf-2/HO-1 antioxidant pathway by generating small amounts of ROS.	astaxanthine	25-36	heme oxygenase 1	Homo sapiens	57-61
29381356-8	2018	Our results suggest that astaxanthin activates the Nrf-2/HO-1 antioxidant pathway by generating small amounts of ROS.	Reactive Oxygen Species	113-116	heme oxygenase 1	Homo sapiens	57-61
28683566-6	2018	Overexpression of miR-92a suppresses expression of heme oxygenase-1 (HO-1), a critical cytoprotective enzyme, whereas inhibition of miR-92a increases HO-1 expression in human umbilical vein ECs (HUVECs) and db/db mouse aortas.	mir-92a	18-25	heme oxygenase 1	Homo sapiens	51-67
29541348-0	2018	Protective Effect of Boswellic Acids against Doxorubicin-Induced Hepatotoxicity: Impact on Nrf2/HO-1 Defense Pathway.	boswellic acid	21-36	heme oxygenase 1	Homo sapiens	96-100
29643980-5	2018	In human keratinocytes, we found that perillaldehyde (1) inhibited BaP-induced AHR activation and ROS production, (2) inhibited BaP/AHR-mediated release of the CCL2 chemokine, and (3) activated the NRF2/HO1 antioxidant pathway.	perillaldehyde	38-52	heme oxygenase 1	Homo sapiens	203-206
29541348-0	2018	Protective Effect of Boswellic Acids against Doxorubicin-Induced Hepatotoxicity: Impact on Nrf2/HO-1 Defense Pathway.	Doxorubicin	45-56	heme oxygenase 1	Homo sapiens	96-100
29541348-8	2018	BAs increased the Nrf2 and HO-1 expression, which provided protection against DOX-induced oxidative insult.	Doxorubicin	78-81	heme oxygenase 1	Homo sapiens	27-31
29394034-7	2018	Furthermore, Fe-binding and Fe-regulatory proteins, such as hepcidin, lipocalin-2/NGAL, heme oxygenase-1, ferritin, and iron-sulfur clusters can display antitumor properties under specific conditions and in particular cancer types.	Iron	13-15	heme oxygenase 1	Homo sapiens	88-104
29560114-9	2018	Intriguingly, we observed that treatment with anti-tumoral epigenetic drugs like LBH-589 (Panobinostat) and Curcumin induced the expression of linc-PINT and HMOX1 in ALL.	Curcumin	108-116	heme oxygenase 1	Homo sapiens	157-162
29246853-7	2018	Further experiments demonstrated that cafestol increased translocation of nuclear factor erythroid 2-related factor 2 (Nrf2) and expression of enhanced heme oxygenase-1.	cafestol	38-46	heme oxygenase 1	Homo sapiens	152-168
29246853-9	2018	Cafestol"s inhibitory effects on interleukin-8 expression and cellular proliferation induced by urotensin II were significantly abrogated by heme oxygenase-1 silencing, suggesting it may be involved in mediating the effects of cafestol.	cafestol	0-8	heme oxygenase 1	Homo sapiens	141-157
29246853-9	2018	Cafestol"s inhibitory effects on interleukin-8 expression and cellular proliferation induced by urotensin II were significantly abrogated by heme oxygenase-1 silencing, suggesting it may be involved in mediating the effects of cafestol.	cafestol	227-235	heme oxygenase 1	Homo sapiens	141-157
29246853-10	2018	This study reports that cafestol inhibits urotensin II-induced interleukin-8 expression and cell proliferation via Nrf2/heme oxygenase-1-dependent mechanism in endothelial cells.	cafestol	24-32	heme oxygenase 1	Homo sapiens	120-136
29309760-9	2018	These results suggested that rosiglitazone-induced HO-1 expression is mediated through PKCalpha/AMPKalpha/p38 MAPKalpha/SIRT1-dependent deacetylation of Ac-PGC1alpha and fragmentation of NCoR/PPARgamma activation in HPAEpiCs.	Rosiglitazone	29-42	heme oxygenase 1	Homo sapiens	51-55
29309760-0	2018	Heme oxygenase-1 induction by rosiglitazone via PKCalpha/AMPKalpha/p38 MAPKalpha/SIRT1/PPARgamma pathway suppresses lipopolysaccharide-mediated pulmonary inflammation.	Rosiglitazone	30-43	heme oxygenase 1	Homo sapiens	0-16
28990726-7	2018	Moreover, DMF was able to induce an activation of manganese superoxide dismutase (MnSOD) and heme-oxygenase-1 (HO-1), decreasing the severity of oxidative stress.	Dimethyl Fumarate	10-13	heme oxygenase 1	Homo sapiens	93-109
29309760-1	2018	HO-1 (heme oxygenase-1), an antioxidant enzyme, induced by rosiglitazone (PPAR ligands) can be a potential treatment of inflammation.	Rosiglitazone	59-72	heme oxygenase 1	Homo sapiens	0-4
29309760-1	2018	HO-1 (heme oxygenase-1), an antioxidant enzyme, induced by rosiglitazone (PPAR ligands) can be a potential treatment of inflammation.	Rosiglitazone	59-72	heme oxygenase 1	Homo sapiens	6-22
29309760-2	2018	However, the mechanisms of rosiglitazone-induced HO-1 expression in human pulmonary alveolar epithelial cells (HPAEpiCs) remain largely unknown.	Rosiglitazone	27-40	heme oxygenase 1	Homo sapiens	49-53
29309760-3	2018	In this study, we found that upregulation of HO-1 in vitro or in vivo by rosiglitazone attenuated VCAM-1 gene expression and monocyte adhesion to HPAEpiCs challenged with lipopolysaccharide (LPS).	Rosiglitazone	73-86	heme oxygenase 1	Homo sapiens	45-49
29309760-4	2018	The inhibitory effects of rosiglitazone on LPS-mediated responses were reversed by transfection with HO-1 siRNA.	Rosiglitazone	26-39	heme oxygenase 1	Homo sapiens	101-105
28681934-3	2018	When human SH-SY5Y neuroblastoma cells were treated with DBL or CAPE, the expression of endoplasmic reticulum (ER) stress-related genes such as HSPA5, HYOU1, DDIT3, and SEC61b increased to a larger extent in response to CAPE treatment, while that of antioxidant genes such as HMOX1, GCLM, and NQO1 increased to a larger extent in response to DBL treatment.	3,4-dihydroxybenzalacetone	57-60	heme oxygenase 1	Homo sapiens	276-281
28681934-3	2018	When human SH-SY5Y neuroblastoma cells were treated with DBL or CAPE, the expression of endoplasmic reticulum (ER) stress-related genes such as HSPA5, HYOU1, DDIT3, and SEC61b increased to a larger extent in response to CAPE treatment, while that of antioxidant genes such as HMOX1, GCLM, and NQO1 increased to a larger extent in response to DBL treatment.	caffeic acid phenethyl ester	64-68	heme oxygenase 1	Homo sapiens	276-281
28084593-11	2018	The PB-induced antioxidant and anti-inflammatory effects are dependent on the heme oxygenate-1 (HO-1) enzyme and on the activation of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2), since HO-1 inhibition (with 0.5 muM ZnPP IX) or Nrf2 silencing (with small interfering RNA (siRNA)) abolished the effects of PB.	pinocembrin	4-6	heme oxygenase 1	Homo sapiens	217-221
28084593-12	2018	Overall, PB afforded cytoprotection by the Nrf2/HO-1 axis in H2O2-treated SH-SY5Y cells.	pinocembrin	9-11	heme oxygenase 1	Homo sapiens	48-52
28084593-0	2018	Pinocembrin Suppresses H2O2-Induced Mitochondrial Dysfunction by a Mechanism Dependent on the Nrf2/HO-1 Axis in SH-SY5Y Cells.	pinocembrin	0-11	heme oxygenase 1	Homo sapiens	99-103
28084593-11	2018	The PB-induced antioxidant and anti-inflammatory effects are dependent on the heme oxygenate-1 (HO-1) enzyme and on the activation of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2), since HO-1 inhibition (with 0.5 muM ZnPP IX) or Nrf2 silencing (with small interfering RNA (siRNA)) abolished the effects of PB.	pinocembrin	4-6	heme oxygenase 1	Homo sapiens	78-94
28084593-12	2018	Overall, PB afforded cytoprotection by the Nrf2/HO-1 axis in H2O2-treated SH-SY5Y cells.	Hydrogen Peroxide	61-65	heme oxygenase 1	Homo sapiens	48-52
28084593-11	2018	The PB-induced antioxidant and anti-inflammatory effects are dependent on the heme oxygenate-1 (HO-1) enzyme and on the activation of the transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2), since HO-1 inhibition (with 0.5 muM ZnPP IX) or Nrf2 silencing (with small interfering RNA (siRNA)) abolished the effects of PB.	pinocembrin	4-6	heme oxygenase 1	Homo sapiens	96-100
29134401-11	2018	Duloxetine also induced nuclear translocation of the Nrf2 and the expression of its target gene, HO-1.	Duloxetine Hydrochloride	0-10	heme oxygenase 1	Homo sapiens	97-101
29063347-8	2018	Furthermore, administration of the ERK inhibitor U0126 or transient (siRNA) silencing of Nrf2 blocked the protective effects of taurine on cell viability and expression levels of Nrf2 and heme oxygenase-1 (HO-1) in the CORT model of neuronal damage.	U 0126	49-54	heme oxygenase 1	Homo sapiens	188-204
29063347-8	2018	Furthermore, administration of the ERK inhibitor U0126 or transient (siRNA) silencing of Nrf2 blocked the protective effects of taurine on cell viability and expression levels of Nrf2 and heme oxygenase-1 (HO-1) in the CORT model of neuronal damage.	Taurine	128-135	heme oxygenase 1	Homo sapiens	188-204
29134401-12	2018	Finally, the HO-1 inhibitor, ZnPP, suppressed the duloxetine protective effect.	zinc protoporphyrin	29-33	heme oxygenase 1	Homo sapiens	13-17
29496161-9	2018	RESULTS: Three of the nine compounds predicted as Nrf2 activators by molecular docking, gallic acid (GA), Z-liguistilide (LIG), and senkyunolide A (SA), were confirmed with highest potency of increasing the Nrf2/ARE promoter activity and upregulating the expression of Hmox1, Nqo1 and Slc7a11.	Gallic Acid	88-99	heme oxygenase 1	Homo sapiens	269-274
29134401-0	2018	Duloxetine Protects Human Neuroblastoma Cells from Oxidative Stress-Induced Cell Death Through Akt/Nrf-2/HO-1 Pathway.	Duloxetine Hydrochloride	0-10	heme oxygenase 1	Homo sapiens	105-109
29134401-5	2018	The phosphatidylinositol 3-kinase/protein kinase B (PI3K/Akt) inhibitor LY294002 (10 microM) and the heme oxygenase 1 (HO-1) inhibitor zinc protoporphyrin IX-ZnPP (5 microM) were added to cultures 1 h prior duloxetine treatments.	zinc protoporphyrin ix-znpp	135-162	heme oxygenase 1	Homo sapiens	119-123
29496161-9	2018	RESULTS: Three of the nine compounds predicted as Nrf2 activators by molecular docking, gallic acid (GA), Z-liguistilide (LIG), and senkyunolide A (SA), were confirmed with highest potency of increasing the Nrf2/ARE promoter activity and upregulating the expression of Hmox1, Nqo1 and Slc7a11.	3-N-butyl-4,5-dihydrophthalide	132-146	heme oxygenase 1	Homo sapiens	269-274
29496161-9	2018	RESULTS: Three of the nine compounds predicted as Nrf2 activators by molecular docking, gallic acid (GA), Z-liguistilide (LIG), and senkyunolide A (SA), were confirmed with highest potency of increasing the Nrf2/ARE promoter activity and upregulating the expression of Hmox1, Nqo1 and Slc7a11.	3-N-butyl-4,5-dihydrophthalide	148-150	heme oxygenase 1	Homo sapiens	269-274
29134401-8	2018	Furthermore, the Nrf2 and HO-1 mRNA expression was carried out after 4-48 h of duloxetine treatment by qRT-PCR.	Duloxetine Hydrochloride	79-89	heme oxygenase 1	Homo sapiens	26-30
29134401-12	2018	Finally, the HO-1 inhibitor, ZnPP, suppressed the duloxetine protective effect.	Duloxetine Hydrochloride	50-60	heme oxygenase 1	Homo sapiens	13-17
29134401-13	2018	Overall, these results indicate that the mechanism of duloxetine neuroprotective action against oxidative stress and cell death might rely on the Akt/Nrf2/HO-1 pathways.	Duloxetine Hydrochloride	54-64	heme oxygenase 1	Homo sapiens	155-159
29496161-9	2018	RESULTS: Three of the nine compounds predicted as Nrf2 activators by molecular docking, gallic acid (GA), Z-liguistilide (LIG), and senkyunolide A (SA), were confirmed with highest potency of increasing the Nrf2/ARE promoter activity and upregulating the expression of Hmox1, Nqo1 and Slc7a11.	z-liguistilide	106-120	heme oxygenase 1	Homo sapiens	269-274
30231242-0	2018	Oxysophocarpine Retards the Growth and Metastasis of Oral Squamous Cell Carcinoma by Targeting the Nrf2/HO-1 Axis.	oxysophocarpine	0-15	heme oxygenase 1	Homo sapiens	104-108
29361943-0	2018	Identification of danthron as an isoform-specific inhibitor of HEME OXYGENASE-1/cytochrome P450 reductase interaction with anti-tumor activity.	danthron	18-26	heme oxygenase 1	Homo sapiens	63-79
29277159-1	2018	The study investigated whether dietary methionine (Met) affects egg weight and antioxidant status through regulating gene expression of ovalbumin (OVAL), nuclear factor erythroid 2 like 2 (Nrf2) and haem oxygenase 1 (HO-1) in laying duck breeders.	Methionine	39-49	heme oxygenase 1	Homo sapiens	199-215
29277159-1	2018	The study investigated whether dietary methionine (Met) affects egg weight and antioxidant status through regulating gene expression of ovalbumin (OVAL), nuclear factor erythroid 2 like 2 (Nrf2) and haem oxygenase 1 (HO-1) in laying duck breeders.	Methionine	39-49	heme oxygenase 1	Homo sapiens	217-221
30064139-11	2018	Zedoarondiol induced nuclear Nrf2 translocation from cytoplasm into nucleus and up-regulated expression of HO-1, NQO1, and Nrf2 in nucleus.	zedoarondiol	0-12	heme oxygenase 1	Homo sapiens	107-111
30064139-13	2018	CONCLUSION: Zedoarondiol attenuates ox-LDL-induced endothelial cells injury by inhibiting oxidative stress and inflammation via Nrf2/HO-1 pathway, suggesting that zedoarondiol might be meaningful on prevention and treatment of atherosclerosis.	zedoarondiol	12-24	heme oxygenase 1	Homo sapiens	133-137
30064139-13	2018	CONCLUSION: Zedoarondiol attenuates ox-LDL-induced endothelial cells injury by inhibiting oxidative stress and inflammation via Nrf2/HO-1 pathway, suggesting that zedoarondiol might be meaningful on prevention and treatment of atherosclerosis.	zedoarondiol	163-175	heme oxygenase 1	Homo sapiens	133-137
29694447-0	2018	Pharmacological versus genetic inhibition of heme oxygenase-1 - the comparison of metalloporphyrins, shRNA and CRISPR/Cas9 system.	Metalloporphyrins	82-99	heme oxygenase 1	Homo sapiens	45-61
29694447-4	2018	Metalloporphyrins decreased HO activity but concomitantly strongly induced HO-1 mRNA and protein in 293T cells.	Metalloporphyrins	0-17	heme oxygenase 1	Homo sapiens	75-79
29694447-8	2018	Furthermore, CRISPR/Cas9-mediated HO-1 depletion decreased 293T viability, growth, clonogenic potential and increased sensitivity to H2O2 treatment.	Hydrogen Peroxide	133-137	heme oxygenase 1	Homo sapiens	34-38
30068872-9	2018	In contrast, DBM effectively increased the expression of nuclear factor E2-related factor 2 (Nrf2) and its target protein, hemeoxygenase-1 (HO-1).	dibenzoylmethane	13-16	heme oxygenase 1	Homo sapiens	123-138
30674243-0	2018	Structural Insights into Azole-based Inhibitors of Heme Oxygenase-1: Development of Selective Compounds for Therapeutic Applications.	Azoles	25-30	heme oxygenase 1	Homo sapiens	51-67
30466076-7	2018	RESULTS: We demonstrated that OI, the cell-permeable derivative of itaconate, induced Keap1-Nrf2 dissociation, Nrf2 protein accumulation, and nuclear translocation, which enabled the transcription and expression of multiple Nrf2-dependentantioxidant enzymes (heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1, and glutamate-cysteine ligase modifier subunit) in THP-1 human macrophages.	itaconic acid	67-76	heme oxygenase 1	Homo sapiens	259-309
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Polyphenols	20-31	heme oxygenase 1	Homo sapiens	239-255
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Polyphenols	20-31	heme oxygenase 1	Homo sapiens	257-261
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Curcumin	40-48	heme oxygenase 1	Homo sapiens	239-255
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Curcumin	40-48	heme oxygenase 1	Homo sapiens	257-261
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Quercetin	50-59	heme oxygenase 1	Homo sapiens	239-255
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Quercetin	50-59	heme oxygenase 1	Homo sapiens	257-261
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Genistein	61-70	heme oxygenase 1	Homo sapiens	239-255
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	Genistein	61-70	heme oxygenase 1	Homo sapiens	257-261
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	caffeic acid phenethyl ester	76-104	heme oxygenase 1	Homo sapiens	239-255
28618991-11	2018	In particular, some polyphenols such as curcumin, quercetin, genistein, and caffeic acid phenethyl ester are able to potently activate nuclear factor erythroid 2-related factor 2 (Nrf2) and related downstream expression of enzymes such as heme oxygenase-1 (HO-1).	caffeic acid phenethyl ester	76-104	heme oxygenase 1	Homo sapiens	257-261
29051011-2	2018	Previously, we reported that heme oxygenase-1 can protect LECs from hydrogen peroxide (H2O2)-induced apoptosis and oxidative stress; however, to the best of our knowledge, these protection mechanisms have not yet been explained.	Hydrogen Peroxide	68-85	heme oxygenase 1	Homo sapiens	29-45
30039754-3	2018	Nutraceutical measures which may address these issues include taurine and N-acetylcysteine - which may boost placental H2S production; spirulina and phase 2 inducers of heme oxygenase-1 such as lipoic acid - which may down-regulate placental NADPH oxidase activity; and citrulline, high-dose folate, and dietary nitrate - which by supporting placental nitric oxide production may aid proper placentation and hence prevent placental hypoxia.	Thioctic Acid	194-205	heme oxygenase 1	Homo sapiens	169-185
29061583-5	2018	Bioengineered NRF2-siRNA was able to significantly knock down NRF2 mRNA and protein levels in human OS 143B and MG63 cells, and subsequently suppressed the expression of NRF2-regulated oxidative enzymes [heme oxygenase-1 and NAD(P)H:quinone oxidoreductase 1] and elevated intracellular levels of reactive oxygen species.	Reactive Oxygen Species	296-319	heme oxygenase 1	Homo sapiens	204-257
29232587-0	2018	Discovery of naphtho[1,2-d]oxazole derivatives as potential anti-HCV agents through inducing heme oxygenase-1 expression.	naphtho[1,2-d]oxazole	13-34	heme oxygenase 1	Homo sapiens	93-109
29051011-2	2018	Previously, we reported that heme oxygenase-1 can protect LECs from hydrogen peroxide (H2O2)-induced apoptosis and oxidative stress; however, to the best of our knowledge, these protection mechanisms have not yet been explained.	Hydrogen Peroxide	87-91	heme oxygenase 1	Homo sapiens	29-45
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Heme	101-105	heme oxygenase 1	Homo sapiens	0-16
28818727-8	2018	In vivo and in vitro experiments have demonstrated the ability of polysaccharide-rich extracts to provide neuroprotective effects through promotion of neurite outgrowth, and NF-kappaB, PI3K/Akt, MAPK, Nrf2/HO-1 signaling pathways.	Polysaccharides	66-80	heme oxygenase 1	Homo sapiens	206-210
29791903-1	2018	In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest.	Carbon Monoxide	117-132	heme oxygenase 1	Homo sapiens	63-79
29791903-1	2018	In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest.	Carbon Monoxide	117-132	heme oxygenase 1	Homo sapiens	81-85
29791903-1	2018	In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest.	Carbon Monoxide	134-136	heme oxygenase 1	Homo sapiens	63-79
29791903-1	2018	In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest.	Carbon Monoxide	134-136	heme oxygenase 1	Homo sapiens	81-85
29791903-1	2018	In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest.	Biliverdine	142-152	heme oxygenase 1	Homo sapiens	63-79
29791903-1	2018	In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest.	Biliverdine	142-152	heme oxygenase 1	Homo sapiens	81-85
28823537-5	2018	4-Hydroperoxy-2-decenoic acid ethyl ester (HPO-DAEE), a synthesized RJ fatty acid derivative, markedly induced antioxidant enzymes such as heme oxygenase-1 (HO-1).	4-hydroperoxy-2-decenoic acid ethyl ester	0-41	heme oxygenase 1	Homo sapiens	139-155
28823537-5	2018	4-Hydroperoxy-2-decenoic acid ethyl ester (HPO-DAEE), a synthesized RJ fatty acid derivative, markedly induced antioxidant enzymes such as heme oxygenase-1 (HO-1).	hpo-daee	43-51	heme oxygenase 1	Homo sapiens	139-155
28823537-5	2018	4-Hydroperoxy-2-decenoic acid ethyl ester (HPO-DAEE), a synthesized RJ fatty acid derivative, markedly induced antioxidant enzymes such as heme oxygenase-1 (HO-1).	Fatty Acids	71-81	heme oxygenase 1	Homo sapiens	139-155
29425644-0	2018	Ligustilide attenuates vascular inflammation and activates Nrf2/HO-1 induction and, NO synthesis in HUVECs.	ligustilide	0-11	heme oxygenase 1	Homo sapiens	64-68
29425644-10	2018	Also, ligustilide treated HUVECs exhibited significant HO-1 induction via Nrf2 nuclear translocation and endothelial NO synthesis.	ligustilide	6-17	heme oxygenase 1	Homo sapiens	55-59
29029310-9	2018	Moreover, LINA-OOH induced a stronger Nrf2 accumulation in correlation with nqo1 and ho-1 gene expression, 2 Nrf2 target genes.	linalool	10-14	heme oxygenase 1	Homo sapiens	85-89
29029310-9	2018	Moreover, LINA-OOH induced a stronger Nrf2 accumulation in correlation with nqo1 and ho-1 gene expression, 2 Nrf2 target genes.	OOH	15-18	heme oxygenase 1	Homo sapiens	85-89
29203625-3	2018	Long version of the guanine-thymine (GTn) microsatellite in the HMOX1 promoter decreases HO-1 expression, and the long maternal repeat is associated with late-onset preeclampsia.	guanine-thymine (gtn	20-40	heme oxygenase 1	Homo sapiens	64-69
29203625-3	2018	Long version of the guanine-thymine (GTn) microsatellite in the HMOX1 promoter decreases HO-1 expression, and the long maternal repeat is associated with late-onset preeclampsia.	guanine-thymine (gtn	20-40	heme oxygenase 1	Homo sapiens	89-93
28083817-0	2018	Carnosic Acid Induces Anti-Inflammatory Effects in Paraquat-Treated SH-SY5Y Cells Through a Mechanism Involving a Crosstalk Between the Nrf2/HO-1 Axis and NF-kappaB.	salvin	0-13	heme oxygenase 1	Homo sapiens	141-145
28083817-0	2018	Carnosic Acid Induces Anti-Inflammatory Effects in Paraquat-Treated SH-SY5Y Cells Through a Mechanism Involving a Crosstalk Between the Nrf2/HO-1 Axis and NF-kappaB.	Paraquat	51-59	heme oxygenase 1	Homo sapiens	141-145
28083817-6	2018	SH-SY5Y cells were pretreated for 12 h with CA at 1 muM before exposure to PQ for further 24 h. CA suppressed the PQ-induced alterations on the levels of interleukin-1beta (IL-1beta), tumor necrosis factor-alpha (TNF-alpha), and cyclooxygenase-2 (COX-2) through a mechanism involving the activation of the Nrf2/HO-1 axis.	Paraquat	114-116	heme oxygenase 1	Homo sapiens	311-315
28083817-7	2018	Furthermore, we observed a crosstalk between the Nrf2/HO-1 signaling pathway and the activation of the nuclear factor-kappaB (NF-kappaB) transcription factor, since administration of ZnPP IX (specific inhibitor of HO-1) or Nrf2 knockdown using small interfering RNA (siRNA) abolished the anti-inflammatory effects induced by CA.	zinc protoporphyrin	183-190	heme oxygenase 1	Homo sapiens	54-58
28083817-7	2018	Furthermore, we observed a crosstalk between the Nrf2/HO-1 signaling pathway and the activation of the nuclear factor-kappaB (NF-kappaB) transcription factor, since administration of ZnPP IX (specific inhibitor of HO-1) or Nrf2 knockdown using small interfering RNA (siRNA) abolished the anti-inflammatory effects induced by CA.	zinc protoporphyrin	183-190	heme oxygenase 1	Homo sapiens	214-218
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Heme	101-105	heme oxygenase 1	Homo sapiens	18-22
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Iron	116-120	heme oxygenase 1	Homo sapiens	0-16
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Iron	116-120	heme oxygenase 1	Homo sapiens	18-22
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Carbon Monoxide	122-137	heme oxygenase 1	Homo sapiens	0-16
29153608-7	2017	There were increased levels of iNOS, TNF-alpha, HO1, Nrf2, Wfs-1, XBP-1 and spliced XBP-1 observed in response to hemin treatment and the signaling was found to be partly mediated by cofilin.	Hemin	114-119	heme oxygenase 1	Homo sapiens	48-51
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Carbon Monoxide	122-137	heme oxygenase 1	Homo sapiens	18-22
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Carbon Monoxide	139-141	heme oxygenase 1	Homo sapiens	0-16
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Carbon Monoxide	139-141	heme oxygenase 1	Homo sapiens	18-22
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Biliverdine	148-158	heme oxygenase 1	Homo sapiens	0-16
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Biliverdine	148-158	heme oxygenase 1	Homo sapiens	18-22
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Bilirubin	197-206	heme oxygenase 1	Homo sapiens	0-16
28756878-1	2017	Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin.	Bilirubin	197-206	heme oxygenase 1	Homo sapiens	18-22
28756878-2	2017	By means of these catabolic end-products and by removal of pro-oxidant heme, HO-1 exerts antioxidant, antiapoptotic, and immune-modulating effects, leading to overall cytoprotective and beneficial functions in mammalian cells.	Heme	71-75	heme oxygenase 1	Homo sapiens	77-81
29216925-9	2017	Docetaxel treatment modestly decreased Bach2 expression and increased HO-1 level in PC3 cells, whereas a modest increase of HO-1 facilitated docetaxel-induced apoptosis.	Docetaxel	0-9	heme oxygenase 1	Homo sapiens	70-74
29216925-9	2017	Docetaxel treatment modestly decreased Bach2 expression and increased HO-1 level in PC3 cells, whereas a modest increase of HO-1 facilitated docetaxel-induced apoptosis.	Docetaxel	141-150	heme oxygenase 1	Homo sapiens	124-128
29216925-10	2017	Notably, docetaxel-induced miR-193a-5p upregulation, which in turn inhibits Bach2 expression and thus relieves Bach2 repression of HO-1 expression, partly counteracted docetaxel-induced apoptosis, as evidenced by the increased Bcl-2 and decreased Bax expression.	Docetaxel	9-18	heme oxygenase 1	Homo sapiens	131-135
29216925-10	2017	Notably, docetaxel-induced miR-193a-5p upregulation, which in turn inhibits Bach2 expression and thus relieves Bach2 repression of HO-1 expression, partly counteracted docetaxel-induced apoptosis, as evidenced by the increased Bcl-2 and decreased Bax expression.	Docetaxel	168-177	heme oxygenase 1	Homo sapiens	131-135
29039478-0	2017	Phosphorylation of eIF2alpha suppresses cisplatin-induced p53 activation and apoptosis by attenuating oxidative stress via ATF4-mediated HO-1 expression in human renal proximal tubular cells.	Cisplatin	40-49	heme oxygenase 1	Homo sapiens	137-141
28970059-3	2017	The present study investigated the structural requirements of flavonoids to induce Hmox1 in human aortic endothelial cells (HAEC).	Flavonoids	62-72	heme oxygenase 1	Homo sapiens	83-88
28749008-0	2017	Propofol post-conditioning alleviates hepatic ischaemia reperfusion injury via BRG1-mediated Nrf2/HO-1 transcriptional activation in human and mice.	Propofol	0-8	heme oxygenase 1	Homo sapiens	98-102
28513870-6	2017	We discovered an increased calcium ion concentration and upregulated Runx2, BMP2, Nrf2, HO-1, gamma-GCS, NQO-1, and LC3II/LC3I expressions in the high phosphorous, si-NC and Nrf2-siRNA, and NC groups, compared with the normal control group.	Phosphorus	151-162	heme oxygenase 1	Homo sapiens	88-103
28513870-6	2017	We discovered an increased calcium ion concentration and upregulated Runx2, BMP2, Nrf2, HO-1, gamma-GCS, NQO-1, and LC3II/LC3I expressions in the high phosphorous, si-NC and Nrf2-siRNA, and NC groups, compared with the normal control group.	Silicon	133-135	heme oxygenase 1	Homo sapiens	88-103
28513870-7	2017	Compared to the high phosphorus and si-NC groups, higher levels of Runx2 and BMP2 but decreased Nrf2, HO-1, gamma-GCS, NQO-1, and LC3II/LC3I expressions were detected in the Nrf2-siRNA group.	Silicon	36-38	heme oxygenase 1	Homo sapiens	102-117
28513870-8	2017	The high phosphorus, si-NC and over-expressed Nrf2 experimental groups all had increased Nrf2, NQO-1, HO-1, gamma-GCS, and LC3II/LC3I expressions as well as high numbers of autophagosomes compared with the normal control group.	Phosphorus	9-19	heme oxygenase 1	Homo sapiens	102-117
29152653-11	2017	Furthermore, elaidic acid resulted in upregulation of nuclear factor erythroid 2-related factor 2 and downregulation of heme oxygenase 1, which are two key antioxidative factors.	elaidic acid	13-25	heme oxygenase 1	Homo sapiens	120-136
29039478-11	2017	Furthermore, cisplatin induced the expression of activating transcription factor 4 (ATF4) and heme oxygenase-1 (HO-1) that were enhanced by Sal003 and reduced by PERK knockdown.	Cisplatin	13-22	heme oxygenase 1	Homo sapiens	94-110
29039478-11	2017	Furthermore, cisplatin induced the expression of activating transcription factor 4 (ATF4) and heme oxygenase-1 (HO-1) that were enhanced by Sal003 and reduced by PERK knockdown.	Cisplatin	13-22	heme oxygenase 1	Homo sapiens	112-116
29039478-12	2017	Taken together, these results suggest that phosphorylation of eIF2alpha suppresses cisplatin-induced p53 activation and apoptosis by attenuating oxidative stress via ATF4-mediated HO-1 expression in HK-2 cells, as ATF4 expression is usually dependent on the phosphorylation of eIF2alpha and may also transcriptionally induce the expression of HO-1 in response to oxidative stress.	Cisplatin	83-92	heme oxygenase 1	Homo sapiens	180-184
29039478-12	2017	Taken together, these results suggest that phosphorylation of eIF2alpha suppresses cisplatin-induced p53 activation and apoptosis by attenuating oxidative stress via ATF4-mediated HO-1 expression in HK-2 cells, as ATF4 expression is usually dependent on the phosphorylation of eIF2alpha and may also transcriptionally induce the expression of HO-1 in response to oxidative stress.	Cisplatin	83-92	heme oxygenase 1	Homo sapiens	343-347
28513870-8	2017	The high phosphorus, si-NC and over-expressed Nrf2 experimental groups all had increased Nrf2, NQO-1, HO-1, gamma-GCS, and LC3II/LC3I expressions as well as high numbers of autophagosomes compared with the normal control group.	Silicon	21-23	heme oxygenase 1	Homo sapiens	102-117
28156185-7	2017	RESULTS: DMF and MMF induced NQO1 and HO1 gene expression in ex vivo-stimulated PBMCs, DMF being the more potent inducer.	Dimethyl Fumarate	9-12	heme oxygenase 1	Homo sapiens	38-41
28156185-7	2017	RESULTS: DMF and MMF induced NQO1 and HO1 gene expression in ex vivo-stimulated PBMCs, DMF being the more potent inducer.	mmf	17-20	heme oxygenase 1	Homo sapiens	38-41
28749008-7	2017	Brg1 and Nrf2 siRNA were used to examine the relationship between Brg1 and Nrf2/HO-1 pathways in propofol-mediated effects in a human hepatocyte(L02) hypoxia/reoxygenation(H/R) model.	Propofol	97-105	heme oxygenase 1	Homo sapiens	80-84
28749008-15	2017	Propofol post-conditioning alleviates HIRI through BRG1-mediated Nrf2/HO-1 transcriptional activation.	Propofol	0-8	heme oxygenase 1	Homo sapiens	70-74
28882558-0	2017	Cinnamaldehyde protects human dental pulp cells against oxidative stress through the Nrf2/HO-1-dependent antioxidant response.	cinnamaldehyde	0-14	heme oxygenase 1	Homo sapiens	90-94
29333383-0	2017	Inhibitory Effects of Butein on Adipogenesis through Upregulation of the Nrf2/HO-1 Pathway in 3T3-L1 Adipocytes.	butein	22-28	heme oxygenase 1	Homo sapiens	78-82
29333383-5	2017	Butein also increased Nrf2 and HO-1 protein expression in a dose-dependent manner.	butein	0-6	heme oxygenase 1	Homo sapiens	31-35
29333383-6	2017	Treatment with zinc protoporphyrin, a specific HO-1 inhibitor, abolished the inhibitory effects of butein on adipogenic transcription factor protein expression.	zinc protoporphyrin	15-34	heme oxygenase 1	Homo sapiens	47-51
29333383-6	2017	Treatment with zinc protoporphyrin, a specific HO-1 inhibitor, abolished the inhibitory effects of butein on adipogenic transcription factor protein expression.	butein	99-105	heme oxygenase 1	Homo sapiens	47-51
29333383-7	2017	Therefore, butein inhibits adipogenesis, at least partially, through upregulation of the Nrf-2/HO-1 signaling pathway in 3T3-L1 adipocytes.	butein	11-17	heme oxygenase 1	Homo sapiens	95-99
29230104-0	2017	Metformin Sensitizes Non-small Cell Lung Cancer Cells to an Epigallocatechin-3-Gallate (EGCG) Treatment by Suppressing the Nrf2/HO-1 Signaling Pathway.	epigallocatechin gallate	60-86	heme oxygenase 1	Homo sapiens	128-132
29230104-0	2017	Metformin Sensitizes Non-small Cell Lung Cancer Cells to an Epigallocatechin-3-Gallate (EGCG) Treatment by Suppressing the Nrf2/HO-1 Signaling Pathway.	epigallocatechin gallate	88-92	heme oxygenase 1	Homo sapiens	128-132
29230104-3	2017	The NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway is considered to mediate cellular resistance to EGCG.	epigallocatechin gallate	124-128	heme oxygenase 1	Homo sapiens	34-50
29230104-3	2017	The NF-E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway is considered to mediate cellular resistance to EGCG.	epigallocatechin gallate	124-128	heme oxygenase 1	Homo sapiens	52-56
29230104-6	2017	In this study, metformin inhibited HO-1 expression and augmented the anti-tumor effect of EGCG.	Metformin	15-24	heme oxygenase 1	Homo sapiens	35-39
29230104-9	2017	Mechanistically, metformin modulated the EGCG-activated Nrf2/HO-1 pathway through Sirtuin 1 (SIRT1)-dependent deacetylation of Nrf2.	Metformin	17-26	heme oxygenase 1	Homo sapiens	61-65
29230104-9	2017	Mechanistically, metformin modulated the EGCG-activated Nrf2/HO-1 pathway through Sirtuin 1 (SIRT1)-dependent deacetylation of Nrf2.	epigallocatechin gallate	41-45	heme oxygenase 1	Homo sapiens	61-65
29230104-12	2017	Based on our findings, metformin sensitized NSCLC cells to the EGCG treatment by suppressing the Nrf2/HO-1 signaling pathway.	Metformin	23-32	heme oxygenase 1	Homo sapiens	102-106
29230104-12	2017	Based on our findings, metformin sensitized NSCLC cells to the EGCG treatment by suppressing the Nrf2/HO-1 signaling pathway.	epigallocatechin gallate	63-67	heme oxygenase 1	Homo sapiens	102-106
29170479-1	2017	Heme oxygenase-1-derived carbon monoxide prevents inflammatory vascular disorders.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
29209333-7	2017	In addition, DMF treatment upregulated antioxidant enzymes heme oxygenase-1 and glutathione S-transferase-alpha1 expressions.	Dimethyl Fumarate	13-16	heme oxygenase 1	Homo sapiens	59-112
29230104-0	2017	Metformin Sensitizes Non-small Cell Lung Cancer Cells to an Epigallocatechin-3-Gallate (EGCG) Treatment by Suppressing the Nrf2/HO-1 Signaling Pathway.	Metformin	0-9	heme oxygenase 1	Homo sapiens	128-132
28882558-5	2017	CA-mediated Nrf2/HO-1 activation reduced the level of reactive oxygen species and protected the hDPCs from H2O2-induced oxidative stress, which induces apoptosis.	Reactive Oxygen Species	54-77	heme oxygenase 1	Homo sapiens	17-21
29022012-11	2017	Vanadium downregulated P38, ERK1/2, JNK, Nrf2, sMaf, GCLC, NQO1 and HO-1 mRNA expression (P &lt; 0.05).	Vanadium	0-8	heme oxygenase 1	Homo sapiens	68-72
28882558-5	2017	CA-mediated Nrf2/HO-1 activation reduced the level of reactive oxygen species and protected the hDPCs from H2O2-induced oxidative stress, which induces apoptosis.	Hydrogen Peroxide	107-111	heme oxygenase 1	Homo sapiens	17-21
28602161-7	2017	Thus, geraniin up-regulates HO-1 expression both through activating its positive regulator Nrf-2 and by down-regulating its negative regulator BACH-1.	Geraniin	6-14	heme oxygenase 1	Homo sapiens	28-32
29125538-3	2017	CYP1A1 is mediated by aryl hydrocarbon receptor signaling, while induction of HO-1 is regulated by oxidative stress, and suppressed by N-acetylcysteine treatment.	Acetylcysteine	135-151	heme oxygenase 1	Homo sapiens	78-82
28950658-5	2017	7,8-DHF also significantly reduced the generation of intracellular reactive oxygen species (ROS), induced the expression of anti-oxidant enzymes, such as catalase, manganese superoxide dismutase (Mn-SOD), and heme oxygenase-1 (HO-1), and scavenged DPPH free radicals.	6,7-dihydroxyflavone	0-7	heme oxygenase 1	Homo sapiens	209-225
28950658-5	2017	7,8-DHF also significantly reduced the generation of intracellular reactive oxygen species (ROS), induced the expression of anti-oxidant enzymes, such as catalase, manganese superoxide dismutase (Mn-SOD), and heme oxygenase-1 (HO-1), and scavenged DPPH free radicals.	6,7-dihydroxyflavone	0-7	heme oxygenase 1	Homo sapiens	227-231
28950658-8	2017	7,8-DHF effectively attenuated oxidative stress by up-regulating the anti-oxidant enzymes catalase, Mn-SOD, and HO-1, and reducing activation of the Akt and MAPKs signaling pathways in aged skin cells.	6,7-dihydroxyflavone	0-7	heme oxygenase 1	Homo sapiens	112-116
28602161-8	2017	Up-regulation of HO-1 also confers protection to HepG2 cells from tertiary butyl hydroperoxide (TBH) induced cytotoxicity.	n-Butylhydroperoxide	75-94	heme oxygenase 1	Homo sapiens	17-21
28602161-8	2017	Up-regulation of HO-1 also confers protection to HepG2 cells from tertiary butyl hydroperoxide (TBH) induced cytotoxicity.	tert-Butylhydroperoxide	96-99	heme oxygenase 1	Homo sapiens	17-21
28732110-0	2017	Growth inhibitory effect of beta-eudesmol on cholangiocarcinoma cells and its potential suppressive effect on heme oxygenase-1 production, STAT1/3 activation, and NF-kappaB downregulation.	beta-eudesmol	28-41	heme oxygenase 1	Homo sapiens	110-126
28732110-2	2017	The present study reports for the first time in vitro growth inhibitory activities of beta-eudesmol, the bioactive sesquiterpenoid present in the rhizome of Atractylodes lancea (Thunb) DC., with respect to its underlying potential effects on heme oxygenase-1 (HO-1) production, STAT1/3 phosphorylation, and NF-kappaB protein expression in human CCA cell line CL-6.	beta-eudesmol	86-99	heme oxygenase 1	Homo sapiens	242-258
28732110-2	2017	The present study reports for the first time in vitro growth inhibitory activities of beta-eudesmol, the bioactive sesquiterpenoid present in the rhizome of Atractylodes lancea (Thunb) DC., with respect to its underlying potential effects on heme oxygenase-1 (HO-1) production, STAT1/3 phosphorylation, and NF-kappaB protein expression in human CCA cell line CL-6.	beta-eudesmol	86-99	heme oxygenase 1	Homo sapiens	260-264
28732110-6	2017	Western blot analysis indicated that beta-eudesmol treatment resulted in significant suppression of HO-1 production in CL-6 cells.	beta-eudesmol	37-50	heme oxygenase 1	Homo sapiens	100-104
28732110-8	2017	Taken together, these results suggest that beta-eudesmol exerts significant growth inhibitory activity on CL-6 cells that may be linked to its inhibitory effect on the production of HO-1, phosphorylation of STAT1/3, and expression of major NF-kappaB proteins.	beta-eudesmol	43-56	heme oxygenase 1	Homo sapiens	182-186
29122256-7	2017	Macrophages phagocytize the erythrocytes in the extravascular space which stimulates the production of Heme Oxygenase-1 (HO-1) to metabolize the heme.	Heme	145-149	heme oxygenase 1	Homo sapiens	103-119
28870684-6	2017	IsoLQ also induced heme oxygenase-1 (HO-1) expression that may be associated with nuclear factor (erythroid-derived 2)-like 2 (Nrf2) nuclear translocation.	isoliquiritigenin	0-5	heme oxygenase 1	Homo sapiens	19-35
29122256-7	2017	Macrophages phagocytize the erythrocytes in the extravascular space which stimulates the production of Heme Oxygenase-1 (HO-1) to metabolize the heme.	Heme	145-149	heme oxygenase 1	Homo sapiens	121-125
28649040-6	2017	The OPAO assay showed the best correlation with the production of intracellular reactive oxygen species by NCI-H292 cell line assessed by DCFH oxidation and with the expression of anti-oxidant genes (superoxide dismutase 2, heme-oxygenase-1) as well as the proinflammatory response (Interleukin 6) when exposed from 1 to 10 mug/cm2.	opao	4-8	heme oxygenase 1	Homo sapiens	224-240
28870684-6	2017	IsoLQ also induced heme oxygenase-1 (HO-1) expression that may be associated with nuclear factor (erythroid-derived 2)-like 2 (Nrf2) nuclear translocation.	isoliquiritigenin	0-5	heme oxygenase 1	Homo sapiens	37-41
29048628-3	2017	In this study, the protein expression of HO-1 in human gastric cancer was measured by immunohistochemistry on paraffin sections of 89 paired gastric carcinoma tissues and adjacent non-cancer tissues.	Paraffin	110-118	heme oxygenase 1	Homo sapiens	41-45
28901402-0	2017	Carbon monoxide-releasing molecule suppresses inflammatory and osteoclastogenic cytokines in nicotine- and lipopolysaccharide-stimulated human periodontal ligament cells via the heme oxygenase-1 pathway.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	178-194
28901402-0	2017	Carbon monoxide-releasing molecule suppresses inflammatory and osteoclastogenic cytokines in nicotine- and lipopolysaccharide-stimulated human periodontal ligament cells via the heme oxygenase-1 pathway.	Nicotine	93-101	heme oxygenase 1	Homo sapiens	178-194
28846887-5	2017	Also, it was demonstrated that nuclear factor erythroid 2-related factor 2 (Nrf2) activation was involved in modulating cellular oxidative stress, where SchB promoted Nrf2 translocation into the nucleus and downstream target gene expression of heme oxygenase-1 (HO-1), NAD(P)H:quinone oxidoreductase 1 (NQO1) and Glutamate-cysteine ligase modifier subunit (GCLM).	schizandrin B	153-157	heme oxygenase 1	Homo sapiens	244-260
28543094-6	2017	Specific inhibitors for HO-1, HSP90, caspase-3, DNase I and EndoG almost completely blocked the DNA fragmentation induced by graphene exposure.	Graphite	125-133	heme oxygenase 1	Homo sapiens	24-28
29048628-5	2017	The effects of decreased HO-1 expression by two strands of small interfered RNAs (siRNAs) on cell apoptosis, proliferation, and invasion of gastric cancer cell lines were examined by flow cytometry, the MTT assay, and the cell migration assay, respectively.	monooxyethylene trimethylolpropane tristearate	203-206	heme oxygenase 1	Homo sapiens	25-29
29451663-8	2017	iNOS levels were positively correlated with ISS scores and blood lactic acid values, and HO-1 and endogenous H2S were negatively correlated with ISS scores and blood lactic acid values.	Lactic Acid	166-177	heme oxygenase 1	Homo sapiens	89-93
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	ammonium ferrous sulfate	68-72	heme oxygenase 1	Homo sapiens	14-18
29260515-7	2017	10 mumol/L and 20 mumol/L ATO treatment activated BACH1 expression and inhibited miR-155,NQO1 and HO-1 expression,leading to decreased total antioxidant capacity.	Arsenic Trioxide	26-29	heme oxygenase 1	Homo sapiens	98-102
29260515-9	2017	Moreover,high expression of miR-155 reduced BACH1 activation and increased NQO1 and HO-1 expression in cells treated with 20 mumol/L ATO ( P&lt;0.05).	Arsenic Trioxide	133-136	heme oxygenase 1	Homo sapiens	84-88
29260515-10	2017	CONCLUSION: Restraining total antioxidant capacity contributes to ATO induced cell death,the underlying mechanisms may be that ATO can activate BACH1 expression through inhibition of the miR-155 level,leading to subsequent inhibition of NQO1 and HO-1 expression.	Arsenic Trioxide	127-130	heme oxygenase 1	Homo sapiens	246-250
29260515-10	2017	CONCLUSION: Restraining total antioxidant capacity contributes to ATO induced cell death,the underlying mechanisms may be that ATO can activate BACH1 expression through inhibition of the miR-155 level,leading to subsequent inhibition of NQO1 and HO-1 expression.	mir-155	187-194	heme oxygenase 1	Homo sapiens	246-250
29163402-1	2017	Heme oxygenase-1 (HO-1) is an inducible enzyme that is expressed in response to physical and chemical stresses, such as ultraviolet radiation, hyperthermia, hypoxia, reactive oxygen species (ROS), as well as cytokines, among others.	Reactive Oxygen Species	166-189	heme oxygenase 1	Homo sapiens	0-16
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	Carbon Monoxide	75-90	heme oxygenase 1	Homo sapiens	14-18
29163402-1	2017	Heme oxygenase-1 (HO-1) is an inducible enzyme that is expressed in response to physical and chemical stresses, such as ultraviolet radiation, hyperthermia, hypoxia, reactive oxygen species (ROS), as well as cytokines, among others.	Reactive Oxygen Species	166-189	heme oxygenase 1	Homo sapiens	18-22
29163402-1	2017	Heme oxygenase-1 (HO-1) is an inducible enzyme that is expressed in response to physical and chemical stresses, such as ultraviolet radiation, hyperthermia, hypoxia, reactive oxygen species (ROS), as well as cytokines, among others.	Reactive Oxygen Species	191-194	heme oxygenase 1	Homo sapiens	0-16
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	Carbon Monoxide	92-94	heme oxygenase 1	Homo sapiens	14-18
29163402-1	2017	Heme oxygenase-1 (HO-1) is an inducible enzyme that is expressed in response to physical and chemical stresses, such as ultraviolet radiation, hyperthermia, hypoxia, reactive oxygen species (ROS), as well as cytokines, among others.	Reactive Oxygen Species	191-194	heme oxygenase 1	Homo sapiens	18-22
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	Biliverdine	100-110	heme oxygenase 1	Homo sapiens	14-18
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	Iron	28-32	heme oxygenase 1	Homo sapiens	14-18
28821394-8	2017	Furthermore, hNSCs exposed to AGEs had significantly lower mRNA levels among other components of normal cellular oxidative defenses (GSH, Catalase and HO-1), which were all rescued by co-treatment with metformin.	Metformin	202-211	heme oxygenase 1	Homo sapiens	151-155
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	Heme	44-48	heme oxygenase 1	Homo sapiens	14-18
29163402-3	2017	Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin.	Iron	54-66	heme oxygenase 1	Homo sapiens	14-18
29085368-5	2017	1,25(OH)2D3 can induce the expression of hemeoxygenase-1 (HO-1), which is essential for blocking HMBG1 nuclear translocation and its secretion.	Calcitriol	0-11	heme oxygenase 1	Homo sapiens	41-62
28935193-1	2017	BACKGROUND AND PURPOSE: Celastrol, a quinone methide triterpene isolated from the root extracts of Tripterygium wilfordii, can greatly induce the gene expression activity of heme oxygenase-1 (HO-1) to achieve disease prevention and control.	celastrol	24-33	heme oxygenase 1	Homo sapiens	192-196
29056901-9	2017	RSL cells upregulated the expression of NRF2 (an ARE ligand) and NR0B2 in response to CoPP (a HMOX1 inducer), but not to ZnPP (a HMOX1 inhibitor).	COPP protocol	86-90	heme oxygenase 1	Homo sapiens	94-99
28935193-10	2017	These antiviral effects were abrogated by treatment with the HO-1-specific inhibitor SnMP or silencing of HO-1 expression by transfection of shRNA, which indicates that HO-1 induction contributes to the anti-HCV activity of celastrol.	celastrol	224-233	heme oxygenase 1	Homo sapiens	61-65
28935193-10	2017	These antiviral effects were abrogated by treatment with the HO-1-specific inhibitor SnMP or silencing of HO-1 expression by transfection of shRNA, which indicates that HO-1 induction contributes to the anti-HCV activity of celastrol.	celastrol	224-233	heme oxygenase 1	Homo sapiens	106-110
28935193-5	2017	The anti-HCV mechanism of celastrol targeting HO-1 expression was clarified using specific inhibitors against several signaling pathways.	celastrol	26-35	heme oxygenase 1	Homo sapiens	46-50
28935193-10	2017	These antiviral effects were abrogated by treatment with the HO-1-specific inhibitor SnMP or silencing of HO-1 expression by transfection of shRNA, which indicates that HO-1 induction contributes to the anti-HCV activity of celastrol.	celastrol	224-233	heme oxygenase 1	Homo sapiens	106-110
28935193-11	2017	JNK mitogen-activated protein kinase and nuclear factor erythroid 2-related factor 2 (Nrf2) were confirmed to be involved in the inductive effect of celastrol on HO-1 expression.	celastrol	149-158	heme oxygenase 1	Homo sapiens	162-166
28935193-9	2017	Celastrol-induced heme oxygenase 1 (HO-1) expression promoted antiviral interferon responses and inhibition of NS3/4A protease activity, thereby blocking HCV replication.	celastrol	0-9	heme oxygenase 1	Homo sapiens	36-40
28935193-10	2017	These antiviral effects were abrogated by treatment with the HO-1-specific inhibitor SnMP or silencing of HO-1 expression by transfection of shRNA, which indicates that HO-1 induction contributes to the anti-HCV activity of celastrol.	tin mesoporphyrin	85-89	heme oxygenase 1	Homo sapiens	61-65
28733231-6	2017	Significantly, these results showed that tussilagonone induces Nrf2 activation and nuclear accumulation, resulting in the upregulation of the detoxifying enzymes NAD(P)H quinone dehydrogenase 1(NQO1) and heme oxygenase-1(HO-1) that protect cells from oxidative stress.	tussilagonone	41-54	heme oxygenase 1	Homo sapiens	204-225
28757460-5	2017	Meanwhile, olaquindox activated AKT and Nrf2/HO-1 pathway, up-regulated Bax/Bcl-2 ratio, disrupted mitochondrial membrane potential (MMP) and subsequently caused cytochrome c release and a cascade activation of caspase, eventually induced apoptosis.	olaquindox	11-21	heme oxygenase 1	Homo sapiens	45-49
28757460-7	2017	Furthermore, knockdown of p21 decreased cell viability, enhanced oxidative stress, aggravated olaquindox-induced mitochondrial apoptosis and S-phase arrest involvement of activating PI3K/AKT and inhibiting Nrf2/HO-1 pathway.	olaquindox	94-104	heme oxygenase 1	Homo sapiens	211-215
28791341-10	2017	Inhibition of HO-1 with zinc protoporphyrin significantly abolished apocynin-induced suppression of MCP-1, indicating that HO-1 is significant in the suppression of MCP-1.	zinc protoporphyrin	24-43	heme oxygenase 1	Homo sapiens	14-18
28791341-10	2017	Inhibition of HO-1 with zinc protoporphyrin significantly abolished apocynin-induced suppression of MCP-1, indicating that HO-1 is significant in the suppression of MCP-1.	acetovanillone	68-76	heme oxygenase 1	Homo sapiens	14-18
28791341-10	2017	Inhibition of HO-1 with zinc protoporphyrin significantly abolished apocynin-induced suppression of MCP-1, indicating that HO-1 is significant in the suppression of MCP-1.	acetovanillone	68-76	heme oxygenase 1	Homo sapiens	123-127
28791341-11	2017	Thus, apocynin exerts antiseptic activity via the suppression of pro-inflammatory signaling pathways and the activation of cytoprotective signaling pathways, such as HO-1/Nrf-2 in RMCs, indicating that apocynin may present as a promising candidate for in vivo evaluation of a therapeutic agent for inflammation-associated renal disorders.	acetovanillone	6-14	heme oxygenase 1	Homo sapiens	166-170
28583303-10	2017	HO-1, a major gene that is upregulated in RNA-sequencing using Keap1-silenced PHEMs, protected melanocytes against H2O2-induced cell death and upregulated MITF and beta-catenin expression.	Hydrogen Peroxide	115-119	heme oxygenase 1	Homo sapiens	0-4
29375050-11	2017	ATB-346 significantly increased Nrf-2 and HO-1 protein expression as compared with vehicle (P &lt; 0.05) but did not affect the protein expression of CSE, CBS, 3-MST or HIF-1alpha.	4-anisyltetrazolium blue	0-3	heme oxygenase 1	Homo sapiens	42-46
28791341-0	2017	Apocynin protects mesangial cells from lipopolysaccharide-induced inflammation by exerting heme oxygenase 1-mediated monocyte chemoattractant protein-1 suppression.	acetovanillone	0-8	heme oxygenase 1	Homo sapiens	91-107
29375050-17	2017	The decreased gastrotoxicity of ATB-346 could be due to upregulation of Nrf-2/HO-1 pathway mediated by the release of H2s.	4-anisyltetrazolium blue	32-35	heme oxygenase 1	Homo sapiens	78-82
29375050-17	2017	The decreased gastrotoxicity of ATB-346 could be due to upregulation of Nrf-2/HO-1 pathway mediated by the release of H2s.	Hydrogen Sulfide	118-121	heme oxygenase 1	Homo sapiens	78-82
27686076-7	2017	We found that the CA-induced Nrf2-dependent HO-1 upregulation ameliorated, at least in part, the mitochondrial function in PQ-treated cells.	Paraquat	123-125	heme oxygenase 1	Homo sapiens	44-48
28782507-0	2017	MAPK/JNK1 activation protects cells against cadmium-induced autophagic cell death via differential regulation of catalase and heme oxygenase-1 in oral cancer cells.	Cadmium	44-51	heme oxygenase 1	Homo sapiens	126-142
28782507-2	2017	We investigated the roles of heme oxygenase-1 (HO-1) and catalase in cadmium (Cd)-induced oxidative stress and the underlying molecular mechanism in oral cancer cells.	Cadmium	69-76	heme oxygenase 1	Homo sapiens	47-51
28782507-8	2017	Catalase inhibition by pharmacological and genetic modulations increased Cd-induced ROS production, autophagy, and apoptosis, but suppressed HO-1, indicating that catalase is required for HO-1 induction.	Cadmium	73-75	heme oxygenase 1	Homo sapiens	188-192
28782507-3	2017	Exposing YD8 cells to Cd reduced the expression levels of catalase and superoxide dismutase 1/2 and induced the expression of HO-1 as well as autophagy and apoptosis, which were reversed by N-acetyl-l-cysteine (NAC).	Cadmium	22-24	heme oxygenase 1	Homo sapiens	126-130
28782507-3	2017	Exposing YD8 cells to Cd reduced the expression levels of catalase and superoxide dismutase 1/2 and induced the expression of HO-1 as well as autophagy and apoptosis, which were reversed by N-acetyl-l-cysteine (NAC).	Acetylcysteine	190-209	heme oxygenase 1	Homo sapiens	126-130
28782507-5	2017	Autophagy inhibition via pharmacologic and genetic modulations enhanced Cd-induced HO-1 expression, caspase-3 cleavage, and the production of reactive oxygen species (ROS).	Cadmium	72-74	heme oxygenase 1	Homo sapiens	83-87
28928455-0	2017	Polydatin inhibits mast cell-mediated allergic inflammation by targeting PI3K/Akt, MAPK, NF-kappaB and Nrf2/HO-1 pathways.	polydatin	0-9	heme oxygenase 1	Homo sapiens	108-112
28669729-7	2017	In addition, Nrf2 and its downstream target effectors (HO1, NQO1) were dramatically attenuated in MC3T3-E cells treatment with H2O2, while MAN can significantly increase the expression of Nrf2, HO1 and NQO1.	Hydrogen Peroxide	127-131	heme oxygenase 1	Homo sapiens	55-58
28669729-7	2017	In addition, Nrf2 and its downstream target effectors (HO1, NQO1) were dramatically attenuated in MC3T3-E cells treatment with H2O2, while MAN can significantly increase the expression of Nrf2, HO1 and NQO1.	Hydrogen Peroxide	127-131	heme oxygenase 1	Homo sapiens	194-197
28912423-9	2017	In conclusion, FAEW counteracted H2O2-induced oxidative stress through KEAP1-NRF2/HO-1 pathway.	Hydrogen Peroxide	33-37	heme oxygenase 1	Homo sapiens	82-86
28735729-13	2017	Moreover, Western blotting analysis demonstrated that protein expressions of Nrf-2 and HO-1 were also up-regulated by flavonoids treatment.	Flavonoids	118-128	heme oxygenase 1	Homo sapiens	87-91
28735729-14	2017	CONCLUSIONS: These results clearly demonstrate that the MeOH extracts and flavonoids from Korean milk thistle protected HepG2 cells against oxidative damage triggered by t-BHP principally by modulating ROS generation and restoring depleted GSH levels in addition to the increased Nrf-2/HO-1 signaling cascade.	Methanol	56-60	heme oxygenase 1	Homo sapiens	286-290
28735729-14	2017	CONCLUSIONS: These results clearly demonstrate that the MeOH extracts and flavonoids from Korean milk thistle protected HepG2 cells against oxidative damage triggered by t-BHP principally by modulating ROS generation and restoring depleted GSH levels in addition to the increased Nrf-2/HO-1 signaling cascade.	Flavonoids	74-84	heme oxygenase 1	Homo sapiens	286-290
28912423-6	2017	Transcriptome-wide microarray analysis indicated NRF2/HO-1 as the common target of FAEW and fluoxetine.	Fluoxetine	92-102	heme oxygenase 1	Homo sapiens	54-58
28859441-8	2017	Baicalein co-administration up-regulated expression of Nrf2 and HO-1 mRNAs and down-regulated the expression of NF-kappaB mRNA, compared with those in the colistin alone group.	baicalein	0-9	heme oxygenase 1	Homo sapiens	64-68
27992083-6	2017	Consistently, the expression of antioxidant genes, including NF-E2-related factor 2 (Nrf2), haem oxygenase-1 (HO-1) and catalase, was enhanced by afzelin treatment.	afzelin	146-153	heme oxygenase 1	Homo sapiens	110-114
27992083-9	2017	The enhancement of HO-1 gene expression by afzelin treatment was reduced by Nrf2-siRNA expression.	afzelin	43-50	heme oxygenase 1	Homo sapiens	19-23
28596283-9	2017	However, CDDO-Me was also found to increase the expression of heme-oxygenase-1, a heat-shock-protein that triggers drug resistance and cell survival.	bardoxolone methyl	9-16	heme oxygenase 1	Homo sapiens	62-78
28596283-10	2017	We therefore combined CDDO-Me with the heme-oxygenase-1 inhibitor SMA-ZnPP, which also resulted in synergistic growth-inhibitory effects.	copoly(styrene-maleic acid)-zinc protoporphyrin	66-74	heme oxygenase 1	Homo sapiens	39-55
28684418-4	2017	Ex vivo experiments indicated that Nrf-2 and HO-1 expression is reduced in T2DM versus non-T2DM OA cartilage (0.57-fold Nrf-2 and 0.34-fold HO-1), and prostaglandin E2 (PGE2) release was increased in samples with low HO-1 expression.	Dinoprostone	151-167	heme oxygenase 1	Homo sapiens	45-49
28684418-4	2017	Ex vivo experiments indicated that Nrf-2 and HO-1 expression is reduced in T2DM versus non-T2DM OA cartilage (0.57-fold Nrf-2 and 0.34-fold HO-1), and prostaglandin E2 (PGE2) release was increased in samples with low HO-1 expression.	Dinoprostone	169-173	heme oxygenase 1	Homo sapiens	45-49
28870911-9	2017	In addition, sunitinib exhibited concentration-dependent induction of oxidative stress genes (heme oxygenase 1 and glutathione transferase A1) through the nuclear factor erythroid 2-related factor 2 pathway.	Sunitinib	13-22	heme oxygenase 1	Homo sapiens	94-110
28651232-8	2017	Further, treatment with silymarin post ICH injury increased Nrf-2/HO-1 and thereby improved overall cytoprotection.	Silymarin	24-33	heme oxygenase 1	Homo sapiens	66-70
28651232-9	2017	These findings together show that silymarin acts as neuroprotective compound by preventing inflammatory activation and up regulating Nrf-2/HO-1 signaling post ICH injury.	Silymarin	34-43	heme oxygenase 1	Homo sapiens	139-143
28552716-7	2017	In vivo, TUDCA treatment increases the expression of Nrf2, Nrf2 stabilizer DJ-1, and Nrf2 downstream target antioxidant enzymes HO-1 and GPx.	ursodoxicoltaurine	9-14	heme oxygenase 1	Homo sapiens	128-132
28684418-7	2017	The HO-1 inducer cobalt protoporphyrin IX more efficiently attenuated PGE2 and IL-6 release in HG+IL-1beta-treated cells than in NG+IL-1beta-treated cells.	Cobalt	17-23	heme oxygenase 1	Homo sapiens	4-8
28684418-7	2017	The HO-1 inducer cobalt protoporphyrin IX more efficiently attenuated PGE2 and IL-6 release in HG+IL-1beta-treated cells than in NG+IL-1beta-treated cells.	protoporphyrin IX	24-41	heme oxygenase 1	Homo sapiens	4-8
28684418-7	2017	The HO-1 inducer cobalt protoporphyrin IX more efficiently attenuated PGE2 and IL-6 release in HG+IL-1beta-treated cells than in NG+IL-1beta-treated cells.	Dinoprostone	70-74	heme oxygenase 1	Homo sapiens	4-8
28732803-0	2017	(-)-7(S)-hydroxymatairesinol protects against tumor necrosis factor-alpha-mediated inflammation response in endothelial cells by blocking the MAPK/NF-kappaB and activating Nrf2/HO-1.	(-)-7(s)-hydroxymatairesinol	0-28	heme oxygenase 1	Homo sapiens	177-181
28633807-0	2017	Differential induction of ATF3 and HO-1 in myeloid cells and keratinocytes via Dimethylfumarate or Cyclosporine A.	Dimethyl Fumarate	79-95	heme oxygenase 1	Homo sapiens	35-39
28633807-0	2017	Differential induction of ATF3 and HO-1 in myeloid cells and keratinocytes via Dimethylfumarate or Cyclosporine A.	Cyclosporine	99-113	heme oxygenase 1	Homo sapiens	35-39
28713890-0	2017	HO-1 alleviates cholesterol-induced oxidative stress through activation of Nrf2/ERK and inhibition of PI3K/AKT pathways in endothelial cells.	Cholesterol	16-27	heme oxygenase 1	Homo sapiens	0-4
28713890-4	2017	It was confirmed that cholesterol stimulation upregulated the expression of HO-1 in a time-dependent manner via the activation and translocation of nuclear factor erythroid 2-related factor 2 (Nrf2), activation of the mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) signaling pathway and increasing intercellular Ca2+ ([Ca2+]i) concentration.	Cholesterol	22-33	heme oxygenase 1	Homo sapiens	76-80
28713890-6	2017	It was confirmed that cholesterol-mediated oxidative damage in vascular endothelial cells induced an increase in the expression of HO-1 via the activation of Nrf2 and the MAPK/ERK signaling pathway, and increasing the [Ca2+]i concentration.	Cholesterol	22-33	heme oxygenase 1	Homo sapiens	131-135
29152091-0	2017	Fibroblast growth factor-2-mediated protection of cardiomyocytes from the toxic effects of doxorubicin requires the mTOR/Nrf-2/HO-1 pathway.	Doxorubicin	91-102	heme oxygenase 1	Homo sapiens	127-131
29152091-7	2017	A selective inhibitor for HO-1, Tin-Protoporphyrin, prevented the FGF-2 protection against cell death.	tin protoporphyrin IX	32-50	heme oxygenase 1	Homo sapiens	26-30
29152091-8	2017	The mTOR inhibitor Rapamycin prevented FGF-2 protection, and blocked the FGF-2 effects on Nrf-2, HO-1 and p62/SQSTM1.	Sirolimus	19-28	heme oxygenase 1	Homo sapiens	97-101
29152091-9	2017	Conclusions: In an acute setting Hi- or Lo-FGF-2 protect cardiomyocytes against multiple Dox-induced deleterious effects, by a mechanism dependent on preservation of mTOR activity, Nrf-2 levels, and the upregulation of HO-1.	Doxorubicin	89-92	heme oxygenase 1	Homo sapiens	219-223
28583762-6	2017	Furthermore, the effect of puerarin was potentially mediated through activating Nrf2/HO-1 antioxidant signaling pathway and inhibiting Abeta1-40-induced phosphorylation of IRE1 and PERK as well as nuclear expression of ATF6alpha.	puerarin	27-35	heme oxygenase 1	Homo sapiens	85-89
28780624-8	2017	Moreover, exogenous CORM-2 could attenuate HO-1 expression, while overexpressed heme oxygenase-1 (HO-1) increased intracellular CO production, attenuated Cx43 expression, hemichannel function, and gap junction function on spinal astrocyte membranes.	Carbon Monoxide	20-22	heme oxygenase 1	Homo sapiens	43-47
29070980-3	2017	The haptoglobin-CD163-heme oxygenase-1 (HO-1) pathway circumvents heme toxicity through enzymatic degradation of heme and transcription of antioxidant genes.	Heme	22-26	heme oxygenase 1	Homo sapiens	40-44
28655775-5	2017	Herein, we demonstrate that HO1 binds to PCBP2, but not to other PCBP family members, namely PCBP1, PCBP3, or PCBP4.	pcbp	41-45	heme oxygenase 1	Homo sapiens	28-31
28806787-7	2017	MG132 increased the levels of HO-1 through the Akt, p38, and Nrf2 signaling pathways.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	heme oxygenase 1	Homo sapiens	30-34
28655775-0	2017	The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.	Iron	4-8	heme oxygenase 1	Homo sapiens	73-89
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	3-7	heme oxygenase 1	Homo sapiens	36-39
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Iron	51-55	heme oxygenase 1	Homo sapiens	93-109
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Iron	51-55	heme oxygenase 1	Homo sapiens	111-114
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	3-7	heme oxygenase 1	Homo sapiens	80-83
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Heme	59-63	heme oxygenase 1	Homo sapiens	93-109
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	22-26	heme oxygenase 1	Homo sapiens	36-39
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Heme	59-63	heme oxygenase 1	Homo sapiens	111-114
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Biliverdine	167-177	heme oxygenase 1	Homo sapiens	93-109
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Biliverdine	167-177	heme oxygenase 1	Homo sapiens	111-114
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Carbon Monoxide	179-194	heme oxygenase 1	Homo sapiens	93-109
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Carbon Monoxide	179-194	heme oxygenase 1	Homo sapiens	111-114
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Iron	208-212	heme oxygenase 1	Homo sapiens	93-109
28655775-1	2017	Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron.	Iron	208-212	heme oxygenase 1	Homo sapiens	111-114
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	22-26	heme oxygenase 1	Homo sapiens	80-83
28655775-9	2017	Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1.	Heme	142-146	heme oxygenase 1	Homo sapiens	99-102
28978146-9	2017	In addition, eriodictyol promoted the expression of nuclear factor erythroid 2 p45 related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) up-regulated by As2O3.	Arsenic Trioxide	151-156	heme oxygenase 1	Homo sapiens	111-127
28790431-2	2017	The role played by the Nrf2/HO-1 system in favoring cell survival of neuroblastoma (NB) cells exposed to hydrogen peroxide (H2O2) has been investigated using undifferentiated or all-trans retinoic acid (ATRA) differentiated SH-SY5Y cells.	Hydrogen Peroxide	105-122	heme oxygenase 1	Homo sapiens	28-32
28790431-4	2017	HO-1 silencing decreased undifferentiated cell viability when exposed to H2O2, proving the role of HO-1 in cell survival.	Hydrogen Peroxide	73-77	heme oxygenase 1	Homo sapiens	0-4
28790431-5	2017	Conversely, ATRA differentiated cells exposed to H2O2 showed a significantly lower induction of HO-1, and only the supplementation with low doses of bilirubin (0,5-1 muM) restored viability.	Hydrogen Peroxide	49-53	heme oxygenase 1	Homo sapiens	96-100
28790431-7	2017	Furthermore, Bach1 was displaced from HO-1 promoter in undifferentiated cells exposed to H2O2, enabling the binding of Nrf2.	Hydrogen Peroxide	89-93	heme oxygenase 1	Homo sapiens	38-42
28790431-8	2017	On the contrary, in ATRA differentiated cells treated with H2O2, Bach1 displacement was impaired, preventing Nrf2 binding and limiting HO-1 transcription.	Hydrogen Peroxide	59-63	heme oxygenase 1	Homo sapiens	135-139
28612103-0	2017	Dihydromyricetin protects human umbilical vein endothelial cells from injury through ERK and Akt mediated Nrf2/HO-1 signaling pathway.	dihydromyricetin	0-16	heme oxygenase 1	Homo sapiens	111-115
28612103-9	2017	The anti-oxidative and anti-apoptotic effects of DMY were abrogated by the transfection of Nrf2 siRNAs and HO-1 inhibitor ZnPP.	dihydromyricetin	49-52	heme oxygenase 1	Homo sapiens	107-111
28612103-9	2017	The anti-oxidative and anti-apoptotic effects of DMY were abrogated by the transfection of Nrf2 siRNAs and HO-1 inhibitor ZnPP.	zinc protoporphyrin	122-126	heme oxygenase 1	Homo sapiens	107-111
28612103-10	2017	Furthermore, DMY might activate the Nrf2/HO-1 pathway through activation of the Akt and ERK1/2 pathways, as shown by the inhibition of Nrf2/HO-1 signaling by the inhibitors PD98059 or LY294002 and the transfection of ERK, Akt siRNAs.	dihydromyricetin	13-16	heme oxygenase 1	Homo sapiens	41-45
28612103-10	2017	Furthermore, DMY might activate the Nrf2/HO-1 pathway through activation of the Akt and ERK1/2 pathways, as shown by the inhibition of Nrf2/HO-1 signaling by the inhibitors PD98059 or LY294002 and the transfection of ERK, Akt siRNAs.	dihydromyricetin	13-16	heme oxygenase 1	Homo sapiens	140-144
28612103-10	2017	Furthermore, DMY might activate the Nrf2/HO-1 pathway through activation of the Akt and ERK1/2 pathways, as shown by the inhibition of Nrf2/HO-1 signaling by the inhibitors PD98059 or LY294002 and the transfection of ERK, Akt siRNAs.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	173-180	heme oxygenase 1	Homo sapiens	41-45
28612103-10	2017	Furthermore, DMY might activate the Nrf2/HO-1 pathway through activation of the Akt and ERK1/2 pathways, as shown by the inhibition of Nrf2/HO-1 signaling by the inhibitors PD98059 or LY294002 and the transfection of ERK, Akt siRNAs.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	173-180	heme oxygenase 1	Homo sapiens	140-144
28612103-10	2017	Furthermore, DMY might activate the Nrf2/HO-1 pathway through activation of the Akt and ERK1/2 pathways, as shown by the inhibition of Nrf2/HO-1 signaling by the inhibitors PD98059 or LY294002 and the transfection of ERK, Akt siRNAs.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	184-192	heme oxygenase 1	Homo sapiens	41-45
28612103-10	2017	Furthermore, DMY might activate the Nrf2/HO-1 pathway through activation of the Akt and ERK1/2 pathways, as shown by the inhibition of Nrf2/HO-1 signaling by the inhibitors PD98059 or LY294002 and the transfection of ERK, Akt siRNAs.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	184-192	heme oxygenase 1	Homo sapiens	140-144
28612103-11	2017	In this study, DMY protects HUVECs from ox-LDL-induced oxidative injury by activating Akt and ERK1/2, which subsequently activates Nrf2/HO-1 signaling, thereby up-regulating antioxidant enzymes and anti-apoptotic proteins.	dihydromyricetin	15-18	heme oxygenase 1	Homo sapiens	136-140
27992676-6	2017	RESULTS: CoPP administration increased human HO-1 expression and significantly reduced viraemia, although changes correlated with promoter length (Delta0.5log and Delta2log reduction with medium- and short-polymorphism respectively).	cobaltiprotoporphyrin	9-13	heme oxygenase 1	Homo sapiens	45-49
28543773-2	2017	We previously found that HO-1 protein expression is reduced in brains of HIV-infected individuals with HIV-associated neurocognitive disorders (HAND) and in HIV-infected macrophages, where this reduction associates with enhanced glutamate release and neurotoxicity.	Glutamic Acid	229-238	heme oxygenase 1	Homo sapiens	25-29
28577438-9	2017	In addition, SchB increased the expression of Nrf2 and HO-1 in a concentration-dependent manner.	schizandrin B	13-17	heme oxygenase 1	Homo sapiens	55-59
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Heme	61-65	heme oxygenase 1	Homo sapiens	0-16
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Heme	61-65	heme oxygenase 1	Homo sapiens	18-22
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Biliverdine	84-94	heme oxygenase 1	Homo sapiens	0-16
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Biliverdine	84-94	heme oxygenase 1	Homo sapiens	18-22
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Bilirubin	109-118	heme oxygenase 1	Homo sapiens	0-16
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Bilirubin	109-118	heme oxygenase 1	Homo sapiens	18-22
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Iron	185-189	heme oxygenase 1	Homo sapiens	0-16
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Iron	185-189	heme oxygenase 1	Homo sapiens	18-22
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	ferric sulfate	191-195	heme oxygenase 1	Homo sapiens	0-16
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	ferric sulfate	191-195	heme oxygenase 1	Homo sapiens	18-22
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Carbon Monoxide	201-216	heme oxygenase 1	Homo sapiens	0-16
28206992-2	2017	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide.	Carbon Monoxide	201-216	heme oxygenase 1	Homo sapiens	18-22
28206992-3	2017	Polymorphisms of the HO-1 gene promoter may modulate transcriptional activity, thereby augmenting or attenuating HO-1 expression with resultant modulation of the production of bilirubin.	Bilirubin	176-185	heme oxygenase 1	Homo sapiens	21-25
28206992-5	2017	In this clinical review, we surveyed the role of HO-1 gene promoter polymorphisms in the control of bilirubin production and further considered their role, if any, in the pathophysiology of neonatal hyperbilirubinemia.	Bilirubin	100-109	heme oxygenase 1	Homo sapiens	49-53
28627599-5	2017	We treated the MCF-7 breast cancer cell line with the HMOX-1 inducer hemin and observed that hemin induced HMOX-1 expression and inhibited migration, invasion and ROS generation in transforming growth factor-beta (TGF-beta)-treated MCF-7 cells using quantitative RT-qPCR, western blotting, wound-healing and cell invasion assays as well as fluorescent probe DCFDA.	Reactive Oxygen Species	163-166	heme oxygenase 1	Homo sapiens	54-60
28627599-6	2017	Hemin inhibited TGF-beta-induced EMT in the MCF-7 cells, whereas HMOX-1 siRNA attenuated the suppressive effect of hemin as determined by the expression and cellular distribution of selected EMT markers.	Hemin	115-120	heme oxygenase 1	Homo sapiens	65-71
28627599-7	2017	In summary, our results revealed that hemin treatment increased HMOX-1 expression and inhibited TGF-beta-induced EMT in MCF-7 cells.	Hemin	38-43	heme oxygenase 1	Homo sapiens	64-70
29108243-1	2017	Heme oxygenase-1 (HO-1) can promote tumor growth and reinforce the resistance of diffuse large B-cell lymphoma (DLBCL) cells to chemotherapeutic drug vincristine.	Vincristine	150-161	heme oxygenase 1	Homo sapiens	0-16
28432984-6	2017	The main mediator of cellular adaption to oxidative stress, nuclear factor erythroid 2-related factor 2 (NRF2) and its target genes heme oxygenase (decycling) 1 (HMOX1) or NAD(P)H quinone dehydrogenase 1 (NQO1) were strongly increased by CSEaq in a dose-dependent manner.	cseaq	238-243	heme oxygenase 1	Homo sapiens	132-160
28432984-6	2017	The main mediator of cellular adaption to oxidative stress, nuclear factor erythroid 2-related factor 2 (NRF2) and its target genes heme oxygenase (decycling) 1 (HMOX1) or NAD(P)H quinone dehydrogenase 1 (NQO1) were strongly increased by CSEaq in a dose-dependent manner.	cseaq	238-243	heme oxygenase 1	Homo sapiens	162-167
28214453-11	2017	Simvastatin decreased iNOS, HO-1, HIF-1alpha and CSE whilst it increased eNOS phosphorylation.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	28-32
28738843-9	2017	Besides, heme oxygenase 1 (HO-1) could be activated by Co exposure; ASX treatment significantly inhibited HO-1 activation, suppressing the oxidative stress induced by Co exposure.	astaxanthine	68-71	heme oxygenase 1	Homo sapiens	27-31
28738843-9	2017	Besides, heme oxygenase 1 (HO-1) could be activated by Co exposure; ASX treatment significantly inhibited HO-1 activation, suppressing the oxidative stress induced by Co exposure.	astaxanthine	68-71	heme oxygenase 1	Homo sapiens	106-110
29108243-1	2017	Heme oxygenase-1 (HO-1) can promote tumor growth and reinforce the resistance of diffuse large B-cell lymphoma (DLBCL) cells to chemotherapeutic drug vincristine.	Vincristine	150-161	heme oxygenase 1	Homo sapiens	18-22
29108243-3	2017	Silencing HO-1 gene expression resisted vorinostat-induced apoptosis and arrested cell cycle in the G0/G1 phase of LY-10 cells.	Vorinostat	40-50	heme oxygenase 1	Homo sapiens	10-14
28724911-0	2017	Honokiol inhibits c-Met-HO-1 tumor-promoting pathway and its cross-talk with calcineurin inhibitor-mediated renal cancer growth.	honokiol	0-8	heme oxygenase 1	Homo sapiens	24-28
28636034-6	2017	However, zinc(ii)-protoporphyrin IX (ZnPPIX), a selective inhibitor of HO-1, restored the GHP-mediated suppression of ROS production and NOX2, TNF-alpha, IL-1beta, IL-6 and iNOS expression.	Reactive Oxygen Species	118-121	heme oxygenase 1	Homo sapiens	71-75
28636034-9	2017	Pharmacological inhibition of Akt, ERK1/2, and p38 abrogated GHP-induced nuclear localization of NF-E2-related factor-2 (Nrf2) and the expression of HO-1.	ghp	61-64	heme oxygenase 1	Homo sapiens	149-153
28636034-10	2017	In summary, GHP inhibits the LPS-induced inflammatory status through upregulating HO-1 expression via PI3K/Akt, ERK1/2 and p38 signaling pathways in RAW264.7 macrophages.	ghp	12-15	heme oxygenase 1	Homo sapiens	82-86
28636034-2	2017	However, whether heme oxygenase-1 (HO-1) is involved in the cytoprotective effect of GHP against the inflammatory status remains unclear.	ghp	85-88	heme oxygenase 1	Homo sapiens	17-33
28636034-2	2017	However, whether heme oxygenase-1 (HO-1) is involved in the cytoprotective effect of GHP against the inflammatory status remains unclear.	ghp	85-88	heme oxygenase 1	Homo sapiens	35-39
28636034-6	2017	However, zinc(ii)-protoporphyrin IX (ZnPPIX), a selective inhibitor of HO-1, restored the GHP-mediated suppression of ROS production and NOX2, TNF-alpha, IL-1beta, IL-6 and iNOS expression.	zinc(ii)-protoporphyrin ix	9-35	heme oxygenase 1	Homo sapiens	71-75
28636034-6	2017	However, zinc(ii)-protoporphyrin IX (ZnPPIX), a selective inhibitor of HO-1, restored the GHP-mediated suppression of ROS production and NOX2, TNF-alpha, IL-1beta, IL-6 and iNOS expression.	znppix	37-43	heme oxygenase 1	Homo sapiens	71-75
28636034-6	2017	However, zinc(ii)-protoporphyrin IX (ZnPPIX), a selective inhibitor of HO-1, restored the GHP-mediated suppression of ROS production and NOX2, TNF-alpha, IL-1beta, IL-6 and iNOS expression.	ghp	90-93	heme oxygenase 1	Homo sapiens	71-75
28955775-4	2017	The enhanced heme synthesis in Caco-2 cells was more pronounced under the effect of the combination of ALA and SFC than under the effect of ALA alone, as reflected by the induced expression of heme oxygenase 1 (HO-1), as well as a reduced protein level of the transcriptional corepressor Bach1.	Heme	13-17	heme oxygenase 1	Homo sapiens	193-209
28955775-4	2017	The enhanced heme synthesis in Caco-2 cells was more pronounced under the effect of the combination of ALA and SFC than under the effect of ALA alone, as reflected by the induced expression of heme oxygenase 1 (HO-1), as well as a reduced protein level of the transcriptional corepressor Bach1.	Heme	13-17	heme oxygenase 1	Homo sapiens	211-215
28955775-4	2017	The enhanced heme synthesis in Caco-2 cells was more pronounced under the effect of the combination of ALA and SFC than under the effect of ALA alone, as reflected by the induced expression of heme oxygenase 1 (HO-1), as well as a reduced protein level of the transcriptional corepressor Bach1.	5-amino levulinic acid	103-106	heme oxygenase 1	Homo sapiens	193-209
28955775-4	2017	The enhanced heme synthesis in Caco-2 cells was more pronounced under the effect of the combination of ALA and SFC than under the effect of ALA alone, as reflected by the induced expression of heme oxygenase 1 (HO-1), as well as a reduced protein level of the transcriptional corepressor Bach1.	5-amino levulinic acid	103-106	heme oxygenase 1	Homo sapiens	211-215
28955775-5	2017	Chromatin immunoprecipitation analysis confirmed Bach1 chromatin occupancy at the enhancer regions of HO-1, which were significantly decreased by the addition of ALA and SFC.	5-amino levulinic acid	162-165	heme oxygenase 1	Homo sapiens	102-106
28347842-0	2017	Potential role of heme metabolism in the inducible expression of heme oxygenase-1.	Heme	18-22	heme oxygenase 1	Homo sapiens	65-81
28704474-6	2017	In these animals the catalytic activity of heme oxygenase 1 contributed to the release of elemental iron from the protoporphyrin ring of heme within enterocytes, which may then be transported by the strongly expressed ferroportin across the basolateral membrane to the circulation.	Iron	100-104	heme oxygenase 1	Homo sapiens	43-59
28704474-6	2017	In these animals the catalytic activity of heme oxygenase 1 contributed to the release of elemental iron from the protoporphyrin ring of heme within enterocytes, which may then be transported by the strongly expressed ferroportin across the basolateral membrane to the circulation.	protoporphyrin IX	114-128	heme oxygenase 1	Homo sapiens	43-59
29089150-0	2017	Hemin Reduces HMGB1 Release by UVB in an AMPK/HO-1-dependent Pathway in Human Keratinocytes HaCaT Cells.	Hemin	0-5	heme oxygenase 1	Homo sapiens	46-50
29089150-2	2017	We hypothesized that hemin might reduce HMGB1 release through the induction of HO-1 in UVB-induced HaCaTs.	Hemin	21-26	heme oxygenase 1	Homo sapiens	79-83
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Heme	11-15	heme oxygenase 1	Homo sapiens	29-33
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Carbon Monoxide	79-94	heme oxygenase 1	Homo sapiens	11-27
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Carbon Monoxide	79-94	heme oxygenase 1	Homo sapiens	29-33
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Carbon Monoxide	96-98	heme oxygenase 1	Homo sapiens	11-27
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Carbon Monoxide	96-98	heme oxygenase 1	Homo sapiens	29-33
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Iron	109-113	heme oxygenase 1	Homo sapiens	11-27
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Iron	109-113	heme oxygenase 1	Homo sapiens	29-33
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	11-27
28347842-2	2017	The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals.	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	29-33
28347842-3	2017	We examined the involvement of heme metabolism in the induction of HO-1 by the inducers sulforaphane and sodium arsenite.	Heme	31-35	heme oxygenase 1	Homo sapiens	67-71
28347842-3	2017	We examined the involvement of heme metabolism in the induction of HO-1 by the inducers sulforaphane and sodium arsenite.	sulforaphane	88-100	heme oxygenase 1	Homo sapiens	67-71
28347842-3	2017	We examined the involvement of heme metabolism in the induction of HO-1 by the inducers sulforaphane and sodium arsenite.	sodium arsenite	105-120	heme oxygenase 1	Homo sapiens	67-71
28445830-0	2017	Overexpression of heme oxygenase-1 in bone marrow stromal cells promotes microenvironment-mediated imatinib resistance in chronic myeloid leukemia.	Imatinib Mesylate	99-107	heme oxygenase 1	Homo sapiens	18-34
28445830-6	2017	Following co-culture of BMSCs and K562 cells, up-regulating HO-1 expression in bone marrow stromal cells increased the imatinib (IM) resistance of K562 cells, whereas the apoptosis of K562 cells was effectively promoted without BMSCs co-culture.	Imatinib Mesylate	119-127	heme oxygenase 1	Homo sapiens	60-64
28347842-4	2017	METHODS: We examined the expression of HO-1 in sulforaphane-, sodium arsenite- and CORM3-treated HEK293T cells, by measuring the transcriptional activity and levels of mRNA and protein.	sulforaphane	47-59	heme oxygenase 1	Homo sapiens	39-43
28347842-4	2017	METHODS: We examined the expression of HO-1 in sulforaphane-, sodium arsenite- and CORM3-treated HEK293T cells, by measuring the transcriptional activity and levels of mRNA and protein.	sodium arsenite	62-77	heme oxygenase 1	Homo sapiens	39-43
28347842-5	2017	RESULTS: The blockade of heme biosynthesis by succinylacetone and N-methyl protoporphyrin, which are inhibitors of heme biosynthesis, markedly decreased the induction of HO-1.	Heme	25-29	heme oxygenase 1	Homo sapiens	170-174
28347842-5	2017	RESULTS: The blockade of heme biosynthesis by succinylacetone and N-methyl protoporphyrin, which are inhibitors of heme biosynthesis, markedly decreased the induction of HO-1.	succinylacetone	46-61	heme oxygenase 1	Homo sapiens	170-174
28347842-5	2017	RESULTS: The blockade of heme biosynthesis by succinylacetone and N-methyl protoporphyrin, which are inhibitors of heme biosynthesis, markedly decreased the induction of HO-1.	N-methylprotoporphyrin IX	66-89	heme oxygenase 1	Homo sapiens	170-174
28499242-9	2017	GSP also inhibited the over-generation of TGF-beta1 and p-Smad3, as well as enhanced the levels of Smad7, Nrf-2, HO-1, gamma-GCLC and miR-133a/b.	gamma-Thio-GTP	0-3	heme oxygenase 1	Homo sapiens	113-129
28347842-5	2017	RESULTS: The blockade of heme biosynthesis by succinylacetone and N-methyl protoporphyrin, which are inhibitors of heme biosynthesis, markedly decreased the induction of HO-1.	Heme	115-119	heme oxygenase 1	Homo sapiens	170-174
28347842-7	2017	The cessation of HO-1 induction occurred at the transcriptional and translational levels, and was mediated by the activation of the heme-binding transcriptional repressor Bach1 and translational factor HRI.	Heme	132-136	heme oxygenase 1	Homo sapiens	17-21
28347842-9	2017	CONCLUSIONS: We demonstrated the importance of heme metabolism in the stress-inducible expression of HO-1, and also that heme and its degradation products are protective factors for self-defense responses.	Heme	47-51	heme oxygenase 1	Homo sapiens	101-105
28347842-10	2017	GENERAL SIGNIFICANCE: The key role of heme metabolism in the stress-inducible expression of HO-1 may promote further studies on heme and its degradation products as protective factors of cellular stresses and iron homeostasis in specialized cells, organs, and whole animal systems.	Heme	38-42	heme oxygenase 1	Homo sapiens	92-96
28347842-10	2017	GENERAL SIGNIFICANCE: The key role of heme metabolism in the stress-inducible expression of HO-1 may promote further studies on heme and its degradation products as protective factors of cellular stresses and iron homeostasis in specialized cells, organs, and whole animal systems.	Heme	128-132	heme oxygenase 1	Homo sapiens	92-96
28206713-6	2017	ZO-1 and human HO-1 in Caco2 were significantly decreased after treatment with TNF-alpha; and this effect was reduced when coculture with MSCs from bone marrow.	caco2	23-28	heme oxygenase 1	Homo sapiens	15-19
28347842-10	2017	GENERAL SIGNIFICANCE: The key role of heme metabolism in the stress-inducible expression of HO-1 may promote further studies on heme and its degradation products as protective factors of cellular stresses and iron homeostasis in specialized cells, organs, and whole animal systems.	Iron	209-213	heme oxygenase 1	Homo sapiens	92-96
28206713-8	2017	In contrast, ZO-1 and human HO-1 increased significantly when the damaged Caco2 was treated with HO-MSCs.	caco2	74-79	heme oxygenase 1	Homo sapiens	28-32
28245071-7	2017	Inhibition of miR-153 significantly promoted the expression of Nrf2 and heme oxygenase-1 (HO-1).	mir-153	14-21	heme oxygenase 1	Homo sapiens	72-88
28473247-0	2017	Oxidized 5-aminosalicylic acid activates Nrf2-HO-1 pathway by covalently binding to Keap1: Implication in anti-inflammatory actions of 5-aminosalicylic acid.	Mesalamine	9-30	heme oxygenase 1	Homo sapiens	46-50
28473247-0	2017	Oxidized 5-aminosalicylic acid activates Nrf2-HO-1 pathway by covalently binding to Keap1: Implication in anti-inflammatory actions of 5-aminosalicylic acid.	Mesalamine	135-156	heme oxygenase 1	Homo sapiens	46-50
28473247-9	2017	In parallel, rectal administration of 5-ASA increased the level of HO-1 and nuclear Nrf2 in the inflamed colonic tissues, but not in normal colonic tissues.	Mesalamine	38-43	heme oxygenase 1	Homo sapiens	67-71
28473247-10	2017	Moreover, oral gavage of sulfasalazine, a colon-specific prodrug of 5-ASA currently used clinically, activated the Nrf2-HO-1 pathway in the colonic tissues where inflammation was in progress, which was not observed when inflammation subsided.	Sulfasalazine	25-38	heme oxygenase 1	Homo sapiens	120-124
28473247-10	2017	Moreover, oral gavage of sulfasalazine, a colon-specific prodrug of 5-ASA currently used clinically, activated the Nrf2-HO-1 pathway in the colonic tissues where inflammation was in progress, which was not observed when inflammation subsided.	Mesalamine	68-73	heme oxygenase 1	Homo sapiens	120-124
28473247-11	2017	Collectively, our data suggest that Nrf2-HO-1 pathway is involved in the anti-inflammatory pharmacology of 5-ASA, which was likely being exerted exclusively in the inflammatory state.	Mesalamine	107-112	heme oxygenase 1	Homo sapiens	41-45
28245071-9	2017	Our study indicates that the inhibition of miR-153 protects neurons against OGD/R-induced injury by regulating Nrf2/HO-1 signaling and suggests a potential therapeutic target for cerebral ischemia/reperfusion injury.	mir-153	43-50	heme oxygenase 1	Homo sapiens	116-120
28559202-10	2017	Treatment with RA remarkably increased the Nrf2 protein expression levels in the nucleus, HO-1 and NQO1 protein expression levels, and the activities of SOD and CAT.	rosmarinic acid	15-17	heme oxygenase 1	Homo sapiens	90-94
28245071-7	2017	Inhibition of miR-153 significantly promoted the expression of Nrf2 and heme oxygenase-1 (HO-1).	mir-153	14-21	heme oxygenase 1	Homo sapiens	90-94
28566367-4	2017	Our results show that after hRSV infection, HO-1 induction with metalloporphyrin cobalt protoporphyrin IX significantly reduces the loss of body weight due to hRSV-induced disease.	metalloporphyrin cobalt protoporphyrin ix	64-105	heme oxygenase 1	Homo sapiens	44-48
28790819-14	2017	The KC-GN-mediated protection against OGD/R-induced neurotoxicity was diminished by NRF2 and heme oxygenase-1 gene knockdowns.	kc-gn	4-9	heme oxygenase 1	Homo sapiens	93-109
28093052-8	2017	Additionally, CCI-induced mitophagy was shown to be mediated by the oxidative stress-related extracellular signal-regulated kinase (ERK)/nuclear factor-erythroid2-like2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway, which may serve to reduce the apoptosis induced by oxidative stress.	CCI	14-17	heme oxygenase 1	Homo sapiens	176-192
28093052-8	2017	Additionally, CCI-induced mitophagy was shown to be mediated by the oxidative stress-related extracellular signal-regulated kinase (ERK)/nuclear factor-erythroid2-like2 (Nrf2)/heme oxygenase-1 (HO-1) signaling pathway, which may serve to reduce the apoptosis induced by oxidative stress.	CCI	14-17	heme oxygenase 1	Homo sapiens	194-198
28093052-9	2017	These results suggest that CCI-induced mitophagy serves to diminish apoptosis-mediated intestinal epithelial cell damage and to improve intestinal permeability, via ERK/Nrf2/HO-1 signaling.	CCI	27-30	heme oxygenase 1	Homo sapiens	174-178
28343048-0	2017	Protective effect of CDDO-ethyl amide against high-glucose-induced oxidative injury via the Nrf2/HO-1 pathway.	2-cyano-3,12-dioxooleana-1,9(11)-dien-28-oic acid ethyl amide	21-37	heme oxygenase 1	Homo sapiens	97-101
28343048-0	2017	Protective effect of CDDO-ethyl amide against high-glucose-induced oxidative injury via the Nrf2/HO-1 pathway.	Glucose	51-58	heme oxygenase 1	Homo sapiens	97-101
28343048-6	2017	The protein expression levels of HO-1 and Nrf2 were measured through Western blot RESULTS: CDDO-EA elicited cytoprotective effects against NP cell apoptosis and ROS accumulation induced by high glucose.	CDDO-EA	91-98	heme oxygenase 1	Homo sapiens	33-37
28343048-7	2017	CDDO-EA treatment increased the HO-1 and Nrf2 expression abrogated by HO-1, Nrf2, and mitogen-activated protein kinase inhibitors.	CDDO-EA	0-7	heme oxygenase 1	Homo sapiens	32-36
28343048-7	2017	CDDO-EA treatment increased the HO-1 and Nrf2 expression abrogated by HO-1, Nrf2, and mitogen-activated protein kinase inhibitors.	CDDO-EA	0-7	heme oxygenase 1	Homo sapiens	70-74
28343048-8	2017	CONCLUSIONS: The phosphorylation and nuclear translocation of Nrf2 are crucial for HO-1 overexpression induced by CDDO-EA, which is essential for the cytoprotection against high-glucose-induced oxidative stress in NP cells.	CDDO-EA	114-121	heme oxygenase 1	Homo sapiens	83-87
28343048-8	2017	CONCLUSIONS: The phosphorylation and nuclear translocation of Nrf2 are crucial for HO-1 overexpression induced by CDDO-EA, which is essential for the cytoprotection against high-glucose-induced oxidative stress in NP cells.	Glucose	178-185	heme oxygenase 1	Homo sapiens	83-87
28978042-0	2017	Translocation of heme oxygenase-1 contributes to imatinib resistance in chronic myelogenous leukemia.	Imatinib Mesylate	49-57	heme oxygenase 1	Homo sapiens	17-33
28978042-1	2017	Heme oxygenase-1 (HO-1) degrades heme to bilirubin.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-16
28978042-1	2017	Heme oxygenase-1 (HO-1) degrades heme to bilirubin.	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
28978042-1	2017	Heme oxygenase-1 (HO-1) degrades heme to bilirubin.	Bilirubin	41-50	heme oxygenase 1	Homo sapiens	0-16
28978042-1	2017	Heme oxygenase-1 (HO-1) degrades heme to bilirubin.	Bilirubin	41-50	heme oxygenase 1	Homo sapiens	18-22
28978042-7	2017	Since translocation of HO-1 disrupts the association with cytochrome P450 reductase, heme degrading activity was higher for ER anchored versus anchorless HO-1.	Heme	85-89	heme oxygenase 1	Homo sapiens	23-27
28978042-7	2017	Since translocation of HO-1 disrupts the association with cytochrome P450 reductase, heme degrading activity was higher for ER anchored versus anchorless HO-1.	Heme	85-89	heme oxygenase 1	Homo sapiens	154-158
28978042-8	2017	Cell viability tests with increasing concentrations of imatinib showed IC50-values for all six cell lines with ER localized HO-1 that were similar to control cells.	Imatinib Mesylate	55-63	heme oxygenase 1	Homo sapiens	124-128
28978042-9	2017	However, out of the seven cell lines with anchorless HO-1, two showed a statistically significant increase in the imatinib IC50 (19.76 muM and 12.35 muM versus 2.35 - 7.57 muM of sensitive cell lines) corresponding to plasma concentrations outside the therapeutic range.	Imatinib Mesylate	114-122	heme oxygenase 1	Homo sapiens	53-57
28978042-10	2017	We conclude that the presence of translocated HO-1 in the cytosol and nucleus supports imatinib resistance while it is not sufficient to cause imatinib resistance in every cell line.	Imatinib Mesylate	87-95	heme oxygenase 1	Homo sapiens	46-50
28978042-11	2017	In contrast, an increase in ER anchored HO-1 with high heme degrading activity does not contribute to imatinib resistance.	Heme	55-59	heme oxygenase 1	Homo sapiens	40-44
28500562-12	2017	In GBM cell lines, 5-ALA induced fluorescence is variable and influenced by EGF-induced downstream activation of HO-1.	5-amino levulinic acid	19-24	heme oxygenase 1	Homo sapiens	113-117
28500562-13	2017	HO-1 protein expression was identified as a negative regulator of 5-ALA induced fluorescence in GBM cells.	5-amino levulinic acid	66-71	heme oxygenase 1	Homo sapiens	0-4
28617444-0	2017	Heme oxygenase-1 derived carbon monoxide suppresses Abeta1-42 toxicity in astrocytes.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
28634389-0	2017	Novel indolyl-chalcone derivatives inhibit A549 lung cancer cell growth through activating Nrf-2/HO-1 and inducing apoptosis in vitro and in vivo.	indolyl chalcone	6-22	heme oxygenase 1	Homo sapiens	97-101
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Carbon Monoxide	147-162	heme oxygenase 1	Homo sapiens	13-29
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Carbon Monoxide	147-162	heme oxygenase 1	Homo sapiens	31-35
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Carbon Monoxide	147-162	heme oxygenase 1	Homo sapiens	206-210
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Carbon Monoxide	164-166	heme oxygenase 1	Homo sapiens	13-29
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Carbon Monoxide	164-166	heme oxygenase 1	Homo sapiens	31-35
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Carbon Monoxide	164-166	heme oxygenase 1	Homo sapiens	206-210
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Reactive Oxygen Species	311-314	heme oxygenase 1	Homo sapiens	13-29
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	Reactive Oxygen Species	311-314	heme oxygenase 1	Homo sapiens	31-35
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	UNII-042A8N37WH	63-68	heme oxygenase 1	Homo sapiens	13-29
28617444-7	2017	Induction of haem oxygenase-1 (HO-1) protected astrocytes from Abeta(1-42) toxicity, and this protective effect was mimicked by application of the carbon monoxide (CO) releasing molecule CORM-2, suggesting HO-1 protection was attributable to its formation of CO. CO suppressed the rise of NADPH oxidase-derived ROS caused by Abeta(1-42).	UNII-042A8N37WH	63-68	heme oxygenase 1	Homo sapiens	31-35
28617444-8	2017	Under hypoxic conditions (0.5% O2, 48 h) HO-1 was induced in astrocytes and Abeta(1-42) toxicity was significantly reduced, an effect which was reversed by the specific HO-1 inhibitor, QC-15.	Oxygen	31-33	heme oxygenase 1	Homo sapiens	41-45
28617444-8	2017	Under hypoxic conditions (0.5% O2, 48 h) HO-1 was induced in astrocytes and Abeta(1-42) toxicity was significantly reduced, an effect which was reversed by the specific HO-1 inhibitor, QC-15.	Oxygen	31-33	heme oxygenase 1	Homo sapiens	169-173
28617444-8	2017	Under hypoxic conditions (0.5% O2, 48 h) HO-1 was induced in astrocytes and Abeta(1-42) toxicity was significantly reduced, an effect which was reversed by the specific HO-1 inhibitor, QC-15.	TERT-BUTYL 6-OXO-2-AZASPIRO[3.3]HEPTANE-2-CARBOXYLATE	185-190	heme oxygenase 1	Homo sapiens	41-45
28617444-8	2017	Under hypoxic conditions (0.5% O2, 48 h) HO-1 was induced in astrocytes and Abeta(1-42) toxicity was significantly reduced, an effect which was reversed by the specific HO-1 inhibitor, QC-15.	TERT-BUTYL 6-OXO-2-AZASPIRO[3.3]HEPTANE-2-CARBOXYLATE	185-190	heme oxygenase 1	Homo sapiens	169-173
28604588-0	2017	Docosahexaenoic Acid Induces Expression of Heme Oxygenase-1 and NAD(P)H:quinone Oxidoreductase through Activation of Nrf2 in Human Mammary Epithelial Cells.	Docosahexaenoic Acids	0-20	heme oxygenase 1	Homo sapiens	43-59
28604588-2	2017	In this study, we found that DHA induced expression of two representative antioxidant/cytoprotective enzymes, heme oxygenase-1 (HO-1) and NAD(P)H:quinone oxidoreductase (NQO1), in human mammary epithealial (MCF-10A) cells.	Docosahexaenoic Acids	29-32	heme oxygenase 1	Homo sapiens	110-126
28604588-9	2017	In conclusion, DHA activates Nrf2, possibly through modification of critical Keap1 cysteine 288 residue and PKCdelta-mediated phosphorylation of Nrf2, leading to upregulation of HO-1 and NQO1 expression.	Docosahexaenoic Acids	15-18	heme oxygenase 1	Homo sapiens	178-182
28604588-4	2017	Nrf2 gene silencing by siRNA abolished the DHA-induced expression of HO-1 and NQO1 proteins.	Docosahexaenoic Acids	43-46	heme oxygenase 1	Homo sapiens	69-73
28604588-5	2017	When MCF-10A cells were transfected with mutant constructs in which the cysteine 151 or 288 residue of Keap1 was replaced by serine, DHA-induced expression of HO-1 and NQO1 was markedly reduced.	Serine	125-131	heme oxygenase 1	Homo sapiens	159-163
28604588-5	2017	When MCF-10A cells were transfected with mutant constructs in which the cysteine 151 or 288 residue of Keap1 was replaced by serine, DHA-induced expression of HO-1 and NQO1 was markedly reduced.	Docosahexaenoic Acids	133-136	heme oxygenase 1	Homo sapiens	159-163
28224676-6	2017	RESULTS: Stimulation of hPVECs and human vaginal epithelial cell line, VK2/E6E7 with H2 O2 augmented the expression of Hb-alpha, Hb-beta, Nrf2, heme oxygenase-1 (HO-1), and reactive oxygen species (ROS).	Hydrogen Peroxide	85-90	heme oxygenase 1	Homo sapiens	144-160
28598396-0	2017	Embryotoxicity Caused by DON-Induced Oxidative Stress Mediated by Nrf2/HO-1 Pathway.	deoxynivalenol	25-28	heme oxygenase 1	Homo sapiens	71-75
28598396-5	2017	At the same time Nrf2/HO-1 pathway is up-regulated by ROS to protect placenta cells from oxidative damage.	ros	54-57	heme oxygenase 1	Homo sapiens	22-26
28598396-6	2017	In DON-treated BeWo cells, the level of ROS has time-effect and dose-effect relationships with HO-1 expression.	ros	40-43	heme oxygenase 1	Homo sapiens	95-99
28598396-9	2017	Besides, Nrf2/HO-1 pathway accompanied by the "threshold effect" also plays an important role against DON-induced oxidative damage in this process.	deoxynivalenol	102-105	heme oxygenase 1	Homo sapiens	14-18
28392465-12	2017	Our study showed that L-carnitine administration activated p38MAPK/Nrf2 signalling, initiating the expression of HO1 and NQO1, which have anti-apoptotic and anti-oxidative effects, respectively.	Carnitine	22-33	heme oxygenase 1	Homo sapiens	113-116
28652743-6	2017	Pretreatment of A549 cells on the apical side of the coculture system with the phagocytosis inhibitor cytochalasin B (CB) blocked ZnO-NP-induced HO-1 and PECAM-1 expression in HCAEC, indicating that endocytosis of ZnO-NPs by alveolar epithelial cells was involved in ZnO-NP-induced HO-1 or PECAM-1 expression in endothelial cells.	Cytochalasin B	102-116	heme oxygenase 1	Homo sapiens	145-149
28652743-6	2017	Pretreatment of A549 cells on the apical side of the coculture system with the phagocytosis inhibitor cytochalasin B (CB) blocked ZnO-NP-induced HO-1 and PECAM-1 expression in HCAEC, indicating that endocytosis of ZnO-NPs by alveolar epithelial cells was involved in ZnO-NP-induced HO-1 or PECAM-1 expression in endothelial cells.	Cytochalasin B	102-116	heme oxygenase 1	Homo sapiens	282-286
28652743-6	2017	Pretreatment of A549 cells on the apical side of the coculture system with the phagocytosis inhibitor cytochalasin B (CB) blocked ZnO-NP-induced HO-1 and PECAM-1 expression in HCAEC, indicating that endocytosis of ZnO-NPs by alveolar epithelial cells was involved in ZnO-NP-induced HO-1 or PECAM-1 expression in endothelial cells.	Zinc Oxide	130-133	heme oxygenase 1	Homo sapiens	145-149
28652743-6	2017	Pretreatment of A549 cells on the apical side of the coculture system with the phagocytosis inhibitor cytochalasin B (CB) blocked ZnO-NP-induced HO-1 and PECAM-1 expression in HCAEC, indicating that endocytosis of ZnO-NPs by alveolar epithelial cells was involved in ZnO-NP-induced HO-1 or PECAM-1 expression in endothelial cells.	Zinc Oxide	130-133	heme oxygenase 1	Homo sapiens	282-286
28652743-8	2017	ZnO-NP treatment induced lung and systemic inflammation, dyslipidemia, increased levels of serum HO-1 and PECAM-1, and aortic pathological damage.	zno-np	0-6	heme oxygenase 1	Homo sapiens	97-101
28224676-6	2017	RESULTS: Stimulation of hPVECs and human vaginal epithelial cell line, VK2/E6E7 with H2 O2 augmented the expression of Hb-alpha, Hb-beta, Nrf2, heme oxygenase-1 (HO-1), and reactive oxygen species (ROS).	Reactive Oxygen Species	173-196	heme oxygenase 1	Homo sapiens	144-160
28224676-6	2017	RESULTS: Stimulation of hPVECs and human vaginal epithelial cell line, VK2/E6E7 with H2 O2 augmented the expression of Hb-alpha, Hb-beta, Nrf2, heme oxygenase-1 (HO-1), and reactive oxygen species (ROS).	Reactive Oxygen Species	198-201	heme oxygenase 1	Homo sapiens	144-160
28366867-8	2017	5muM Cd2+ exposure significantly augmented nuclear Nrf2, GSH and GCLC, GCLM, HMOX1, TNFalpha and IL-6 mRNA expression but not GSR, however these upsurges were significantly abrogated by ALA or 1muM Cd2+ pre-treatments.	Thioctic Acid	186-189	heme oxygenase 1	Homo sapiens	77-82
28596808-7	2017	In addition, signaling pathways involving heme oxygenase-1 and p38 mitogen-activated protein kinase are associated with the alleviative effects of saturated hydrogen saline on LPS-induced autophagy.	saturated hydrogen saline	147-172	heme oxygenase 1	Homo sapiens	42-58
28229933-5	2017	We investigated the activation of nuclear factor-E2-related factor 2 (Nrf2) which regulates various antioxidant genes including heme oxygenase-1 (HMOX1), following exposure to sodium arsenite or cadmium chloride in lamin knockdown human cell lines and primary HGPS human fibroblasts.	sodium arsenite	176-191	heme oxygenase 1	Homo sapiens	128-144
28675952-4	2017	The expression of three antioxidant proteins, superoxide dismutase (SOD)-2, haem oxygenase (HO)-1, and sirtuin (SIRT) 1, was reduced upon H2O2 stimulation in miR-200c-overexpressed A549 cells.	Hydrogen Peroxide	138-142	heme oxygenase 1	Homo sapiens	76-97
28440398-0	2017	Lycopene inhibits NF-kappaB activation and adhesion molecule expression through Nrf2-mediated heme oxygenase-1 in endothelial cells.	Lycopene	0-8	heme oxygenase 1	Homo sapiens	94-110
28440398-8	2017	Subsequently, lycopene induced nuclear factor-erythroid 2 related factor 2 (Nrf2) activation, leading to the increased expression of downstream of heme oxygenase-1 (HO-1).	Lycopene	14-22	heme oxygenase 1	Homo sapiens	147-163
28440398-8	2017	Subsequently, lycopene induced nuclear factor-erythroid 2 related factor 2 (Nrf2) activation, leading to the increased expression of downstream of heme oxygenase-1 (HO-1).	Lycopene	14-22	heme oxygenase 1	Homo sapiens	165-169
28440398-9	2017	The use of siRNA targeting HO-1 blocked the inhibitory effects of lycopene on IkappaB degradation and ICAM-1 expression.	Lycopene	66-74	heme oxygenase 1	Homo sapiens	27-31
28440398-10	2017	The inhibitory effects of lycopene thus appear to be mediated through its induction of Nrf2-mediated HO-1 expression.	Lycopene	26-34	heme oxygenase 1	Homo sapiens	101-105
28440398-11	2017	Therefore, the findings of the present study indicate that lycopene suppresses the activation of TNFalpha-induced signaling pathways through the upregulation of Nrf2-mediated HO-1 expression.	Lycopene	59-67	heme oxygenase 1	Homo sapiens	175-179
28542559-5	2017	Inhibition of ERK5 by siRNA or BIX02189 (a specific ERK5 inhibitor) reduced the statin-induced upregulations of Nrf2, NQO1, and HO-1.	BIX 02189	31-39	heme oxygenase 1	Homo sapiens	128-132
28534853-4	2017	Results from in vitro experiments show that 1T3O effectively inhibits 6-hydroxydopamine-induced (6-OHDA-induced) activation of both p38 mitogen-activated protein kinase (MAPK) and caspase-3 in SH-SY5Y cells; and enhances nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expression via phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) signaling.	Oxidopamine	70-87	heme oxygenase 1	Homo sapiens	276-292
28534853-4	2017	Results from in vitro experiments show that 1T3O effectively inhibits 6-hydroxydopamine-induced (6-OHDA-induced) activation of both p38 mitogen-activated protein kinase (MAPK) and caspase-3 in SH-SY5Y cells; and enhances nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expression via phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) signaling.	Oxidopamine	70-87	heme oxygenase 1	Homo sapiens	294-298
28534853-4	2017	Results from in vitro experiments show that 1T3O effectively inhibits 6-hydroxydopamine-induced (6-OHDA-induced) activation of both p38 mitogen-activated protein kinase (MAPK) and caspase-3 in SH-SY5Y cells; and enhances nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expression via phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) signaling.	Oxidopamine	97-103	heme oxygenase 1	Homo sapiens	276-292
28534853-4	2017	Results from in vitro experiments show that 1T3O effectively inhibits 6-hydroxydopamine-induced (6-OHDA-induced) activation of both p38 mitogen-activated protein kinase (MAPK) and caspase-3 in SH-SY5Y cells; and enhances nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) expression via phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) signaling.	Oxidopamine	97-103	heme oxygenase 1	Homo sapiens	294-298
28513573-5	2017	Oxidative molecules were altered after the H2O2 exposure, whereby the signaling of Nrf2 was activated with an increase in its downstream effectors, heme oxygenase-1 (HO-1), NAD(P)H:quinone oxidoreductase 1 (NQO1) and gamma-glutamyl cysteine synthetase (gamma-GCS).	Hydrogen Peroxide	43-47	heme oxygenase 1	Homo sapiens	148-164
28553288-8	2017	We found that Mtb-induced HO-1 expression requires NADPH oxidase-dependent reactive oxygen species production induced by the early-secreted antigen ESAT-6, which in turn triggers nuclear translocation of the transcription factor NRF-2.	Reactive Oxygen Species	75-98	heme oxygenase 1	Homo sapiens	26-30
28500309-7	2017	In HUVECs, resveratrol significantly increased mRNA of anti-oxidant enzymes HO-1, NQO1, GCLC and TXN but did not significantly alter HO-1 protein expression, whilst reducing HO-1 protein in trophoblast.	Resveratrol	11-22	heme oxygenase 1	Homo sapiens	76-80
27960551-0	2017	Date fruits inhibit hepatocyte apoptosis and modulate the expression of hepatocyte growth factor, cytochrome P450 2E1 and heme oxygenase-1 in carbon tetrachloride-induced liver fibrosis.	Carbon Tetrachloride	142-162	heme oxygenase 1	Homo sapiens	122-138
28229933-5	2017	We investigated the activation of nuclear factor-E2-related factor 2 (Nrf2) which regulates various antioxidant genes including heme oxygenase-1 (HMOX1), following exposure to sodium arsenite or cadmium chloride in lamin knockdown human cell lines and primary HGPS human fibroblasts.	sodium arsenite	176-191	heme oxygenase 1	Homo sapiens	146-151
28229933-5	2017	We investigated the activation of nuclear factor-E2-related factor 2 (Nrf2) which regulates various antioxidant genes including heme oxygenase-1 (HMOX1), following exposure to sodium arsenite or cadmium chloride in lamin knockdown human cell lines and primary HGPS human fibroblasts.	Cadmium Chloride	195-211	heme oxygenase 1	Homo sapiens	146-151
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
28243792-0	2017	HMOX1 as a marker of iron excess-induced adipose tissue dysfunction, affecting glucose uptake and respiratory capacity in human adipocytes.	Iron	21-25	heme oxygenase 1	Homo sapiens	0-5
28243792-0	2017	HMOX1 as a marker of iron excess-induced adipose tissue dysfunction, affecting glucose uptake and respiratory capacity in human adipocytes.	Glucose	79-86	heme oxygenase 1	Homo sapiens	0-5
28243792-2	2017	Here, we aimed to investigate the possible role of haem oxygenase 1 (HMOX1) in iron excess-induced adipose tissue dysfunction.	Iron	79-83	heme oxygenase 1	Homo sapiens	51-67
28243792-2	2017	Here, we aimed to investigate the possible role of haem oxygenase 1 (HMOX1) in iron excess-induced adipose tissue dysfunction.	Iron	79-83	heme oxygenase 1	Homo sapiens	69-74
28243792-5	2017	RESULTS: Adipose tissue HMOX1 was increased in obese participants (p = 0.01) and positively associated with obesity-related metabolic disturbances, and markers of iron accumulation, inflammation and oxidative stress (p &lt; 0.01).	Iron	163-167	heme oxygenase 1	Homo sapiens	24-29
28243792-10	2017	In human adipocytes, iron excess and inflammation led to increased HMOX1 mRNA levels.	Iron	21-25	heme oxygenase 1	Homo sapiens	67-72
28243792-11	2017	HMOX1 induction (by haem arginate [hemin] administration), resulted in a significant reduction of mitochondrial respiratory capacity (including basal respiration and spare respiratory capacity), glucose uptake and adipogenesis in parallel with increased expression of inflammatory- and iron excess-related genes.	heme arginate	20-33	heme oxygenase 1	Homo sapiens	0-5
28243792-11	2017	HMOX1 induction (by haem arginate [hemin] administration), resulted in a significant reduction of mitochondrial respiratory capacity (including basal respiration and spare respiratory capacity), glucose uptake and adipogenesis in parallel with increased expression of inflammatory- and iron excess-related genes.	heme arginate	35-40	heme oxygenase 1	Homo sapiens	0-5
28243792-11	2017	HMOX1 induction (by haem arginate [hemin] administration), resulted in a significant reduction of mitochondrial respiratory capacity (including basal respiration and spare respiratory capacity), glucose uptake and adipogenesis in parallel with increased expression of inflammatory- and iron excess-related genes.	Glucose	195-202	heme oxygenase 1	Homo sapiens	0-5
28243792-11	2017	HMOX1 induction (by haem arginate [hemin] administration), resulted in a significant reduction of mitochondrial respiratory capacity (including basal respiration and spare respiratory capacity), glucose uptake and adipogenesis in parallel with increased expression of inflammatory- and iron excess-related genes.	Iron	286-290	heme oxygenase 1	Homo sapiens	0-5
28243792-12	2017	CONCLUSIONS/INTERPRETATION: HMOX1 is an important marker of iron excess-induced adipose tissue dysfunction and metabolic disturbances in human obesity.	Iron	60-64	heme oxygenase 1	Homo sapiens	28-33
28440458-7	2017	Heme oxygenase-1 (HO-1; a microsomal enzyme) expression was significantly decreased while the reactive oxygen species (ROS) level was increased in the CBS siRNA-transfected SMMC-7721 cells.	smmc	173-177	heme oxygenase 1	Homo sapiens	0-16
28276576-2	2017	Our group reported decreased risk for ET in carriers of the minor alleles of the rs2071746 and rs1051308 SNPs in the haem-oxygenases 1 and 2 (HMOX1 and HMOX2), respectively, involved in haem metabolism.	Heme	117-121	heme oxygenase 1	Homo sapiens	142-147
28212891-9	2017	Although SFN promotes Nrf2 accumulation to upregulate cytoprotective genes (e.g., heme oxygenase-1 and thioredoxin-1), downregulation of endogenous Nrf2 by target-specific siRNA reveals an Nrf2-independent effect for SFN-mediated inhibition of mTOR/p70S6K/S6 signaling and suppression of VSMC proliferation.	sulforaphane	9-12	heme oxygenase 1	Homo sapiens	82-98
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Biliverdine	61-71	heme oxygenase 1	Homo sapiens	0-16
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Biliverdine	61-71	heme oxygenase 1	Homo sapiens	18-22
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Iron	78-82	heme oxygenase 1	Homo sapiens	0-16
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Iron	78-82	heme oxygenase 1	Homo sapiens	18-22
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	0-16
28186648-1	2017	Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	18-22
29050217-4	2017	The drug efflux transporter P-glycoprotein (P-gp) and the intracellular antioxidant systems, involving Glutathione S-Transferase pi, Glutathione and heme oxygenase-1, were also inhibited via the ROS-depressed Akt/NF-E2-related factor 2 pathway.	Reactive Oxygen Species	195-198	heme oxygenase 1	Homo sapiens	149-165
28445528-9	2017	On the other hand, CO production by RuCO (a CO donor) ameliorated PA-induced ER stress, suggesting that CO production followed by HO-1 induction may contribute to the protective effects of baicalein against PA-induced beta-cell dysfunction.	Palmitates	66-68	heme oxygenase 1	Homo sapiens	130-134
28445528-9	2017	On the other hand, CO production by RuCO (a CO donor) ameliorated PA-induced ER stress, suggesting that CO production followed by HO-1 induction may contribute to the protective effects of baicalein against PA-induced beta-cell dysfunction.	baicalein	189-198	heme oxygenase 1	Homo sapiens	130-134
28445528-9	2017	On the other hand, CO production by RuCO (a CO donor) ameliorated PA-induced ER stress, suggesting that CO production followed by HO-1 induction may contribute to the protective effects of baicalein against PA-induced beta-cell dysfunction.	Palmitates	207-209	heme oxygenase 1	Homo sapiens	130-134
28420988-8	2017	Second, heme oxygenases (HOs), in particular the inducible HO isozyme, HO-1, can provide antioxidant cytoprotection via enzymatic degradation of intracellular heme.	Heme	8-12	heme oxygenase 1	Homo sapiens	71-75
28286125-0	2017	n-Propyl gallate suppresses lipopolysaccharide-induced inducible nitric oxide synthase activation through protein kinase Cdelta-mediated up-regulation of heme oxygenase-1 in RAW264.7 macrophages.	Propyl Gallate	0-16	heme oxygenase 1	Homo sapiens	154-170
28286125-3	2017	In the present study, we showed that n-propyl gallate increases the expression and activity of the heme oxygenase-1 (HO-1), a stress-inducible protein with potent anti-inflammatory activity, in RAW264.7 macrophages.	Propyl Gallate	37-53	heme oxygenase 1	Homo sapiens	99-115
28286125-3	2017	In the present study, we showed that n-propyl gallate increases the expression and activity of the heme oxygenase-1 (HO-1), a stress-inducible protein with potent anti-inflammatory activity, in RAW264.7 macrophages.	Propyl Gallate	37-53	heme oxygenase 1	Homo sapiens	117-121
28286125-4	2017	The inhibition of the HO-1 activity by treatment with zinc (II) protoporphyrin IX (ZnPP) or by knockdown of the HO-1 expression with small interference RNA significantly reversed the inhibitory effect of n-Propyl gallate on activations of nuclear factor-kappaB (NF-kappaB) and inducible nitric oxide synthase (iNOS) induced by lipopolysaccharide (LPS).	protoporphyrin IX	64-81	heme oxygenase 1	Homo sapiens	22-26
28286125-4	2017	The inhibition of the HO-1 activity by treatment with zinc (II) protoporphyrin IX (ZnPP) or by knockdown of the HO-1 expression with small interference RNA significantly reversed the inhibitory effect of n-Propyl gallate on activations of nuclear factor-kappaB (NF-kappaB) and inducible nitric oxide synthase (iNOS) induced by lipopolysaccharide (LPS).	zinc protoporphyrin	83-87	heme oxygenase 1	Homo sapiens	22-26
28286125-4	2017	The inhibition of the HO-1 activity by treatment with zinc (II) protoporphyrin IX (ZnPP) or by knockdown of the HO-1 expression with small interference RNA significantly reversed the inhibitory effect of n-Propyl gallate on activations of nuclear factor-kappaB (NF-kappaB) and inducible nitric oxide synthase (iNOS) induced by lipopolysaccharide (LPS).	Propyl Gallate	204-220	heme oxygenase 1	Homo sapiens	22-26
28286125-4	2017	The inhibition of the HO-1 activity by treatment with zinc (II) protoporphyrin IX (ZnPP) or by knockdown of the HO-1 expression with small interference RNA significantly reversed the inhibitory effect of n-Propyl gallate on activations of nuclear factor-kappaB (NF-kappaB) and inducible nitric oxide synthase (iNOS) induced by lipopolysaccharide (LPS).	Propyl Gallate	204-220	heme oxygenase 1	Homo sapiens	112-116
28286125-5	2017	An additional mechanism study using inhibitors of signaling kinases revealed the involvement of protein kinase Cdelta (PKCdelta) in the expression of HO-1 induced by n-Propyl gallate.	Propyl Gallate	166-182	heme oxygenase 1	Homo sapiens	150-154
28286125-8	2017	Taken together, these findings provide the first evidence that n-Propyl gallate exerts its anti-inflammatory effect through PKCdelta-mediated up-regulation of HO-1 in macrophages.	Propyl Gallate	63-79	heme oxygenase 1	Homo sapiens	159-163
28139396-7	2017	These beneficial effects of HO-1 induction during AKI are mediated in part by the by-products of the HO reaction (iron, carbon monoxide, and bile pigments).	Iron	114-118	heme oxygenase 1	Homo sapiens	28-32
28421060-3	2017	HO-1 catalyzes the rate-limiting step in the conversion of heme into iron, biliverdin and the gasotransmitter carbon monoxide (CO), all of which share anti-apoptotic, anti-inflammatory, pro-survival, and tumorigenic activities.	Heme	59-63	heme oxygenase 1	Homo sapiens	0-4
28421060-3	2017	HO-1 catalyzes the rate-limiting step in the conversion of heme into iron, biliverdin and the gasotransmitter carbon monoxide (CO), all of which share anti-apoptotic, anti-inflammatory, pro-survival, and tumorigenic activities.	Iron	69-73	heme oxygenase 1	Homo sapiens	0-4
28421060-3	2017	HO-1 catalyzes the rate-limiting step in the conversion of heme into iron, biliverdin and the gasotransmitter carbon monoxide (CO), all of which share anti-apoptotic, anti-inflammatory, pro-survival, and tumorigenic activities.	Biliverdine	75-85	heme oxygenase 1	Homo sapiens	0-4
28421060-3	2017	HO-1 catalyzes the rate-limiting step in the conversion of heme into iron, biliverdin and the gasotransmitter carbon monoxide (CO), all of which share anti-apoptotic, anti-inflammatory, pro-survival, and tumorigenic activities.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	0-4
28421060-3	2017	HO-1 catalyzes the rate-limiting step in the conversion of heme into iron, biliverdin and the gasotransmitter carbon monoxide (CO), all of which share anti-apoptotic, anti-inflammatory, pro-survival, and tumorigenic activities.	Carbon Monoxide	127-129	heme oxygenase 1	Homo sapiens	0-4
27995330-0	2017	Piceatannol attenuates homocysteine-induced endoplasmic reticulum stress and endothelial cell damage via heme oxygenase-1 expression.	3,3',4,5'-tetrahydroxystilbene	0-11	heme oxygenase 1	Homo sapiens	105-121
27995330-0	2017	Piceatannol attenuates homocysteine-induced endoplasmic reticulum stress and endothelial cell damage via heme oxygenase-1 expression.	Homocysteine	23-35	heme oxygenase 1	Homo sapiens	105-121
27995330-8	2017	Interestingly, the inhibitory effects of Pic on Hcy-induced apoptosis, ROS generation and ER stress were abolished by down-regulation of HO-1 expression, while mimicked by treatment of ECs with the HO-1 inducer hemin.	3,3',4,5'-tetrahydroxystilbene	41-44	heme oxygenase 1	Homo sapiens	137-141
27995330-8	2017	Interestingly, the inhibitory effects of Pic on Hcy-induced apoptosis, ROS generation and ER stress were abolished by down-regulation of HO-1 expression, while mimicked by treatment of ECs with the HO-1 inducer hemin.	3,3',4,5'-tetrahydroxystilbene	41-44	heme oxygenase 1	Homo sapiens	198-202
27995330-8	2017	Interestingly, the inhibitory effects of Pic on Hcy-induced apoptosis, ROS generation and ER stress were abolished by down-regulation of HO-1 expression, while mimicked by treatment of ECs with the HO-1 inducer hemin.	Homocysteine	48-51	heme oxygenase 1	Homo sapiens	137-141
27995330-8	2017	Interestingly, the inhibitory effects of Pic on Hcy-induced apoptosis, ROS generation and ER stress were abolished by down-regulation of HO-1 expression, while mimicked by treatment of ECs with the HO-1 inducer hemin.	Homocysteine	48-51	heme oxygenase 1	Homo sapiens	198-202
27995330-9	2017	Overall, these results suggest that Pic may protect ECs against Hcy-induced apoptosis, oxidative stress and ER stress via Nrf2-dependent HO-1 expression.	3,3',4,5'-tetrahydroxystilbene	36-39	heme oxygenase 1	Homo sapiens	137-141
27995330-9	2017	Overall, these results suggest that Pic may protect ECs against Hcy-induced apoptosis, oxidative stress and ER stress via Nrf2-dependent HO-1 expression.	Homocysteine	64-67	heme oxygenase 1	Homo sapiens	137-141
28139396-7	2017	These beneficial effects of HO-1 induction during AKI are mediated in part by the by-products of the HO reaction (iron, carbon monoxide, and bile pigments).	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	28-32
28089584-5	2017	Moreover, the levels of nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1) and glutathione S-transferase (GST) were elevated after PTE treatment.	pterostilbene	156-159	heme oxygenase 1	Homo sapiens	76-92
28213291-5	2017	Furthermore, 2"-O-GH stimulation resulted in a fast and dramatic activation of Akt and nuclear translocation of the NF-E2-related factor 2 (Nrf2), along with the increased expression of heme oxygenase-1 (HO-1) and levels of glutathione (GSH).	2"-o-gh	13-20	heme oxygenase 1	Homo sapiens	186-202
28100868-8	2017	In contrast, retinol treatment significantly increased the mRNA expression of endoplasmic reticulum (ER) stress factors (heme oxygenase 1 (HMOX1), CCAAT/enhancer-binding protein homologous protein (CHOP), 78 kDa glucose-regulated protein (GRP78), and DnaJ (Hsp40) homolog, subfamily B, member 9 (DNAJB9)).	Vitamin A	13-20	heme oxygenase 1	Homo sapiens	121-137
28100868-8	2017	In contrast, retinol treatment significantly increased the mRNA expression of endoplasmic reticulum (ER) stress factors (heme oxygenase 1 (HMOX1), CCAAT/enhancer-binding protein homologous protein (CHOP), 78 kDa glucose-regulated protein (GRP78), and DnaJ (Hsp40) homolog, subfamily B, member 9 (DNAJB9)).	Vitamin A	13-20	heme oxygenase 1	Homo sapiens	139-144
28103505-0	2017	Hesperetin protects against H2O2-triggered oxidative damage via upregulation of the Keap1-Nrf2/HO-1 signal pathway in ARPE-19 cells.	hesperetin	0-10	heme oxygenase 1	Homo sapiens	95-99
28103505-0	2017	Hesperetin protects against H2O2-triggered oxidative damage via upregulation of the Keap1-Nrf2/HO-1 signal pathway in ARPE-19 cells.	Hydrogen Peroxide	28-32	heme oxygenase 1	Homo sapiens	95-99
28274716-0	2017	Atractylenolide I restores HO-1 expression and inhibits Ox-LDL-induced VSMCs proliferation, migration and inflammatory responses in vitro.	(+)-Atractylenolide	0-15	heme oxygenase 1	Homo sapiens	27-31
28274716-5	2017	More importantly, the specific heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin (ZnPP) IX partially abolished the beneficial effects of atractylenolide I on Ox-LDL-induced VSMCs.	zinc protoporphyrin	65-84	heme oxygenase 1	Homo sapiens	31-47
28274716-5	2017	More importantly, the specific heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin (ZnPP) IX partially abolished the beneficial effects of atractylenolide I on Ox-LDL-induced VSMCs.	zinc protoporphyrin	65-84	heme oxygenase 1	Homo sapiens	49-53
28274716-5	2017	More importantly, the specific heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin (ZnPP) IX partially abolished the beneficial effects of atractylenolide I on Ox-LDL-induced VSMCs.	zinc protoporphyrin	86-90	heme oxygenase 1	Homo sapiens	31-47
28274716-5	2017	More importantly, the specific heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin (ZnPP) IX partially abolished the beneficial effects of atractylenolide I on Ox-LDL-induced VSMCs.	zinc protoporphyrin	86-90	heme oxygenase 1	Homo sapiens	49-53
28274716-5	2017	More importantly, the specific heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin (ZnPP) IX partially abolished the beneficial effects of atractylenolide I on Ox-LDL-induced VSMCs.	(+)-Atractylenolide	141-156	heme oxygenase 1	Homo sapiens	31-47
28274716-5	2017	More importantly, the specific heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin (ZnPP) IX partially abolished the beneficial effects of atractylenolide I on Ox-LDL-induced VSMCs.	(+)-Atractylenolide	141-156	heme oxygenase 1	Homo sapiens	49-53
28259922-4	2017	HK-2 human tubular epithelial cells exposed to H/R injury were pretreated with LXA4, signal molecule inhibitors or the HO-1 inhibitor zinc protoporphyrin-IX, or were transfected with PPARgamma small interfering RNA (siRNA) or nuclear factor E2-related factor 2 (Nrf2) siRNA.	zinc protoporphyrin	134-156	heme oxygenase 1	Homo sapiens	119-123
28070834-0	2017	Resveratrol modulates GSH system in C6 astroglial cells through heme oxygenase 1 pathway.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	64-80
28070834-0	2017	Resveratrol modulates GSH system in C6 astroglial cells through heme oxygenase 1 pathway.	Glutathione	22-25	heme oxygenase 1	Homo sapiens	64-80
28070834-7	2017	Additionally, we observed that pharmacological inhibition of heme oxygenase 1 (HO-1), an essential cellular defense against oxidative and inflammatory injuries, abolished all the protective effects of resveratrol.	Resveratrol	201-212	heme oxygenase 1	Homo sapiens	61-77
28070834-7	2017	Additionally, we observed that pharmacological inhibition of heme oxygenase 1 (HO-1), an essential cellular defense against oxidative and inflammatory injuries, abolished all the protective effects of resveratrol.	Resveratrol	201-212	heme oxygenase 1	Homo sapiens	79-83
28070834-8	2017	These observations suggest HO-1 pathway as a cellular effector in the mechanism by which resveratrol protects astroglial cells against GSH depletion, a condition that may be associated to neurodegenerative diseases.	Resveratrol	89-100	heme oxygenase 1	Homo sapiens	27-31
28070834-8	2017	These observations suggest HO-1 pathway as a cellular effector in the mechanism by which resveratrol protects astroglial cells against GSH depletion, a condition that may be associated to neurodegenerative diseases.	Glutathione	135-138	heme oxygenase 1	Homo sapiens	27-31
28259922-15	2017	Therefore, LXA4-induced renoprotection is associated with activation of the p38 MAPK/PPARgamma/Nrf2-ARE/HO-1 pathway.	lipoxin A4	11-15	heme oxygenase 1	Homo sapiens	104-108
28480030-1	2017	Carbon monoxide (CO) formed endogenously is considered to be cytoprotective, and the vast majority of CO formation is attributed to the degradation of heme by heme oxygenases-1 and -2 (HO-1, HO-2).	Heme	151-155	heme oxygenase 1	Homo sapiens	159-183
28480030-1	2017	Carbon monoxide (CO) formed endogenously is considered to be cytoprotective, and the vast majority of CO formation is attributed to the degradation of heme by heme oxygenases-1 and -2 (HO-1, HO-2).	Heme	151-155	heme oxygenase 1	Homo sapiens	185-189
28298633-8	2017	Prior administration of hemin to renal IRI was associated with significant increase of the renal HO-1+ CD11b+ F4/80lo myeloid cells in comparison to control mice.	Hemin	24-29	heme oxygenase 1	Homo sapiens	97-101
28109747-8	2017	Adaptation to acrolein is related to Nrf2 translocation, increased mRNA expression of gammaGCS, HO-1 and increased GSH levels and the increased GSH levels can explain the hormetic effect.	Acrolein	14-22	heme oxygenase 1	Homo sapiens	96-100
28350337-7	2017	In addition, DBL enhanced cytoprotective effects through elevated antioxidant enzymes including heme oxygenase 1 (HO-1), catalase, glutathione peroxidase (GPx), and superoxide dismutase (SOD).	disialyllactose	13-16	heme oxygenase 1	Homo sapiens	96-112
28350337-7	2017	In addition, DBL enhanced cytoprotective effects through elevated antioxidant enzymes including heme oxygenase 1 (HO-1), catalase, glutathione peroxidase (GPx), and superoxide dismutase (SOD).	disialyllactose	13-16	heme oxygenase 1	Homo sapiens	114-118
28189672-0	2017	Valproic acid downregulates heme oxygenase-1 independently of Nrf2 by increasing ubiquitination and proteasomal degradation.	Valproic Acid	0-13	heme oxygenase 1	Homo sapiens	28-44
27561292-7	2017	Meanwhile, allicin decreased NF-kappaB level and upregulated expression of proteins reduced by As2O3 including nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase 1, nicotinamide adenine dinucleotide phosphate:quinone oxidoreductase 1, and Kruppel-like factor 9 (KLF9).	allicin	11-18	heme oxygenase 1	Homo sapiens	163-179
28107189-5	2017	Mechanistic studies demonstrated that DSF enhances DHA-induced cellular oxidative stress as evidenced by up-regulation of Nrf2-mediated heme oxygenase 1 (HO-1) gene transcription.	Docosahexaenoic Acids	51-54	heme oxygenase 1	Homo sapiens	136-152
28107189-5	2017	Mechanistic studies demonstrated that DSF enhances DHA-induced cellular oxidative stress as evidenced by up-regulation of Nrf2-mediated heme oxygenase 1 (HO-1) gene transcription.	Docosahexaenoic Acids	51-54	heme oxygenase 1	Homo sapiens	154-158
28055290-6	2017	In addition, we have demonstrated that heme degradation by HMOX1/HO-1 (heme oxygenase 1) is required and that Fe is essential for the formation of ALIS, as heme analogs lacking the central atom of Fe are not able to induce these structures.	Heme	39-43	heme oxygenase 1	Homo sapiens	59-64
28055290-6	2017	In addition, we have demonstrated that heme degradation by HMOX1/HO-1 (heme oxygenase 1) is required and that Fe is essential for the formation of ALIS, as heme analogs lacking the central atom of Fe are not able to induce these structures.	Heme	39-43	heme oxygenase 1	Homo sapiens	65-87
28055290-6	2017	In addition, we have demonstrated that heme degradation by HMOX1/HO-1 (heme oxygenase 1) is required and that Fe is essential for the formation of ALIS, as heme analogs lacking the central atom of Fe are not able to induce these structures.	Heme	71-75	heme oxygenase 1	Homo sapiens	59-64
28082120-2	2017	Under several stress stimuli, HO-1 expression and activity is up-regulated to catalyze the rate-limiting enzymatic step of heme degradation into carbon monoxide, free iron, and biliverdin.	Carbon Monoxide	145-160	heme oxygenase 1	Homo sapiens	30-34
28082120-2	2017	Under several stress stimuli, HO-1 expression and activity is up-regulated to catalyze the rate-limiting enzymatic step of heme degradation into carbon monoxide, free iron, and biliverdin.	Iron	167-171	heme oxygenase 1	Homo sapiens	30-34
28082120-2	2017	Under several stress stimuli, HO-1 expression and activity is up-regulated to catalyze the rate-limiting enzymatic step of heme degradation into carbon monoxide, free iron, and biliverdin.	Biliverdine	177-187	heme oxygenase 1	Homo sapiens	30-34
27297870-12	2017	Taken together, these results suggest that andrographolide suppresses hypoxia-induced pro-inflammatory ET-1 expression by activating Nrf2/HO-1, inhibiting p38 MAPK signaling, and promoting PHD2/3 expression.	andrographolide	43-58	heme oxygenase 1	Homo sapiens	138-142
27297870-0	2017	Andrographolide inhibits hypoxia-induced HIF-1alpha-driven endothelin 1 secretion by activating Nrf2/HO-1 and promoting the expression of prolyl hydroxylases 2/3 in human endothelial cells.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	101-105
27297870-9	2017	Silencing Nrf2 and heme oxygenase 1 (HO-1) reversed the inhibitory effects of andrographolide on hypxoia-induced HIF-1alpha mRNA and protein expression.	andrographolide	78-93	heme oxygenase 1	Homo sapiens	19-35
27996348-0	2017	Involvement of the activation of Nrf2/HO-1, p38 MAPK signaling pathways and endoplasmic reticulum stress in furazolidone induced cytotoxicity and S phase arrest in human hepatocyte L02 cells: modulation of curcumin.	Furazolidone	108-120	heme oxygenase 1	Homo sapiens	38-42
27297870-9	2017	Silencing Nrf2 and heme oxygenase 1 (HO-1) reversed the inhibitory effects of andrographolide on hypxoia-induced HIF-1alpha mRNA and protein expression.	andrographolide	78-93	heme oxygenase 1	Homo sapiens	37-41
26780453-0	2017	Protocatechualdehyde Protects Against Cerebral Ischemia-Reperfusion-Induced Oxidative Injury Via Protein Kinase Cepsilon/Nrf2/HO-1 Pathway.	protocatechualdehyde	0-20	heme oxygenase 1	Homo sapiens	126-130
28115238-0	2017	NGF protects against oxygen and glucose deprivation-induced oxidative stress and apoptosis by up-regulation of HO-1 through MEK/ERK pathway.	Oxygen	21-27	heme oxygenase 1	Homo sapiens	111-115
27996348-7	2017	Moreover, compared with the control, FZD exposure activated the protein and mRNA expression levels of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase 1 (HO-1), which were further activated by curcumin treatment.	Curcumin	214-222	heme oxygenase 1	Homo sapiens	157-173
27996348-7	2017	Moreover, compared with the control, FZD exposure activated the protein and mRNA expression levels of nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase 1 (HO-1), which were further activated by curcumin treatment.	Curcumin	214-222	heme oxygenase 1	Homo sapiens	175-179
27996348-8	2017	These results reveal that curcumin could prevent FZD induced cytotoxicity and S phase arrest, which may involve the activation of Nrf2/HO-1 pathway and the inhibition of p38 MAPK pathway and ER stress.	Curcumin	26-34	heme oxygenase 1	Homo sapiens	135-139
28088947-0	2017	Heme oxygenase-1 (HO-1)/carbon monoxide (CO) axis suppresses RANKL-induced osteoclastic differentiation by inhibiting redox-sensitive NF-kappaB activation.	Carbon Monoxide	41-43	heme oxygenase 1	Homo sapiens	0-16
27996348-8	2017	These results reveal that curcumin could prevent FZD induced cytotoxicity and S phase arrest, which may involve the activation of Nrf2/HO-1 pathway and the inhibition of p38 MAPK pathway and ER stress.	Furazolidone	49-52	heme oxygenase 1	Homo sapiens	135-139
28270832-0	2017	Actin Family Proteins in the Human INO80 Chromatin Remodeling Complex Exhibit Functional Roles in the Induction of Heme Oxygenase-1 with Hemin.	Hemin	137-142	heme oxygenase 1	Homo sapiens	115-131
28108387-5	2017	Selegiline also reversed CSM-induced changes of anti-oxidant enzymes superoxide dismutase (SOD) and catalase (CAT) activities, GSH/GSSG ratio, as well expression of heme oxygenase-1 (HO-1) and NAD(P)H quinone dehydrogenase 1 (NQO1).	Selegiline	0-10	heme oxygenase 1	Homo sapiens	165-181
28055957-5	2017	The latter is known to generate reactive oxygen species, and consequently, expression of the antioxidant enzyme heme oxygenase 1 (HMOX1) was significantly upregulated in 5-FU-treated cells, indicative for oxidative stress.	Reactive Oxygen Species	32-55	heme oxygenase 1	Homo sapiens	112-128
28055957-5	2017	The latter is known to generate reactive oxygen species, and consequently, expression of the antioxidant enzyme heme oxygenase 1 (HMOX1) was significantly upregulated in 5-FU-treated cells, indicative for oxidative stress.	Reactive Oxygen Species	32-55	heme oxygenase 1	Homo sapiens	130-135
28055957-5	2017	The latter is known to generate reactive oxygen species, and consequently, expression of the antioxidant enzyme heme oxygenase 1 (HMOX1) was significantly upregulated in 5-FU-treated cells, indicative for oxidative stress.	Fluorouracil	170-174	heme oxygenase 1	Homo sapiens	112-128
28055957-5	2017	The latter is known to generate reactive oxygen species, and consequently, expression of the antioxidant enzyme heme oxygenase 1 (HMOX1) was significantly upregulated in 5-FU-treated cells, indicative for oxidative stress.	Fluorouracil	170-174	heme oxygenase 1	Homo sapiens	130-135
28055957-7	2017	Also in vivo, 5-FU significantly induced hepatic ACOX1 and HMOX1 expression as well as JNK-activation, pro-inflammatory gene expression and immune cell infiltration.	Fluorouracil	14-18	heme oxygenase 1	Homo sapiens	59-64
28088947-1	2017	Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases.	Heme	32-36	heme oxygenase 1	Homo sapiens	16-20
28088947-1	2017	Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases.	Carbon Monoxide	40-55	heme oxygenase 1	Homo sapiens	16-20
28088947-1	2017	Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases.	Carbon Monoxide	57-59	heme oxygenase 1	Homo sapiens	16-20
28088947-1	2017	Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases.	Biliverdine	62-72	heme oxygenase 1	Homo sapiens	16-20
28088947-1	2017	Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases.	Bilirubin	73-82	heme oxygenase 1	Homo sapiens	16-20
28088947-1	2017	Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases.	Iron	88-92	heme oxygenase 1	Homo sapiens	16-20
28119605-0	2016	Agrimonolide and Desmethylagrimonolide Induced HO-1 Expression in HepG2 Cells through Nrf2-Transduction and p38 Inactivation.	Desmethylagrimonolide	17-38	heme oxygenase 1	Homo sapiens	47-51
28035393-9	2017	Fluoxetine inhibited MA-induced increases in the expression levels of serotonin transporter (SERT) and p-p38 mitogen-activated protein kinase (MAPK), and reversed the MA-induced decrease in nuclear Nrf2 and human heme oxygenase-1 in lungs.	Fluoxetine	0-10	heme oxygenase 1	Homo sapiens	213-229
28120861-5	2017	CNT exposure activates an oxidative stress-dependent production of iron via Nrf2 nuclear translocation, Ferritin H and Heme oxygenase 1 translation.	Iron	67-71	heme oxygenase 1	Homo sapiens	119-135
28116663-11	2017	HO-1 was inhibited by Sn-protoporphyrin, HO-1 inhibitor, and increased by cobalt protopophyrin, HO-1 inducer.	tin protoporphyrin IX	22-39	heme oxygenase 1	Homo sapiens	0-4
28116663-11	2017	HO-1 was inhibited by Sn-protoporphyrin, HO-1 inhibitor, and increased by cobalt protopophyrin, HO-1 inducer.	cobalt protopophyrin	74-94	heme oxygenase 1	Homo sapiens	0-4
28098837-0	2017	Casein Glycomacropeptide Hydrolysates Exert Cytoprotective Effect against Cellular Oxidative Stress by Up-Regulating HO-1 Expression in HepG2 Cells.	glycomacropeptide hydrolysates	7-37	heme oxygenase 1	Homo sapiens	117-121
28098837-4	2017	Further, GHP concentration-dependently induced heme oxygenase-1 (HO-1) expression and increased nuclear factor-erythroid 2-related factor 2 (Nrf2) nuclear translocation.	ghp	9-12	heme oxygenase 1	Homo sapiens	47-63
28098837-4	2017	Further, GHP concentration-dependently induced heme oxygenase-1 (HO-1) expression and increased nuclear factor-erythroid 2-related factor 2 (Nrf2) nuclear translocation.	ghp	9-12	heme oxygenase 1	Homo sapiens	65-69
28098837-5	2017	Moreover, pretreatment of GHP increased the activation of p38 mitogen-activated protein kinase (p38 MAPK) and extracellular signal-regulated protein kinase 1/2 (ERK1/2), which were shown to contribute to Nrf2-mediated HO-1 expression.	ghp	26-29	heme oxygenase 1	Homo sapiens	218-222
28161055-11	2017	In isolated primary trophoblasts, HSP70 and HO-1 were upregulated by increasing oxygen tension, but not by hyperglycemia or TNF-alpha.	Oxygen	80-86	heme oxygenase 1	Homo sapiens	44-48
28119605-5	2016	Western blotting and luciferase assay revealed that exposure of HepG2 cells to agrimonolide or desmethylagrimonolide leads to increased heme oxygenase-1 (HO-1) expression by activating ARE through induction of Nrf2 and suppression of Kelch-like ECH-associated protein 1 (Keap1).	agrimonolide	79-91	heme oxygenase 1	Homo sapiens	136-152
28119605-5	2016	Western blotting and luciferase assay revealed that exposure of HepG2 cells to agrimonolide or desmethylagrimonolide leads to increased heme oxygenase-1 (HO-1) expression by activating ARE through induction of Nrf2 and suppression of Kelch-like ECH-associated protein 1 (Keap1).	agrimonolide	79-91	heme oxygenase 1	Homo sapiens	154-158
28119605-5	2016	Western blotting and luciferase assay revealed that exposure of HepG2 cells to agrimonolide or desmethylagrimonolide leads to increased heme oxygenase-1 (HO-1) expression by activating ARE through induction of Nrf2 and suppression of Kelch-like ECH-associated protein 1 (Keap1).	Desmethylagrimonolide	95-116	heme oxygenase 1	Homo sapiens	136-152
28119605-5	2016	Western blotting and luciferase assay revealed that exposure of HepG2 cells to agrimonolide or desmethylagrimonolide leads to increased heme oxygenase-1 (HO-1) expression by activating ARE through induction of Nrf2 and suppression of Kelch-like ECH-associated protein 1 (Keap1).	Desmethylagrimonolide	95-116	heme oxygenase 1	Homo sapiens	154-158
28119605-7	2016	In conclusion, our results indicated that transcriptional activation of Nrf2/ARE is critical in agrimonolide and desmethylagrimonolide-mediated HO-1 induction, which can be regulated partially by the blockade of p38 MAPK signaling pathway and inhibiting nuclear translocation of Nrf2.	agrimonolide	96-108	heme oxygenase 1	Homo sapiens	144-148
28119605-7	2016	In conclusion, our results indicated that transcriptional activation of Nrf2/ARE is critical in agrimonolide and desmethylagrimonolide-mediated HO-1 induction, which can be regulated partially by the blockade of p38 MAPK signaling pathway and inhibiting nuclear translocation of Nrf2.	Desmethylagrimonolide	113-134	heme oxygenase 1	Homo sapiens	144-148
27873232-7	2017	We demonstrated that heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway prevents placental stress and suppresses sFlt-1 and sEng release.	Carbon Monoxide	45-60	heme oxygenase 1	Homo sapiens	21-37
27438141-0	2017	4-Hydroxyestradiol induces mammary epithelial cell transformation through Nrf2-mediated heme oxygenase-1 overexpression.	4-hydroxyestradiol	0-18	heme oxygenase 1	Homo sapiens	88-104
27438141-3	2017	In this study, 4-OHE2, but not E2, increased the expression of heme oxygenase-1 (HO-1), a sensor and regulator of oxidative stress, in MCF-10A cells.	4-hydroxyestradiol	15-21	heme oxygenase 1	Homo sapiens	63-79
27438141-3	2017	In this study, 4-OHE2, but not E2, increased the expression of heme oxygenase-1 (HO-1), a sensor and regulator of oxidative stress, in MCF-10A cells.	4-hydroxyestradiol	15-21	heme oxygenase 1	Homo sapiens	81-85
27438141-4	2017	Silencing the HO-1 gene in MCF-10A cells suppressed 4-OHE2-induced cell proliferation and transformation.	4-hydroxyestradiol	52-58	heme oxygenase 1	Homo sapiens	14-18
27438141-5	2017	In addition, subcutaneous administration of 4-OHE2 markedly enhanced the growth of the MDA-MB-231 human breast cancer xenografts, which was retarded by zinc protoporphyrin, a pharmacological inhibitor of HO-1.	4-hydroxyestradiol	44-50	heme oxygenase 1	Homo sapiens	204-208
27438141-5	2017	In addition, subcutaneous administration of 4-OHE2 markedly enhanced the growth of the MDA-MB-231 human breast cancer xenografts, which was retarded by zinc protoporphyrin, a pharmacological inhibitor of HO-1.	zinc protoporphyrin	152-171	heme oxygenase 1	Homo sapiens	204-208
27438141-6	2017	4-OHE2-induced HO-1 expression was mediated by NF-E2-related factor 2 (Nrf2).	4-hydroxyestradiol	0-6	heme oxygenase 1	Homo sapiens	15-19
27873232-7	2017	We demonstrated that heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway prevents placental stress and suppresses sFlt-1 and sEng release.	Carbon Monoxide	62-64	heme oxygenase 1	Homo sapiens	21-37
27943244-1	2017	OBJECTIVE: The present study was undertaken to investigate the genotype and allele frequencies of the variants in the four bilirubin metabolism genes (UGT1A1, OATP2, HMOX1, and BLVRA) and their association with hyperbilirubinemia.	Bilirubin	123-132	heme oxygenase 1	Homo sapiens	166-171
28356018-0	2017	Enhancement of the Effect of Methyl Pyropheophorbide-a-Mediated Photodynamic Therapy was Achieved by Increasing ROS through Inhibition of Nrf2-HO-1 or Nrf2-ABCG2 Signaling.	methyl pyropheophorbide-a	29-54	heme oxygenase 1	Homo sapiens	143-147
28356018-0	2017	Enhancement of the Effect of Methyl Pyropheophorbide-a-Mediated Photodynamic Therapy was Achieved by Increasing ROS through Inhibition of Nrf2-HO-1 or Nrf2-ABCG2 Signaling.	Reactive Oxygen Species	112-115	heme oxygenase 1	Homo sapiens	143-147
28356018-7	2017	Nrf2 down -regulation increased reactive oxygen species (ROS) levels by attenuating antioxidants or pumping Mppa out of cells,which resulted from the inhibition of Nrf2-HO-1 or Nrf2- ABCG2 signaling.	Reactive Oxygen Species	32-55	heme oxygenase 1	Homo sapiens	169-173
28503569-7	2017	These results indicate that TNFRI-Fc and hHO-1 overexpression may apparently induce free iron in the liver and exert oxidative stress by enhancing reactive oxygen species production and block normal postneonatal liver metabolism.	Iron	89-93	heme oxygenase 1	Homo sapiens	41-46
28356018-7	2017	Nrf2 down -regulation increased reactive oxygen species (ROS) levels by attenuating antioxidants or pumping Mppa out of cells,which resulted from the inhibition of Nrf2-HO-1 or Nrf2- ABCG2 signaling.	Reactive Oxygen Species	57-60	heme oxygenase 1	Homo sapiens	169-173
28107860-3	2017	RESULTS: Following exposure to the HO-1 inducer CoPPIX at all concentrations, the HBMEC cells apoptosis occurred, which could be prominently observed at 15 muM of 3 h exposure.	coppix	48-54	heme oxygenase 1	Homo sapiens	35-39
28107860-6	2017	For the effect of the HO-1 inhibitor ZnPPIX, HBMEC cell morphology was mostly unchanged, but significant inhibitory effect on cell apoptosis was seen at 10 muM for the exposure period of 3 h (37.17% of baseline level).	zinc protoporphyrin	37-43	heme oxygenase 1	Homo sapiens	22-26
27641735-10	2017	Restoration of HO-1 expression by hemin (20 mumol/L) abolished the inhibition of miR-1304 on cell growth and rescued miR-1304-induced apoptosis in A549 cells.	Hemin	34-39	heme oxygenase 1	Homo sapiens	15-19
28503569-7	2017	These results indicate that TNFRI-Fc and hHO-1 overexpression may apparently induce free iron in the liver and exert oxidative stress by enhancing reactive oxygen species production and block normal postneonatal liver metabolism.	Reactive Oxygen Species	147-170	heme oxygenase 1	Homo sapiens	41-46
27249374-12	2017	Sublethal concentration of acrolein upregulated HO-1 mRNA expression in retinal microvascular endothelial cells.	Acrolein	27-35	heme oxygenase 1	Homo sapiens	48-52
28228072-8	2017	Dietary curcumin supplementation can also increase antioxidant activity through the induction of heme oxygenase-1, a scavenger of free radicals, and by reduction of reactive oxygen species and Nox-2.	Curcumin	8-16	heme oxygenase 1	Homo sapiens	97-113
28382863-6	2017	Fenofibrate significantly upregulated heme oxygenase 1 (HO-1) at protein and mRNA levels in human glioblastoma LN-18 cells and rat brain astrocytes respectively, but nuclear factor kappalight- chain-enhancer of activated B cells (NFkappaB) was downregulated after fenofibrate treatment.	Fenofibrate	0-11	heme oxygenase 1	Homo sapiens	38-54
28382863-6	2017	Fenofibrate significantly upregulated heme oxygenase 1 (HO-1) at protein and mRNA levels in human glioblastoma LN-18 cells and rat brain astrocytes respectively, but nuclear factor kappalight- chain-enhancer of activated B cells (NFkappaB) was downregulated after fenofibrate treatment.	Fenofibrate	0-11	heme oxygenase 1	Homo sapiens	56-60
28382863-7	2017	Results showed that fenofibrate-induced upregulation of HO-1 expression were inhibited after LN-18 cells were transfected with 50nM small interfering RNA (siRNAs) for 48 hours to knockdown PPARalpha.	Fenofibrate	20-31	heme oxygenase 1	Homo sapiens	56-60
28190391-0	2017	Novel Caffeic Acid Phenethyl Ester (Cape) Analogues as Inducers of Heme Oxygenase-1.	caffeic acid phenethyl ester	6-34	heme oxygenase 1	Homo sapiens	67-83
28228072-8	2017	Dietary curcumin supplementation can also increase antioxidant activity through the induction of heme oxygenase-1, a scavenger of free radicals, and by reduction of reactive oxygen species and Nox-2.	Free Radicals	130-143	heme oxygenase 1	Homo sapiens	97-113
28190391-0	2017	Novel Caffeic Acid Phenethyl Ester (Cape) Analogues as Inducers of Heme Oxygenase-1.	caffeic acid phenethyl ester	36-40	heme oxygenase 1	Homo sapiens	67-83
28190391-4	2017	Caffeic acid phenethyl ester, a natural polyphenolic compound, behaves as HO-1 inducer and possesses a plethora of beneficial effects under oxidative stress conditions.	caffeic acid phenethyl ester	0-28	heme oxygenase 1	Homo sapiens	74-78
28412905-2	2017	Among a battery of therapeutic targets, the heme oxygenase- 1 (HO-1)/carbon monoxide (CO) system has been evaluated for the development of new therapies against I/R injury.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	44-61
28190391-5	2017	OBJECTIVES: A small focused series of caffeic acid phenethyl ester (Cape) analogues was designed and synthesized with the aim of obtaining more potent HO-1 inducers.	caffeic acid phenethyl ester	38-66	heme oxygenase 1	Homo sapiens	151-155
28190391-5	2017	OBJECTIVES: A small focused series of caffeic acid phenethyl ester (Cape) analogues was designed and synthesized with the aim of obtaining more potent HO-1 inducers.	caffeic acid phenethyl ester	68-72	heme oxygenase 1	Homo sapiens	151-155
28190391-8	2017	VP961 tested to measure HO-1 protein expression and HO activity in in vitro system resulted more potent than the parent compound Cape both as inducer and as direct activator of the enzyme.	caffeic acid phenethyl ester	129-133	heme oxygenase 1	Homo sapiens	24-28
28412905-3	2017	The enzyme HO-1 catalyzes the degradation of heme into three biologically active end products, namely biliverdin/bilirubin, CO and ferrous ion.	Heme	45-49	heme oxygenase 1	Homo sapiens	11-15
28412905-3	2017	The enzyme HO-1 catalyzes the degradation of heme into three biologically active end products, namely biliverdin/bilirubin, CO and ferrous ion.	Biliverdine	102-112	heme oxygenase 1	Homo sapiens	11-15
28412905-3	2017	The enzyme HO-1 catalyzes the degradation of heme into three biologically active end products, namely biliverdin/bilirubin, CO and ferrous ion.	Bilirubin	113-122	heme oxygenase 1	Homo sapiens	11-15
28412905-10	2017	The regulation of HO-1/CO expression has been achieved either by genetic overexpression of HO-1 cDNA or pharmacological induction with drugs including curcumin and resveratrol.	Curcumin	151-159	heme oxygenase 1	Homo sapiens	18-25
28412905-10	2017	The regulation of HO-1/CO expression has been achieved either by genetic overexpression of HO-1 cDNA or pharmacological induction with drugs including curcumin and resveratrol.	Curcumin	151-159	heme oxygenase 1	Homo sapiens	18-22
28412905-10	2017	The regulation of HO-1/CO expression has been achieved either by genetic overexpression of HO-1 cDNA or pharmacological induction with drugs including curcumin and resveratrol.	Resveratrol	164-175	heme oxygenase 1	Homo sapiens	18-25
28412905-10	2017	The regulation of HO-1/CO expression has been achieved either by genetic overexpression of HO-1 cDNA or pharmacological induction with drugs including curcumin and resveratrol.	Resveratrol	164-175	heme oxygenase 1	Homo sapiens	18-22
27908781-3	2017	To elucidate the mechanisms involved, here we assess whether the HO-1 downstream metabolites biliverdin (BV) and/or iron mediate the HO-1 antiviral effect.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	65-69
27867098-3	2017	Exogenously administered ammonia, given as ammonium chloride or ammonium hydroxide, or endogenously generated ammonia stimulated HO-1 protein expression in cultured human and murine endothelial cells.	Ammonia	25-32	heme oxygenase 1	Homo sapiens	129-133
27908781-3	2017	To elucidate the mechanisms involved, here we assess whether the HO-1 downstream metabolites biliverdin (BV) and/or iron mediate the HO-1 antiviral effect.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	133-137
27867098-3	2017	Exogenously administered ammonia, given as ammonium chloride or ammonium hydroxide, or endogenously generated ammonia stimulated HO-1 protein expression in cultured human and murine endothelial cells.	Ammonium Hydroxide	64-82	heme oxygenase 1	Homo sapiens	129-133
27867098-3	2017	Exogenously administered ammonia, given as ammonium chloride or ammonium hydroxide, or endogenously generated ammonia stimulated HO-1 protein expression in cultured human and murine endothelial cells.	Ammonia	110-117	heme oxygenase 1	Homo sapiens	129-133
27908781-3	2017	To elucidate the mechanisms involved, here we assess whether the HO-1 downstream metabolites biliverdin (BV) and/or iron mediate the HO-1 antiviral effect.	Biliverdine	105-107	heme oxygenase 1	Homo sapiens	65-69
27908781-3	2017	To elucidate the mechanisms involved, here we assess whether the HO-1 downstream metabolites biliverdin (BV) and/or iron mediate the HO-1 antiviral effect.	Biliverdine	105-107	heme oxygenase 1	Homo sapiens	133-137
27908781-3	2017	To elucidate the mechanisms involved, here we assess whether the HO-1 downstream metabolites biliverdin (BV) and/or iron mediate the HO-1 antiviral effect.	Iron	116-120	heme oxygenase 1	Homo sapiens	133-137
27908781-8	2017	Collectively, our findings identify a HO-1-BV/BR-NO-cGMP/PKG cascade as a novel pathway underlying the host cell antiviral effect.	Cyclic GMP	52-56	heme oxygenase 1	Homo sapiens	38-42
27922667-6	2017	Moreover, while downregulation of HO-1 by the small-molecule inhibitor tin protoporphyrin (SnPP) promoted migration, upregulation of HO-1 by the small-molecule activator cobalt protoporphyrin (CoPP) showed the opposite effect.	tin protoporphyrin IX	71-89	heme oxygenase 1	Homo sapiens	34-38
27976481-5	2017	Accumulation of ROS and subsequent activation of NRF2, p53, AP-1 and NF-kappaB-dependent pathways, with downstream activation of antioxidant mechanisms (e.g., SOD2 and HMOX1 expression), is observed in the UV-treated cells.	Reactive Oxygen Species	16-19	heme oxygenase 1	Homo sapiens	168-173
27922667-6	2017	Moreover, while downregulation of HO-1 by the small-molecule inhibitor tin protoporphyrin (SnPP) promoted migration, upregulation of HO-1 by the small-molecule activator cobalt protoporphyrin (CoPP) showed the opposite effect.	S-Nitroso-N-propionyl-D,L-penicillamine	91-95	heme oxygenase 1	Homo sapiens	34-38
27922667-6	2017	Moreover, while downregulation of HO-1 by the small-molecule inhibitor tin protoporphyrin (SnPP) promoted migration, upregulation of HO-1 by the small-molecule activator cobalt protoporphyrin (CoPP) showed the opposite effect.	cobaltiprotoporphyrin	170-191	heme oxygenase 1	Homo sapiens	133-137
27720465-10	2017	CONCLUSION: Cinnamaldehyde has two independent biological activities; namely, an inhibitory action on AHR activation and an antioxidant effect mediated by NRF2/HO1 signaling.	cinnamaldehyde	12-26	heme oxygenase 1	Homo sapiens	160-163
27856716-1	2017	Endogenous carbon monoxide (CO) levels are recognized as a surrogate marker for activity of heme oxygenase-1, which is induced by various factors, including hypoxia and oxidative stress.	Carbon Monoxide	11-26	heme oxygenase 1	Homo sapiens	92-108
27856716-1	2017	Endogenous carbon monoxide (CO) levels are recognized as a surrogate marker for activity of heme oxygenase-1, which is induced by various factors, including hypoxia and oxidative stress.	Carbon Monoxide	28-30	heme oxygenase 1	Homo sapiens	92-108
27720465-8	2017	Cinnamaldehyde also activated the NRF2/HO1 pathway and significantly alleviated the production of reactive oxygen species in keratinocytes.	cinnamaldehyde	0-14	heme oxygenase 1	Homo sapiens	39-42
27959441-0	2017	Protective effects of Cambodian medicinal plants on tert-butyl hydroperoxide-induced hepatotoxicity via Nrf2-mediated heme oxygenase-1.	tert-Butylhydroperoxide	52-76	heme oxygenase 1	Homo sapiens	118-134
28740855-6	2017	In addition, fidarestat augmented the HG-induced Nrf2 expression and activity and also upregulated the expression of Nrf2-dependent proteins such as hemeoxygenase-1 (HO1) and NQO1 in Thp1 cells.	fidarestat	13-23	heme oxygenase 1	Homo sapiens	149-169
27959441-9	2017	These results indicated that, of the 64 Cambodian plants, P. weberi and T. crispa exhibited hepatoprotective effects on t-BHP-induced cytotoxicity in HepG2 cells, possibly by the induction of Nrf2-mediated expression of HO-1.	tert-Butylhydroperoxide	120-125	heme oxygenase 1	Homo sapiens	220-224
28123555-3	2017	HO-1 expression was evaluated using immunohistochemistry in 147 formalin-fixed tissue specimens.	Formaldehyde	64-72	heme oxygenase 1	Homo sapiens	0-4
26742524-0	2017	High-Glucose-Derived Oxidative Stress-Dependent Heme Oxygenase-1 Expression from Astrocytes Contributes to the Neuronal Apoptosis.	high-glucose	0-12	heme oxygenase 1	Homo sapiens	48-64
26742524-6	2017	We demonstrated that HG induced HO-1 expression via a reactive oxygen species (ROS)-dependent signaling pathway.	Reactive Oxygen Species	54-77	heme oxygenase 1	Homo sapiens	32-36
26742524-6	2017	We demonstrated that HG induced HO-1 expression via a reactive oxygen species (ROS)-dependent signaling pathway.	Reactive Oxygen Species	79-82	heme oxygenase 1	Homo sapiens	32-36
26742524-9	2017	These results indicated that in brain astrocytes, activation of MAPK-mediated NF-kappaB and c-Fos/AP-1 cascades by Nox/ROS and mitoROS-dependent events is essential for HO-1 up-regulation induced by HG.	Reactive Oxygen Species	119-122	heme oxygenase 1	Homo sapiens	169-173
26742524-9	2017	These results indicated that in brain astrocytes, activation of MAPK-mediated NF-kappaB and c-Fos/AP-1 cascades by Nox/ROS and mitoROS-dependent events is essential for HO-1 up-regulation induced by HG.	mitoros	127-134	heme oxygenase 1	Homo sapiens	169-173
26993631-3	2017	In addition we tested also the hypothesis that CO can decrease the pre-existing condition of oxidative stress in the mouse model for the human medical condition systemic lupus erythematosus by increasing two protective enzymes heme-oxygenase-1 (HO-1), and superoxide dismutase-2 (SOD-2).	Carbon Monoxide	47-49	heme oxygenase 1	Homo sapiens	227-243
26993631-3	2017	In addition we tested also the hypothesis that CO can decrease the pre-existing condition of oxidative stress in the mouse model for the human medical condition systemic lupus erythematosus by increasing two protective enzymes heme-oxygenase-1 (HO-1), and superoxide dismutase-2 (SOD-2).	Carbon Monoxide	47-49	heme oxygenase 1	Homo sapiens	245-249
28694915-6	2017	Overall, our study is the first to demonstrate that the cytoprotective actions of halophenols involve their antiapoptotic, antioxidant, and anti-inflammatory abilities, which are mediated by the upregulation of Nrf2-dependent HO-1 expression and reductions in ROS and TNF-alpha generation via the activation of Erk1/2 and PI3K/Akt in EA.hy926 cells.	halophenols	82-93	heme oxygenase 1	Homo sapiens	226-230
28694915-0	2017	Heme Oxygenase-1, a Key Enzyme for the Cytoprotective Actions of Halophenols by Upregulating Nrf2 Expression via Activating Erk1/2 and PI3K/Akt in EA.hy926 Cells.	halophenols	65-76	heme oxygenase 1	Homo sapiens	0-16
28473878-0	2017	HO-1 Is Essential for Tetrahydroxystilbene Glucoside Mediated Mitochondrial Biogenesis and Anti-Inflammation Process in LPS-Treated RAW264.7 Macrophages.	2',3',4',5'-tetrahydroxystilbene-2-O-beta-D-glucoside	22-52	heme oxygenase 1	Homo sapiens	0-4
28473878-7	2017	Zinc Protoporphyrin (ZnPP), a selective inhibitor of HO-1 activity, was able to attenuate TSG mediated mitochondrial biogenesis and anti-inflammatory process.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	53-57
28473878-7	2017	Zinc Protoporphyrin (ZnPP), a selective inhibitor of HO-1 activity, was able to attenuate TSG mediated mitochondrial biogenesis and anti-inflammatory process.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	53-57
28694915-6	2017	Overall, our study is the first to demonstrate that the cytoprotective actions of halophenols involve their antiapoptotic, antioxidant, and anti-inflammatory abilities, which are mediated by the upregulation of Nrf2-dependent HO-1 expression and reductions in ROS and TNF-alpha generation via the activation of Erk1/2 and PI3K/Akt in EA.hy926 cells.	ros	260-263	heme oxygenase 1	Homo sapiens	226-230
28694915-3	2017	In the present study, we demonstrated that these halophenols exhibited significant protective effects against H2O2-induced injury in EA.hy926 cells by inhibition of apoptosis and ROS and TNF-alpha production, as well as induction of the upregulation of HO-1, the magnitude of which correlated with their cytoprotective actions.	halophenols	49-60	heme oxygenase 1	Homo sapiens	253-257
28694915-3	2017	In the present study, we demonstrated that these halophenols exhibited significant protective effects against H2O2-induced injury in EA.hy926 cells by inhibition of apoptosis and ROS and TNF-alpha production, as well as induction of the upregulation of HO-1, the magnitude of which correlated with their cytoprotective actions.	Hydrogen Peroxide	110-114	heme oxygenase 1	Homo sapiens	253-257
28694915-7	2017	HO-1 may thus be an important potential target for further research into the cytoprotective actions of halophenols.	halophenols	103-114	heme oxygenase 1	Homo sapiens	0-4
28694916-0	2017	The Protective Effect of Indole-3-Acetic Acid (IAA) on H2O2-Damaged Human Dental Pulp Stem Cells Is Mediated by the AKT Pathway and Involves Increased Expression of the Transcription Factor Nuclear Factor-Erythroid 2-Related Factor 2 (Nrf2) and Its Downstream Target Heme Oxygenase 1 (HO-1).	indoleacetic acid	25-45	heme oxygenase 1	Homo sapiens	267-283
28694916-0	2017	The Protective Effect of Indole-3-Acetic Acid (IAA) on H2O2-Damaged Human Dental Pulp Stem Cells Is Mediated by the AKT Pathway and Involves Increased Expression of the Transcription Factor Nuclear Factor-Erythroid 2-Related Factor 2 (Nrf2) and Its Downstream Target Heme Oxygenase 1 (HO-1).	indoleacetic acid	25-45	heme oxygenase 1	Homo sapiens	285-289
28694916-0	2017	The Protective Effect of Indole-3-Acetic Acid (IAA) on H2O2-Damaged Human Dental Pulp Stem Cells Is Mediated by the AKT Pathway and Involves Increased Expression of the Transcription Factor Nuclear Factor-Erythroid 2-Related Factor 2 (Nrf2) and Its Downstream Target Heme Oxygenase 1 (HO-1).	indoleacetic acid	47-50	heme oxygenase 1	Homo sapiens	267-283
28694916-0	2017	The Protective Effect of Indole-3-Acetic Acid (IAA) on H2O2-Damaged Human Dental Pulp Stem Cells Is Mediated by the AKT Pathway and Involves Increased Expression of the Transcription Factor Nuclear Factor-Erythroid 2-Related Factor 2 (Nrf2) and Its Downstream Target Heme Oxygenase 1 (HO-1).	indoleacetic acid	47-50	heme oxygenase 1	Homo sapiens	285-289
28694916-8	2017	To further investigate the mechanism of IAA, Nrf2-related antioxidant pathway was examined and the results showed that the level of Nrf2 and HO-1 expressions, stimulated by H2O2, decreased after treatment of IAA.	Hydrogen Peroxide	173-177	heme oxygenase 1	Homo sapiens	141-145
28694916-8	2017	To further investigate the mechanism of IAA, Nrf2-related antioxidant pathway was examined and the results showed that the level of Nrf2 and HO-1 expressions, stimulated by H2O2, decreased after treatment of IAA.	indoleacetic acid	40-43	heme oxygenase 1	Homo sapiens	141-145
28694916-9	2017	Moreover, IAA treatment protected hDPSCs against H2O2-induced oxidative stress via increased expression of Nrf2 and HO-1, mediated by the AKT pathway.	Hydrogen Peroxide	49-53	heme oxygenase 1	Homo sapiens	116-120
27627465-5	2017	RESULTS: We found that salidroside pretreatment upregulated Nrf2 translocation to the nucleus and transcription activity in HaCaT cells, as reflected by the increased nuclear accumulation of Nrf2 as well as the gene and protein expression of downstream Nrf2 antioxidants, including NQO1 and HO-1.	rhodioloside	23-34	heme oxygenase 1	Homo sapiens	291-295
29158871-3	2017	Because a crosstalk exists between nitric oxide (NO) and HO-1 in promotion of cell survival under oxidative stress, we designed novel NO-releasing molecules also capable to induce HO-1.	Nitric Oxide	35-47	heme oxygenase 1	Homo sapiens	180-184
29158871-4	2017	Starting from curcumin and caffeic acid phenethyl ester (CAPE), two known HO-1 inducers, the molecules were chemically modified by acylation with 4-bromo-butanoyl chloride and 2-chloro-propanoyl chloride, respectively, and then treated in the dark with AgNO3 to obtain the nitrate derivatives VP10/12 and VP10/39.	Curcumin	14-22	heme oxygenase 1	Homo sapiens	74-78
29158871-4	2017	Starting from curcumin and caffeic acid phenethyl ester (CAPE), two known HO-1 inducers, the molecules were chemically modified by acylation with 4-bromo-butanoyl chloride and 2-chloro-propanoyl chloride, respectively, and then treated in the dark with AgNO3 to obtain the nitrate derivatives VP10/12 and VP10/39.	caffeic acid phenethyl ester	27-55	heme oxygenase 1	Homo sapiens	74-78
29158871-4	2017	Starting from curcumin and caffeic acid phenethyl ester (CAPE), two known HO-1 inducers, the molecules were chemically modified by acylation with 4-bromo-butanoyl chloride and 2-chloro-propanoyl chloride, respectively, and then treated in the dark with AgNO3 to obtain the nitrate derivatives VP10/12 and VP10/39.	caffeic acid phenethyl ester	57-61	heme oxygenase 1	Homo sapiens	74-78
30263473-0	2016	Effect of (-)-epigallocatechin-3-gallate on anti-inflammatory response via heme oxygenase-1 induction during adipocyte-macrophage interactions.	epigallocatechin gallate	10-40	heme oxygenase 1	Homo sapiens	75-91
28255307-6	2017	Then, MSC or MSC-HO-1 was cocultured with retinal ganglion cells (RGC-5) in H2O2-simulated oxidative condition and their protection on RGC-5 was systemically valuated in vitro.	Hydrogen Peroxide	76-80	heme oxygenase 1	Homo sapiens	17-21
28255307-7	2017	Compared with MSC, MSC-HO-1 significantly attenuated H2O2-induced injury of RGC-5, including decrease in cellular ROS level and apoptosis, activation of antiapoptotic proteins p-Akt and Bcl-2, and blockage of proapoptotic proteins cleaved caspase 3 and Bax.	Hydrogen Peroxide	53-57	heme oxygenase 1	Homo sapiens	23-27
28255307-7	2017	Compared with MSC, MSC-HO-1 significantly attenuated H2O2-induced injury of RGC-5, including decrease in cellular ROS level and apoptosis, activation of antiapoptotic proteins p-Akt and Bcl-2, and blockage of proapoptotic proteins cleaved caspase 3 and Bax.	ros	114-117	heme oxygenase 1	Homo sapiens	23-27
28751936-7	2017	Furthermore, we also found that the protective effects of MaR 1 on lung tissue injury and oxidative stress were reversed by HO-1 activity inhibitor, Znpp-IX.	zinc protoporphyrin	149-156	heme oxygenase 1	Homo sapiens	124-128
28751936-8	2017	Nrf-2 transcription factor inhibitor, brusatol, significantly decreased MaR 1-induced nuclear Nrf-2 and cytosolic HO-1 expression.	brusatol	38-46	heme oxygenase 1	Homo sapiens	114-118
30263473-1	2016	In this study, we examined the effects of (-)-epigallocatechin-3-gallate (EGCG) on anti-inflammatory responses through the induction of heme oxygenase-1 (HO-1) in cocultured macrophages and adipocytes.	epigallocatechin gallate	42-72	heme oxygenase 1	Homo sapiens	136-152
30263473-1	2016	In this study, we examined the effects of (-)-epigallocatechin-3-gallate (EGCG) on anti-inflammatory responses through the induction of heme oxygenase-1 (HO-1) in cocultured macrophages and adipocytes.	epigallocatechin gallate	42-72	heme oxygenase 1	Homo sapiens	154-158
30263473-1	2016	In this study, we examined the effects of (-)-epigallocatechin-3-gallate (EGCG) on anti-inflammatory responses through the induction of heme oxygenase-1 (HO-1) in cocultured macrophages and adipocytes.	epigallocatechin gallate	74-78	heme oxygenase 1	Homo sapiens	136-152
30263473-1	2016	In this study, we examined the effects of (-)-epigallocatechin-3-gallate (EGCG) on anti-inflammatory responses through the induction of heme oxygenase-1 (HO-1) in cocultured macrophages and adipocytes.	epigallocatechin gallate	74-78	heme oxygenase 1	Homo sapiens	154-158
30263473-6	2016	These results indicate that EGCG inhibited inflammatory responses by suppressing the production of proinflammatory cytokines through HO-1 induction during adipocyte-macrophage interaction.	epigallocatechin gallate	28-32	heme oxygenase 1	Homo sapiens	133-137
28050122-14	2016	CDECM induced nuclear factor erythroid-2 related factor 2 (Nrf2) mediated-antioxidant enzyme heme oxygenase-1 (HO-1).	cdecm	0-5	heme oxygenase 1	Homo sapiens	93-109
27795439-3	2017	In this study, inhibition of PRRSV replication was demonstrated to be mediated by carbon monoxide (CO), a downstream metabolite of HO-1.	Carbon Monoxide	82-97	heme oxygenase 1	Homo sapiens	131-135
27997582-2	2016	The cytoprotective enzyme heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation and it has been shown to exert anti-inflammatory functions.	Heme	26-30	heme oxygenase 1	Homo sapiens	44-48
27795439-3	2017	In this study, inhibition of PRRSV replication was demonstrated to be mediated by carbon monoxide (CO), a downstream metabolite of HO-1.	Carbon Monoxide	99-101	heme oxygenase 1	Homo sapiens	131-135
27795439-12	2017	Carbon monoxide (CO), a metabolite of HO-1, has been shown to have antimicrobial and antiviral activities in infected cells.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	38-42
27795439-12	2017	Carbon monoxide (CO), a metabolite of HO-1, has been shown to have antimicrobial and antiviral activities in infected cells.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	38-42
27863411-6	2016	Meanwhile, sesamin was found to up-regulate the expression of Nrf2 and HO-1.	sesamin	11-18	heme oxygenase 1	Homo sapiens	71-75
27912883-7	2016	RESULTS: Miltirone-induced Nrf2 and HO-1 expression was related to mitogen-activated protein kinase (MAPK) pathways.	miltirone	9-18	heme oxygenase 1	Homo sapiens	36-40
27912883-9	2016	However, miltirone-induced Nrf2/HO-1 expression can only be effectively blocked by JNK inhibitor SP600125.	miltirone	9-18	heme oxygenase 1	Homo sapiens	32-36
27912883-9	2016	However, miltirone-induced Nrf2/HO-1 expression can only be effectively blocked by JNK inhibitor SP600125.	pyrazolanthrone	97-105	heme oxygenase 1	Homo sapiens	32-36
27912883-10	2016	CONCLUSION: Our findings reveal that miltirone exerts protective functions on endothelial cells in response to ox-LDL-induced oxidative stress, and does so via Nrf2/HO-1, which provides novel insights into the antioxidant capacity of miltirone.	miltirone	37-46	heme oxygenase 1	Homo sapiens	165-169
27912883-0	2016	Miltirone protects human EA.hy926 endothelial cells from oxidized low-density lipoprotein-derived oxidative stress via a heme oxygenase-1 and MAPK/Nrf2 dependent pathway.	miltirone	0-9	heme oxygenase 1	Homo sapiens	121-137
27912883-4	2016	STUDY DESIGN/METHOD: In the present study, miltirone increased the expression of nuclear translocation and transcriptional activities of NF-E2-related factor 2 (Nrf2), which led to augmented expression of antioxidant-response element (ARE)-dependent heme oxygenase-1 (HO-1) and NAD(P)H-quinone oxidoreductase 1 (NQO1).	miltirone	43-52	heme oxygenase 1	Homo sapiens	250-266
27912883-5	2016	Inhibition of Nrf2/HO-1 by RNA interference abolished miltirone-induced cytoprotective effects against ox-LDL, which suggested that Nrf2 and the downstream expression of HO-1 are required for the functional effects of miltirone.	miltirone	54-63	heme oxygenase 1	Homo sapiens	19-23
27912883-5	2016	Inhibition of Nrf2/HO-1 by RNA interference abolished miltirone-induced cytoprotective effects against ox-LDL, which suggested that Nrf2 and the downstream expression of HO-1 are required for the functional effects of miltirone.	miltirone	54-63	heme oxygenase 1	Homo sapiens	170-174
27912883-5	2016	Inhibition of Nrf2/HO-1 by RNA interference abolished miltirone-induced cytoprotective effects against ox-LDL, which suggested that Nrf2 and the downstream expression of HO-1 are required for the functional effects of miltirone.	miltirone	218-227	heme oxygenase 1	Homo sapiens	19-23
27912883-5	2016	Inhibition of Nrf2/HO-1 by RNA interference abolished miltirone-induced cytoprotective effects against ox-LDL, which suggested that Nrf2 and the downstream expression of HO-1 are required for the functional effects of miltirone.	miltirone	218-227	heme oxygenase 1	Homo sapiens	170-174
27829220-0	2016	Gene expression profile induced by arsenic trioxide in chronic lymphocytic leukemia cells reveals a central role for heme oxygenase-1 in apoptosis and regulation of matrix metalloproteinase-9.	Arsenic Trioxide	35-51	heme oxygenase 1	Homo sapiens	117-133
27829220-4	2016	ATO modulated many genes, largely involved in oxidative stress, being HMOX1 the most upregulated gene, also induced at the protein level.	Arsenic Trioxide	0-3	heme oxygenase 1	Homo sapiens	70-75
27829220-9	2016	Cell viability analyses upon modulation of HMOX1 expression or activity demonstrated that HMOX1 had a pro-apoptotic role and enhanced the cytotoxic effect of ATO in CLL cells.	Arsenic Trioxide	158-161	heme oxygenase 1	Homo sapiens	43-48
27829220-9	2016	Cell viability analyses upon modulation of HMOX1 expression or activity demonstrated that HMOX1 had a pro-apoptotic role and enhanced the cytotoxic effect of ATO in CLL cells.	Arsenic Trioxide	158-161	heme oxygenase 1	Homo sapiens	90-95
27725188-0	2016	Omeprazole induces heme oxygenase-1 in fetal human pulmonary microvascular endothelial cells via hydrogen peroxide-independent Nrf2 signaling pathway.	Omeprazole	0-10	heme oxygenase 1	Homo sapiens	19-35
30461238-0	2016	Translational toxicology from basic sciences to clinical toxicology Toxicological significance of heme oxygenase-1 induction, the enzyme of carbon monoxide production.	Carbon Monoxide	140-155	heme oxygenase 1	Homo sapiens	98-114
26593436-7	2016	IsoLQ also induced the expression of Nrf2 target phase II enzymes, such as heme oxygenase-1, glutamate-cysteine ligase catalytic subunit and NAD(P)H:quinone oxidoreductase 1.	isolq	0-5	heme oxygenase 1	Homo sapiens	75-91
27931585-8	2016	Further, resveratrol activated the expression of sirtuin-1 and Nrf2, and inhibited the expression of osteopontin, runt-related transcription factor 2, and heme oxygenase-1.	Resveratrol	9-20	heme oxygenase 1	Homo sapiens	155-171
27853236-7	2016	Luteolin enhanced antioxidant defense system based on Keap1, Nrf2, HO-1, NQO1, and KLF9.	Luteolin	0-8	heme oxygenase 1	Homo sapiens	67-71
27725188-11	2016	Although N-acetyl cysteine (NAC) significantly decreased H2O2 levels in OM-treated cells, we observed that OM further increased HO-1 mRNA and protein expression in NAC-pretreated compared to vehicle-pretreated cells, suggesting that OM induces HO-1 via H2O2-independent mechanisms.	Acetylcysteine	164-167	heme oxygenase 1	Homo sapiens	128-132
27725188-11	2016	Although N-acetyl cysteine (NAC) significantly decreased H2O2 levels in OM-treated cells, we observed that OM further increased HO-1 mRNA and protein expression in NAC-pretreated compared to vehicle-pretreated cells, suggesting that OM induces HO-1 via H2O2-independent mechanisms.	Acetylcysteine	164-167	heme oxygenase 1	Homo sapiens	244-248
27725188-12	2016	In conclusion, we provide evidence that OM transcriptionally induces HO-1 via AhR - and H2O2 - independent, but Nrf2 - dependent mechanisms.	Hydrogen Peroxide	88-92	heme oxygenase 1	Homo sapiens	69-73
27725188-0	2016	Omeprazole induces heme oxygenase-1 in fetal human pulmonary microvascular endothelial cells via hydrogen peroxide-independent Nrf2 signaling pathway.	Hydrogen Peroxide	97-114	heme oxygenase 1	Homo sapiens	19-35
27725188-9	2016	Interestingly, the concentration at which OM induced HO-1 also increased H2O2 levels.	Hydrogen Peroxide	73-77	heme oxygenase 1	Homo sapiens	53-57
27725188-10	2016	Furthermore, H2O2 independently augmented HO-1 expression.	Hydrogen Peroxide	13-17	heme oxygenase 1	Homo sapiens	42-46
27591243-13	2016	14,15-EET treatment resulted in a significant reduction in IL-6, IL-8, and MCP-1 secretion, and increased accumulation of Nrf2 and expression of HO-1.	14,15-epoxy-5,8,11-eicosatrienoic acid	0-9	heme oxygenase 1	Homo sapiens	145-149
27782264-7	2016	Phase 2 enzymes in term of antioxidant response, such as heme oxygenase 1 (HMOX1) and the regulating subunit of the glutamate-cysteine ligase (GCLM) were slightly upregulated, but these observations may be linked solely to metal homeostasis disruptions, as these actors are involved in both metal and ROS responses.	Metals	223-228	heme oxygenase 1	Homo sapiens	57-73
27782264-7	2016	Phase 2 enzymes in term of antioxidant response, such as heme oxygenase 1 (HMOX1) and the regulating subunit of the glutamate-cysteine ligase (GCLM) were slightly upregulated, but these observations may be linked solely to metal homeostasis disruptions, as these actors are involved in both metal and ROS responses.	Metals	223-228	heme oxygenase 1	Homo sapiens	75-80
27782264-7	2016	Phase 2 enzymes in term of antioxidant response, such as heme oxygenase 1 (HMOX1) and the regulating subunit of the glutamate-cysteine ligase (GCLM) were slightly upregulated, but these observations may be linked solely to metal homeostasis disruptions, as these actors are involved in both metal and ROS responses.	Metals	291-296	heme oxygenase 1	Homo sapiens	57-73
27782264-7	2016	Phase 2 enzymes in term of antioxidant response, such as heme oxygenase 1 (HMOX1) and the regulating subunit of the glutamate-cysteine ligase (GCLM) were slightly upregulated, but these observations may be linked solely to metal homeostasis disruptions, as these actors are involved in both metal and ROS responses.	Metals	291-296	heme oxygenase 1	Homo sapiens	75-80
27782264-7	2016	Phase 2 enzymes in term of antioxidant response, such as heme oxygenase 1 (HMOX1) and the regulating subunit of the glutamate-cysteine ligase (GCLM) were slightly upregulated, but these observations may be linked solely to metal homeostasis disruptions, as these actors are involved in both metal and ROS responses.	ros	301-304	heme oxygenase 1	Homo sapiens	57-73
27782264-7	2016	Phase 2 enzymes in term of antioxidant response, such as heme oxygenase 1 (HMOX1) and the regulating subunit of the glutamate-cysteine ligase (GCLM) were slightly upregulated, but these observations may be linked solely to metal homeostasis disruptions, as these actors are involved in both metal and ROS responses.	ros	301-304	heme oxygenase 1	Homo sapiens	75-80
27412172-10	2016	Moreover, MG also protects adipocytes from oxidative stress by alleviating intracellular reactive oxygen species and activating Nrf2, HO-1, and PRDX3.	methyl gallate	10-12	heme oxygenase 1	Homo sapiens	134-138
27374075-9	2016	Multiple logistic regression analysis, however, showed that only rs2364723 significantly reduced levels of serum HMOX1 in T2DM patients for the GG genotype carriers compared with participants with CG+CC genotype.	cysteinylglycine	197-199	heme oxygenase 1	Homo sapiens	113-118
27694475-8	2016	Finally, peripheral blood monocytes (PBMCs) from elderly patients with P-NTM also demonstrated attenuated HO-1 responses after M. avium stimulation and increased cell death due to cellular necrosis (9.69% +- 2.02) compared with apoptosis (4.75% +- 0.98).	p-ntm	71-76	heme oxygenase 1	Homo sapiens	106-110
27418236-0	2016	Andrographolide protects liver cells from H2O2 induced cell death by upregulation of Nrf-2/HO-1 mediated via adenosine A2a receptor signalling.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	91-95
27418236-0	2016	Andrographolide protects liver cells from H2O2 induced cell death by upregulation of Nrf-2/HO-1 mediated via adenosine A2a receptor signalling.	Hydrogen Peroxide	42-46	heme oxygenase 1	Homo sapiens	91-95
27418236-6	2016	RESULTS: We clearly show that andrographolide via adenosine A2A receptor signalling leads to activation of p38 MAP kinase, resulting in upregulation of Nrf-2, its translocation to nucleus and activation of HO-1.	andrographolide	30-45	heme oxygenase 1	Homo sapiens	206-210
27418236-9	2016	CONCLUSIONS: Thus, andrographolide probably by binding to adenosine A2a receptor activates Nrf-2 transcription and also inhibits its exclusion from the nucleus by inactivating GSK-3beta, together resulting in activation of HO-1.	andrographolide	19-34	heme oxygenase 1	Homo sapiens	223-227
27671470-8	2016	A mechanistic study showed that Co-Cr alloys activates the NRF2 pathway and up-regulate antioxidant enzymes including heme oxygenase-1 (HO-1).	co-cr	32-37	heme oxygenase 1	Homo sapiens	118-134
27505325-0	2016	GT-repeat length polymorphism in heme oxygenase-1 promoter determines the effect of cilostazol on vascular smooth muscle cells.	Cilostazol	84-94	heme oxygenase 1	Homo sapiens	33-49
27505325-2	2016	The aim of this study is to investigate whether the inhibitory effect of cilostazol on VSMC proliferation is operated via heme oxygenase-1 (HO-1).	Cilostazol	73-83	heme oxygenase 1	Homo sapiens	122-138
27505325-2	2016	The aim of this study is to investigate whether the inhibitory effect of cilostazol on VSMC proliferation is operated via heme oxygenase-1 (HO-1).	Cilostazol	73-83	heme oxygenase 1	Homo sapiens	140-144
27505325-2	2016	The aim of this study is to investigate whether the inhibitory effect of cilostazol on VSMC proliferation is operated via heme oxygenase-1 (HO-1).	vsmc	87-91	heme oxygenase 1	Homo sapiens	122-138
27505325-2	2016	The aim of this study is to investigate whether the inhibitory effect of cilostazol on VSMC proliferation is operated via heme oxygenase-1 (HO-1).	vsmc	87-91	heme oxygenase 1	Homo sapiens	140-144
27505325-4	2016	Treatment of human VSMCs with cilostazol enhanced the expression of HO-1, which was mainly regulated at the transcriptional level.	Cilostazol	30-40	heme oxygenase 1	Homo sapiens	68-72
27505325-5	2016	Small interfering RNA knock-down of HO-1 attenuated the inhibitory effect of cilostazol on VSMC proliferation, suggesting the critical role of HO-1 in cilostazol effect.	Cilostazol	77-87	heme oxygenase 1	Homo sapiens	36-40
27505325-5	2016	Small interfering RNA knock-down of HO-1 attenuated the inhibitory effect of cilostazol on VSMC proliferation, suggesting the critical role of HO-1 in cilostazol effect.	Cilostazol	77-87	heme oxygenase 1	Homo sapiens	143-147
27505325-5	2016	Small interfering RNA knock-down of HO-1 attenuated the inhibitory effect of cilostazol on VSMC proliferation, suggesting the critical role of HO-1 in cilostazol effect.	vsmc	91-95	heme oxygenase 1	Homo sapiens	36-40
27505325-5	2016	Small interfering RNA knock-down of HO-1 attenuated the inhibitory effect of cilostazol on VSMC proliferation, suggesting the critical role of HO-1 in cilostazol effect.	Cilostazol	151-161	heme oxygenase 1	Homo sapiens	36-40
27505325-5	2016	Small interfering RNA knock-down of HO-1 attenuated the inhibitory effect of cilostazol on VSMC proliferation, suggesting the critical role of HO-1 in cilostazol effect.	Cilostazol	151-161	heme oxygenase 1	Homo sapiens	143-147
27505325-6	2016	The transcriptional responsiveness of HO-1 to cilostazol was inversely correlated with the length of GT-repeat in human HO-1 promoter.	Cilostazol	46-56	heme oxygenase 1	Homo sapiens	38-42
27505325-6	2016	The transcriptional responsiveness of HO-1 to cilostazol was inversely correlated with the length of GT-repeat in human HO-1 promoter.	Cilostazol	46-56	heme oxygenase 1	Homo sapiens	120-124
27505325-7	2016	Deletion and mutational analysis of HO-1 promoter along with chromatin immunoprecipitation showed that cyclic AMP response element (CRE)-binding protein (CREB) participated in cilostazol-induced HO-1 transcription.	Cyclic AMP	103-113	heme oxygenase 1	Homo sapiens	36-40
27505325-7	2016	Deletion and mutational analysis of HO-1 promoter along with chromatin immunoprecipitation showed that cyclic AMP response element (CRE)-binding protein (CREB) participated in cilostazol-induced HO-1 transcription.	Cyclic AMP	103-113	heme oxygenase 1	Homo sapiens	195-199
27505325-7	2016	Deletion and mutational analysis of HO-1 promoter along with chromatin immunoprecipitation showed that cyclic AMP response element (CRE)-binding protein (CREB) participated in cilostazol-induced HO-1 transcription.	Cilostazol	176-186	heme oxygenase 1	Homo sapiens	36-40
27505325-7	2016	Deletion and mutational analysis of HO-1 promoter along with chromatin immunoprecipitation showed that cyclic AMP response element (CRE)-binding protein (CREB) participated in cilostazol-induced HO-1 transcription.	Cilostazol	176-186	heme oxygenase 1	Homo sapiens	195-199
27505325-8	2016	Furthermore, cilostazol triggered a linkage between the CRE and GT-repeat regions in the HO-1 promoter.	Cilostazol	13-23	heme oxygenase 1	Homo sapiens	89-93
27505325-9	2016	The promoting effect of cilostazol on HO-1 expression, proliferation inhibition, and chromatin conformation in the HO-1 promoter was greater in VSMCs from subjects with shorter GT-repeat alleles than those with longer alleles.	Cilostazol	24-34	heme oxygenase 1	Homo sapiens	38-42
27505325-9	2016	The promoting effect of cilostazol on HO-1 expression, proliferation inhibition, and chromatin conformation in the HO-1 promoter was greater in VSMCs from subjects with shorter GT-repeat alleles than those with longer alleles.	Cilostazol	24-34	heme oxygenase 1	Homo sapiens	115-119
27505325-10	2016	CONCLUSIONS: Cilostazol inhibits VSMC proliferation involving an association between CREB and HO-1.	Cilostazol	13-23	heme oxygenase 1	Homo sapiens	94-98
27505325-10	2016	CONCLUSIONS: Cilostazol inhibits VSMC proliferation involving an association between CREB and HO-1.	vsmc	33-37	heme oxygenase 1	Homo sapiens	94-98
27505325-11	2016	The length polymorphism of GT-repeat in human HO-1 promoter determines the effect of cilostazol.	Cilostazol	85-95	heme oxygenase 1	Homo sapiens	46-50
27397680-7	2016	Alternatively, GGT5 overexpression induces heme oxygenase 1 (HO-1) expression, which, as a key catalyst responsible for the oxidative degradation of heme, may inhibit the activities of the cytochrome P450 monooxygenases, thus substantially impairing testicular steroidogenesis.	Heme	43-47	heme oxygenase 1	Homo sapiens	61-65
27397680-8	2016	These results, coupled with the differential roles of mitogen-activated protein kinases and HO-1 signaling in spermatogenesis, lead us to propose a model in which a delicate balance between these two pathways modulated by the GGT5/oxidative stress cascade plays a central role during LH-stimulated steroidogenesis.	Luteinizing Hormone	284-286	heme oxygenase 1	Homo sapiens	92-96
27662012-0	2016	Mutating heme oxygenase-1 into a peroxidase causes a defect in bilirubin synthesis associated with microcytic anemia and severe hyperinflammation.	Bilirubin	63-72	heme oxygenase 1	Homo sapiens	9-25
27257045-1	2016	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme, which may be involved in the pathogenesis of AKI.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
27257045-1	2016	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme, which may be involved in the pathogenesis of AKI.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
27257045-2	2016	Length polymorphisms in the number of GT dinucleotide repeats in the HO-1 gene (HMOX1) promoter inversely associate with HMOX1 mRNA expression.	gt dinucleotide	38-53	heme oxygenase 1	Homo sapiens	69-73
27257045-2	2016	Length polymorphisms in the number of GT dinucleotide repeats in the HO-1 gene (HMOX1) promoter inversely associate with HMOX1 mRNA expression.	gt dinucleotide	38-53	heme oxygenase 1	Homo sapiens	80-85
27257045-2	2016	Length polymorphisms in the number of GT dinucleotide repeats in the HO-1 gene (HMOX1) promoter inversely associate with HMOX1 mRNA expression.	gt dinucleotide	38-53	heme oxygenase 1	Homo sapiens	121-126
27571925-5	2016	Iron, one of HO-1 catalytic products, was an important mediator in this regulation.	Iron	0-4	heme oxygenase 1	Homo sapiens	13-17
27283929-4	2016	AIMS: To compare effects of hemin and placebo infusions on HO1 activity and protein, GE, autonomic function, and gastrointestinal symptoms in diabetic gastroparesis.	Hemin	28-33	heme oxygenase 1	Homo sapiens	59-62
27283929-12	2016	Further studies are necessary to ascertain whether more frequent hemin infusions or other drugs would have a more sustained effect on HO1 and improve GE.	Hemin	65-70	heme oxygenase 1	Homo sapiens	134-137
27678042-0	2016	Calycosin suppresses expression of pro-inflammatory cytokines via the activation of p62/Nrf2-linked heme oxygenase 1 in rheumatoid arthritis synovial fibroblasts.	7,3'-dihydroxy-4'-methoxyisoflavone	0-9	heme oxygenase 1	Homo sapiens	100-116
27620489-8	2016	Cd exposure to p53-overexpressing YD10B cells enhanced Cd-induced HO-1 and LC3-II levels, whereas genetic knockdown of p53 in YD8 cells resulted in the suppression of Cd-induced levels of HO-1 and LC3-II, indicating that p53 is required in the sensing of HO-1 and induction of autophagy.	Cadmium	55-57	heme oxygenase 1	Homo sapiens	66-70
27795400-1	2016	Heme oxygenase-1 (HO-1) is a stress response antioxidant enzyme which catalyzes the degradation of heme released during inflammation.	Heme	99-103	heme oxygenase 1	Homo sapiens	18-22
27795400-4	2016	To address this controversy, we administered tin protoporphyrin IX (SnPPIX), a well-characterized HO-1 enzymatic inhibitor, to mice during acute M. tuberculosis infection.	tin protoporphyrin IX	45-66	heme oxygenase 1	Homo sapiens	98-102
27795400-4	2016	To address this controversy, we administered tin protoporphyrin IX (SnPPIX), a well-characterized HO-1 enzymatic inhibitor, to mice during acute M. tuberculosis infection.	tin protoporphyrin IX	68-74	heme oxygenase 1	Homo sapiens	98-102
27795400-13	2016	Here, we describe a potential strategy for treating TB based on pharmacological inhibition of the host heme-degrading enzyme HO-1.	Heme	103-107	heme oxygenase 1	Homo sapiens	125-129
27562971-8	2016	Decreasing NADH pharmacologically with MTOB or genetically blocking CtBP1 with siRNA upregulated the cyclin-dependent genes (p15 and p21) and proapoptotic regulators (NOXA and PERP), attenuated proliferation, corrected the glycolytic reprogramming phenotype of PH-Fibs, and augmented transcription of the anti-inflammatory gene HMOX1.	NAD	11-15	heme oxygenase 1	Homo sapiens	328-333
27620489-0	2016	Heme oxygenase-1-mediated apoptosis under cadmium-induced oxidative stress is regulated by autophagy, which is sensitized by tumor suppressor p53.	Cadmium	42-49	heme oxygenase 1	Homo sapiens	0-16
27411481-6	2016	HO-1 expression levels were determined with western blot in monocytes before and after induction of HO-1 with cobalt protoporphyrin (CoPP) with or without CXCL4.	cobaltiprotoporphyrin	110-131	heme oxygenase 1	Homo sapiens	100-104
27411481-8	2016	RESULTS: SSc patients have lower plasma levels of bilirubin, suggestive of an aberrant HO-1 function.	Bilirubin	50-59	heme oxygenase 1	Homo sapiens	87-91
27411481-9	2016	We demonstrated low HO-1 expression in immune cells from SSc patients, whereas induction with CoPP was able to restore HO-1 levels in DCs from SSc patients, almost normalizing the increased TLR response observed in SSc.	cobaltiprotoporphyrin	94-98	heme oxygenase 1	Homo sapiens	119-123
27411481-10	2016	Co-exposure to CXCL4 completely abrogated CoPP-induced HO-1 expression, suggesting that the high CXCL4 levels present in SSc patients block the normal induction of HO-1 and its function.	cobaltiprotoporphyrin	42-46	heme oxygenase 1	Homo sapiens	55-59
27411481-10	2016	Co-exposure to CXCL4 completely abrogated CoPP-induced HO-1 expression, suggesting that the high CXCL4 levels present in SSc patients block the normal induction of HO-1 and its function.	cobaltiprotoporphyrin	42-46	heme oxygenase 1	Homo sapiens	164-168
27620489-4	2016	Here we show that the role of HO-1 under Cd-induced oxidative stress is dependent upon autophagy, which is sensitized by the tumor suppressor p53.	Cadmium	41-43	heme oxygenase 1	Homo sapiens	30-34
27620489-7	2016	In both cell lines, Cd exposure resulted in caspase-3-mediated PARP-1 cleavage and the induction of CHOP, LC3-II, and HO-1, which were limited in YD10B and H1299 cells exposed to high concentrations of Cd.	Cadmium	20-22	heme oxygenase 1	Homo sapiens	106-122
27620489-9	2016	The inhibition of autophagy using small interfering RNA (siRNA) for the autophagy-related gene atg5 enhanced HO-1, CHOP, and PARP-1 cleavage induced by Cd.	Cadmium	152-154	heme oxygenase 1	Homo sapiens	109-113
27620489-7	2016	In both cell lines, Cd exposure resulted in caspase-3-mediated PARP-1 cleavage and the induction of CHOP, LC3-II, and HO-1, which were limited in YD10B and H1299 cells exposed to high concentrations of Cd.	Cadmium	202-204	heme oxygenase 1	Homo sapiens	106-122
27620489-10	2016	However, transfection with HO-1 siRNA increased Cd-induced LC3-II, and suppressed the expression of CHOP and cleavage of PARP-1.	Cadmium	48-50	heme oxygenase 1	Homo sapiens	27-31
27620489-8	2016	Cd exposure to p53-overexpressing YD10B cells enhanced Cd-induced HO-1 and LC3-II levels, whereas genetic knockdown of p53 in YD8 cells resulted in the suppression of Cd-induced levels of HO-1 and LC3-II, indicating that p53 is required in the sensing of HO-1 and induction of autophagy.	Cadmium	0-2	heme oxygenase 1	Homo sapiens	66-70
27620489-8	2016	Cd exposure to p53-overexpressing YD10B cells enhanced Cd-induced HO-1 and LC3-II levels, whereas genetic knockdown of p53 in YD8 cells resulted in the suppression of Cd-induced levels of HO-1 and LC3-II, indicating that p53 is required in the sensing of HO-1 and induction of autophagy.	Cadmium	0-2	heme oxygenase 1	Homo sapiens	188-192
27598034-0	2016	15-Deoxy-Delta12,14-prostaglandin J2 stabilizes hypoxia inducible factor-1alpha through induction of heme oxygenase-1 and direct modification ofprolyl-4-hydroxylase 2.	14-prostaglandin j2	17-36	heme oxygenase 1	Homo sapiens	101-117
27620489-8	2016	Cd exposure to p53-overexpressing YD10B cells enhanced Cd-induced HO-1 and LC3-II levels, whereas genetic knockdown of p53 in YD8 cells resulted in the suppression of Cd-induced levels of HO-1 and LC3-II, indicating that p53 is required in the sensing of HO-1 and induction of autophagy.	Cadmium	0-2	heme oxygenase 1	Homo sapiens	188-192
27620489-8	2016	Cd exposure to p53-overexpressing YD10B cells enhanced Cd-induced HO-1 and LC3-II levels, whereas genetic knockdown of p53 in YD8 cells resulted in the suppression of Cd-induced levels of HO-1 and LC3-II, indicating that p53 is required in the sensing of HO-1 and induction of autophagy.	Cadmium	55-57	heme oxygenase 1	Homo sapiens	66-70
27375080-0	2016	Propyl gallate sensitizes human lung cancer cells to cisplatin-induced apoptosis by targeting heme oxygenase-1 for TRC8-mediated degradation.	Propyl Gallate	0-14	heme oxygenase 1	Homo sapiens	94-110
27375080-0	2016	Propyl gallate sensitizes human lung cancer cells to cisplatin-induced apoptosis by targeting heme oxygenase-1 for TRC8-mediated degradation.	Cisplatin	53-62	heme oxygenase 1	Homo sapiens	94-110
27375080-3	2016	In the present study, we investigated whether PG exhibit an anti-cancer effect through modulating HO-1 activation.	Propyl Gallate	46-48	heme oxygenase 1	Homo sapiens	98-102
27375080-4	2016	In human non-small cell lung cancer (NSCLC) cells, treatment with PG dose-dependently diminished HO-1 protein levels without changing its mRNA levels and consequently decreased HO-1 activity.	Propyl Gallate	66-68	heme oxygenase 1	Homo sapiens	97-101
27375080-4	2016	In human non-small cell lung cancer (NSCLC) cells, treatment with PG dose-dependently diminished HO-1 protein levels without changing its mRNA levels and consequently decreased HO-1 activity.	Propyl Gallate	66-68	heme oxygenase 1	Homo sapiens	177-181
27375080-5	2016	PG also significantly enhanced the sensitivity of NSCLC cells to cisplatin-induced apoptosis, and this effect was attenuated by overexpression of HO-1.	Propyl Gallate	0-2	heme oxygenase 1	Homo sapiens	146-150
27375080-5	2016	PG also significantly enhanced the sensitivity of NSCLC cells to cisplatin-induced apoptosis, and this effect was attenuated by overexpression of HO-1.	Cisplatin	65-74	heme oxygenase 1	Homo sapiens	146-150
27375080-6	2016	Mechanistically, PG exerted its chemosensitization effect by down-regulating HO-1 protein expression through a TRC8 (translocation in renal carcinoma, chromosome 8)-mediated ubiquitin-proteasome pathway.	Propyl Gallate	17-19	heme oxygenase 1	Homo sapiens	77-81
27375080-7	2016	Collectively, our data provide the potential application of PG in combination chemotherapy to enhance drug sensitivity in lung cancer by targeting HO-1.	Propyl Gallate	60-62	heme oxygenase 1	Homo sapiens	147-151
27822409-13	2016	NAC</protein-id> (ROS scavenging agent) could inhibit the migration and invasion through reversing EMT and decrease the expression of HO-1.	Reactive Oxygen Species	18-21	heme oxygenase 1	Homo sapiens	134-138
27822409-14	2016	What"s more, Znpp (HO-1 inhibitor) impaired the migration and invasion through reversing EMT.	zinc protoporphyrin	13-17	heme oxygenase 1	Homo sapiens	19-23
27822409-15	2016	In conclusion, our results suggest that autophagy inhibition may promote EMT through ROS/HO-1 pathway in ovarian cancer cells.	Reactive Oxygen Species	85-88	heme oxygenase 1	Homo sapiens	89-93
27698370-4	2016	Both inhibition of Na/K-ATPase oxidant amplification with pNaKtide and induction of heme oxygenase-1 (HO-1) with cobalt protoporphyrin (CoPP) markedly attenuated the development of phenotypical features of uremic cardiomyopathy.	cobaltiprotoporphyrin	113-134	heme oxygenase 1	Homo sapiens	84-100
27698370-4	2016	Both inhibition of Na/K-ATPase oxidant amplification with pNaKtide and induction of heme oxygenase-1 (HO-1) with cobalt protoporphyrin (CoPP) markedly attenuated the development of phenotypical features of uremic cardiomyopathy.	cobaltiprotoporphyrin	136-140	heme oxygenase 1	Homo sapiens	84-100
27488535-5	2016	Inhibition of HO-1 by tin protoporphyrin (SnPP) or siRNA downregulated Pax3/7-FoxO1 target genes and induced a myogenic program in RMS.	tin protoporphyrin IX	22-40	heme oxygenase 1	Homo sapiens	14-18
27488535-5	2016	Inhibition of HO-1 by tin protoporphyrin (SnPP) or siRNA downregulated Pax3/7-FoxO1 target genes and induced a myogenic program in RMS.	S-Nitroso-N-propionyl-D,L-penicillamine	42-46	heme oxygenase 1	Homo sapiens	14-18
27488535-6	2016	These effects were not mediated by altered myoD expression; instead, cells with elevated HO-1 produced less reactive oxygen species, resulting in nuclear localization of HDAC4 and miR-206 repression.	Reactive Oxygen Species	108-131	heme oxygenase 1	Homo sapiens	89-93
27598034-4	2016	Pretreatment with zinc protoporphyrin IX, a pharmacological inhibitor of heme oxygenase-1 (HO-1), as well as siRNA knockdown of HO-1 gene in MCF-7 cells attenuated 15d-PGJ2-mediated HIF-1alpha accumulation.	zinc protoporphyrin	18-40	heme oxygenase 1	Homo sapiens	73-89
27598034-4	2016	Pretreatment with zinc protoporphyrin IX, a pharmacological inhibitor of heme oxygenase-1 (HO-1), as well as siRNA knockdown of HO-1 gene in MCF-7 cells attenuated 15d-PGJ2-mediated HIF-1alpha accumulation.	15-deoxy-delta(12,14)-prostaglandin J2	164-172	heme oxygenase 1	Homo sapiens	91-95
27598034-4	2016	Pretreatment with zinc protoporphyrin IX, a pharmacological inhibitor of heme oxygenase-1 (HO-1), as well as siRNA knockdown of HO-1 gene in MCF-7 cells attenuated 15d-PGJ2-mediated HIF-1alpha accumulation.	15-deoxy-delta(12,14)-prostaglandin J2	164-172	heme oxygenase 1	Homo sapiens	128-132
27598034-5	2016	15d-PGJ2 treatment increased intracellular production of reactive oxygen species (ROS), which was mediated by HO-1 induction.	15-deoxy-delta(12,14)-prostaglandin J2	0-8	heme oxygenase 1	Homo sapiens	110-114
27598034-5	2016	15d-PGJ2 treatment increased intracellular production of reactive oxygen species (ROS), which was mediated by HO-1 induction.	Reactive Oxygen Species	57-80	heme oxygenase 1	Homo sapiens	110-114
27598034-5	2016	15d-PGJ2 treatment increased intracellular production of reactive oxygen species (ROS), which was mediated by HO-1 induction.	Reactive Oxygen Species	82-85	heme oxygenase 1	Homo sapiens	110-114
27598034-6	2016	Preincubation of MCF-7 cells with trolox, a water-soluble form of vitamin E, attenuated 15d-PGJ2-induced HIF-1alpha expression although HO-1 expression was unchanged.	6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid	34-40	heme oxygenase 1	Homo sapiens	136-140
27598034-7	2016	This finding suggests that ROS accumulated as a consequence of HO-1 up-regulation can enhance HIF-1alpha expression in MCF-7 cells treated with 15d-PGJ2.	Reactive Oxygen Species	27-30	heme oxygenase 1	Homo sapiens	63-67
27598034-7	2016	This finding suggests that ROS accumulated as a consequence of HO-1 up-regulation can enhance HIF-1alpha expression in MCF-7 cells treated with 15d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	144-152	heme oxygenase 1	Homo sapiens	63-67
27604527-1	2016	Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin.	Heme	96-100	heme oxygenase 1	Homo sapiens	46-51
27573874-0	2016	Resveratrol pretreatment attenuates injury and promotes proliferation of neural stem cells following oxygen-glucose deprivation/reoxygenation by upregulating the expression of Nrf2, HO-1 and NQO1 in vitro.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	182-186
27573874-10	2016	These findings suggested that resveratrol attenuated injury and promoted proliferation of the NSCs, at least in part, by upregulating the expression of Nrf2, HO-1 and NQO1 following OGD/R injury in vitro.	Resveratrol	30-41	heme oxygenase 1	Homo sapiens	158-162
27428762-5	2016	On the other hand, Mycophenolate mofetil induced GPX1 mRNA, although it suppressed mRNA level of UGT1A4/1A9/2B7/2B10, GSTA1/O1/T1, GSR and HMOX1 in HepG2 cells.	Mycophenolic Acid	19-40	heme oxygenase 1	Homo sapiens	139-144
27222475-1	2016	The nuclear factor erythroid-derived two-like 2-antioxidant response element (Nrf2-ARE) pathway and its downstream antioxidant enzyme heme oxygenase-1 (HMOX1 or HO-1) play essential roles in H2 O2 -induced oxidative damage in human melanocytes.	Hydrogen Peroxide	191-196	heme oxygenase 1	Homo sapiens	134-150
27222475-1	2016	The nuclear factor erythroid-derived two-like 2-antioxidant response element (Nrf2-ARE) pathway and its downstream antioxidant enzyme heme oxygenase-1 (HMOX1 or HO-1) play essential roles in H2 O2 -induced oxidative damage in human melanocytes.	Hydrogen Peroxide	191-196	heme oxygenase 1	Homo sapiens	152-157
27222475-1	2016	The nuclear factor erythroid-derived two-like 2-antioxidant response element (Nrf2-ARE) pathway and its downstream antioxidant enzyme heme oxygenase-1 (HMOX1 or HO-1) play essential roles in H2 O2 -induced oxidative damage in human melanocytes.	Hydrogen Peroxide	191-196	heme oxygenase 1	Homo sapiens	161-165
27604527-1	2016	Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin.	Carbon Monoxide	104-119	heme oxygenase 1	Homo sapiens	46-51
27604527-1	2016	Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin.	Carbon Monoxide	121-123	heme oxygenase 1	Homo sapiens	46-51
27604527-1	2016	Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin.	Iron	126-138	heme oxygenase 1	Homo sapiens	46-51
27604527-1	2016	Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin.	Biliverdine	144-154	heme oxygenase 1	Homo sapiens	46-51
27454768-6	2016	Furthermore, quercetin induced activation of the nuclear factor erythroid 2-related factor 2 (Nrf2) and subsequent mRNA and protein expression of the antioxidant enzymes, heme oxygenase-1 (HO-1), NAD(P)H dehydrogenase, quinone 1, and glutamate-cysteine ligase.	Quercetin	13-22	heme oxygenase 1	Homo sapiens	171-187
27604527-1	2016	Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin.	Bilirubin	205-214	heme oxygenase 1	Homo sapiens	46-51
27685634-13	2016	The functional link between HO-1 activity and bile acid toxicity was established in RIP3-deficient primary hepatocytes.	Bile Acids and Salts	46-55	heme oxygenase 1	Homo sapiens	28-32
27538638-0	2016	Inhibition of beta-amyloid-induced neurotoxicity by pinocembrin through Nrf2/HO-1 pathway in SH-SY5Y cells.	pinocembrin	52-63	heme oxygenase 1	Homo sapiens	77-81
27542238-5	2016	In addition, treatment with ANM eliminated HG-induced reactive oxygen species (ROS) through the induction of anti-oxidant genes, HO-1 and NQO-1 via transcriptional activation of Nrf2.	Reactive Oxygen Species	79-82	heme oxygenase 1	Homo sapiens	129-133
27609268-0	2016	Depression-like behaviors and heme oxygenase-1 are regulated by Lycopene in lipopolysaccharide-induced neuroinflammation.	Lycopene	64-72	heme oxygenase 1	Homo sapiens	30-46
27538638-8	2016	PCB treatment also resulted in an increase in Nrf2 protein levels and subsequent induction of heme oxygenase-1(HO-1) expression in SH-SY5Y cells.	pinocembrin	0-3	heme oxygenase 1	Homo sapiens	94-115
27609268-10	2016	Furthermore, lycopene decreased LPS-induced expression of IL-1beta and HO-1 in the hippocampus together with decreasing level of IL-6 and TNF-alpha in the plasma.	Lycopene	13-21	heme oxygenase 1	Homo sapiens	71-75
27609268-11	2016	Taken together, these results suggest that lycopene can attenuate LPS-induced inflammation and depression-like behaviors, which may be involved in regulating HO-1 in the hippocampus.	Lycopene	43-51	heme oxygenase 1	Homo sapiens	158-162
27538638-9	2016	RNA interference-mediated knockdown of Nrf2 expression suppressed the PCB-induced HO-1 expression.	pinocembrin	70-73	heme oxygenase 1	Homo sapiens	82-86
27538638-10	2016	Notably, we found that the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) markedly diminished the neuroprotective effect of PCB against Abeta-mediated neurotoxicity.	zinc protoporphyrin	42-64	heme oxygenase 1	Homo sapiens	27-31
27538638-10	2016	Notably, we found that the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) markedly diminished the neuroprotective effect of PCB against Abeta-mediated neurotoxicity.	zinc protoporphyrin	66-70	heme oxygenase 1	Homo sapiens	27-31
27538638-10	2016	Notably, we found that the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) markedly diminished the neuroprotective effect of PCB against Abeta-mediated neurotoxicity.	pinocembrin	122-125	heme oxygenase 1	Homo sapiens	27-31
27538638-11	2016	Taken together, these results indicated that PCB protects SH-SY5Y cells from Abeta25-35-induced neurotoxicity through activation of Nrf2/HO-1 pathways.	pinocembrin	45-48	heme oxygenase 1	Homo sapiens	137-141
26404762-7	2016	TMP inhibited arsenic-induced activations of JNK, p38 MAPK, ERK, AP-1 and Nrf2 and block HO-1 protein expression.	Arsenic	14-21	heme oxygenase 1	Homo sapiens	89-93
26404762-11	2016	In summary, our study highlighted a role of HO-1 in the protection against arsenic-induced cytotoxicity downstream from the primary targets of TMP and further indicated that TMP may be used as a potential therapeutic agent in the treatment of arsenic-induced nephrotoxicity.	Arsenic	75-82	heme oxygenase 1	Homo sapiens	44-48
26404762-0	2016	2,3,5,6-Tetramethylpyrazine (TMP) down-regulated arsenic-induced heme oxygenase-1 and ARS2 expression by inhibiting Nrf2, NF-kappaB, AP-1 and MAPK pathways in human proximal tubular cells.	tetramethylpyrazine	0-27	heme oxygenase 1	Homo sapiens	65-81
26404762-11	2016	In summary, our study highlighted a role of HO-1 in the protection against arsenic-induced cytotoxicity downstream from the primary targets of TMP and further indicated that TMP may be used as a potential therapeutic agent in the treatment of arsenic-induced nephrotoxicity.	tetramethylpyrazine	174-177	heme oxygenase 1	Homo sapiens	44-48
26404762-0	2016	2,3,5,6-Tetramethylpyrazine (TMP) down-regulated arsenic-induced heme oxygenase-1 and ARS2 expression by inhibiting Nrf2, NF-kappaB, AP-1 and MAPK pathways in human proximal tubular cells.	tetramethylpyrazine	29-32	heme oxygenase 1	Homo sapiens	65-81
26404762-0	2016	2,3,5,6-Tetramethylpyrazine (TMP) down-regulated arsenic-induced heme oxygenase-1 and ARS2 expression by inhibiting Nrf2, NF-kappaB, AP-1 and MAPK pathways in human proximal tubular cells.	Arsenic	49-56	heme oxygenase 1	Homo sapiens	65-81
26404762-11	2016	In summary, our study highlighted a role of HO-1 in the protection against arsenic-induced cytotoxicity downstream from the primary targets of TMP and further indicated that TMP may be used as a potential therapeutic agent in the treatment of arsenic-induced nephrotoxicity.	Arsenic	243-250	heme oxygenase 1	Homo sapiens	44-48
26404762-2	2016	The present study demonstrated that arsenic exposure resulted in protein and enzymatic induction of heme oxygenase-1 (HO-1) in dose- and time-dependent manners in HK-2 cells.	Arsenic	36-43	heme oxygenase 1	Homo sapiens	100-116
26938875-2	2016	Haem-oxygenase-1 (HO-1) is an enzyme responsible for the degradation of haem that can suppress inflammation, through the production of carbon monoxide (CO).	Carbon Monoxide	135-150	heme oxygenase 1	Homo sapiens	0-16
26404762-2	2016	The present study demonstrated that arsenic exposure resulted in protein and enzymatic induction of heme oxygenase-1 (HO-1) in dose- and time-dependent manners in HK-2 cells.	Arsenic	36-43	heme oxygenase 1	Homo sapiens	118-122
26404762-3	2016	Blocking HO-1 enzymatic activity by zinc protoporphyrin (ZnPP) augmented arsenic-induced apoptosis, ROS production and mitochondrial dysfunction, suggesting a critical role for HO-1 as a renal protectant in this procession.	zinc protoporphyrin	36-55	heme oxygenase 1	Homo sapiens	9-13
26404762-3	2016	Blocking HO-1 enzymatic activity by zinc protoporphyrin (ZnPP) augmented arsenic-induced apoptosis, ROS production and mitochondrial dysfunction, suggesting a critical role for HO-1 as a renal protectant in this procession.	zinc protoporphyrin	57-61	heme oxygenase 1	Homo sapiens	9-13
26404762-3	2016	Blocking HO-1 enzymatic activity by zinc protoporphyrin (ZnPP) augmented arsenic-induced apoptosis, ROS production and mitochondrial dysfunction, suggesting a critical role for HO-1 as a renal protectant in this procession.	zinc protoporphyrin	57-61	heme oxygenase 1	Homo sapiens	177-181
26404762-3	2016	Blocking HO-1 enzymatic activity by zinc protoporphyrin (ZnPP) augmented arsenic-induced apoptosis, ROS production and mitochondrial dysfunction, suggesting a critical role for HO-1 as a renal protectant in this procession.	Arsenic	73-80	heme oxygenase 1	Homo sapiens	9-13
26404762-3	2016	Blocking HO-1 enzymatic activity by zinc protoporphyrin (ZnPP) augmented arsenic-induced apoptosis, ROS production and mitochondrial dysfunction, suggesting a critical role for HO-1 as a renal protectant in this procession.	Arsenic	73-80	heme oxygenase 1	Homo sapiens	177-181
26404762-3	2016	Blocking HO-1 enzymatic activity by zinc protoporphyrin (ZnPP) augmented arsenic-induced apoptosis, ROS production and mitochondrial dysfunction, suggesting a critical role for HO-1 as a renal protectant in this procession.	ros	100-103	heme oxygenase 1	Homo sapiens	9-13
26404762-4	2016	On the other hand, TMP, upstream of HO-1, inhibited arsenic-induced ROS production and ROS-dependent HO-1 expression.	tetramethylpyrazine	19-22	heme oxygenase 1	Homo sapiens	36-40
26404762-4	2016	On the other hand, TMP, upstream of HO-1, inhibited arsenic-induced ROS production and ROS-dependent HO-1 expression.	tetramethylpyrazine	19-22	heme oxygenase 1	Homo sapiens	101-105
26404762-4	2016	On the other hand, TMP, upstream of HO-1, inhibited arsenic-induced ROS production and ROS-dependent HO-1 expression.	Arsenic	52-59	heme oxygenase 1	Homo sapiens	36-40
26404762-4	2016	On the other hand, TMP, upstream of HO-1, inhibited arsenic-induced ROS production and ROS-dependent HO-1 expression.	ros	68-71	heme oxygenase 1	Homo sapiens	36-40
26404762-4	2016	On the other hand, TMP, upstream of HO-1, inhibited arsenic-induced ROS production and ROS-dependent HO-1 expression.	ros	87-90	heme oxygenase 1	Homo sapiens	36-40
26404762-4	2016	On the other hand, TMP, upstream of HO-1, inhibited arsenic-induced ROS production and ROS-dependent HO-1 expression.	ros	87-90	heme oxygenase 1	Homo sapiens	101-105
26404762-6	2016	Our results revealed that the regulation of arsenic-induced HO-1 expression was performed through multiple ROS-dependent signal pathways and the corresponding transcription factors, including p38 MAPK and JNK (but not ERK), AP-1, Nrf2 and NF-kappaB.	Arsenic	44-51	heme oxygenase 1	Homo sapiens	60-64
26404762-6	2016	Our results revealed that the regulation of arsenic-induced HO-1 expression was performed through multiple ROS-dependent signal pathways and the corresponding transcription factors, including p38 MAPK and JNK (but not ERK), AP-1, Nrf2 and NF-kappaB.	ros	107-110	heme oxygenase 1	Homo sapiens	60-64
26404762-7	2016	TMP inhibited arsenic-induced activations of JNK, p38 MAPK, ERK, AP-1 and Nrf2 and block HO-1 protein expression.	tetramethylpyrazine	0-3	heme oxygenase 1	Homo sapiens	89-93
27375190-0	2016	Curcumin attenuates quinocetone induced apoptosis and inflammation via the opposite modulation of Nrf2/HO-1 and NF-kB pathway in human hepatocyte L02 cells.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	103-107
27375190-6	2016	Meanwhile, curcumin pretreatment markedly down-regulated the expression of nuclear factor -kB (NF-kB) and iNOS mRNAs, but up-regulated the expressions of Nrf2 and HO-1 mRNAs, compared to the QCT alone group.	Curcumin	11-19	heme oxygenase 1	Homo sapiens	163-167
27375190-7	2016	Zinc protoporphyrin IX, a HO-1 inhibitor, markedly partly abolished the cytoprotective effect of curcumin against QCT-induced caspase activation, NF-kB mRNA expression.	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	26-30
27375190-7	2016	Zinc protoporphyrin IX, a HO-1 inhibitor, markedly partly abolished the cytoprotective effect of curcumin against QCT-induced caspase activation, NF-kB mRNA expression.	Curcumin	97-105	heme oxygenase 1	Homo sapiens	26-30
27373419-7	2016	However, resveratrol prevented these effects, protecting hippocampal astrocytes against azide-induced cytotoxicity through the heme-oxygenase-1 (HO-1) pathway and inhibiting p38 mitogen-activated protein kinase (p38 MAPK) and nuclear factor kappa B (NFkappaB) activation.	Resveratrol	9-20	heme oxygenase 1	Homo sapiens	127-143
27373419-7	2016	However, resveratrol prevented these effects, protecting hippocampal astrocytes against azide-induced cytotoxicity through the heme-oxygenase-1 (HO-1) pathway and inhibiting p38 mitogen-activated protein kinase (p38 MAPK) and nuclear factor kappa B (NFkappaB) activation.	Azides	88-93	heme oxygenase 1	Homo sapiens	127-143
27146412-0	2016	Resveratrol Protects Oxidative Stress-Induced Intestinal Epithelial Barrier Dysfunction by Upregulating Heme Oxygenase-1 Expression.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	104-120
27146412-9	2016	Moreover, Res which protected Caco-2 cells from H2O2-induced oxidative damage clearly reduced malondialdehyde level and intracellular reactive oxygen species accumulation, but increased the expression levels of superoxide dismutase and heme oxygenase-1 (HO-1).	Hydrogen Peroxide	48-52	heme oxygenase 1	Homo sapiens	236-252
27146412-9	2016	Moreover, Res which protected Caco-2 cells from H2O2-induced oxidative damage clearly reduced malondialdehyde level and intracellular reactive oxygen species accumulation, but increased the expression levels of superoxide dismutase and heme oxygenase-1 (HO-1).	Hydrogen Peroxide	48-52	heme oxygenase 1	Homo sapiens	254-258
27146412-11	2016	Interestingly, these effects of Res were abolished by the HO-1 inhibitor zinc protoporphyrin or knockdown of HO-1 by siRNA.	zinc protoporphyrin	73-92	heme oxygenase 1	Homo sapiens	58-62
27375190-8	2016	These results indicate that curcumin could effectively inhibit QCT induced apoptosis and inflammatory response in L02 cells, which may involve the activation of Nrf2/HO-1 and inhibition of NF-kB pathway.	Curcumin	28-36	heme oxygenase 1	Homo sapiens	166-170
26938875-2	2016	Haem-oxygenase-1 (HO-1) is an enzyme responsible for the degradation of haem that can suppress inflammation, through the production of carbon monoxide (CO).	Carbon Monoxide	135-150	heme oxygenase 1	Homo sapiens	18-22
26938875-2	2016	Haem-oxygenase-1 (HO-1) is an enzyme responsible for the degradation of haem that can suppress inflammation, through the production of carbon monoxide (CO).	Carbon Monoxide	152-154	heme oxygenase 1	Homo sapiens	0-16
26938875-2	2016	Haem-oxygenase-1 (HO-1) is an enzyme responsible for the degradation of haem that can suppress inflammation, through the production of carbon monoxide (CO).	Carbon Monoxide	152-154	heme oxygenase 1	Homo sapiens	18-22
27722139-0	2016	Fraxetin Induces Heme Oxygenase-1 Expression by Activation of Akt/Nrf2 or AMP-activated Protein Kinase alpha/Nrf2 Pathway in HaCaT Cells.	fraxetin	0-8	heme oxygenase 1	Homo sapiens	17-33
27722139-10	2016	Pharmacological inhibition of Akt and AMPKalpha abrogated fraxetin-induced expression of HO-1 and nuclear localization of Nrf2.	ampkalpha	38-47	heme oxygenase 1	Homo sapiens	89-93
27722139-10	2016	Pharmacological inhibition of Akt and AMPKalpha abrogated fraxetin-induced expression of HO-1 and nuclear localization of Nrf2.	fraxetin	58-66	heme oxygenase 1	Homo sapiens	89-93
27722139-12	2016	CONCLUSIONS: Fraxetin induces HO-1 expression through activation of Akt/Nrf2 or AMPKalpha/Nrf2 pathway in HaCaT cells.	fraxetin	13-21	heme oxygenase 1	Homo sapiens	30-34
27490825-6	2016	X-ray crystallographic structures of human HO1 H25R with bound heme and additional functional studies suggest that HO mutant activity inside these cells does not involve heme ligation by a proximal amino acid.	Heme	63-67	heme oxygenase 1	Homo sapiens	43-46
27354356-1	2016	Epoxygenase-dependent metabolites of arachidonc acid, EETs and the heme-oxygenase (HO)-1/carbon monoxide/bilverdin system share similarities in their activity and mediators.	Carbon Monoxide	89-104	heme oxygenase 1	Homo sapiens	67-88
27354356-1	2016	Epoxygenase-dependent metabolites of arachidonc acid, EETs and the heme-oxygenase (HO)-1/carbon monoxide/bilverdin system share similarities in their activity and mediators.	bilverdin	105-114	heme oxygenase 1	Homo sapiens	67-88
27447561-0	2016	Targeting of heme oxygenase-1 attenuates the negative impact of Ikaros isoform 6 in adult BCR-ABL1-positive B-ALL.	ikaros	64-70	heme oxygenase 1	Homo sapiens	13-29
27553905-5	2016	Western blot analysis illustrated that sulforaphane increased the expression of nuclear factor (erythroid-derived 2)-like 2 (Nrf2), heme oxygenase-1 (HO-1), and NAD(P)H quinone oxidoreductase (NQO1), the latter two of which are anti-oxidative enzymes.	sulforaphane	39-51	heme oxygenase 1	Homo sapiens	132-148
27553905-5	2016	Western blot analysis illustrated that sulforaphane increased the expression of nuclear factor (erythroid-derived 2)-like 2 (Nrf2), heme oxygenase-1 (HO-1), and NAD(P)H quinone oxidoreductase (NQO1), the latter two of which are anti-oxidative enzymes.	sulforaphane	39-51	heme oxygenase 1	Homo sapiens	150-154
27183873-5	2016	Using the heme oxygenase-1 (HO-1) as a model of phase II enzyme gene, we found that methylation of Nrf2 by PRMT1 led to a moderate increase of its DNA-binding activity and transactivation, which subsequently protected cells against the tBHP-induced glutathione depletion and cell death.	tert-Butylhydroperoxide	236-240	heme oxygenase 1	Homo sapiens	10-26
27642551-0	2016	Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase-1.	Heme	13-17	heme oxygenase 1	Homo sapiens	96-112
27365395-4	2016	Under endoplasmic reticulum stress conditions, induction of CSE and up-regulation of the CBS inhibitor, CO, a product of heme oxygenase-1, flip the operating preference of CSE from cystathionine to cysteine, transiently stimulating H2S production.	Cystathionine	181-194	heme oxygenase 1	Homo sapiens	121-137
27365395-4	2016	Under endoplasmic reticulum stress conditions, induction of CSE and up-regulation of the CBS inhibitor, CO, a product of heme oxygenase-1, flip the operating preference of CSE from cystathionine to cysteine, transiently stimulating H2S production.	Cysteine	198-206	heme oxygenase 1	Homo sapiens	121-137
27365395-4	2016	Under endoplasmic reticulum stress conditions, induction of CSE and up-regulation of the CBS inhibitor, CO, a product of heme oxygenase-1, flip the operating preference of CSE from cystathionine to cysteine, transiently stimulating H2S production.	Hydrogen Sulfide	232-235	heme oxygenase 1	Homo sapiens	121-137
27183873-5	2016	Using the heme oxygenase-1 (HO-1) as a model of phase II enzyme gene, we found that methylation of Nrf2 by PRMT1 led to a moderate increase of its DNA-binding activity and transactivation, which subsequently protected cells against the tBHP-induced glutathione depletion and cell death.	tert-Butylhydroperoxide	236-240	heme oxygenase 1	Homo sapiens	28-32
27183873-5	2016	Using the heme oxygenase-1 (HO-1) as a model of phase II enzyme gene, we found that methylation of Nrf2 by PRMT1 led to a moderate increase of its DNA-binding activity and transactivation, which subsequently protected cells against the tBHP-induced glutathione depletion and cell death.	Glutathione	249-260	heme oxygenase 1	Homo sapiens	10-26
27183873-5	2016	Using the heme oxygenase-1 (HO-1) as a model of phase II enzyme gene, we found that methylation of Nrf2 by PRMT1 led to a moderate increase of its DNA-binding activity and transactivation, which subsequently protected cells against the tBHP-induced glutathione depletion and cell death.	Glutathione	249-260	heme oxygenase 1	Homo sapiens	28-32
27190261-8	2016	These results indicated that the 1R, 1"S-isotetrandrine ameliorated tert-butyl hydroperoxide-induced oxidative damage through upregulation of heme oxygenase-1 expression by the dissociation of Nrf2 from Nrf2-Keap1 complex via extracellular signal-regulated protein kinase and c-Jun NH2-terminal kinase activation and Keap1 inactivation.	tert-Butylhydroperoxide	68-92	heme oxygenase 1	Homo sapiens	142-158
26758041-3	2016	Using double immunofluorescence and sequential iron and immunohistochemistry staining, we showed that marrow iron colocalizes with HO1 and H-ferritin to CD163 + macrophages.	Iron	109-113	heme oxygenase 1	Homo sapiens	131-134
27387768-9	2016	DCA and other dihydroxy-bile acids, but not PDC, induced up-regulation of both BVRalpha and heme oxygenase-1 (HO-1) in liver cells through a FXR independent and BV insensitive mechanism.	Deoxycholic Acid	0-3	heme oxygenase 1	Homo sapiens	92-108
27387768-9	2016	DCA and other dihydroxy-bile acids, but not PDC, induced up-regulation of both BVRalpha and heme oxygenase-1 (HO-1) in liver cells through a FXR independent and BV insensitive mechanism.	dihydroxy-bile acids	14-34	heme oxygenase 1	Homo sapiens	92-108
27494347-6	2016	Protocatechuic aldehyde exhibited a suppressive effect on intracellular reactive oxygen species generation and upregulated heme oxygenase-1 expression in Western blot analysis.	Aldehydes	15-23	heme oxygenase 1	Homo sapiens	123-139
27190261-0	2016	Isotetrandrine ameliorates tert-butyl hydroperoxide-induced oxidative stress through upregulation of heme oxygenase-1 expression.	tetrandrine	0-14	heme oxygenase 1	Homo sapiens	101-117
27190261-0	2016	Isotetrandrine ameliorates tert-butyl hydroperoxide-induced oxidative stress through upregulation of heme oxygenase-1 expression.	tert-Butylhydroperoxide	27-51	heme oxygenase 1	Homo sapiens	101-117
27190261-4	2016	Additionally, our study confirmed that 1R, 1"S-isotetrandrine significantly increased the antioxidant enzyme heme oxygenase-1 expression and nuclear translocation of factor-erythroid 2 p45-related factor 2 (Nrf2).	1r, 1"s-isotetrandrine	39-61	heme oxygenase 1	Homo sapiens	109-125
27190261-8	2016	These results indicated that the 1R, 1"S-isotetrandrine ameliorated tert-butyl hydroperoxide-induced oxidative damage through upregulation of heme oxygenase-1 expression by the dissociation of Nrf2 from Nrf2-Keap1 complex via extracellular signal-regulated protein kinase and c-Jun NH2-terminal kinase activation and Keap1 inactivation.	1r, 1"s-isotetrandrine	33-55	heme oxygenase 1	Homo sapiens	142-158
26758041-1	2016	Iron overload and transfusion dependance portend poor risk in myelodysplastic syndromes (MDS); bone marrow macrophages store iron and limit oxidative damage through heme oxygenase-1 (HO1).	Iron	0-4	heme oxygenase 1	Homo sapiens	183-186
26758041-1	2016	Iron overload and transfusion dependance portend poor risk in myelodysplastic syndromes (MDS); bone marrow macrophages store iron and limit oxidative damage through heme oxygenase-1 (HO1).	Iron	125-129	heme oxygenase 1	Homo sapiens	183-186
26966892-6	2016	Zinc protoporphyrin IX, a specific competitive inhibitor of HO-1, efficiently inhibited RAR whereas hemin, an inducer of HO-1, could mimic priming dose of X-rays to induce RAR.	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	60-64
26795735-6	2016	Inhibition of TrxR using lower auranofin concentrations induced HO-1 protein expression in myeloma cells.	Auranofin	31-40	heme oxygenase 1	Homo sapiens	64-68
27444578-6	2016	Molecular data revealed that Zn-doped TiO2 NPs induced the down-regulation of super oxide dismutase gene while the up-regulation of heme oxygenase-1 gene in MCF-7 cells.	Zinc	29-31	heme oxygenase 1	Homo sapiens	132-148
26795735-8	2016	TrxR was shown to regulate HO-1 via the Nrf2 signaling pathway in a ROS-dependent manner.	ros	68-71	heme oxygenase 1	Homo sapiens	27-31
26795735-9	2016	Increased HO-1 mRNA levels were observed in bortezomib-resistant myeloma cells compared to parent cells and HO-1 inhibition restored the sensitivity to bortezomib in bortezomib-resistant myeloma cells.	Bortezomib	44-54	heme oxygenase 1	Homo sapiens	10-14
26795735-9	2016	Increased HO-1 mRNA levels were observed in bortezomib-resistant myeloma cells compared to parent cells and HO-1 inhibition restored the sensitivity to bortezomib in bortezomib-resistant myeloma cells.	Bortezomib	152-162	heme oxygenase 1	Homo sapiens	108-112
26795735-9	2016	Increased HO-1 mRNA levels were observed in bortezomib-resistant myeloma cells compared to parent cells and HO-1 inhibition restored the sensitivity to bortezomib in bortezomib-resistant myeloma cells.	Bortezomib	152-162	heme oxygenase 1	Homo sapiens	108-112
26795735-10	2016	These findings indicate that concurrent inhibition of HO-1 with either a TrxR inhibitor or with bortezomib would improve therapeutic outcomes in MM patients.	Bortezomib	96-106	heme oxygenase 1	Homo sapiens	54-58
27444578-6	2016	Molecular data revealed that Zn-doped TiO2 NPs induced the down-regulation of super oxide dismutase gene while the up-regulation of heme oxygenase-1 gene in MCF-7 cells.	titanium dioxide	38-42	heme oxygenase 1	Homo sapiens	132-148
26991755-6	2016	Up-regulation of HMOX1, a key regulator of cellular response to ROS, was independent of TP53 mutational status.	Reactive Oxygen Species	64-67	heme oxygenase 1	Homo sapiens	17-22
27477937-11	2016	Upregulation of HO-1 by cobalt-protoporphyrin treatment increased the osteogenic differentiation of pMSCs under hypoxia, while inhibition of HO-1 by Zn-protoporphyrin reduced the osteogenic differentiation of hypoxic pMSCs.	cobaltiprotoporphyrin	24-45	heme oxygenase 1	Homo sapiens	16-20
27477937-11	2016	Upregulation of HO-1 by cobalt-protoporphyrin treatment increased the osteogenic differentiation of pMSCs under hypoxia, while inhibition of HO-1 by Zn-protoporphyrin reduced the osteogenic differentiation of hypoxic pMSCs.	zn-protoporphyrin	149-166	heme oxygenase 1	Homo sapiens	141-145
27323826-0	2016	Simvastatin induces heme oxygenase-1 via NF-E2-related factor 2 (Nrf2) activation through ERK and PI3K/Akt pathway in colon cancer.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	20-36
27323826-6	2016	We evaluated which signal pathway such as ERK or PI3K pathway affect Nrf2 activation and whether simvastatin induces antioxidant enzymes (heme oxygenase-1 (HO-1), NAD(P)H: quinine oxidoreductase 1 (NQO1), gamma-glutamate-cysteine ligase catalytic subunit (GCLC)).	Simvastatin	97-108	heme oxygenase 1	Homo sapiens	138-154
27323826-8	2016	We also demonstrated that simvastatin-induced anti-oxidant enzymes (HO-1, NQO1, and GCLC) in HT-29 and HCT 116 cells.	Simvastatin	26-37	heme oxygenase 1	Homo sapiens	68-72
27323826-9	2016	PI3K/Akt inhibitor (LY294002) and ERK inhibitor (PD98059) suppressed simvastatin-induced Nrf2 and HO-1 expression in both HT-29 and HCT 116 cells.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	20-28	heme oxygenase 1	Homo sapiens	98-102
27323826-9	2016	PI3K/Akt inhibitor (LY294002) and ERK inhibitor (PD98059) suppressed simvastatin-induced Nrf2 and HO-1 expression in both HT-29 and HCT 116 cells.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	49-56	heme oxygenase 1	Homo sapiens	98-102
27323826-9	2016	PI3K/Akt inhibitor (LY294002) and ERK inhibitor (PD98059) suppressed simvastatin-induced Nrf2 and HO-1 expression in both HT-29 and HCT 116 cells.	Simvastatin	69-80	heme oxygenase 1	Homo sapiens	98-102
27381978-7	2016	In the human endothelial Ea.hy926 cell line, we demonstrated that intracellular bilirubin (3-5 pmol mg(-1) protein) could be modulated by either extracellular bilirubin uptake, or by up-regulation of heme oxygenase-1, a cellular enzyme related to endogenous bilirubin synthesis.	Bilirubin	80-89	heme oxygenase 1	Homo sapiens	200-216
26991755-10	2016	In conclusion, ROS induction is important for antileukaemic activities of APR-246 and inhibiting the protective response of the Nrf-2/HMOX1 axis using PI3K inhibitors, enhances the antileukaemic effects.	Reactive Oxygen Species	15-18	heme oxygenase 1	Homo sapiens	134-139
27381601-0	2016	Simvastatin Inhibits Epithelial-to-Mesenchymal Transition Through Induction of HO-1 in Cultured Renal Proximal Tubule Cells.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	79-83
27317992-5	2016	In addition, dioscin markedly up-regulated the expression levels of SIRT1, HO-1, NQO1, GST and GCLM through increasing nuclear translocation of Nrf2 against oxidative stress.	dioscin	13-20	heme oxygenase 1	Homo sapiens	75-79
27107768-0	2016	Rupestonic acid derivative YZH-106 suppresses influenza virus replication by activation of heme oxygenase-1-mediated interferon response.	rupestonic acid	0-15	heme oxygenase 1	Homo sapiens	91-107
27107768-0	2016	Rupestonic acid derivative YZH-106 suppresses influenza virus replication by activation of heme oxygenase-1-mediated interferon response.	YZH-106	27-34	heme oxygenase 1	Homo sapiens	91-107
27107768-6	2016	Mechanistically, YZH-106 induced p38 MAPK and ERK1/2 phosphorylation, which led to the activation of erythroid 2-related factor 2 (Nrf2) that up-regulated heme oxygenase-1 (HO-1) expression in addition to other genes.	YZH-106	17-24	heme oxygenase 1	Homo sapiens	155-171
27107768-6	2016	Mechanistically, YZH-106 induced p38 MAPK and ERK1/2 phosphorylation, which led to the activation of erythroid 2-related factor 2 (Nrf2) that up-regulated heme oxygenase-1 (HO-1) expression in addition to other genes.	YZH-106	17-24	heme oxygenase 1	Homo sapiens	173-177
27107768-8	2016	These results suggest that YZH-106 inhibits IAV by up-regulating HO-1-mediated IFN response.	YZH-106	27-34	heme oxygenase 1	Homo sapiens	65-69
26588813-8	2016	These results were validated by quantitative reverse transcriptase-polymerase chain reaction (RT-PCR) and Western blotting, confirming a concentration-dependent increase in HMOX1 and a decrease in THBS1 expression in ASC following iAs exposure.	4-Iodoacetamidosalicylic acid	231-234	heme oxygenase 1	Homo sapiens	173-178
27381601-1	2016	BACKGROUND/AIM: Studies have shown that simvastatin (SIM) inhibits epithelial-mesenchymal transition (EMT), a key step in fibrosis, and activates the anti-fibrotic heme oxygenase-1 (HO-1) gene in renal proximal tubule cells independent of its lipid-lowering.	Simvastatin	40-51	heme oxygenase 1	Homo sapiens	164-180
27381601-1	2016	BACKGROUND/AIM: Studies have shown that simvastatin (SIM) inhibits epithelial-mesenchymal transition (EMT), a key step in fibrosis, and activates the anti-fibrotic heme oxygenase-1 (HO-1) gene in renal proximal tubule cells independent of its lipid-lowering.	Simvastatin	40-51	heme oxygenase 1	Homo sapiens	182-186
27381601-2	2016	We tested the hypothesis that SIM inhibits EMT via HO-1-dependent suppression of reactive oxygen species (ROS) release.	Reactive Oxygen Species	81-104	heme oxygenase 1	Homo sapiens	51-55
27381601-2	2016	We tested the hypothesis that SIM inhibits EMT via HO-1-dependent suppression of reactive oxygen species (ROS) release.	Reactive Oxygen Species	106-109	heme oxygenase 1	Homo sapiens	51-55
27381601-7	2016	CONCLUSION: SIM, via HO-1, suppresses TGFbeta1-dependent ROS production and, hence, EMT.	Reactive Oxygen Species	57-60	heme oxygenase 1	Homo sapiens	21-25
27151894-11	2016	Expression of some key oxidative stress-responsive genes, such as heme oxygenase-1 and metallothionein-1, was also stimulated by iAs exposure.	4-Iodoacetamidosalicylic acid	129-132	heme oxygenase 1	Homo sapiens	66-82
26969214-0	2016	Aspirin induces Nrf2-mediated transcriptional activation of haem oxygenase-1 in protection of human melanocytes from H2 O2 -induced oxidative stress.	Aspirin	0-7	heme oxygenase 1	Homo sapiens	60-76
26969214-0	2016	Aspirin induces Nrf2-mediated transcriptional activation of haem oxygenase-1 in protection of human melanocytes from H2 O2 -induced oxidative stress.	Hydrogen Peroxide	117-122	heme oxygenase 1	Homo sapiens	60-76
26969214-9	2016	Furthermore, we found ASA dramatically induced NRF2 nuclear translocation, enhanced ARE-luciferase activity, increased both p- NRF2 and total NRF2 levels, and induced the expression of haem oxygenase-1 (HO-1) in human melanocytes.	Aspirin	22-25	heme oxygenase 1	Homo sapiens	185-201
26969214-9	2016	Furthermore, we found ASA dramatically induced NRF2 nuclear translocation, enhanced ARE-luciferase activity, increased both p- NRF2 and total NRF2 levels, and induced the expression of haem oxygenase-1 (HO-1) in human melanocytes.	Aspirin	22-25	heme oxygenase 1	Homo sapiens	203-207
26969214-10	2016	In addition, knockdown of Nrf2 expression or pharmacological inhibition of HO-1 abrogated the protective action of ASA on melanocytes against H2 O2 -induced cytotoxicity and apoptosis.	Aspirin	115-118	heme oxygenase 1	Homo sapiens	75-79
26969214-10	2016	In addition, knockdown of Nrf2 expression or pharmacological inhibition of HO-1 abrogated the protective action of ASA on melanocytes against H2 O2 -induced cytotoxicity and apoptosis.	Hydrogen Peroxide	142-147	heme oxygenase 1	Homo sapiens	75-79
26969214-11	2016	These results suggest that ASA protects human melanocytes against H2 O2 -induced oxidative stress via Nrf2-driven transcriptional activation of HO-1.	Aspirin	27-30	heme oxygenase 1	Homo sapiens	144-148
26969214-11	2016	These results suggest that ASA protects human melanocytes against H2 O2 -induced oxidative stress via Nrf2-driven transcriptional activation of HO-1.	Hydrogen Peroxide	66-71	heme oxygenase 1	Homo sapiens	144-148
27176599-0	2016	In vivo response of heme-oxygenase-1 to metal ions released from metal-on-metal hip prostheses.	Metals	40-45	heme oxygenase 1	Homo sapiens	20-36
27211510-9	2016	Combination of the NF-kappaB inhibitor Bay11-7082 and the lentivirus vector Lenti-siHO-1 significantly decreased HO-1 protein expression and increased apoptosis in OCI-ly10 cells.	3-(4-methylphenylsulfonyl)-2-propenenitrile	39-49	heme oxygenase 1	Homo sapiens	84-88
27087120-8	2016	SHSY5Y cells treated with quercetin also increased the expression of Nrf2 (via a decrease in the levels of Keap1), heme oxygenase-1 (HO-1), and nitric oxide synthase 1 (NOS1), which provide further protection from oxidative stress.	Quercetin	26-35	heme oxygenase 1	Homo sapiens	115-131
27087120-8	2016	SHSY5Y cells treated with quercetin also increased the expression of Nrf2 (via a decrease in the levels of Keap1), heme oxygenase-1 (HO-1), and nitric oxide synthase 1 (NOS1), which provide further protection from oxidative stress.	Quercetin	26-35	heme oxygenase 1	Homo sapiens	133-137
27087120-10	2016	We hypothesize that SUMOylated HIF-1alpha plays a fundamental role in the protection afforded and may underlie some of quercetin"s ability to protect cells from oxygen/glucose deprivation-induced cell death, via an up-regulation of HO-1 and NOS1, which ultimately leads to the induction of pro-life NOS1/protein kinase G signaling.	Quercetin	119-128	heme oxygenase 1	Homo sapiens	232-236
27206323-8	2016	NO2 elicited the greatest HMOX1 response, whereas O3 more greatly induced IL-6, IL-8 and PTGS2 expression.	Nitrogen Dioxide	0-3	heme oxygenase 1	Homo sapiens	26-31
27176599-0	2016	In vivo response of heme-oxygenase-1 to metal ions released from metal-on-metal hip prostheses.	Metals	65-70	heme oxygenase 1	Homo sapiens	20-36
27176599-3	2016	The aim of the present study was to verify whether, in patients with a MoM hip prosthesis, mRNA and protein expression of HMOX-1 was modulated by the presence of metal ions and whether patients without prostheses exhibit a different expression pattern of this enzyme.	Metals	162-167	heme oxygenase 1	Homo sapiens	122-128
28933402-5	2016	Although other chemopreventive mechanisms have been identified, the primary mechanism believed to be responsible for the observed chemoprevention from GSHPs is the induction of antioxidant enzymes, such as NAD(P)H quinone reductase (NQO1), heme oxygenase 1 (HO-1), glutamate-cysteine ligase catalytic subunit (GCLC), and glutathione S transferases (GSTs), through the Keap1-Nrf2-ARE signaling pathway.	gshps	151-156	heme oxygenase 1	Homo sapiens	240-256
27176653-9	2016	A series of increased oxidative stress toxicological responses, including cellular ROS production, heme oxygenase-1 expression, cellular GSH depletion, and mitochondrial dysfunctions, were triggered by faceted TiO2 nanocrystals with progressively increased {001} percentages, demonstrating the toxicological roles of {001} facets.	titanium dioxide	210-214	heme oxygenase 1	Homo sapiens	99-115
28933402-5	2016	Although other chemopreventive mechanisms have been identified, the primary mechanism believed to be responsible for the observed chemoprevention from GSHPs is the induction of antioxidant enzymes, such as NAD(P)H quinone reductase (NQO1), heme oxygenase 1 (HO-1), glutamate-cysteine ligase catalytic subunit (GCLC), and glutathione S transferases (GSTs), through the Keap1-Nrf2-ARE signaling pathway.	gshps	151-156	heme oxygenase 1	Homo sapiens	258-262
27122182-1	2016	Increasing evidence has demonstrated that the activation of heme oxygenase (HO)-1 reduces autophagy stimulated by oxidative stress injury, in which the supraphysiological production of reactive oxygen species (ROS) is detected.	Reactive Oxygen Species	185-208	heme oxygenase 1	Homo sapiens	60-81
27142241-5	2016	Many nuclear processes are influenced by a spatial switch involving the proteins {KPNA2, KPNB1, PCNA, PTMA, SET} and heme/iron proteins HMOX1 and FTH1.	Iron	122-126	heme oxygenase 1	Homo sapiens	136-141
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	Bromine	64-67	heme oxygenase 1	Homo sapiens	106-122
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	Bromine	64-67	heme oxygenase 1	Homo sapiens	124-128
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	Heme	84-88	heme oxygenase 1	Homo sapiens	106-122
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	Heme	84-88	heme oxygenase 1	Homo sapiens	124-128
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	Heme	106-110	heme oxygenase 1	Homo sapiens	124-128
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	bilverdin	162-171	heme oxygenase 1	Homo sapiens	106-122
27244263-4	2016	Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin.	bilverdin	162-171	heme oxygenase 1	Homo sapiens	124-128
27244263-7	2016	However, therapeutic reduction of heme levels, by either scavenging with hemopexin or degradation by HO-1, improved lung function and survival.	Heme	34-38	heme oxygenase 1	Homo sapiens	101-105
27044026-2	2016	The inducible enzyme heme oxygenase-1 (HO-1) protects cells against inflammation and can be induced by electrophilic compounds like the chalcones (1,3-diphenylprop-2-enones) from the class of alpha,beta-unsaturated carbonyl compounds.	Chalcones	136-145	heme oxygenase 1	Homo sapiens	39-43
27044026-2	2016	The inducible enzyme heme oxygenase-1 (HO-1) protects cells against inflammation and can be induced by electrophilic compounds like the chalcones (1,3-diphenylprop-2-enones) from the class of alpha,beta-unsaturated carbonyl compounds.	1,3-diphenylprop-2-enones	147-172	heme oxygenase 1	Homo sapiens	39-43
27044026-2	2016	The inducible enzyme heme oxygenase-1 (HO-1) protects cells against inflammation and can be induced by electrophilic compounds like the chalcones (1,3-diphenylprop-2-enones) from the class of alpha,beta-unsaturated carbonyl compounds.	alpha,beta-unsaturated carbonyl compounds	192-233	heme oxygenase 1	Homo sapiens	39-43
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Heme	170-174	heme oxygenase 1	Homo sapiens	188-192
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Carbon Monoxide	283-298	heme oxygenase 1	Homo sapiens	170-186
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Carbon Monoxide	283-298	heme oxygenase 1	Homo sapiens	188-192
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Biliverdine	300-310	heme oxygenase 1	Homo sapiens	170-186
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Biliverdine	300-310	heme oxygenase 1	Homo sapiens	188-192
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Iron	316-320	heme oxygenase 1	Homo sapiens	170-186
27283533-4	2016	Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron.	Iron	316-320	heme oxygenase 1	Homo sapiens	188-192
26899309-7	2016	We further demonstrated the antioxidant effect of tangeretin by showing that tangeretin inhibited reactive oxygen species production and p47(phox) phosphorylation, while enhancing the expression of heme oxygenase-1 and the DNA binding activity of nuclear factor-erythroid 2-related factor 2 to the antioxidant response element in LPS-stimulated microglia.	tangeretin	50-60	heme oxygenase 1	Homo sapiens	198-214
26899309-7	2016	We further demonstrated the antioxidant effect of tangeretin by showing that tangeretin inhibited reactive oxygen species production and p47(phox) phosphorylation, while enhancing the expression of heme oxygenase-1 and the DNA binding activity of nuclear factor-erythroid 2-related factor 2 to the antioxidant response element in LPS-stimulated microglia.	tangeretin	77-87	heme oxygenase 1	Homo sapiens	198-214
27122182-1	2016	Increasing evidence has demonstrated that the activation of heme oxygenase (HO)-1 reduces autophagy stimulated by oxidative stress injury, in which the supraphysiological production of reactive oxygen species (ROS) is detected.	Reactive Oxygen Species	210-213	heme oxygenase 1	Homo sapiens	60-81
26930712-0	2016	Heme oxygenase-1 nuclear translocation regulates bortezomibinduced cytotoxicity and mediates genomic instability in myeloma cells.	bortezomibinduced	49-66	heme oxygenase 1	Homo sapiens	0-16
27198537-2	2016	After ICH, overproduction of iron associated with induction of heme oxygenase-1 (HO-1) in brain was observed.	Iron	29-33	heme oxygenase 1	Homo sapiens	63-79
27198537-2	2016	After ICH, overproduction of iron associated with induction of heme oxygenase-1 (HO-1) in brain was observed.	Iron	29-33	heme oxygenase 1	Homo sapiens	81-85
27198537-5	2016	The present results showed a higher level of HO-1 expression associated with more severe injury in males compared with females after FC-infusion.	ferrous citrate	133-135	heme oxygenase 1	Homo sapiens	45-49
27198537-11	2016	These findings open up the prospect for male-specific neuroprotection targeting HO-1 suppression for patients suffering from striatal iron overload.	Iron	134-138	heme oxygenase 1	Homo sapiens	80-84
27035791-11	2016	We also demonstrated that Rev-AuNPs induced heme oxygenase-1 (HO-1) expression and that the inhibition of MMP-9 and COX-2 expression and MMP-9 enzymatic activity of Rev-AuNPs were abrogated by siRNA knockdown of HO-1 expression.	rev-aunps	26-35	heme oxygenase 1	Homo sapiens	44-60
27035791-11	2016	We also demonstrated that Rev-AuNPs induced heme oxygenase-1 (HO-1) expression and that the inhibition of MMP-9 and COX-2 expression and MMP-9 enzymatic activity of Rev-AuNPs were abrogated by siRNA knockdown of HO-1 expression.	rev-aunps	26-35	heme oxygenase 1	Homo sapiens	62-66
27035791-11	2016	We also demonstrated that Rev-AuNPs induced heme oxygenase-1 (HO-1) expression and that the inhibition of MMP-9 and COX-2 expression and MMP-9 enzymatic activity of Rev-AuNPs were abrogated by siRNA knockdown of HO-1 expression.	rev-aunps	165-174	heme oxygenase 1	Homo sapiens	44-60
27035791-11	2016	We also demonstrated that Rev-AuNPs induced heme oxygenase-1 (HO-1) expression and that the inhibition of MMP-9 and COX-2 expression and MMP-9 enzymatic activity of Rev-AuNPs were abrogated by siRNA knockdown of HO-1 expression.	rev-aunps	165-174	heme oxygenase 1	Homo sapiens	62-66
27035791-11	2016	We also demonstrated that Rev-AuNPs induced heme oxygenase-1 (HO-1) expression and that the inhibition of MMP-9 and COX-2 expression and MMP-9 enzymatic activity of Rev-AuNPs were abrogated by siRNA knockdown of HO-1 expression.	rev-aunps	165-174	heme oxygenase 1	Homo sapiens	212-216
27035791-12	2016	Our findings revealed that the anti-invasive effects of Rev-AuNPs in response to TPA-stimulation were mediated by the suppression of MMP-9, COX-2, NF-kappaB, AP-1, PI3K/Akt and ERK and/or the activation of HO-1 signaling cascades.	rev-aunps	56-65	heme oxygenase 1	Homo sapiens	206-210
27035791-12	2016	Our findings revealed that the anti-invasive effects of Rev-AuNPs in response to TPA-stimulation were mediated by the suppression of MMP-9, COX-2, NF-kappaB, AP-1, PI3K/Akt and ERK and/or the activation of HO-1 signaling cascades.	Tetradecanoylphorbol Acetate	81-84	heme oxygenase 1	Homo sapiens	206-210
26930712-3	2016	The aim of the present research was to evaluate the impact of HO-1 in MM following bortezomib (BTZ) treatment and how HO-1 is implicated in the mechanisms of chemoresistance.	Bortezomib	83-93	heme oxygenase 1	Homo sapiens	62-66
26930712-3	2016	The aim of the present research was to evaluate the impact of HO-1 in MM following bortezomib (BTZ) treatment and how HO-1 is implicated in the mechanisms of chemoresistance.	Bortezomib	95-98	heme oxygenase 1	Homo sapiens	62-66
26930712-10	2016	In conclusion, our data suggest that BTZ sensitivity depends on HO-1 nuclear compartmentalization and not on its enzymatic activity and this finding may represent an important tool to overcome BTZ chemoresistance in MM patients.	Bortezomib	37-40	heme oxygenase 1	Homo sapiens	64-68
27059143-0	2016	Methionine sulfoxide reductase B3 deficiency stimulates heme oxygenase-1 expression via ROS-dependent and Nrf2 activation pathways.	Reactive Oxygen Species	88-91	heme oxygenase 1	Homo sapiens	56-72
27059143-10	2016	Taken together, these data suggest that MsrB3 attenuates HO-1 induction by inhibiting ROS production, ER stress, and Nrf2 activation.	Reactive Oxygen Species	86-89	heme oxygenase 1	Homo sapiens	57-61
27059143-7	2016	Treatment with N-acetylcysteine as an ROS scavenger reduced augmented HO-1 levels in MsrB3-depleted cells.	Acetylcysteine	15-31	heme oxygenase 1	Homo sapiens	70-74
27059143-7	2016	Treatment with N-acetylcysteine as an ROS scavenger reduced augmented HO-1 levels in MsrB3-depleted cells.	Reactive Oxygen Species	38-41	heme oxygenase 1	Homo sapiens	70-74
27094403-9	2016	The pretreatments with monohydroxy-DMC and monohydroxy-BDMC reduced c-jun and c-fos mRNA expression and p53 tumor suppressor protein expression and increased HO-1 protein expression and glutathione peroxidase (GPx) activity, respectively, compared to cells with direct hydrogen peroxide treatments.	monohydroxy-dmc	23-38	heme oxygenase 1	Homo sapiens	158-162
27005776-7	2016	MT protein was further induced by as little as 0.5muM cadmium, reaching a 6-fold induction at 20muM, whereas for HO-1, a 5muM cadmium concentration was required for initial induction and at 20muM cadmium reached a 15-fold induction.	Cadmium	126-133	heme oxygenase 1	Homo sapiens	113-117
27005776-7	2016	MT protein was further induced by as little as 0.5muM cadmium, reaching a 6-fold induction at 20muM, whereas for HO-1, a 5muM cadmium concentration was required for initial induction and at 20muM cadmium reached a 15-fold induction.	Cadmium	126-133	heme oxygenase 1	Homo sapiens	113-117
27005776-10	2016	In conclusion although cultured PTC, do express CYP proteins, (CYP2E1, CYP3A4, and CYP4F2), Cd-induced cell stress as indicted by induction of HO-1 and MT does not alter expression of these CYP proteins at 48h.	Cadmium	92-94	heme oxygenase 1	Homo sapiens	143-154
27094403-9	2016	The pretreatments with monohydroxy-DMC and monohydroxy-BDMC reduced c-jun and c-fos mRNA expression and p53 tumor suppressor protein expression and increased HO-1 protein expression and glutathione peroxidase (GPx) activity, respectively, compared to cells with direct hydrogen peroxide treatments.	monohydroxy-bdmc	43-59	heme oxygenase 1	Homo sapiens	158-162
26795536-9	2016	In addition, Trp increased the expression of the Nrf2-dependent antioxidant genes NQO1, HO-1 and GCS in hepatocytes both in vitro and in vivo.	Tryptophan	13-16	heme oxygenase 1	Homo sapiens	88-92
27164116-6	2016	Furthermore, DMSP was able to prevent the cytotoxic effects exerted by TDA, including the breakdown of the mitochondrial membrane potential, upregulation of heat shock protein Hsp32 and activation of the extracellular signal-regulated kinases 1/2 (ERK1/2).	dimethylpropiothetin	13-17	heme oxygenase 1	Homo sapiens	176-181
26889770-3	2016	Our results showed that pretreatment with l-carnitine augmented Nrf2 nuclear translocation, DNA binding activity and heme oxygenase-1 (HO-1) expression in H2O2-treated HL7702 cells, although l-carnitine treatment alone had no effect on them.	Carnitine	42-53	heme oxygenase 1	Homo sapiens	117-133
26889770-3	2016	Our results showed that pretreatment with l-carnitine augmented Nrf2 nuclear translocation, DNA binding activity and heme oxygenase-1 (HO-1) expression in H2O2-treated HL7702 cells, although l-carnitine treatment alone had no effect on them.	Carnitine	42-53	heme oxygenase 1	Homo sapiens	135-139
26889770-4	2016	Analysis using Nrf2 siRNA demonstrated that Nrf2 activation was involved in l-carnitine-induced HO-1 expression.	Carnitine	76-87	heme oxygenase 1	Homo sapiens	96-100
26889770-8	2016	Moreover, our finding demonstrated that the induction of Nrf2 translocation and HO-1 expression by l-carnitine directly correlated with the Akt pathway because Akt inhibitor showed inhibitory effects on the Nrf2 translocation and HO-1 expression.	Carnitine	99-110	heme oxygenase 1	Homo sapiens	80-84
26889770-8	2016	Moreover, our finding demonstrated that the induction of Nrf2 translocation and HO-1 expression by l-carnitine directly correlated with the Akt pathway because Akt inhibitor showed inhibitory effects on the Nrf2 translocation and HO-1 expression.	Carnitine	99-110	heme oxygenase 1	Homo sapiens	230-234
26889770-3	2016	Our results showed that pretreatment with l-carnitine augmented Nrf2 nuclear translocation, DNA binding activity and heme oxygenase-1 (HO-1) expression in H2O2-treated HL7702 cells, although l-carnitine treatment alone had no effect on them.	Hydrogen Peroxide	155-159	heme oxygenase 1	Homo sapiens	117-133
26889770-3	2016	Our results showed that pretreatment with l-carnitine augmented Nrf2 nuclear translocation, DNA binding activity and heme oxygenase-1 (HO-1) expression in H2O2-treated HL7702 cells, although l-carnitine treatment alone had no effect on them.	Hydrogen Peroxide	155-159	heme oxygenase 1	Homo sapiens	135-139
26878775-4	2016	ECG attenuated lipopolysaccharide (LPS)-induced inflammatory mediator expression and intracellular reactive oxygen species (ROS) generation through the induction of Nrf2/antioxidant response element (ARE)-driven glutathione (GSH) and hemeoxygenase-1 (HO-1) levels, interference with NF-kappaB and Nfr2/ARE transcriptional activities, and suppression of the MAPKs (JNK1/2 and p38) and PI3K/Akt signaling pathways.	epicatechin gallate	0-3	heme oxygenase 1	Homo sapiens	234-255
26992777-0	2016	Heme oxygenase-1 (HO-1) protects human lens epithelial cells (SRA01/04) against hydrogen peroxide (H2O2)-induced oxidative stress and apoptosis.	Hydrogen Peroxide	80-97	heme oxygenase 1	Homo sapiens	0-16
26992777-0	2016	Heme oxygenase-1 (HO-1) protects human lens epithelial cells (SRA01/04) against hydrogen peroxide (H2O2)-induced oxidative stress and apoptosis.	Hydrogen Peroxide	80-97	heme oxygenase 1	Homo sapiens	18-22
26992777-0	2016	Heme oxygenase-1 (HO-1) protects human lens epithelial cells (SRA01/04) against hydrogen peroxide (H2O2)-induced oxidative stress and apoptosis.	Hydrogen Peroxide	99-103	heme oxygenase 1	Homo sapiens	0-16
26992777-0	2016	Heme oxygenase-1 (HO-1) protects human lens epithelial cells (SRA01/04) against hydrogen peroxide (H2O2)-induced oxidative stress and apoptosis.	Hydrogen Peroxide	99-103	heme oxygenase 1	Homo sapiens	18-22
26992777-1	2016	OBJECTIVES: This study aimed to investigate the protective role of heme oxygenase-1 (HO-1) in H2O2-induced oxidative stress and apoptosis in human lens epithelial cells (hLEC; SRA01/04).	Hydrogen Peroxide	94-98	heme oxygenase 1	Homo sapiens	67-83
26992777-1	2016	OBJECTIVES: This study aimed to investigate the protective role of heme oxygenase-1 (HO-1) in H2O2-induced oxidative stress and apoptosis in human lens epithelial cells (hLEC; SRA01/04).	Hydrogen Peroxide	94-98	heme oxygenase 1	Homo sapiens	85-89
26992777-12	2016	RESULTS: HO-1 significantly restored the cell viability under H2O2 injury via reducing the generation of ROS and increasing the levels of SOD and GSH activity.	Hydrogen Peroxide	62-66	heme oxygenase 1	Homo sapiens	9-13
26992777-12	2016	RESULTS: HO-1 significantly restored the cell viability under H2O2 injury via reducing the generation of ROS and increasing the levels of SOD and GSH activity.	Reactive Oxygen Species	105-108	heme oxygenase 1	Homo sapiens	9-13
26992777-12	2016	RESULTS: HO-1 significantly restored the cell viability under H2O2 injury via reducing the generation of ROS and increasing the levels of SOD and GSH activity.	Glutathione	146-149	heme oxygenase 1	Homo sapiens	9-13
26968795-0	2016	Heme oxygenase-1-derived bilirubin counteracts HIV protease inhibitor-mediated endothelial cell dysfunction.	Bilirubin	25-34	heme oxygenase 1	Homo sapiens	0-16
26992777-13	2016	Moreover, HO-1 also inhibited H2O2-induced caspase-8 and caspase-3 proteins, thus significantly reducing the apoptosis of SRA01/04.	Hydrogen Peroxide	30-34	heme oxygenase 1	Homo sapiens	10-14
26878775-4	2016	ECG attenuated lipopolysaccharide (LPS)-induced inflammatory mediator expression and intracellular reactive oxygen species (ROS) generation through the induction of Nrf2/antioxidant response element (ARE)-driven glutathione (GSH) and hemeoxygenase-1 (HO-1) levels, interference with NF-kappaB and Nfr2/ARE transcriptional activities, and suppression of the MAPKs (JNK1/2 and p38) and PI3K/Akt signaling pathways.	Glutathione	212-223	heme oxygenase 1	Homo sapiens	234-255
26992777-15	2016	CONCLUSIONS: These findings suggested that HO-1 protects human lens epithelial cells from H2O2-induced oxidant stress by upregulating antioxidant enzyme activity, reducing ROS generation, and thus inhibiting caspase family-dependent apoptosis.	Hydrogen Peroxide	90-94	heme oxygenase 1	Homo sapiens	43-47
26992777-15	2016	CONCLUSIONS: These findings suggested that HO-1 protects human lens epithelial cells from H2O2-induced oxidant stress by upregulating antioxidant enzyme activity, reducing ROS generation, and thus inhibiting caspase family-dependent apoptosis.	Reactive Oxygen Species	172-175	heme oxygenase 1	Homo sapiens	43-47
26968795-4	2016	We found that three distinct PIs, including ritonavir, atazanavir, and lopinavir, stimulated the expression of HO-1 protein and mRNA.	Ritonavir	44-53	heme oxygenase 1	Homo sapiens	111-115
26968795-4	2016	We found that three distinct PIs, including ritonavir, atazanavir, and lopinavir, stimulated the expression of HO-1 protein and mRNA.	Atazanavir Sulfate	55-65	heme oxygenase 1	Homo sapiens	111-115
27097841-6	2016	For neurons, the HO-1 activator cobalt protoporphyrin IX (CoPPIX) exerted protective effects against MPP(+) or alpha-synuclein during moderate HO-1 upregulation, but it aggravated damage at the peak of the HO-1 response.	cobaltiprotoporphyrin	32-56	heme oxygenase 1	Homo sapiens	143-147
26968795-4	2016	We found that three distinct PIs, including ritonavir, atazanavir, and lopinavir, stimulated the expression of HO-1 protein and mRNA.	Lopinavir	71-80	heme oxygenase 1	Homo sapiens	111-115
26968795-5	2016	The induction of HO-1 was associated with an increase in NF-E2-related factor-2 (Nrf2) activity and reactive oxygen species (ROS).	Reactive Oxygen Species	100-123	heme oxygenase 1	Homo sapiens	17-21
26968795-5	2016	The induction of HO-1 was associated with an increase in NF-E2-related factor-2 (Nrf2) activity and reactive oxygen species (ROS).	Reactive Oxygen Species	125-128	heme oxygenase 1	Homo sapiens	17-21
26968795-7	2016	In addition, the PI-mediated induction of HO-1 was abolished by N-acetyl-l-cysteine and rotenone.	Acetylcysteine	64-83	heme oxygenase 1	Homo sapiens	42-46
26968795-7	2016	In addition, the PI-mediated induction of HO-1 was abolished by N-acetyl-l-cysteine and rotenone.	Rotenone	88-96	heme oxygenase 1	Homo sapiens	42-46
26968795-9	2016	Inhibition of HO-1 activity or expression potentiated the anti-proliferative and inflammatory actions of PIs which was reversed by bilirubin but not carbon monoxide.	Bilirubin	131-140	heme oxygenase 1	Homo sapiens	14-18
26968795-12	2016	Thus, induction of HO-1 via the ROS-Nrf2 pathway in human ECs counteracts the anti-proliferative and inflammatory actions of PIs by generating bilirubin.	Reactive Oxygen Species	32-35	heme oxygenase 1	Homo sapiens	19-23
26968795-12	2016	Thus, induction of HO-1 via the ROS-Nrf2 pathway in human ECs counteracts the anti-proliferative and inflammatory actions of PIs by generating bilirubin.	Bilirubin	143-152	heme oxygenase 1	Homo sapiens	19-23
27124156-5	2016	In vitro study showed that OSCC cell lines, especially HO1-N-1 cells stimulated NOTCH3 expression in normal human dermal fibroblasts (NHDFs) through direct cell-to-cell contact.	nhdfs	134-139	heme oxygenase 1	Homo sapiens	55-58
26993595-4	2016	We show that the effects of CO on tumor stroma and reprogramming of macrophages towards the anti-tumoral phenotype is mediated by reactive oxygen species (ROS)-dependent activation of MAPK/Erk1/2-c-myc pathway as well as Notch 1-dependent negative feedback on the metabolic enzyme heme oxygenase-1 (HO-1).	Reactive Oxygen Species	130-153	heme oxygenase 1	Homo sapiens	281-297
26993595-4	2016	We show that the effects of CO on tumor stroma and reprogramming of macrophages towards the anti-tumoral phenotype is mediated by reactive oxygen species (ROS)-dependent activation of MAPK/Erk1/2-c-myc pathway as well as Notch 1-dependent negative feedback on the metabolic enzyme heme oxygenase-1 (HO-1).	Reactive Oxygen Species	130-153	heme oxygenase 1	Homo sapiens	299-303
26993595-4	2016	We show that the effects of CO on tumor stroma and reprogramming of macrophages towards the anti-tumoral phenotype is mediated by reactive oxygen species (ROS)-dependent activation of MAPK/Erk1/2-c-myc pathway as well as Notch 1-dependent negative feedback on the metabolic enzyme heme oxygenase-1 (HO-1).	Reactive Oxygen Species	155-158	heme oxygenase 1	Homo sapiens	281-297
26993595-4	2016	We show that the effects of CO on tumor stroma and reprogramming of macrophages towards the anti-tumoral phenotype is mediated by reactive oxygen species (ROS)-dependent activation of MAPK/Erk1/2-c-myc pathway as well as Notch 1-dependent negative feedback on the metabolic enzyme heme oxygenase-1 (HO-1).	Reactive Oxygen Species	155-158	heme oxygenase 1	Homo sapiens	299-303
26679389-8	2016	RESULTS: Our results show that monomethyl fumarate induced nuclear translocation of nuclear factor (erythroid-derived 2)-like 2 and concomitant production of the antioxidant enzymes heme oxygenase-1 and NADPH:quinone oxidoreductase-1 in brain endothelial cells.	citraconic acid	31-50	heme oxygenase 1	Homo sapiens	182-198
27459794-3	2016	Western blot was used to evaluate the expression of Nrf2, quinone oxidoreductase 1 (NQO1) and heme oxygenase-1 (10-1) during sodium arsenite-induced transformation of HBE cells.	sodium arsenite	125-140	heme oxygenase 1	Homo sapiens	94-110
27459794-7	2016	CONCLUSION: The transformation of HBE cells induced by chronic exposure to sodium arsenite is mediated by decreased Nrf2 level and its downstream NQO1 and HO-1 protein, which subsequently promote the malignant proliferation.	sodium arsenite	75-90	heme oxygenase 1	Homo sapiens	155-159
27097841-3	2016	The results showed a time-dependent HO-1 upregulation in primary cultured ventral mesencephalon neurons and astrocytes treated with the mitochondria complex I inhibitor 1-methyl-4-phenylpyridinium (MPP(+)) or recombinant alpha-synuclein.	1-Methyl-4-phenylpyridinium	169-196	heme oxygenase 1	Homo sapiens	36-40
27097841-3	2016	The results showed a time-dependent HO-1 upregulation in primary cultured ventral mesencephalon neurons and astrocytes treated with the mitochondria complex I inhibitor 1-methyl-4-phenylpyridinium (MPP(+)) or recombinant alpha-synuclein.	mangion-purified polysaccharide (Candida albicans)	198-201	heme oxygenase 1	Homo sapiens	36-40
27097841-5	2016	The HO-1 inhibitor zinc protoporphyrin (ZnPP) aggravated MPP(+)- or alpha-synuclein-induced oxidative damage in both astrocytes and neurons, indicating that this HO-1 response was cytoprotective.	zinc protoporphyrin	19-38	heme oxygenase 1	Homo sapiens	4-8
27097841-5	2016	The HO-1 inhibitor zinc protoporphyrin (ZnPP) aggravated MPP(+)- or alpha-synuclein-induced oxidative damage in both astrocytes and neurons, indicating that this HO-1 response was cytoprotective.	zinc protoporphyrin	19-38	heme oxygenase 1	Homo sapiens	162-166
27097841-5	2016	The HO-1 inhibitor zinc protoporphyrin (ZnPP) aggravated MPP(+)- or alpha-synuclein-induced oxidative damage in both astrocytes and neurons, indicating that this HO-1 response was cytoprotective.	zinc protoporphyrin	40-44	heme oxygenase 1	Homo sapiens	4-8
27097841-5	2016	The HO-1 inhibitor zinc protoporphyrin (ZnPP) aggravated MPP(+)- or alpha-synuclein-induced oxidative damage in both astrocytes and neurons, indicating that this HO-1 response was cytoprotective.	zinc protoporphyrin	40-44	heme oxygenase 1	Homo sapiens	162-166
27097841-6	2016	For neurons, the HO-1 activator cobalt protoporphyrin IX (CoPPIX) exerted protective effects against MPP(+) or alpha-synuclein during moderate HO-1 upregulation, but it aggravated damage at the peak of the HO-1 response.	cobaltiprotoporphyrin	32-56	heme oxygenase 1	Homo sapiens	17-21
27097841-6	2016	For neurons, the HO-1 activator cobalt protoporphyrin IX (CoPPIX) exerted protective effects against MPP(+) or alpha-synuclein during moderate HO-1 upregulation, but it aggravated damage at the peak of the HO-1 response.	cobaltiprotoporphyrin	32-56	heme oxygenase 1	Homo sapiens	143-147
27097841-6	2016	For neurons, the HO-1 activator cobalt protoporphyrin IX (CoPPIX) exerted protective effects against MPP(+) or alpha-synuclein during moderate HO-1 upregulation, but it aggravated damage at the peak of the HO-1 response.	cobaltiprotoporphyrin	58-64	heme oxygenase 1	Homo sapiens	17-21
27097841-6	2016	For neurons, the HO-1 activator cobalt protoporphyrin IX (CoPPIX) exerted protective effects against MPP(+) or alpha-synuclein during moderate HO-1 upregulation, but it aggravated damage at the peak of the HO-1 response.	cobaltiprotoporphyrin	58-64	heme oxygenase 1	Homo sapiens	143-147
27097841-6	2016	For neurons, the HO-1 activator cobalt protoporphyrin IX (CoPPIX) exerted protective effects against MPP(+) or alpha-synuclein during moderate HO-1 upregulation, but it aggravated damage at the peak of the HO-1 response.	cobaltiprotoporphyrin	58-64	heme oxygenase 1	Homo sapiens	143-147
26595750-1	2016	Heme oxygenase (HO)-1 catalyzes the degradation of cytotoxic heme into biliverdin and blocks antitumor immune responses, thus protecting cancer against host defense.	Heme	61-65	heme oxygenase 1	Homo sapiens	0-21
26595750-1	2016	Heme oxygenase (HO)-1 catalyzes the degradation of cytotoxic heme into biliverdin and blocks antitumor immune responses, thus protecting cancer against host defense.	Biliverdine	71-81	heme oxygenase 1	Homo sapiens	0-21
26566708-1	2016	Heme oxygenase (HO)-1 is upregulated by many stressful stimuli, including arsenic.	Arsenic	74-81	heme oxygenase 1	Homo sapiens	0-21
26595750-5	2016	On the basis of this observation we aimed to target HO-1 by systemic as well as tumor-specific zinc protoporphyrin-mediated HO-1 suppression in a syngeneic immunocompetent NB mouse model.	zinc protoporphyrin	95-114	heme oxygenase 1	Homo sapiens	124-128
26566708-4	2016	We prospectively investigated the associations between HO-1 (GT)n polymorphism and cancer risk related to arsenic from drinking water.	Arsenic	106-113	heme oxygenase 1	Homo sapiens	55-59
26945724-0	2016	Iron depletion in HCT116 cells diminishes the upregulatory effect of phenethyl isothiocyanate on heme oxygenase-1.	Iron	0-4	heme oxygenase 1	Homo sapiens	97-113
26566708-4	2016	We prospectively investigated the associations between HO-1 (GT)n polymorphism and cancer risk related to arsenic from drinking water.	Water	128-133	heme oxygenase 1	Homo sapiens	55-59
26566708-13	2016	Associations of HO-1 (GT)n polymorphism with cancer risk differs by histological subtype and the polymorphism should be considered a modifier in the risk assessment of arsenic exposure.	Arsenic	168-175	heme oxygenase 1	Homo sapiens	16-20
26945724-0	2016	Iron depletion in HCT116 cells diminishes the upregulatory effect of phenethyl isothiocyanate on heme oxygenase-1.	phenethyl isothiocyanate	69-93	heme oxygenase 1	Homo sapiens	97-113
26945724-3	2016	Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC).	Iron	51-55	heme oxygenase 1	Homo sapiens	113-129
26945724-3	2016	Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC).	Iron	51-55	heme oxygenase 1	Homo sapiens	131-135
26945724-3	2016	Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC).	phenethyl isothiocyanate	153-177	heme oxygenase 1	Homo sapiens	113-129
26945724-3	2016	Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC).	phenethyl isothiocyanate	153-177	heme oxygenase 1	Homo sapiens	131-135
26945724-3	2016	Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC).	phenethyl isothiocyanate	179-184	heme oxygenase 1	Homo sapiens	113-129
26945724-3	2016	Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC).	phenethyl isothiocyanate	179-184	heme oxygenase 1	Homo sapiens	131-135
26945724-7	2016	To elucidate these findings, it was found that PEITC-induced HO-1 upregulation can be inhibited with thiol antioxidants (glutathione and N-acetylcysteine).	phenethyl isothiocyanate	47-52	heme oxygenase 1	Homo sapiens	61-65
26945724-7	2016	To elucidate these findings, it was found that PEITC-induced HO-1 upregulation can be inhibited with thiol antioxidants (glutathione and N-acetylcysteine).	Sulfhydryl Compounds	101-106	heme oxygenase 1	Homo sapiens	61-65
26945724-7	2016	To elucidate these findings, it was found that PEITC-induced HO-1 upregulation can be inhibited with thiol antioxidants (glutathione and N-acetylcysteine).	Glutathione	121-132	heme oxygenase 1	Homo sapiens	61-65
26945724-7	2016	To elucidate these findings, it was found that PEITC-induced HO-1 upregulation can be inhibited with thiol antioxidants (glutathione and N-acetylcysteine).	Acetylcysteine	137-153	heme oxygenase 1	Homo sapiens	61-65
26945724-8	2016	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin) and a superoxide scavenger (Tiron) each inhibited PEITC-induced HO-1 upregulation.	diphenyleneiodonium	39-58	heme oxygenase 1	Homo sapiens	137-141
26945724-8	2016	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin) and a superoxide scavenger (Tiron) each inhibited PEITC-induced HO-1 upregulation.	acetovanillone	63-71	heme oxygenase 1	Homo sapiens	137-141
26945724-8	2016	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin) and a superoxide scavenger (Tiron) each inhibited PEITC-induced HO-1 upregulation.	Superoxides	79-89	heme oxygenase 1	Homo sapiens	137-141
26945724-8	2016	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin) and a superoxide scavenger (Tiron) each inhibited PEITC-induced HO-1 upregulation.	1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt	101-106	heme oxygenase 1	Homo sapiens	137-141
26945724-8	2016	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin) and a superoxide scavenger (Tiron) each inhibited PEITC-induced HO-1 upregulation.	phenethyl isothiocyanate	123-128	heme oxygenase 1	Homo sapiens	137-141
26945724-10	2016	Collectively, the results imply that the HO-1 upregulation by PEITC involves an iron-dependent, oxidant signaling pathway.	Iron	80-84	heme oxygenase 1	Homo sapiens	41-45
26945724-11	2016	Therefore, it is concluded that ample iron is required to enable PEITC to fully upregulate HO-1 expression in HCT116 cells.	Iron	38-42	heme oxygenase 1	Homo sapiens	91-95
26792743-6	2016	Engagement of the hIL-10 receptor (hIL-10R) by cmvIL-10 led to upregulation of heme oxygenase 1 (HO-1), an enzyme linked with suppression of inflammatory responses, and this upregulation was required for cmvIL-10-mediated upregulation of hIL-10.	cmvil-10	47-55	heme oxygenase 1	Homo sapiens	79-95
27071063-3	2016	We found that activation of NRF2 with sulforaphane (SFN) in erythroid progenitors significantly increased the expression of NRF2 targets HMOX1, NQO1, and HBG1 (subunit of fetal hemoglobin) in a dose-dependent manner.	sulforaphane	38-50	heme oxygenase 1	Homo sapiens	137-142
27071063-3	2016	We found that activation of NRF2 with sulforaphane (SFN) in erythroid progenitors significantly increased the expression of NRF2 targets HMOX1, NQO1, and HBG1 (subunit of fetal hemoglobin) in a dose-dependent manner.	sulforaphane	52-55	heme oxygenase 1	Homo sapiens	137-142
27071063-8	2016	We observed an increase in the mean relative whole blood mRNA levels for the NRF2 target HMOX1 (p = 0.02) on the last day of BSH treatment, compared to pre-treatment.	benzenesulfohydrazide	125-128	heme oxygenase 1	Homo sapiens	89-94
27058954-8	2016	In addition to neuroglioma cells, we also found Abeta-induced epigenetic regulation of HMOX1 in human T lymphocyte Jurkat cells.	UNII-042A8N37WH	48-53	heme oxygenase 1	Homo sapiens	87-92
26801320-0	2016	Inhibition of heme oxygenase-1 enhances the chemosensitivity of laryngeal squamous cell cancer Hep-2 cells to cisplatin.	Cisplatin	110-119	heme oxygenase 1	Homo sapiens	14-30
26801320-2	2016	In this research we proved that cisplatin induced cell injuries and heme oxygenase-1 (HO-1) expression in laryngeal squamous cell cancer Hep-2 cells through ROS generation.	Cisplatin	32-41	heme oxygenase 1	Homo sapiens	68-84
26801320-2	2016	In this research we proved that cisplatin induced cell injuries and heme oxygenase-1 (HO-1) expression in laryngeal squamous cell cancer Hep-2 cells through ROS generation.	Cisplatin	32-41	heme oxygenase 1	Homo sapiens	86-90
26801320-2	2016	In this research we proved that cisplatin induced cell injuries and heme oxygenase-1 (HO-1) expression in laryngeal squamous cell cancer Hep-2 cells through ROS generation.	ros	157-160	heme oxygenase 1	Homo sapiens	68-84
26801320-2	2016	In this research we proved that cisplatin induced cell injuries and heme oxygenase-1 (HO-1) expression in laryngeal squamous cell cancer Hep-2 cells through ROS generation.	ros	157-160	heme oxygenase 1	Homo sapiens	86-90
26801320-3	2016	The induction of HO-1 clearly protected Hep-2 cells from cisplatin-induced cell death and ROS reaction, and the inhibitor of HO-1 enhanced the cell death and ROS generation induced by cisplatin.	Cisplatin	57-66	heme oxygenase 1	Homo sapiens	17-21
26801320-3	2016	The induction of HO-1 clearly protected Hep-2 cells from cisplatin-induced cell death and ROS reaction, and the inhibitor of HO-1 enhanced the cell death and ROS generation induced by cisplatin.	ros	90-93	heme oxygenase 1	Homo sapiens	17-21
26801320-3	2016	The induction of HO-1 clearly protected Hep-2 cells from cisplatin-induced cell death and ROS reaction, and the inhibitor of HO-1 enhanced the cell death and ROS generation induced by cisplatin.	ros	158-161	heme oxygenase 1	Homo sapiens	125-129
26801320-3	2016	The induction of HO-1 clearly protected Hep-2 cells from cisplatin-induced cell death and ROS reaction, and the inhibitor of HO-1 enhanced the cell death and ROS generation induced by cisplatin.	Cisplatin	184-193	heme oxygenase 1	Homo sapiens	125-129
26801320-4	2016	Furthermore, the HO-1 expression induced by cisplatin was strongly inhibited by the knockdown of nuclear factor-erythroid-2-related factor-2 (Nrf-2), and the oxidative damages induced by cisplatin were significantly enhanced.	Cisplatin	44-53	heme oxygenase 1	Homo sapiens	17-21
26801320-4	2016	Furthermore, the HO-1 expression induced by cisplatin was strongly inhibited by the knockdown of nuclear factor-erythroid-2-related factor-2 (Nrf-2), and the oxidative damages induced by cisplatin were significantly enhanced.	Cisplatin	187-196	heme oxygenase 1	Homo sapiens	17-21
26801320-5	2016	Therefore, it may be concluded that the inhibition of HO-1 or the knockdown of Nrf-2 significantly enhanced cisplatin"s anticancer effects on Hep-2 cells.	Cisplatin	108-117	heme oxygenase 1	Homo sapiens	54-58
26801320-6	2016	In clinic, with the overexpression of HO-1 in laryngeal squamous cancer tissues, the combination of cisplatin with the inhibitor of HO-1 or Nrf-2 siRNA may act as a new method to the treatment of laryngeal squamous cancer.	Cisplatin	100-109	heme oxygenase 1	Homo sapiens	38-42
26801320-6	2016	In clinic, with the overexpression of HO-1 in laryngeal squamous cancer tissues, the combination of cisplatin with the inhibitor of HO-1 or Nrf-2 siRNA may act as a new method to the treatment of laryngeal squamous cancer.	Cisplatin	100-109	heme oxygenase 1	Homo sapiens	132-136
26780849-15	2016	Knockdown of HO-1 promoted apoptosis through activation of a ROS-mediated caspase apoptosis pathway.	Reactive Oxygen Species	61-64	heme oxygenase 1	Homo sapiens	13-17
27023064-0	2016	Role of Nrf2, HO-1 and GSH in Neuroblastoma Cell Resistance to Bortezomib.	Bortezomib	63-73	heme oxygenase 1	Homo sapiens	14-18
27023064-4	2016	BTZ treatment favours the binding of Nrf2 to the ARE sequences in the promoter regions of target genes such as heme oxygenase 1 (HO-1), the modulatory subunit of gamma-glutamylcysteine ligase (GCLM) and the transporter for cysteine (x-CT), enabling their transcription.	Bortezomib	0-3	heme oxygenase 1	Homo sapiens	111-127
27023064-4	2016	BTZ treatment favours the binding of Nrf2 to the ARE sequences in the promoter regions of target genes such as heme oxygenase 1 (HO-1), the modulatory subunit of gamma-glutamylcysteine ligase (GCLM) and the transporter for cysteine (x-CT), enabling their transcription.	Bortezomib	0-3	heme oxygenase 1	Homo sapiens	129-133
27023064-4	2016	BTZ treatment favours the binding of Nrf2 to the ARE sequences in the promoter regions of target genes such as heme oxygenase 1 (HO-1), the modulatory subunit of gamma-glutamylcysteine ligase (GCLM) and the transporter for cysteine (x-CT), enabling their transcription.	Cysteine	176-184	heme oxygenase 1	Homo sapiens	111-127
27023064-4	2016	BTZ treatment favours the binding of Nrf2 to the ARE sequences in the promoter regions of target genes such as heme oxygenase 1 (HO-1), the modulatory subunit of gamma-glutamylcysteine ligase (GCLM) and the transporter for cysteine (x-CT), enabling their transcription.	Cysteine	176-184	heme oxygenase 1	Homo sapiens	129-133
27023064-6	2016	The up-regulation of Nrf2 target genes is responsible for cell resistance since HO-1 silencing and GSH depletion synergistically decrease BTZ-treated cell viability.	Bortezomib	138-141	heme oxygenase 1	Homo sapiens	80-84
27023064-7	2016	Moreover, cell exposure to all-trans-Retinoic acid (ATRA, 3 muM) reduces the binding of Nrf2 to the ARE sequences, decreases HO-1 induction and lowers GSH level increasing the efficacy of bortezomib.	Tretinoin	27-50	heme oxygenase 1	Homo sapiens	125-129
27023064-7	2016	Moreover, cell exposure to all-trans-Retinoic acid (ATRA, 3 muM) reduces the binding of Nrf2 to the ARE sequences, decreases HO-1 induction and lowers GSH level increasing the efficacy of bortezomib.	Tretinoin	52-56	heme oxygenase 1	Homo sapiens	125-129
27023064-7	2016	Moreover, cell exposure to all-trans-Retinoic acid (ATRA, 3 muM) reduces the binding of Nrf2 to the ARE sequences, decreases HO-1 induction and lowers GSH level increasing the efficacy of bortezomib.	Bortezomib	188-198	heme oxygenase 1	Homo sapiens	125-129
27023064-8	2016	These data suggest the role of Nrf2, HO-1 and GSH as molecular targets to improve the efficacy of low doses of bortezomib in the treatment of malignant neuroblastoma.	Bortezomib	111-121	heme oxygenase 1	Homo sapiens	37-41
26792743-6	2016	Engagement of the hIL-10 receptor (hIL-10R) by cmvIL-10 led to upregulation of heme oxygenase 1 (HO-1), an enzyme linked with suppression of inflammatory responses, and this upregulation was required for cmvIL-10-mediated upregulation of hIL-10.	cmvil-10	47-55	heme oxygenase 1	Homo sapiens	97-101
26792743-6	2016	Engagement of the hIL-10 receptor (hIL-10R) by cmvIL-10 led to upregulation of heme oxygenase 1 (HO-1), an enzyme linked with suppression of inflammatory responses, and this upregulation was required for cmvIL-10-mediated upregulation of hIL-10.	cmvil-10	204-212	heme oxygenase 1	Homo sapiens	79-95
26792743-6	2016	Engagement of the hIL-10 receptor (hIL-10R) by cmvIL-10 led to upregulation of heme oxygenase 1 (HO-1), an enzyme linked with suppression of inflammatory responses, and this upregulation was required for cmvIL-10-mediated upregulation of hIL-10.	cmvil-10	204-212	heme oxygenase 1	Homo sapiens	97-101
26801686-0	2016	Activation of the MAPK/Akt/Nrf2-Egr1/HO-1-GCLc axis protects MG-63 osteosarcoma cells against 15d-PGJ2-mediated cell death.	9-deoxy-delta-9-prostaglandin D2	98-102	heme oxygenase 1	Homo sapiens	37-41
26876575-0	2016	MicroRNA-218 promotes high glucose-induced apoptosis in podocytes by targeting heme oxygenase-1.	Glucose	27-34	heme oxygenase 1	Homo sapiens	79-95
27023525-18	2016	CORM-2 decreased NO and increased HO-1 expression and CO and COHb content, downregulated HIF-1alpha, as well as WRS-elevated COX-2 and iNOS mRNAs.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	34-38
26801686-5	2016	This pathway induced nuclear expression of Nrf2 and Egr1, and increased transcription of haem oxygenase-1 (HO-1) and the catalytic subunit of glutamate cysteine ligase (GCLc), catalysing the first step in GSH synthesis.	Glutathione	205-208	heme oxygenase 1	Homo sapiens	89-105
26801686-5	2016	This pathway induced nuclear expression of Nrf2 and Egr1, and increased transcription of haem oxygenase-1 (HO-1) and the catalytic subunit of glutamate cysteine ligase (GCLc), catalysing the first step in GSH synthesis.	Glutathione	205-208	heme oxygenase 1	Homo sapiens	107-111
26801686-6	2016	Silencing of Nrf2, Egr1 and HO-1 significantly elevated 15d-PGJ2-mediated reduction of cellular metabolic activity.	15-deoxy-delta(12,14)-prostaglandin J2	56-64	heme oxygenase 1	Homo sapiens	28-32
26801686-7	2016	Activation of cell survival genes including HO-1 and GCLc inhibited 15d-PGJ2-induced cleavage of pro-caspase-3 and PARP.	9-deoxy-delta-9-prostaglandin D2	72-76	heme oxygenase 1	Homo sapiens	44-48
26801686-12	2016	Pharmacological or genetic interference of the pro-survival pathway, the p38 MAPK/Akt/Nrf2-Egr1/HO-1-GCLc axis, sensitizes MG-63 cells towards 15d-PGJ2-mediated apoptosis.	9-deoxy-delta-9-prostaglandin D2	147-151	heme oxygenase 1	Homo sapiens	96-105
26725491-0	2016	Heme Oxygenase-1/Carbon Monoxide System and Embryonic Stem Cell Differentiation and Maturation into Cardiomyocytes.	Carbon Monoxide	17-32	heme oxygenase 1	Homo sapiens	0-16
26725491-3	2016	In this study, we tested whether the redox-sensitive heme oxygenase-1/carbon monoxide (HO-1/CO) system, operating through mitochondrial biogenesis, acts as a mechanism for ES cell differentiation and cardiomyocyte maturation.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	53-69
26725491-3	2016	In this study, we tested whether the redox-sensitive heme oxygenase-1/carbon monoxide (HO-1/CO) system, operating through mitochondrial biogenesis, acts as a mechanism for ES cell differentiation and cardiomyocyte maturation.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	87-94
26898422-0	2016	Heme oxygenase-1 contributes to imatinib resistance by promoting autophagy in chronic myeloid leukemia through disrupting the mTOR signaling pathway.	Imatinib Mesylate	32-40	heme oxygenase 1	Homo sapiens	0-16
26700310-0	2016	Potential crosstalk of the interleukin-6-heme oxygenase-1-dependent mechanism involved in resistance to lenalidomide in multiple myeloma cells.	Lenalidomide	104-116	heme oxygenase 1	Homo sapiens	41-57
26700310-7	2016	In contrast, without IL-6 coculture, enhanced HO-1 expression in U266, RPMI8226 and bone marrow CD138(+) cells from MM patients significantly inreased IL-6 mRNA expression levels and facilitated autocrine IL-6 production.	rpmi8226	71-79	heme oxygenase 1	Homo sapiens	46-50
26898422-1	2016	Heme oxygenase-1 (HO-1) has been verified to play an important role in imatinib (IM)-resistant chronic myeloid leukemia (CML) cells, but the mechanism remains unclear.	Imatinib Mesylate	71-79	heme oxygenase 1	Homo sapiens	0-16
26700310-9	2016	Reduced HO-1 expression sensitized MM cells to lenalidomide.	Lenalidomide	47-59	heme oxygenase 1	Homo sapiens	8-12
26898422-1	2016	Heme oxygenase-1 (HO-1) has been verified to play an important role in imatinib (IM)-resistant chronic myeloid leukemia (CML) cells, but the mechanism remains unclear.	Imatinib Mesylate	71-79	heme oxygenase 1	Homo sapiens	18-22
27051648-6	2016	In the present study, the protective effects of hyperoside against hydrogen peroxide-induced oxidative stress in human lens epithelial cells, HLE-B3, were investigated in terms of HO-1 induction.	hyperoside	48-58	heme oxygenase 1	Homo sapiens	180-184
26698668-4	2016	Affymetrix array profiling and subsequent qPCR/protein validation revealed that induction of select Nrf2 target genes, HO-1 and NQO1, was significantly attenuated in cells adapted to 5% O2, despite nuclear accumulation and DNA binding of Nrf2.	Oxygen	186-188	heme oxygenase 1	Homo sapiens	119-123
26698668-5	2016	Diminished HO-1 induction under 5% O2 was stimulus independent and reversible upon re-adaptation to air or silencing of the Nrf2 repressor Bach1, notably elevated under 5% O2.	Oxygen	35-37	heme oxygenase 1	Homo sapiens	11-15
26698668-5	2016	Diminished HO-1 induction under 5% O2 was stimulus independent and reversible upon re-adaptation to air or silencing of the Nrf2 repressor Bach1, notably elevated under 5% O2.	Oxygen	172-174	heme oxygenase 1	Homo sapiens	11-15
27051648-11	2016	RESULTS: Hyperoside increased both the mRNA and protein expression of HO-1 in a time- and dose-dependent manner.	hyperoside	9-19	heme oxygenase 1	Homo sapiens	70-74
27051648-14	2016	CONCLUSIONS: Hyperoside is an effective compound to protect cells against oxidative stress via HO-1 induction.	hyperoside	13-23	heme oxygenase 1	Homo sapiens	95-99
27263286-3	2016	RESULTS: 10 mumol/L arsenic trioxide can decreased the cell viability, while cell apoptosis rate, ROS level, HO-1 and Nrf2 protein expression was increased (P &lt; 0.05).	Arsenic Trioxide	20-36	heme oxygenase 1	Homo sapiens	109-113
26681403-11	2016	In contrast, Nrf2 and HO-1 expression were markedly increased (P = 0.0001, P = 0.0049, respectively) after smokers took melatonin orally.	Melatonin	120-129	heme oxygenase 1	Homo sapiens	22-26
27263286-4	2016	When compared with arsenic trioxide alone, co-treatment of arsenic trioxide with aspirin in different concentration (0, 0.1, 1.0, 2.5, 5.0 mmol/L) exhibited dual effects in intracellular ROS level, HO-1 and Nrf2 expression.	Arsenic Trioxide	59-75	heme oxygenase 1	Homo sapiens	198-202
27263286-7	2016	On the contrary, 5 mmol/L aspirin could increase the sensitivity of HepG2 to arsenic trioxide through enhancing the arsenic trioxide-induced apoptosis by ROS accumulation resulting in inhibiting the Nrf2-HO-1 pathway.	Arsenic Trioxide	116-132	heme oxygenase 1	Homo sapiens	204-208
27263286-4	2016	When compared with arsenic trioxide alone, co-treatment of arsenic trioxide with aspirin in different concentration (0, 0.1, 1.0, 2.5, 5.0 mmol/L) exhibited dual effects in intracellular ROS level, HO-1 and Nrf2 expression.	Aspirin	81-88	heme oxygenase 1	Homo sapiens	198-202
27263286-5	2016	Specifically, with the increasing of aspirin concentrations, the level of ROS induced by arsenic trioxide showed a rising trend after the first reduction, whereas, HO-1 and Nrf2 protein expression were decreased at first and then increased.	Aspirin	37-44	heme oxygenase 1	Homo sapiens	164-168
27263286-6	2016	CONCLUSION: Low concentration, less than 2.5 mmol/L, of aspirin may reduce the ROS accumulation through activating of Nrf2-HO-1 pathway, therefore decreasing the apoptotic cell death induced by arsenic trioxide.	Aspirin	56-63	heme oxygenase 1	Homo sapiens	123-127
27263286-7	2016	On the contrary, 5 mmol/L aspirin could increase the sensitivity of HepG2 to arsenic trioxide through enhancing the arsenic trioxide-induced apoptosis by ROS accumulation resulting in inhibiting the Nrf2-HO-1 pathway.	Aspirin	26-33	heme oxygenase 1	Homo sapiens	204-208
27263286-7	2016	On the contrary, 5 mmol/L aspirin could increase the sensitivity of HepG2 to arsenic trioxide through enhancing the arsenic trioxide-induced apoptosis by ROS accumulation resulting in inhibiting the Nrf2-HO-1 pathway.	Arsenic Trioxide	77-93	heme oxygenase 1	Homo sapiens	204-208
27033569-10	2016	The HO-1 mRNA level before the stimulation was 1.000, and 17.264+-4.275 after the stimulation of 1 ng/ml IL-17A (U=0, P&lt;0.05), 19.128+-4.605 after the stimulation of 10 ng/ml IL-17A (U=0, P&lt;0.05), but was significantly suppressed after stimulation with glucocorticoids (dexamethasone, DEX).	Dexamethasone	276-289	heme oxygenase 1	Homo sapiens	4-8
27033569-10	2016	The HO-1 mRNA level before the stimulation was 1.000, and 17.264+-4.275 after the stimulation of 1 ng/ml IL-17A (U=0, P&lt;0.05), 19.128+-4.605 after the stimulation of 10 ng/ml IL-17A (U=0, P&lt;0.05), but was significantly suppressed after stimulation with glucocorticoids (dexamethasone, DEX).	Dextromethorphan	291-294	heme oxygenase 1	Homo sapiens	4-8
26869854-10	2016	Noteworthy, the impaired TCA cycle in HT-1080 cells were associated with high mTORC1 activity, negligible protein level and activity of mTORC2, high expression of interleukin-1beta, interleukin-6 and heme oxygenase-1 which may contribute to the compensatory mechanism of TCA deficiency.	Trichloroacetic Acid	25-28	heme oxygenase 1	Homo sapiens	200-216
30263273-7	2016	6-shogaol exerts an indirect cellular anti-oxidant activity based on up-regulation of GCS and HO-1 via a JNK-mediated Nrf2 signaling pathway.	shogaol	0-9	heme oxygenase 1	Homo sapiens	94-98
26721585-1	2016	Carbon monoxide (CO) is generated by heme oxygenase-1 (HO-1) and displays important signaling, anti-apoptotic and anti-inflammatory activities, indicating that pharmacological agents mimicking its action may have therapeutic benefit.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	37-53
26721585-1	2016	Carbon monoxide (CO) is generated by heme oxygenase-1 (HO-1) and displays important signaling, anti-apoptotic and anti-inflammatory activities, indicating that pharmacological agents mimicking its action may have therapeutic benefit.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	55-59
26721585-1	2016	Carbon monoxide (CO) is generated by heme oxygenase-1 (HO-1) and displays important signaling, anti-apoptotic and anti-inflammatory activities, indicating that pharmacological agents mimicking its action may have therapeutic benefit.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	37-53
26721585-1	2016	Carbon monoxide (CO) is generated by heme oxygenase-1 (HO-1) and displays important signaling, anti-apoptotic and anti-inflammatory activities, indicating that pharmacological agents mimicking its action may have therapeutic benefit.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	55-59
26483091-1	2016	BACKGROUND: Heme-oxygenase 1 (HO-1), an inducible heme-degrading enzyme, has antiatherogenic effects through its enzymatic end products.	Heme	50-54	heme oxygenase 1	Homo sapiens	12-28
26866373-10	2016	EGCG down-regulated NLRP3 expression, which was blocked by ZnPP, indicating that HO-1 links EGCG with NLRP3.	epigallocatechin gallate	0-4	heme oxygenase 1	Homo sapiens	81-85
26866373-10	2016	EGCG down-regulated NLRP3 expression, which was blocked by ZnPP, indicating that HO-1 links EGCG with NLRP3.	zinc protoporphyrin	59-63	heme oxygenase 1	Homo sapiens	81-85
26866373-10	2016	EGCG down-regulated NLRP3 expression, which was blocked by ZnPP, indicating that HO-1 links EGCG with NLRP3.	epigallocatechin gallate	92-96	heme oxygenase 1	Homo sapiens	81-85
26866373-11	2016	Therefore, EGCG, via up-regulation of HO-1, protects against CIN by amelioration of oxidative stress and inflammation.	epigallocatechin gallate	11-15	heme oxygenase 1	Homo sapiens	38-42
26723515-6	2016	Furthermore, eriodictyol was found to up-regulate the expression of Nrf2/HO-1 and inhibited CP-induced NF-kappaB activation in kidney tissues.	eriodictyol	13-24	heme oxygenase 1	Homo sapiens	73-77
26845693-0	2016	Modification of Caffeic Acid with Pyrrolidine Enhances Antioxidant Ability by Activating AKT/HO-1 Pathway in Heart.	caffeic acid	16-28	heme oxygenase 1	Homo sapiens	93-97
26845693-0	2016	Modification of Caffeic Acid with Pyrrolidine Enhances Antioxidant Ability by Activating AKT/HO-1 Pathway in Heart.	pyrrolidine	34-45	heme oxygenase 1	Homo sapiens	93-97
25575725-6	2016	Studies of human umbilical vein endothelial cells (HUVEC) and arterial endothelial cells (HAEC) showed that therapeutically relevant concentrations of MTX phosphorylate AMPKalpha(Thr172), and induce cytoprotective genes including manganese superoxide dismutase (MnSOD) and haem oxygenase-1 (HO-1).	Methotrexate	151-154	heme oxygenase 1	Homo sapiens	273-289
25575725-6	2016	Studies of human umbilical vein endothelial cells (HUVEC) and arterial endothelial cells (HAEC) showed that therapeutically relevant concentrations of MTX phosphorylate AMPKalpha(Thr172), and induce cytoprotective genes including manganese superoxide dismutase (MnSOD) and haem oxygenase-1 (HO-1).	Methotrexate	151-154	heme oxygenase 1	Homo sapiens	291-295
25575725-9	2016	Mechanistically, MTX treatment led to cyclic AMP response element-binding protein (CREB)(Ser133) phosphorylation, while AMPK depletion attenuated this response and the induction of MnSOD and HO-1.	Methotrexate	17-20	heme oxygenase 1	Homo sapiens	191-195
26866373-0	2016	Targeting HO-1 by Epigallocatechin-3-Gallate Reduces Contrast-Induced Renal Injury via Anti-Oxidative Stress and Anti-Inflammation Pathways.	epigallocatechin gallate	18-44	heme oxygenase 1	Homo sapiens	10-14
26866373-5	2016	Because EGCG is a potent inducer of the antioxidant heme oxygenase-1 (HO-1), we studied HO-1 signaling in CIN.	epigallocatechin gallate	8-12	heme oxygenase 1	Homo sapiens	52-68
26866373-5	2016	Because EGCG is a potent inducer of the antioxidant heme oxygenase-1 (HO-1), we studied HO-1 signaling in CIN.	epigallocatechin gallate	8-12	heme oxygenase 1	Homo sapiens	70-74
26866373-5	2016	Because EGCG is a potent inducer of the antioxidant heme oxygenase-1 (HO-1), we studied HO-1 signaling in CIN.	epigallocatechin gallate	8-12	heme oxygenase 1	Homo sapiens	88-92
26866373-6	2016	HO-1 levels were increased in CIN; treatment with EGCG further increased HO-1 levels, accompanied by an increase in Nrf2, a regulator of antioxidant proteins.	epigallocatechin gallate	50-54	heme oxygenase 1	Homo sapiens	0-4
26866373-6	2016	HO-1 levels were increased in CIN; treatment with EGCG further increased HO-1 levels, accompanied by an increase in Nrf2, a regulator of antioxidant proteins.	epigallocatechin gallate	50-54	heme oxygenase 1	Homo sapiens	73-77
26866373-7	2016	Interestingly, blockade of HO-1 with protoporphyrin IX zinc(II) (ZnPP) prevented the protective effect of EGCG on CIN.	protoporphyrin ix zinc(ii)	37-63	heme oxygenase 1	Homo sapiens	27-31
26866373-7	2016	Interestingly, blockade of HO-1 with protoporphyrin IX zinc(II) (ZnPP) prevented the protective effect of EGCG on CIN.	zinc protoporphyrin	65-69	heme oxygenase 1	Homo sapiens	27-31
26866373-7	2016	Interestingly, blockade of HO-1 with protoporphyrin IX zinc(II) (ZnPP) prevented the protective effect of EGCG on CIN.	epigallocatechin gallate	106-110	heme oxygenase 1	Homo sapiens	27-31
26866373-8	2016	ZnPP also blocked the ability of EGCG to increase the activity of an antioxidant (superoxide dismutase), and decrease markers of oxidative stress (myeloperoxidase and malondialdehyde) and inflammation (myeloperoxidase and IL-1beta), indicating that HO-1 is the upstream molecule that regulates the EGCG-mediated protection.	zinc protoporphyrin	0-4	heme oxygenase 1	Homo sapiens	249-253
26866373-8	2016	ZnPP also blocked the ability of EGCG to increase the activity of an antioxidant (superoxide dismutase), and decrease markers of oxidative stress (myeloperoxidase and malondialdehyde) and inflammation (myeloperoxidase and IL-1beta), indicating that HO-1 is the upstream molecule that regulates the EGCG-mediated protection.	epigallocatechin gallate	33-37	heme oxygenase 1	Homo sapiens	249-253
26483091-1	2016	BACKGROUND: Heme-oxygenase 1 (HO-1), an inducible heme-degrading enzyme, has antiatherogenic effects through its enzymatic end products.	Heme	50-54	heme oxygenase 1	Homo sapiens	30-34
26483091-2	2016	HO-1 gene expression is modulated by a guanidine thymidine dinucleotide ([GT]n) repeat polymorphism in the promoter region.	guanidine thymidine dinucleotide	39-71	heme oxygenase 1	Homo sapiens	0-4
26689473-6	2016	The 27-OH-exerted induction of Nrf2 and subsequently of the target genes, HO-1 and NQO-1, was proved to be: (i) dependent upon the activation of ERK and Akt pathways, (ii) directly responsible for the quenching of intracellular oxidative stress and by this way (iii) ultimately responsible for the observed oxysterol-induced pro-survival response.	27-hydroxycholesterol	4-9	heme oxygenase 1	Homo sapiens	74-78
26467701-8	2016	DHT induced a significant increase in expression of the androgen-responsive genes FKBP5, HMOX1, FBXO32, VEGFA, WNT5A, and KLK3 only in AR-positive cells in vitro.	Dihydrotestosterone	0-3	heme oxygenase 1	Homo sapiens	89-94
26721592-10	2016	CA also reversed the APAP-induced decreased mRNA and protein expression of heme oxygenase 1 (HO-1) and NAD(P)H: quinone oxidoreductase 1(NQO1).	Acetaminophen	21-25	heme oxygenase 1	Homo sapiens	75-91
26726846-9	2016	Suppression of HO-1 by Zn-protoporphyrin (ZnPP) enhanced cytotoxicity to GEM in CCA cells, validated in CCA xenografts.	zn-protoporphyrin	23-40	heme oxygenase 1	Homo sapiens	15-19
26726846-9	2016	Suppression of HO-1 by Zn-protoporphyrin (ZnPP) enhanced cytotoxicity to GEM in CCA cells, validated in CCA xenografts.	Zinc protoporphyrin	42-46	heme oxygenase 1	Homo sapiens	15-19
26698667-9	2016	On the other hand, induction of the Nrf2-regulated enzyme heme oxygenase 1 (HO-1) by cardamonin was diminished in Se-replete compared to Se-deficient cells.	cardamonin	85-95	heme oxygenase 1	Homo sapiens	58-74
26698667-9	2016	On the other hand, induction of the Nrf2-regulated enzyme heme oxygenase 1 (HO-1) by cardamonin was diminished in Se-replete compared to Se-deficient cells.	Selenium	114-116	heme oxygenase 1	Homo sapiens	58-74
26698667-9	2016	On the other hand, induction of the Nrf2-regulated enzyme heme oxygenase 1 (HO-1) by cardamonin was diminished in Se-replete compared to Se-deficient cells.	Selenium	137-139	heme oxygenase 1	Homo sapiens	58-74
26721592-11	2016	In addition, HO-1 inhibitor zinc protoporphyrin (ZnPP) and NQO1 inhibitor diminutol (Dim) reduced the protection of CA against APAP-induced hepatotoxicity.	zinc protoporphyrin	28-47	heme oxygenase 1	Homo sapiens	13-17
26689473-6	2016	The 27-OH-exerted induction of Nrf2 and subsequently of the target genes, HO-1 and NQO-1, was proved to be: (i) dependent upon the activation of ERK and Akt pathways, (ii) directly responsible for the quenching of intracellular oxidative stress and by this way (iii) ultimately responsible for the observed oxysterol-induced pro-survival response.	Oxysterols	307-316	heme oxygenase 1	Homo sapiens	74-78
26721592-11	2016	In addition, HO-1 inhibitor zinc protoporphyrin (ZnPP) and NQO1 inhibitor diminutol (Dim) reduced the protection of CA against APAP-induced hepatotoxicity.	zinc protoporphyrin	49-53	heme oxygenase 1	Homo sapiens	13-17
26721592-11	2016	In addition, HO-1 inhibitor zinc protoporphyrin (ZnPP) and NQO1 inhibitor diminutol (Dim) reduced the protection of CA against APAP-induced hepatotoxicity.	Acetaminophen	127-131	heme oxygenase 1	Homo sapiens	13-17
26618301-9	2016	The antioxidant response genes (Nqo1 and Hmox1) were moderately associated with polyaromatic hydrocarbons (PAHs) and showed a good correlation (r-Pearson of &gt;0.7) with metals linked to vehicle-related emissions (i.e. Cu, Zn and Sb).	polyaromatic hydrocarbons	80-105	heme oxygenase 1	Homo sapiens	41-46
26721592-15	2016	In conclusion, we demonstrated that CA prevented APAP-induced hepatotoxicity by decreasing Keap1 expression, inhibiting binding of Keap1 to Nrf2, and thus activating Nrf2 and leading to increased expression of antioxidative signals including HO-1 and NQO1.	Acetaminophen	49-53	heme oxygenase 1	Homo sapiens	242-246
26691217-2	2016	The aim of this study was to assess the effects of CUGBP2-mediated post-transcriptional regulation of COX-2 and HO-1 in pancreatic cancer cells in regard of response to gemcitabine (GEM) treatment.	gemcitabine	169-180	heme oxygenase 1	Homo sapiens	112-116
26691217-2	2016	The aim of this study was to assess the effects of CUGBP2-mediated post-transcriptional regulation of COX-2 and HO-1 in pancreatic cancer cells in regard of response to gemcitabine (GEM) treatment.	gemcitabine	182-185	heme oxygenase 1	Homo sapiens	112-116
26691217-9	2016	Induction of CUGBP2 expression by curcumin resulted in the downregulation of HO-1 and COX-2 and strongly sensitized tumor cells to GEM treatment.	Curcumin	34-42	heme oxygenase 1	Homo sapiens	77-81
27186034-2	2016	Activity of heme oxygenase-1 is regulated by a guanine-thymine dinucleotide length polymorphism in the heme oxygenase-1 gene promoter.	guanine-thymine dinucleotide	47-75	heme oxygenase 1	Homo sapiens	12-28
27186034-2	2016	Activity of heme oxygenase-1 is regulated by a guanine-thymine dinucleotide length polymorphism in the heme oxygenase-1 gene promoter.	guanine-thymine dinucleotide	47-75	heme oxygenase 1	Homo sapiens	103-119
26827637-0	2016	Sulforaphane exerts its anti-inflammatory effect against amyloid-beta peptide via STAT-1 dephosphorylation and activation of Nrf2/HO-1 cascade in human THP-1 macrophages.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	130-134
26827637-5	2016	Sulforaphane also increased nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation, which was followed by upregulation of heme-oxygenase 1 (HO-1).	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	140-156
26827637-5	2016	Sulforaphane also increased nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation, which was followed by upregulation of heme-oxygenase 1 (HO-1).	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	158-162
26827637-6	2016	The anti-inflammatory effect of sulforaphane on Abeta1-42-induced IL-1beta production was diminished by small interfering RNA-mediated knockdown of Nrf2 or HO-1.	sulforaphane	32-44	heme oxygenase 1	Homo sapiens	156-160
26827637-9	2016	These results indicate that signal transducer and activator of transcription-1 dephosphorylation, HO-1 and its upstream effector, Nrf2, play a pivotal role in triggering an anti-inflammatory signaling cascade of sulforaphane that results in decreases of IL-1beta release and microRNA-146a production in Abeta1-42-stimulated human microglia-like cells.	sulforaphane	212-224	heme oxygenase 1	Homo sapiens	98-102
26618301-9	2016	The antioxidant response genes (Nqo1 and Hmox1) were moderately associated with polyaromatic hydrocarbons (PAHs) and showed a good correlation (r-Pearson of &gt;0.7) with metals linked to vehicle-related emissions (i.e. Cu, Zn and Sb).	pahs	107-111	heme oxygenase 1	Homo sapiens	41-46
26618301-9	2016	The antioxidant response genes (Nqo1 and Hmox1) were moderately associated with polyaromatic hydrocarbons (PAHs) and showed a good correlation (r-Pearson of &gt;0.7) with metals linked to vehicle-related emissions (i.e. Cu, Zn and Sb).	Copper	220-222	heme oxygenase 1	Homo sapiens	41-46
26618301-9	2016	The antioxidant response genes (Nqo1 and Hmox1) were moderately associated with polyaromatic hydrocarbons (PAHs) and showed a good correlation (r-Pearson of &gt;0.7) with metals linked to vehicle-related emissions (i.e. Cu, Zn and Sb).	Zinc	224-226	heme oxygenase 1	Homo sapiens	41-46
26618301-9	2016	The antioxidant response genes (Nqo1 and Hmox1) were moderately associated with polyaromatic hydrocarbons (PAHs) and showed a good correlation (r-Pearson of &gt;0.7) with metals linked to vehicle-related emissions (i.e. Cu, Zn and Sb).	Antimony	231-233	heme oxygenase 1	Homo sapiens	41-46
26730678-2	2016	We synthesized a series of cobalt-based hybrid molecules (HYCOs) that combine an Nrf2 inducer with a releaser of carbon monoxide (CO), an anti-inflammatory product of HO-1.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	167-171
26730678-2	2016	We synthesized a series of cobalt-based hybrid molecules (HYCOs) that combine an Nrf2 inducer with a releaser of carbon monoxide (CO), an anti-inflammatory product of HO-1.	Carbon Monoxide	60-62	heme oxygenase 1	Homo sapiens	167-171
26730678-0	2016	Diverse Nrf2 Activators Coordinated to Cobalt Carbonyls Induce Heme Oxygenase-1 and Release Carbon Monoxide in Vitro and in Vivo.	cobalt carbonyls	39-55	heme oxygenase 1	Homo sapiens	63-79
26655464-0	2016	Pinocembrin attenuates MPP(+)-induced neurotoxicity by the induction of heme oxygenase-1 through ERK1/2 pathway.	pinocembrin	0-11	heme oxygenase 1	Homo sapiens	72-88
26730678-2	2016	We synthesized a series of cobalt-based hybrid molecules (HYCOs) that combine an Nrf2 inducer with a releaser of carbon monoxide (CO), an anti-inflammatory product of HO-1.	Cobalt	27-33	heme oxygenase 1	Homo sapiens	167-171
26822586-0	2016	Blocking heme oxygenase-1 by zinc protoporphyrin reduces tumor hypoxia-mediated VEGF release and inhibits tumor angiogenesis as a potential therapeutic agent against colorectal cancer.	zinc protoporphyrin	29-48	heme oxygenase 1	Homo sapiens	9-25
26822586-3	2016	Zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, is potential to inhibit tumor proliferation and progression.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	30-46
26822586-3	2016	Zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, is potential to inhibit tumor proliferation and progression.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	48-52
26822586-3	2016	Zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, is potential to inhibit tumor proliferation and progression.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	30-46
26822586-3	2016	Zinc protoporphyrin (ZnPP), a heme oxygenase-1 (HO-1) inhibitor, is potential to inhibit tumor proliferation and progression.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	48-52
26822586-5	2016	We hypothesize that ZnPP may modulate HIF-1alpha through inhibiting HO-1, and then inhibit angiogenesis and tumor progression.	zinc protoporphyrin	20-24	heme oxygenase 1	Homo sapiens	68-72
26822586-11	2016	Moreover, we observed that the HO-1 inhibitor ZnPP inhibited the expressions of HIF-1alpha and VEGF coupled with cell proliferations of HCT-15 cells, suggesting that ZnPP blocked HIF-1alpha expression, and then inhibited the consequent VEGF production.	zinc protoporphyrin	46-50	heme oxygenase 1	Homo sapiens	31-35
26822586-11	2016	Moreover, we observed that the HO-1 inhibitor ZnPP inhibited the expressions of HIF-1alpha and VEGF coupled with cell proliferations of HCT-15 cells, suggesting that ZnPP blocked HIF-1alpha expression, and then inhibited the consequent VEGF production.	zinc protoporphyrin	166-170	heme oxygenase 1	Homo sapiens	31-35
26822586-14	2016	The HO-1 inhibitor, ZnPP, possessed the properties of anti-tumor agent by decreasing HIF-1alpha levels, blocking VEGF production, impairing tumor angiogenesis, and inhibiting tumor growth.	zinc protoporphyrin	20-24	heme oxygenase 1	Homo sapiens	4-8
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	pinocembrin	47-49	heme oxygenase 1	Homo sapiens	60-76
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	pinocembrin	47-49	heme oxygenase 1	Homo sapiens	78-82
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	pinocembrin	47-49	heme oxygenase 1	Homo sapiens	185-189
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	protoporphyrin IX	195-212	heme oxygenase 1	Homo sapiens	60-76
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	protoporphyrin IX	195-212	heme oxygenase 1	Homo sapiens	78-82
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	protoporphyrin IX	195-212	heme oxygenase 1	Homo sapiens	185-189
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	pinocembrin	247-249	heme oxygenase 1	Homo sapiens	60-76
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	pinocembrin	247-249	heme oxygenase 1	Homo sapiens	78-82
26655464-3	2016	In the present study, we demonstrate here that PB increased heme oxygenase-1 (HO-1) expression, which conferred protection against MPP(+)-induced cytotoxicity, because the inhibitor of HO-1 zinc protoporphyrin-IX attenuated the neuroprotection of PB.	pinocembrin	247-249	heme oxygenase 1	Homo sapiens	185-189
26655464-6	2016	Taken together, the results suggest that PB enhances HO-1 expression to suppress MPP(+)-induced oxidative damage via ERK1/2 signaling pathways.	pinocembrin	41-43	heme oxygenase 1	Homo sapiens	53-57
26655464-7	2016	These results revealed the mechanisms of PB enhances HO-1 expression, and contribute to shed some light on the mechanisms whereby PB inhibits the MPP(+)-induced neurotoxicity.	pinocembrin	41-43	heme oxygenase 1	Homo sapiens	53-57
26834769-10	2015	Together, these results clearly suggest that HO-1 is involved in the alleviation of GA-induced PCD of drought-triggered rice aleurone layers by associating with NO.	Gallium	84-86	heme oxygenase 1	Homo sapiens	45-49
26631587-9	2016	Key messages Bilirubin levels are inversely related to cardiovascular disease, and overexpression of heme oxygenase-1 (the enzyme that determines bilirubin production) has prevented post-infarction ventricular remodeling in experimental animals, but the association between bilirubin levels and the progression of ventricular volumes and function in patients with acute myocardial infarction remained unexplored.	Bilirubin	146-155	heme oxygenase 1	Homo sapiens	101-117
26834769-2	2015	Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)).	Heme	79-83	heme oxygenase 1	Homo sapiens	18-22
26834769-2	2015	Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)).	Biliverdine	87-105	heme oxygenase 1	Homo sapiens	18-22
26834769-2	2015	Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)).	Carbon Monoxide	107-122	heme oxygenase 1	Homo sapiens	18-22
26834769-2	2015	Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)).	Carbon Monoxide	124-126	heme oxygenase 1	Homo sapiens	18-22
26834769-2	2015	Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)).	Iron	138-142	heme oxygenase 1	Homo sapiens	18-22
26834769-2	2015	Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)).	Iron	149-151	heme oxygenase 1	Homo sapiens	18-22
26834769-4	2015	Our previous studies confirmed that HO-1 inducer hematin (Ht) promotes the germination of rice seeds in drought (20% polyethylene glycol-6000, PEG) conditions, but the corresponding effects of HO-1 on the alleviation of germination-triggered PCD in GA-treated rice aleurone layers remain unknown.	Polyethylene Glycol 6000	117-141	heme oxygenase 1	Homo sapiens	36-40
26834769-4	2015	Our previous studies confirmed that HO-1 inducer hematin (Ht) promotes the germination of rice seeds in drought (20% polyethylene glycol-6000, PEG) conditions, but the corresponding effects of HO-1 on the alleviation of germination-triggered PCD in GA-treated rice aleurone layers remain unknown.	Polyethylene Glycol 6000	143-146	heme oxygenase 1	Homo sapiens	36-40
26834769-5	2015	The present study has determined that GA co-treated with PEG results in lower HO-1 transcript levels and HO activity, which in turn results in the development of vacuoles in aleurone cells, followed by PCD.	Gallium	38-40	heme oxygenase 1	Homo sapiens	78-82
26834769-5	2015	The present study has determined that GA co-treated with PEG results in lower HO-1 transcript levels and HO activity, which in turn results in the development of vacuoles in aleurone cells, followed by PCD.	Polyethylene Glycol 6000	57-60	heme oxygenase 1	Homo sapiens	78-82
26834769-6	2015	The pharmacology approach illustrated that up- or down-regulated HO-1 gene expression and HO activity delayed or accelerated GA-induced PCD.	Gallium	125-127	heme oxygenase 1	Homo sapiens	65-69
26834769-7	2015	Furthermore, the application of the HO-1 inducer Ht and nitric oxide (NO) donor sodium nitroprusside (SNP) not only activated HO-1 gene expression, HO activity, and endogenous NO content, but also blocked GA-induced rapid vacuolation and accelerated aleurone layers PCD under drought stress.	Nitric Oxide	56-68	heme oxygenase 1	Homo sapiens	36-40
26834769-7	2015	Furthermore, the application of the HO-1 inducer Ht and nitric oxide (NO) donor sodium nitroprusside (SNP) not only activated HO-1 gene expression, HO activity, and endogenous NO content, but also blocked GA-induced rapid vacuolation and accelerated aleurone layers PCD under drought stress.	Nitric Oxide	56-68	heme oxygenase 1	Homo sapiens	126-130
26834769-7	2015	Furthermore, the application of the HO-1 inducer Ht and nitric oxide (NO) donor sodium nitroprusside (SNP) not only activated HO-1 gene expression, HO activity, and endogenous NO content, but also blocked GA-induced rapid vacuolation and accelerated aleurone layers PCD under drought stress.	Nitroprusside	80-100	heme oxygenase 1	Homo sapiens	36-40
26834769-7	2015	Furthermore, the application of the HO-1 inducer Ht and nitric oxide (NO) donor sodium nitroprusside (SNP) not only activated HO-1 gene expression, HO activity, and endogenous NO content, but also blocked GA-induced rapid vacuolation and accelerated aleurone layers PCD under drought stress.	Nitroprusside	80-100	heme oxygenase 1	Homo sapiens	126-130
26834769-8	2015	However, both HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX) and NO scavenger 2-(4-carboxyphenyl0-4, 4,5,5-tetramethylimidazoline-l-oxyl-3-oxide potassium salt (cPTIO) reserved the effects of Ht and SNP on rice aleurone layer PCD under drought stress by down-regulating endogenous HO-1 and NO, respectively.	zinc protoporphyrin	29-51	heme oxygenase 1	Homo sapiens	14-18
26834769-8	2015	However, both HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX) and NO scavenger 2-(4-carboxyphenyl0-4, 4,5,5-tetramethylimidazoline-l-oxyl-3-oxide potassium salt (cPTIO) reserved the effects of Ht and SNP on rice aleurone layer PCD under drought stress by down-regulating endogenous HO-1 and NO, respectively.	zinc protoporphyrin	53-59	heme oxygenase 1	Homo sapiens	14-18
26834769-8	2015	However, both HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX) and NO scavenger 2-(4-carboxyphenyl0-4, 4,5,5-tetramethylimidazoline-l-oxyl-3-oxide potassium salt (cPTIO) reserved the effects of Ht and SNP on rice aleurone layer PCD under drought stress by down-regulating endogenous HO-1 and NO, respectively.	2-(4-carboxyphenyl0-4, 4,5,5-tetramethylimidazoline-l-oxyl-3-oxide potassium salt	78-159	heme oxygenase 1	Homo sapiens	281-285
26652036-6	2016	Furthermore, heme hydroxylation proceeds three times more slowly, and the oxy-Fe(II) state is 100-fold less stable in HO2 than in HO1.	oxy-fe(ii)	74-84	heme oxygenase 1	Homo sapiens	130-133
26652036-0	2016	Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction Studies.	Heme	32-36	heme oxygenase 1	Homo sapiens	54-78
26652036-1	2016	The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO.	Heme	26-30	heme oxygenase 1	Homo sapiens	42-45
26652036-1	2016	The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO.	Biliverdine	97-107	heme oxygenase 1	Homo sapiens	42-45
26652036-1	2016	The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO.	Iron	109-111	heme oxygenase 1	Homo sapiens	42-45
26652036-1	2016	The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO.	Carbon Monoxide	117-119	heme oxygenase 1	Homo sapiens	42-45
26779023-0	2015	Ferulic Acid Regulates the Nrf2/Heme Oxygenase-1 System and Counteracts Trimethyltin-Induced Neuronal Damage in the Human Neuroblastoma Cell Line SH-SY5Y.	ferulic acid	0-12	heme oxygenase 1	Homo sapiens	32-48
26779023-1	2015	Over the past years, several lines of evidence have pointed out the efficacy of ferulic acid (FA) in counteracting oxidative stress elicited by beta-amyloid or free radical initiators, based on the ability of this natural antioxidant to up-regulate the heme oxygenase-1 (HO-1) and biliverdin reductase (BVR) system.	ferulic acid	80-92	heme oxygenase 1	Homo sapiens	253-269
26779023-1	2015	Over the past years, several lines of evidence have pointed out the efficacy of ferulic acid (FA) in counteracting oxidative stress elicited by beta-amyloid or free radical initiators, based on the ability of this natural antioxidant to up-regulate the heme oxygenase-1 (HO-1) and biliverdin reductase (BVR) system.	ferulic acid	80-92	heme oxygenase 1	Homo sapiens	271-275
26779023-9	2015	All together, these results corroborate the neuroprotective effect of FA through the up-regulation of the HO-1/BVR system, via carbon monoxide and BR formation, and provide the first evidence on the role of HO-1/Nrf2 axis in FA-related enhancement of cell stress response in human neurons.	Carbon Monoxide	127-142	heme oxygenase 1	Homo sapiens	106-114
26779023-9	2015	All together, these results corroborate the neuroprotective effect of FA through the up-regulation of the HO-1/BVR system, via carbon monoxide and BR formation, and provide the first evidence on the role of HO-1/Nrf2 axis in FA-related enhancement of cell stress response in human neurons.	Carbon Monoxide	127-142	heme oxygenase 1	Homo sapiens	106-110
26779023-9	2015	All together, these results corroborate the neuroprotective effect of FA through the up-regulation of the HO-1/BVR system, via carbon monoxide and BR formation, and provide the first evidence on the role of HO-1/Nrf2 axis in FA-related enhancement of cell stress response in human neurons.	Bilirubin	147-149	heme oxygenase 1	Homo sapiens	106-114
26779023-9	2015	All together, these results corroborate the neuroprotective effect of FA through the up-regulation of the HO-1/BVR system, via carbon monoxide and BR formation, and provide the first evidence on the role of HO-1/Nrf2 axis in FA-related enhancement of cell stress response in human neurons.	Bilirubin	147-149	heme oxygenase 1	Homo sapiens	106-110
26430779-7	2016	The sTNF-alphaR-Fc/HO-1 group showed the best glucose tolerance.	Glucose	46-53	heme oxygenase 1	Homo sapiens	19-23
26631587-9	2016	Key messages Bilirubin levels are inversely related to cardiovascular disease, and overexpression of heme oxygenase-1 (the enzyme that determines bilirubin production) has prevented post-infarction ventricular remodeling in experimental animals, but the association between bilirubin levels and the progression of ventricular volumes and function in patients with acute myocardial infarction remained unexplored.	Bilirubin	274-283	heme oxygenase 1	Homo sapiens	101-117
26759705-4	2016	Furthermore, RA increased the expression and activity of superoxide dismutase, catalase, heme oxygenase-1, and their transcription factor Nrf2, which are decreased by UVB radiation.	rosmarinic acid	13-15	heme oxygenase 1	Homo sapiens	89-105
27251503-3	2016	Although hemin treatment caused the increased expression of heme oxygenase (HO)-1, the inhibition of HO activity resulted in the aggravation of hemin-induced barrier dysfunction.	Hemin	9-14	heme oxygenase 1	Homo sapiens	60-81
27080946-0	2016	Tanshinone IIA Induces Heme Oxygenase 1 Expression and Inhibits Cyclic Strain-Induced Interleukin 8 Expression in Vascular Endothelial Cells.	tanshinone	0-10	heme oxygenase 1	Homo sapiens	23-39
27080946-6	2016	HO-1 silencing significantly abrogated the repressive effects of tanshinone IIA on strain-induced IL-8 expression, which suggests HO-1 has a role in mediating the effects of tanshinone IIA.	tanshinone	65-75	heme oxygenase 1	Homo sapiens	0-4
27080946-6	2016	HO-1 silencing significantly abrogated the repressive effects of tanshinone IIA on strain-induced IL-8 expression, which suggests HO-1 has a role in mediating the effects of tanshinone IIA.	tanshinone	65-75	heme oxygenase 1	Homo sapiens	130-134
27080946-6	2016	HO-1 silencing significantly abrogated the repressive effects of tanshinone IIA on strain-induced IL-8 expression, which suggests HO-1 has a role in mediating the effects of tanshinone IIA.	tanshinone	65-79	heme oxygenase 1	Homo sapiens	0-4
27080946-6	2016	HO-1 silencing significantly abrogated the repressive effects of tanshinone IIA on strain-induced IL-8 expression, which suggests HO-1 has a role in mediating the effects of tanshinone IIA.	tanshinone	65-79	heme oxygenase 1	Homo sapiens	130-134
27080946-7	2016	This study reports for the first time that tanshinone IIA inhibits cyclic strain-induced IL-8 expression via the induction of HO-1 in endothelial cells, providing valuable new insight into the molecular pathways that may contribute to the effects of tanshinone IIA.	tanshinone	43-53	heme oxygenase 1	Homo sapiens	126-130
27080946-7	2016	This study reports for the first time that tanshinone IIA inhibits cyclic strain-induced IL-8 expression via the induction of HO-1 in endothelial cells, providing valuable new insight into the molecular pathways that may contribute to the effects of tanshinone IIA.	tanshinone	250-260	heme oxygenase 1	Homo sapiens	126-130
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	Technetium	29-31	heme oxygenase 1	Homo sapiens	97-118
26277982-5	2016	In addition, DMHC induced HO-1 expression as well as NRF2 activation.	dmhc	13-17	heme oxygenase 1	Homo sapiens	26-30
26277982-6	2016	Furthermore, HO-1 knockdown using siRNA reversed the inhibitory effect of DMHC on TNF-alpha-induced ICAM-1 expression and adhesion of monocytes to keratinocytes.	dmhc	74-78	heme oxygenase 1	Homo sapiens	13-17
26277982-7	2016	These results suggest that DMHC may inhibit TNF-alpha-induced ICAM-1 expression and adhesion of monocytes to keratinocytes by suppressing the signaling cascades leading to NF-kappaB activation and inducing HO-1 expression in keratinocytes.	dmhc	27-31	heme oxygenase 1	Homo sapiens	206-210
27412411-1	2016	Heme oxygenase 1 (HO-1) is an inducible stress-response enzyme that not only catalyzes the degradation of heme (e.g., released from erythrocytes) but also has an important function in various physiological and pathophysiological states associated with cellular stress, such as ischemic/reperfusion injury.	Heme	106-110	heme oxygenase 1	Homo sapiens	0-16
27412411-1	2016	Heme oxygenase 1 (HO-1) is an inducible stress-response enzyme that not only catalyzes the degradation of heme (e.g., released from erythrocytes) but also has an important function in various physiological and pathophysiological states associated with cellular stress, such as ischemic/reperfusion injury.	Heme	106-110	heme oxygenase 1	Homo sapiens	18-22
26277982-0	2016	2,3-Dimethoxy-2"-hydroxychalcone ameliorates TNF-alpha-induced ICAM-1 expression and subsequent monocyte adhesiveness via NF-kappaB inhibition and HO-1 induction in HaCaT cells.	2,3-dimethoxy-2'-hydroxychalcone	0-32	heme oxygenase 1	Homo sapiens	147-151
27322610-6	2016	HO-1 knockdown experiments were done to confirm its role in the action of periostin in high glucose-exposed HUVECs.	Glucose	92-99	heme oxygenase 1	Homo sapiens	0-4
27322610-11	2016	HO-1 silencing restored high glucose-induced ROS generation and apoptotic response in periostin-overexpressing HUVECs.	Glucose	29-36	heme oxygenase 1	Homo sapiens	0-4
27322610-11	2016	HO-1 silencing restored high glucose-induced ROS generation and apoptotic response in periostin-overexpressing HUVECs.	Reactive Oxygen Species	45-48	heme oxygenase 1	Homo sapiens	0-4
27322610-12	2016	CONCLUSION: Periostin mitigates high glucose-induced mitochondrial apoptosis in endothelial cells, via activation of Nrf2/HO-1 signaling and reduction of ROS formation.	Glucose	37-44	heme oxygenase 1	Homo sapiens	122-126
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	Technetium	29-31	heme oxygenase 1	Homo sapiens	136-140
27412411-7	2016	Our results indicate that HO-1 is an inhibitor of hematopoietic cell migration in response to crucial BM homing chemoattractants such as stromal-derived factor 1 (SDF-1) and sphingosine-1-phosphate (S1P).	sphingosine 1-phosphate	174-197	heme oxygenase 1	Homo sapiens	26-30
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	zinc protoporphyrin	50-72	heme oxygenase 1	Homo sapiens	97-118
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	zinc protoporphyrin	50-72	heme oxygenase 1	Homo sapiens	136-140
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	zinc protoporphyrin	74-78	heme oxygenase 1	Homo sapiens	97-118
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	zinc protoporphyrin	74-78	heme oxygenase 1	Homo sapiens	136-140
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	Technetium	186-188	heme oxygenase 1	Homo sapiens	97-118
27383847-6	2016	All those effects induced by TC were inhibited by zinc protoporphyrin IX (ZnPP), an inhibitor of heme oxygenase (HO)-1, indicating that HO-1 was responsible the anti-psoriatic effect of TC.	Technetium	186-188	heme oxygenase 1	Homo sapiens	136-140
27383847-9	2016	Overexpression of p65 NF-x03BA;B significantly suppressed TC-induced decrease of TNFalpha, IL-17A and IL-23 expression and keratinocyte proliferation, indicating that HO-1-mediated downregulation of NF-x03BA;B was involved in the anti-psoriatic effect of TC.	Technetium	58-60	heme oxygenase 1	Homo sapiens	167-171
27383847-9	2016	Overexpression of p65 NF-x03BA;B significantly suppressed TC-induced decrease of TNFalpha, IL-17A and IL-23 expression and keratinocyte proliferation, indicating that HO-1-mediated downregulation of NF-x03BA;B was involved in the anti-psoriatic effect of TC.	Technetium	255-257	heme oxygenase 1	Homo sapiens	167-171
26865999-5	2016	Cultures of normal human melanocytes were treated with the HO-1 inducer cobalt protoporphyrin (CoPP) or the HO-1 inhibitor zinc protoporphyrin (ZnPP).	zinc protoporphyrin	123-142	heme oxygenase 1	Homo sapiens	108-112
26573721-0	2016	Vanadium(III)-L-cysteine protects cisplatin-induced nephropathy through activation of Nrf2/HO-1 pathway.	vanadium(III)-cysteine	0-24	heme oxygenase 1	Homo sapiens	91-95
27558512-5	2016	Macrophage treatment with the iron oxide NPs showed a dose-dependent increase of heme oxygenase 1 (HO-1) and NAD(P)H:quinone oxidoreductase (NQO-1).	ferric oxide	30-40	heme oxygenase 1	Homo sapiens	81-97
26573721-0	2016	Vanadium(III)-L-cysteine protects cisplatin-induced nephropathy through activation of Nrf2/HO-1 pathway.	Cisplatin	34-43	heme oxygenase 1	Homo sapiens	91-95
26573721-11	2016	VC-III administration also stimulated Nrf2-mediated antioxidant defense system by promotion of downstream antioxidant enzymes, such as HO-1.	vc-iii	0-6	heme oxygenase 1	Homo sapiens	135-139
27764834-10	2016	Nuclear Nrf2 protein and HO-1 mRNA levels were both increased in the HTR-8/SVneo cell line following stimulation with tBHQ (p &lt; 0.05).	2-tert-butylhydroquinone	118-122	heme oxygenase 1	Homo sapiens	25-29
26602157-4	2016	Among the genes upregulated in response to manumycin were HMOX-1, TNFRSF10A, IL-1R1, TICAM2, NLRP12 after 4h and only IL-1R1 after 8h.	manumycin	43-52	heme oxygenase 1	Homo sapiens	58-64
26386740-0	2016	Chlorogenic acid improves ex vivo vessel function and protects endothelial cells against HOCl-induced oxidative damage, via increased production of nitric oxide and induction of Hmox-1.	Chlorogenic Acid	0-16	heme oxygenase 1	Homo sapiens	178-184
26403645-6	2016	Knockdown of p62, quinone oxidoreductase-1, heme oxygenase-1, and ferritin heavy chain-1 by RNA interference in HCC cells promoted ferroptosis in response to erastin and sorafenib.	erastin	158-165	heme oxygenase 1	Homo sapiens	18-60
26403645-6	2016	Knockdown of p62, quinone oxidoreductase-1, heme oxygenase-1, and ferritin heavy chain-1 by RNA interference in HCC cells promoted ferroptosis in response to erastin and sorafenib.	Sorafenib	170-179	heme oxygenase 1	Homo sapiens	18-60
26302870-1	2016	Previous studies indicated the potential of zinc protoporphyrin (ZnPP) as an antitumor agent targeting to the tumor survival factor heme oxygenase-1, and/or for photodynamic therapy (PDT).	zinc protoporphyrin	44-63	heme oxygenase 1	Homo sapiens	132-148
26302870-1	2016	Previous studies indicated the potential of zinc protoporphyrin (ZnPP) as an antitumor agent targeting to the tumor survival factor heme oxygenase-1, and/or for photodynamic therapy (PDT).	zinc protoporphyrin	65-69	heme oxygenase 1	Homo sapiens	132-148
26058377-9	2016	D006 promoted the expression of HO-1 protein in a time-dependent manner while the HO-1 inhibitor, Znpp, reversed the protective effects of D006.	d006	0-4	heme oxygenase 1	Homo sapiens	32-36
26058377-9	2016	D006 promoted the expression of HO-1 protein in a time-dependent manner while the HO-1 inhibitor, Znpp, reversed the protective effects of D006.	zinc protoporphyrin	98-102	heme oxygenase 1	Homo sapiens	82-86
26058377-9	2016	D006 promoted the expression of HO-1 protein in a time-dependent manner while the HO-1 inhibitor, Znpp, reversed the protective effects of D006.	d006	139-143	heme oxygenase 1	Homo sapiens	82-86
26058377-11	2016	In conclusion, our results indicate that a new DSS derivative exhibits promising protective effects against Dox-induced cardiotoxicity both in vivo and in vitro, an effect at least partially mediated by induction of HO-1 expression and the activation of mitochondrial biogenesis.	3,4-dihydroxyphenyllactic acid	47-50	heme oxygenase 1	Homo sapiens	216-220
26058377-11	2016	In conclusion, our results indicate that a new DSS derivative exhibits promising protective effects against Dox-induced cardiotoxicity both in vivo and in vitro, an effect at least partially mediated by induction of HO-1 expression and the activation of mitochondrial biogenesis.	Doxorubicin	108-111	heme oxygenase 1	Homo sapiens	216-220
26630500-5	2016	Additionally, these Pb concentrations induced oxidative stress in HepG2 cells in terms of production of reactive oxygen species (ROS) and induced heme oxygenase-1 mRNA expression in a concentration-dependent phenomenon.	Lead	20-22	heme oxygenase 1	Homo sapiens	146-162
26386740-0	2016	Chlorogenic acid improves ex vivo vessel function and protects endothelial cells against HOCl-induced oxidative damage, via increased production of nitric oxide and induction of Hmox-1.	Hypochlorous Acid	89-93	heme oxygenase 1	Homo sapiens	178-184
27110594-4	2016	Relative to WT mice, mice globally overexpressing human HO-1 were protected from DOX-induced dilated cardiomyopathy, cardiac cytoarchitectural derangement, and infiltration of CD11b+ mononuclear phagocytes.	Doxorubicin	81-84	heme oxygenase 1	Homo sapiens	56-60
27057275-0	2016	Synergistic Effects of Cilostazol and Probucol on ER Stress-Induced Hepatic Steatosis via Heme Oxygenase-1-Dependent Activation of Mitochondrial Biogenesis.	Cilostazol	23-33	heme oxygenase 1	Homo sapiens	90-106
26542248-6	2016	We further demonstrated that HO-1 could be induced by PbAc through the P38, ERK1/2, and PI3K/AKT signaling pathways in a ROS-dependent manner and through the JNK pathway in a ROS-independent manner.	Reactive Oxygen Species	121-124	heme oxygenase 1	Homo sapiens	29-33
26542248-6	2016	We further demonstrated that HO-1 could be induced by PbAc through the P38, ERK1/2, and PI3K/AKT signaling pathways in a ROS-dependent manner and through the JNK pathway in a ROS-independent manner.	Reactive Oxygen Species	175-178	heme oxygenase 1	Homo sapiens	29-33
26542248-7	2016	Further investigation revealed that HO-1 overexpression significantly restrained cell apoptosis and ROS production induced by PbAc in SH-SY5Y cells.	Reactive Oxygen Species	100-103	heme oxygenase 1	Homo sapiens	36-40
26542248-8	2016	Moreover, HO-1 knockdown aggravated PbAc-induced cell apoptosis and ROS production.	Reactive Oxygen Species	68-71	heme oxygenase 1	Homo sapiens	10-14
26798413-0	2016	t-BHQ Provides Protection against Lead Neurotoxicity via Nrf2/HO-1 Pathway.	2-tert-butylhydroquinone	0-5	heme oxygenase 1	Homo sapiens	62-66
26798413-10	2016	However, knockdown of Nrf2 or HO-1 adversely affected the protective effects of t-BHQ against lead toxicity in SH-SY5Y cells.	2-tert-butylhydroquinone	80-85	heme oxygenase 1	Homo sapiens	30-34
26798413-11	2016	Thus, t-BHQ can protect against lead neurotoxicity, depending on the Nrf2/HO-1 pathway.	2-tert-butylhydroquinone	6-11	heme oxygenase 1	Homo sapiens	74-78
27057275-0	2016	Synergistic Effects of Cilostazol and Probucol on ER Stress-Induced Hepatic Steatosis via Heme Oxygenase-1-Dependent Activation of Mitochondrial Biogenesis.	Probucol	38-46	heme oxygenase 1	Homo sapiens	90-106
26765462-4	2016	Addition of ALA strongly attenuated ROS production and further increased HO-1 expression.	Thioctic Acid	12-15	heme oxygenase 1	Homo sapiens	73-77
26765462-5	2016	However, by pretreatment of zinc protoporphyrin (ZnPP), HO-1 inhibitor, ALA inhibition of ROS generation by H2O2 was abolished.	Thioctic Acid	72-75	heme oxygenase 1	Homo sapiens	56-60
26765462-5	2016	However, by pretreatment of zinc protoporphyrin (ZnPP), HO-1 inhibitor, ALA inhibition of ROS generation by H2O2 was abolished.	Reactive Oxygen Species	90-93	heme oxygenase 1	Homo sapiens	56-60
26765462-5	2016	However, by pretreatment of zinc protoporphyrin (ZnPP), HO-1 inhibitor, ALA inhibition of ROS generation by H2O2 was abolished.	Hydrogen Peroxide	108-112	heme oxygenase 1	Homo sapiens	56-60
27034731-3	2016	The results showed that these anthocyanins decreased the levels of ROS and XO-1 but increased the levels of SOD and HO-1.	Anthocyanins	30-42	heme oxygenase 1	Homo sapiens	116-120
27313828-7	2016	SPRC-induced HO-1 expression and Nrf2 translocation were abolished by the phosphoinositide 3-kinase (PI3K) inhibitor LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	117-125	heme oxygenase 1	Homo sapiens	13-17
26680374-1	2016	BACKGROUND: The enzyme heme oxygenase-1 (HO-1) degrades heme and protects against ischemia-reperfusion injury.	Heme	23-27	heme oxygenase 1	Homo sapiens	41-45
27313828-8	2016	Moreover, the antioxidative effect of SPRC was abolished by CSE inhibitor DL-propargylglycine (PAG) and HO-1 siRNA.	S-propargylcysteine	38-42	heme oxygenase 1	Homo sapiens	104-108
27313828-9	2016	Therefore, these results proved that SPRC produced an antioxidative effect on NAFLD through the PI3K/Akt/Nrf2/HO-1 signaling pathway.	S-propargylcysteine	37-41	heme oxygenase 1	Homo sapiens	110-114
27050899-7	2016	We demonstrated that nicorandil increased HO-1 expression in HUVECs.	Nicorandil	21-31	heme oxygenase 1	Homo sapiens	42-46
27050899-8	2016	In addition, cobalt protoporphyrin (10 mumol/l), an inducer of HO-1 expression, mimicked the effects of nicorandil and inhibited IL-8 expression under cyclic strain, whereas zinc protoporphyrin IX (10 mumol/l), an inhibitor of HO-1 expression, antagonized the effect of nicorandil.	cobaltiprotoporphyrin	13-34	heme oxygenase 1	Homo sapiens	63-67
27050899-8	2016	In addition, cobalt protoporphyrin (10 mumol/l), an inducer of HO-1 expression, mimicked the effects of nicorandil and inhibited IL-8 expression under cyclic strain, whereas zinc protoporphyrin IX (10 mumol/l), an inhibitor of HO-1 expression, antagonized the effect of nicorandil.	cobaltiprotoporphyrin	13-34	heme oxygenase 1	Homo sapiens	227-231
27050899-8	2016	In addition, cobalt protoporphyrin (10 mumol/l), an inducer of HO-1 expression, mimicked the effects of nicorandil and inhibited IL-8 expression under cyclic strain, whereas zinc protoporphyrin IX (10 mumol/l), an inhibitor of HO-1 expression, antagonized the effect of nicorandil.	Nicorandil	104-114	heme oxygenase 1	Homo sapiens	63-67
27050899-9	2016	HO-1 silencing significantly abrogated the inhibitory effects of nicorandil on cyclic strain-induced IL-8 expression, suggesting that HO-1 plays a role in the mechanism of action of nicorandil.	Nicorandil	65-75	heme oxygenase 1	Homo sapiens	0-4
27050899-9	2016	HO-1 silencing significantly abrogated the inhibitory effects of nicorandil on cyclic strain-induced IL-8 expression, suggesting that HO-1 plays a role in the mechanism of action of nicorandil.	Nicorandil	65-75	heme oxygenase 1	Homo sapiens	134-138
27050899-9	2016	HO-1 silencing significantly abrogated the inhibitory effects of nicorandil on cyclic strain-induced IL-8 expression, suggesting that HO-1 plays a role in the mechanism of action of nicorandil.	Nicorandil	182-192	heme oxygenase 1	Homo sapiens	0-4
27050899-9	2016	HO-1 silencing significantly abrogated the inhibitory effects of nicorandil on cyclic strain-induced IL-8 expression, suggesting that HO-1 plays a role in the mechanism of action of nicorandil.	Nicorandil	182-192	heme oxygenase 1	Homo sapiens	134-138
27050899-10	2016	KEY MESSAGES: This study is the first to report that nicorandil inhibits cyclic strain-induced IL-8 expression through the induction of HO-1 expression in HUVECs.	Nicorandil	53-63	heme oxygenase 1	Homo sapiens	136-140
26681956-2	2016	To examine the mechanisms by which this occurs, we hypothesized that an increase in heme oxygenase 1, a potent antioxidant gene, will decrease uric acid levels and adipocyte dysfunction via suppression of ROS and xanthine oxidase (XO) levels.	Uric Acid	143-152	heme oxygenase 1	Homo sapiens	84-100
26681956-2	2016	To examine the mechanisms by which this occurs, we hypothesized that an increase in heme oxygenase 1, a potent antioxidant gene, will decrease uric acid levels and adipocyte dysfunction via suppression of ROS and xanthine oxidase (XO) levels.	ros	205-208	heme oxygenase 1	Homo sapiens	84-100
26515032-4	2016	Recent reports indicate that HO-1/HO-2 protein expression and HO activity have several important roles in hemostasis and reactive oxygen species (ROS)-dependent perturbations associated with metabolic syndrome.	Reactive Oxygen Species	121-144	heme oxygenase 1	Homo sapiens	29-38
26515032-4	2016	Recent reports indicate that HO-1/HO-2 protein expression and HO activity have several important roles in hemostasis and reactive oxygen species (ROS)-dependent perturbations associated with metabolic syndrome.	Reactive Oxygen Species	146-149	heme oxygenase 1	Homo sapiens	29-38
27313828-0	2016	S-Propargyl-cysteine Exerts a Novel Protective Effect on Methionine and Choline Deficient Diet-Induced Fatty Liver via Akt/Nrf2/HO-1 Pathway.	S-propargylcysteine	0-20	heme oxygenase 1	Homo sapiens	128-132
27578289-3	2016	In the present study, we have investigated the effects of bortezomib, a clinically used proteasome inhibitor, on the regulation of HO-1 and COX-2 in cultured human microvascular endothelial cells (HMECs).	Bortezomib	58-68	heme oxygenase 1	Homo sapiens	131-135
27578289-4	2016	Bortezomib treatment of HMECS induced dose- and time-dependent expression of HO-1 and COX-2 mRNA and protein, and triggered nuclear translocation of nuclear factor erythroid 2-related transcription factor (Nrf2).	Bortezomib	0-10	heme oxygenase 1	Homo sapiens	77-81
27578289-5	2016	These findings suggest that HO-1/COX-2-mediated induction of antioxidant mechanisms via Nrf2 activation may contribute to the cytoprotective effects of bortezomib in microvascular endothelium.	Bortezomib	152-162	heme oxygenase 1	Homo sapiens	28-32
28124024-0	2016	Iron Supplementation Alters Heme and Heme Oxygenase 1 (HO-1) Levels In Pregnant Women in Ghana.	Iron	0-4	heme oxygenase 1	Homo sapiens	37-53
28124024-0	2016	Iron Supplementation Alters Heme and Heme Oxygenase 1 (HO-1) Levels In Pregnant Women in Ghana.	Iron	0-4	heme oxygenase 1	Homo sapiens	55-59
28124024-4	2016	We hypothesized that pregnant women with malaria who took iron supplements will have higher levels of Heme/HO-1 than those who did not take iron supplements.	Iron	58-62	heme oxygenase 1	Homo sapiens	107-111
26166253-2	2016	HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR).	Carbon Monoxide	132-147	heme oxygenase 1	Homo sapiens	0-4
26166253-2	2016	HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR).	Carbon Monoxide	149-151	heme oxygenase 1	Homo sapiens	0-4
26166253-2	2016	HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR).	Iron	154-158	heme oxygenase 1	Homo sapiens	0-4
26166253-2	2016	HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR).	Biliverdine	164-182	heme oxygenase 1	Homo sapiens	0-4
26166253-2	2016	HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR).	Bilirubin	222-239	heme oxygenase 1	Homo sapiens	0-4
29668174-0	2016	Induction of Heme oxygenase 1 protects hepatocytes from Isoniazid - Rifampicin induced cell death: an in vitro study.	isoniazid - rifampicin	56-78	heme oxygenase 1	Homo sapiens	13-29
29668174-5	2016	The E47 cells were treated with hemin chloride to induce HO-1 expression during INH-RMP treatment.	Hemin	32-46	heme oxygenase 1	Homo sapiens	57-61
29668174-10	2016	Addition of Hemin chloride during treatment of INH-RMP induced HO-1 in E47 cells and reversed the drug induced liver injury.	Hemin	12-26	heme oxygenase 1	Homo sapiens	63-67
29668174-11	2016	Silencing the HO-1 gene using siRNA potentiated INH-RMP induced cell death of the E47 cells Conclusion: Induction of HO-1 ameliorated INH-RMP induced cell death of hepatocytes.	inh-rmp	48-55	heme oxygenase 1	Homo sapiens	14-18
29668174-11	2016	Silencing the HO-1 gene using siRNA potentiated INH-RMP induced cell death of the E47 cells Conclusion: Induction of HO-1 ameliorated INH-RMP induced cell death of hepatocytes.	inh-rmp	48-55	heme oxygenase 1	Homo sapiens	117-121
26680374-3	2016	Heme arginate (HA) safely induces HO-1 in humans.	heme arginate	0-13	heme oxygenase 1	Homo sapiens	34-38
26680374-3	2016	Heme arginate (HA) safely induces HO-1 in humans.	heme arginate	15-17	heme oxygenase 1	Homo sapiens	34-38
26680374-12	2016	Heme arginate increased day 5 tissue HO-1 protein immunopositivity compared with placebo: HA 0.21 versus placebo -0.03 (P = 0.02) and % HO-1-positive renal macrophage also increased: HA 50.8 cells per high power field versus placebo 22.3 (P = 0.012).	heme arginate	0-13	heme oxygenase 1	Homo sapiens	37-41
26680374-12	2016	Heme arginate increased day 5 tissue HO-1 protein immunopositivity compared with placebo: HA 0.21 versus placebo -0.03 (P = 0.02) and % HO-1-positive renal macrophage also increased: HA 50.8 cells per high power field versus placebo 22.3 (P = 0.012).	heme arginate	0-13	heme oxygenase 1	Homo sapiens	136-140
27725392-5	2016	Under the gaseous phase administration, acetic acid and mixed acids caused a slight increase, decrease and increase on the interleukin-8 production, the mRNA expression of the heme oxygenase-1 (HO-1) gene and the HO-1 production, respectively, at one or more time points.	Acetic Acid	40-51	heme oxygenase 1	Homo sapiens	176-192
27725392-5	2016	Under the gaseous phase administration, acetic acid and mixed acids caused a slight increase, decrease and increase on the interleukin-8 production, the mRNA expression of the heme oxygenase-1 (HO-1) gene and the HO-1 production, respectively, at one or more time points.	Acetic Acid	40-51	heme oxygenase 1	Homo sapiens	194-198
27725392-5	2016	Under the gaseous phase administration, acetic acid and mixed acids caused a slight increase, decrease and increase on the interleukin-8 production, the mRNA expression of the heme oxygenase-1 (HO-1) gene and the HO-1 production, respectively, at one or more time points.	Acetic Acid	40-51	heme oxygenase 1	Homo sapiens	213-217
26670903-11	2015	CONCLUSION: In summary, the present study showed that HO-1 attenuates the Cd-induced caspase 3 dependent pathway of apoptosis in HepG2 cells, probably by modulating Cd-induced oxidative stress.	Cadmium	74-76	heme oxygenase 1	Homo sapiens	54-58
26690352-6	2015	Pharmacological induction of HO-1 with cobalt-protoporphyrin IX reduced, whereas inhibition of HO-1 with either zinc-protoporphyrin IX or siRNA-mediated knockdown increased HLA I Ab-dependent up-regulation of VCAM-1.	cobaltiprotoporphyrin	39-63	heme oxygenase 1	Homo sapiens	29-33
26690352-6	2015	Pharmacological induction of HO-1 with cobalt-protoporphyrin IX reduced, whereas inhibition of HO-1 with either zinc-protoporphyrin IX or siRNA-mediated knockdown increased HLA I Ab-dependent up-regulation of VCAM-1.	zinc protoporphyrin	112-134	heme oxygenase 1	Homo sapiens	95-99
26782424-0	2015	Role of heme oxygenase-1 in demethylating effects on SKM-1 cells induced by decitabine.	Decitabine	76-86	heme oxygenase 1	Homo sapiens	8-24
26782424-1	2015	We evaluated the influence of heme oxygenase-1 (HO-1) gene inhibition in myelodysplastic syndrome (MDS) cell line SKM-1 on enhancement of the demethylating effects of decitabine on p15, and explored the possible mechanism.	Decitabine	167-177	heme oxygenase 1	Homo sapiens	48-52
26782424-7	2015	CCK-8 assay showed that after HO-1 gene expression was inhibited; the proliferation rate of SKM-1 cells treated by decitabine (70.91 +- 0.05%) was significantly higher than that of the control group (53.67 +- 0.05%).	Decitabine	115-125	heme oxygenase 1	Homo sapiens	30-34
26782424-8	2015	Flow cytometry showed that the apoptotic rate of SKM- 1 cells treated by decitabine in combination with HO-1 expression inhibition (44.25 +- 0.05%) exceeded that of the cells treated by this drug alone (37.70 +- 0.05%).	Decitabine	73-83	heme oxygenase 1	Homo sapiens	104-108
26782424-10	2015	As suggested by western blot, the degree of methylation of the p15 protein was changed after decitabine treatment when the expression of the HO-1 protein was changed, being associated with the affected DNMT1 expression.	Decitabine	93-103	heme oxygenase 1	Homo sapiens	141-145
26782424-11	2015	Inhibited HO-1 expression attenuated the hypermethylation of CDKN2B by suppressing DNMT1, which was conducive to treatment by cooperating with decitabine.	Decitabine	143-153	heme oxygenase 1	Homo sapiens	10-14
26670903-0	2015	Heme oxygenase-1 attenuates cadmium-induced mitochondrial-caspase 3- dependent apoptosis in human hepatoma cell line.	Cadmium	28-35	heme oxygenase 1	Homo sapiens	0-16
26670903-2	2015	In this study, we examined the role of heme oxygenase-1 (HO-1) in modulating the Cd-induced apoptosis in human hepatoma (HepG2) cells after 24 h exposure.	Cadmium	81-83	heme oxygenase 1	Homo sapiens	39-55
26670903-2	2015	In this study, we examined the role of heme oxygenase-1 (HO-1) in modulating the Cd-induced apoptosis in human hepatoma (HepG2) cells after 24 h exposure.	Cadmium	81-83	heme oxygenase 1	Homo sapiens	57-61
26670903-11	2015	CONCLUSION: In summary, the present study showed that HO-1 attenuates the Cd-induced caspase 3 dependent pathway of apoptosis in HepG2 cells, probably by modulating Cd-induced oxidative stress.	Cadmium	165-167	heme oxygenase 1	Homo sapiens	54-58
26655408-6	2015	RESULTS: Oleacein (OC) together with complexes HbHp11 or HbHp22 stimulated the expression of CD163 (30-100-fold), IL-10 (170-300-fold) and HO-1 secretion (60-130-fold) after 5 days of coincubation.	oleacein	9-17	heme oxygenase 1	Homo sapiens	139-143
26423448-1	2015	The phenomenon that heme oxygenase-1 (HO-1) protects cell from injury yet its enzymatic product, iron, may facilitate generation of free radical has been long puzzling.	Iron	97-101	heme oxygenase 1	Homo sapiens	20-36
26674355-2	2015	Our previous study demonstrated that the flavonoid hyperoside elicits cytoprotection against oxidative stress by activating the Keap1-Nrf2-ARE signaling pathway, thus increasing the expression of antioxidant enzymes, such as heme oxygenase-1 (HO-1), superoxide dismutase (SOD) and catalase.	Flavonoids	41-50	heme oxygenase 1	Homo sapiens	225-241
26674355-2	2015	Our previous study demonstrated that the flavonoid hyperoside elicits cytoprotection against oxidative stress by activating the Keap1-Nrf2-ARE signaling pathway, thus increasing the expression of antioxidant enzymes, such as heme oxygenase-1 (HO-1), superoxide dismutase (SOD) and catalase.	Flavonoids	41-50	heme oxygenase 1	Homo sapiens	243-247
26674355-2	2015	Our previous study demonstrated that the flavonoid hyperoside elicits cytoprotection against oxidative stress by activating the Keap1-Nrf2-ARE signaling pathway, thus increasing the expression of antioxidant enzymes, such as heme oxygenase-1 (HO-1), superoxide dismutase (SOD) and catalase.	hyperoside	51-61	heme oxygenase 1	Homo sapiens	225-241
26674355-2	2015	Our previous study demonstrated that the flavonoid hyperoside elicits cytoprotection against oxidative stress by activating the Keap1-Nrf2-ARE signaling pathway, thus increasing the expression of antioxidant enzymes, such as heme oxygenase-1 (HO-1), superoxide dismutase (SOD) and catalase.	hyperoside	51-61	heme oxygenase 1	Homo sapiens	243-247
26674355-6	2015	Further study showed that LiCl and siRNA-mediated inhibition of GSK-3beta increased hyperoside-induced HO-1 expression, and the effect was dependent upon enhanced Nrf2 nuclear translocation and gene expression.	hyperoside	84-94	heme oxygenase 1	Homo sapiens	103-107
26674355-8	2015	Furthermore, the siRNA-mediated inhibition of Keap1 also enhanced hyperoside-induced Nrf2 nuclear accumulation and HO-1 expression, which was relatively smaller than the effects obtained from GSK-3beta siRNA administration.	hyperoside	66-76	heme oxygenase 1	Homo sapiens	115-119
26674585-0	2015	Effect of oral N-acetylcysteine on COPD patients with microsatellite polymorphism in the heme oxygenase-1 gene promoter.	Acetylcysteine	15-31	heme oxygenase 1	Homo sapiens	89-105
26783548-5	2016	RESULTS: Monocytes from multiple sclerosis (MS) patients receiving DMF had reduced expression of the proinflammatory micro-RNA miR-155 and of antioxidant genes HMOX1 and OSGIN1 compared to untreated MS patients; similar changes were observed in patients receiving FTY720 and/or natalizumab.	Dimethyl Fumarate	67-70	heme oxygenase 1	Homo sapiens	160-165
26783548-6	2016	In vitro addition of DMF but not MMF to MDMs and microglia inhibited lipopolysaccharide-induced production of inflammatory cytokines and increased expression of the antioxidant gene HMOX1 in the absence of significant cytotoxicity.	Dimethyl Fumarate	21-24	heme oxygenase 1	Homo sapiens	182-187
26163109-6	2015	Moreover, the HO-1 inducers, resveratrol and piceatannol decrease the expression of miR-183, resulting in attenuated osteoclastogenesis.	3,3',4,5'-tetrahydroxystilbene	45-56	heme oxygenase 1	Homo sapiens	14-18
26423448-1	2015	The phenomenon that heme oxygenase-1 (HO-1) protects cell from injury yet its enzymatic product, iron, may facilitate generation of free radical has been long puzzling.	Iron	97-101	heme oxygenase 1	Homo sapiens	38-42
26423448-6	2015	RNA interference of HO-1 makes the cell more susceptible to hydrogen peroxide, which can be rescued by forced expression of wild-type FHC but not mutants that lose the capacity of iron storage and ferroxidase activity.	Hydrogen Peroxide	60-77	heme oxygenase 1	Homo sapiens	20-24
26423448-6	2015	RNA interference of HO-1 makes the cell more susceptible to hydrogen peroxide, which can be rescued by forced expression of wild-type FHC but not mutants that lose the capacity of iron storage and ferroxidase activity.	Iron	180-184	heme oxygenase 1	Homo sapiens	20-24
26670322-7	2015	In addition, the induction of HO-1 was also confirmed in normal fibroblasts following incubation with 10-100 micromol/L NAC for 4 h. RESULTS: Following NAC therapy we observed an increase in expression of the antioxidants HO-1 (~4-fold) and its effector ferritin (~160-fold) in patient samples as compared with baseline.	Acetylcysteine	120-123	heme oxygenase 1	Homo sapiens	30-34
26670322-7	2015	In addition, the induction of HO-1 was also confirmed in normal fibroblasts following incubation with 10-100 micromol/L NAC for 4 h. RESULTS: Following NAC therapy we observed an increase in expression of the antioxidants HO-1 (~4-fold) and its effector ferritin (~160-fold) in patient samples as compared with baseline.	Acetylcysteine	120-123	heme oxygenase 1	Homo sapiens	222-226
26670322-7	2015	In addition, the induction of HO-1 was also confirmed in normal fibroblasts following incubation with 10-100 micromol/L NAC for 4 h. RESULTS: Following NAC therapy we observed an increase in expression of the antioxidants HO-1 (~4-fold) and its effector ferritin (~160-fold) in patient samples as compared with baseline.	Acetylcysteine	152-155	heme oxygenase 1	Homo sapiens	30-34
26670322-7	2015	In addition, the induction of HO-1 was also confirmed in normal fibroblasts following incubation with 10-100 micromol/L NAC for 4 h. RESULTS: Following NAC therapy we observed an increase in expression of the antioxidants HO-1 (~4-fold) and its effector ferritin (~160-fold) in patient samples as compared with baseline.	Acetylcysteine	152-155	heme oxygenase 1	Homo sapiens	222-226
26087413-9	2015	HO-1 inhibitor and Nrf2 siRNA blocked the milk-induced inflammatory response such as production of ROS, expression of cytokines, chemokines, and MMPs.	Reactive Oxygen Species	99-102	heme oxygenase 1	Homo sapiens	0-4
26670322-8	2015	We also observed that NAC exposure significantly increased HO-1 expression in fibroblasts.	Acetylcysteine	22-25	heme oxygenase 1	Homo sapiens	59-63
26670322-9	2015	CONCLUSION: Our data suggest that HO-1 is a possible target protein of NAC and a mediator of its cytoprotective effects in these patients.	Acetylcysteine	71-74	heme oxygenase 1	Homo sapiens	34-38
26461179-1	2015	Heme-oxygenase 1 (HO-1) prevents T cell-mediated inflammatory disease by producing carbon monoxide (CO) and impairing DC immunogenicity.	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	0-16
26461179-1	2015	Heme-oxygenase 1 (HO-1) prevents T cell-mediated inflammatory disease by producing carbon monoxide (CO) and impairing DC immunogenicity.	Carbon Monoxide	100-102	heme oxygenase 1	Homo sapiens	0-16
26456836-11	2015	Curcumin also inhibited superoxide anion-induced leukocyte recruitment in the peritoneal cavity and in the paw skin inhibited myeloperoxidase activity, oxidative stress, IL-1beta and TNF-alpha production and NF-kappaB activation as well as enhanced IL-10 production, and HO-1 and Nrf2 mRNA expression.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	271-275
26315932-2	2015	We have previously shown that the liberation of heme in acute hemolysis can induce heme oxygenase-1 during granulopoiesis, impairing the ability of developing neutrophils to mount a bactericidal oxidative burst, and increasing susceptibility to bacterial infection.	Heme	48-52	heme oxygenase 1	Homo sapiens	83-99
26456060-12	2015	PAMPs such as bacterial endotoxin activate HO-1, and the CO that is generated diffuses into the extracellular milieu where it interacts with bacteria, altering their behavior to increase production of ATP, which then functions as a second signal danger molecule.	Adenosine Triphosphate	201-204	heme oxygenase 1	Homo sapiens	43-47
26507166-4	2015	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes oxidation of heme to biliverdin, and has anti-inflammatory and anti-oxidant properties.	Heme	65-69	heme oxygenase 1	Homo sapiens	0-16
26456836-11	2015	Curcumin also inhibited superoxide anion-induced leukocyte recruitment in the peritoneal cavity and in the paw skin inhibited myeloperoxidase activity, oxidative stress, IL-1beta and TNF-alpha production and NF-kappaB activation as well as enhanced IL-10 production, and HO-1 and Nrf2 mRNA expression.	Superoxides	24-40	heme oxygenase 1	Homo sapiens	271-275
26507166-4	2015	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes oxidation of heme to biliverdin, and has anti-inflammatory and anti-oxidant properties.	Heme	65-69	heme oxygenase 1	Homo sapiens	18-22
26507166-4	2015	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes oxidation of heme to biliverdin, and has anti-inflammatory and anti-oxidant properties.	Biliverdine	73-83	heme oxygenase 1	Homo sapiens	0-16
26507166-4	2015	Heme oxygenase-1 (HO-1) is an enzyme that catalyzes oxidation of heme to biliverdin, and has anti-inflammatory and anti-oxidant properties.	Biliverdine	73-83	heme oxygenase 1	Homo sapiens	18-22
26507166-11	2015	IL-13 significantly increased goblet cells, MUC5AC protein secretion (p b 0.01) and MUC5AC mRNA (p b 0.001), and these were decreased by hemin by way of HO-1.	Hemin	137-142	heme oxygenase 1	Homo sapiens	153-157
26507166-12	2015	Tin protoporphyrin (SnPP)-IX, a HO-1 inhibitor, blocked the effect of hemin restoring MUC5AC protein secretion (p b 0.05) and goblet cell hyperplasia.	tin protoporphyrin IX	0-18	heme oxygenase 1	Homo sapiens	32-36
26507166-12	2015	Tin protoporphyrin (SnPP)-IX, a HO-1 inhibitor, blocked the effect of hemin restoring MUC5AC protein secretion (p b 0.05) and goblet cell hyperplasia.	S-Nitroso-N-propionyl-D,L-penicillamine	20-24	heme oxygenase 1	Homo sapiens	32-36
26590114-0	2015	Fisetin inhibits TNF-alpha-induced inflammatory action and hydrogen peroxide-induced oxidative damage in human keratinocyte HaCaT cells through PI3K/AKT/Nrf-2-mediated heme oxygenase-1 expression.	fisetin	0-7	heme oxygenase 1	Homo sapiens	168-184
26590114-5	2015	When HaCaT cells were treated with non-cytotoxic concentrations of fisetin (1-20muM), heme oxygenase (HO)-1 mRNA and protein expression increased in a dose-dependent manner.	fisetin	67-74	heme oxygenase 1	Homo sapiens	86-107
26431832-0	2015	Guanosine inhibits LPS-induced pro-inflammatory response and oxidative stress in hippocampal astrocytes through the heme oxygenase-1 pathway.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	116-132
26240115-4	2015	Olmesartan, an Ang II type 1 receptor blocker, possesses antioxidant and activating nitric oxide system-related effects, which we have shown in terms of p22(phox) reduction, heme oxygenase-1 and calcitonin gene-related peptide increase.	olmesartan	0-10	heme oxygenase 1	Homo sapiens	174-190
26432957-5	2015	HO-1 degrades heme to biliverdin, carbon monoxide (CO) and free iron.	Biliverdine	22-32	heme oxygenase 1	Homo sapiens	0-4
26432957-5	2015	HO-1 degrades heme to biliverdin, carbon monoxide (CO) and free iron.	Carbon Monoxide	34-49	heme oxygenase 1	Homo sapiens	0-4
26432957-5	2015	HO-1 degrades heme to biliverdin, carbon monoxide (CO) and free iron.	Carbon Monoxide	51-53	heme oxygenase 1	Homo sapiens	0-4
26432957-5	2015	HO-1 degrades heme to biliverdin, carbon monoxide (CO) and free iron.	Iron	64-68	heme oxygenase 1	Homo sapiens	0-4
26432957-6	2015	Biliverdin and CO are gaining particular interest because these two have been found to mediate most of anti-inflammatory, antioxidant and anti-apoptotic effects of HO-1.	Biliverdine	0-10	heme oxygenase 1	Homo sapiens	164-168
26432957-6	2015	Biliverdin and CO are gaining particular interest because these two have been found to mediate most of anti-inflammatory, antioxidant and anti-apoptotic effects of HO-1.	Carbon Monoxide	15-17	heme oxygenase 1	Homo sapiens	164-168
26431832-2	2015	Our group recently demonstrated that guanosine exhibits glioprotective effects in the C6 astroglial cell line by associating the heme oxygenase-1 (HO-1) signaling pathway with protection against azide-induced oxidative stress.	Guanosine	37-46	heme oxygenase 1	Homo sapiens	129-145
26431832-2	2015	Our group recently demonstrated that guanosine exhibits glioprotective effects in the C6 astroglial cell line by associating the heme oxygenase-1 (HO-1) signaling pathway with protection against azide-induced oxidative stress.	Guanosine	37-46	heme oxygenase 1	Homo sapiens	147-151
26431832-2	2015	Our group recently demonstrated that guanosine exhibits glioprotective effects in the C6 astroglial cell line by associating the heme oxygenase-1 (HO-1) signaling pathway with protection against azide-induced oxidative stress.	Azides	195-200	heme oxygenase 1	Homo sapiens	129-145
26431832-2	2015	Our group recently demonstrated that guanosine exhibits glioprotective effects in the C6 astroglial cell line by associating the heme oxygenase-1 (HO-1) signaling pathway with protection against azide-induced oxidative stress.	Azides	195-200	heme oxygenase 1	Homo sapiens	147-151
26431832-8	2015	Guanosine was able to prevent these effects, protecting the hippocampal astrocytes against LPS-induced cytotoxicity through activation of the HO-1 pathway.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	142-146
26414010-8	2015	Alpha-lipoic acid, an oxidative stress inhibitor, prevented the development of superoxide acutely and increased antiapoptotic markers B-cell lymphoma 2 (t = 3.079, P &lt; 0.05) and heme oxygenase 1 (t = 8.169, P &lt; 0.001) after single blast.	Thioctic Acid	0-17	heme oxygenase 1	Homo sapiens	181-197
26299779-2	2015	We have previously demonstrated that preconditioning human CSCs (hCSCs) with the heme oxygenase-1 inducer, cobalt protoporphyrin (CoPP), has significant cytoprotective effects in vitro.	cobaltiprotoporphyrin	107-128	heme oxygenase 1	Homo sapiens	81-97
26299779-2	2015	We have previously demonstrated that preconditioning human CSCs (hCSCs) with the heme oxygenase-1 inducer, cobalt protoporphyrin (CoPP), has significant cytoprotective effects in vitro.	cobaltiprotoporphyrin	130-134	heme oxygenase 1	Homo sapiens	81-97
26385185-1	2015	Carbon monoxide (CO) is one of the cytoprotective byproducts of heme oxygenase (HO)-1 and exerts anti-inflammatory action in various models.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	64-85
26385185-1	2015	Carbon monoxide (CO) is one of the cytoprotective byproducts of heme oxygenase (HO)-1 and exerts anti-inflammatory action in various models.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	64-85
26318273-8	2015	Moreover, we demonstrated that heme oxygenase 1 (HO1), an enzyme that is part of the cellular defense system, mediated some of the effects of resveratrol.	Resveratrol	142-153	heme oxygenase 1	Homo sapiens	31-47
26318273-8	2015	Moreover, we demonstrated that heme oxygenase 1 (HO1), an enzyme that is part of the cellular defense system, mediated some of the effects of resveratrol.	Resveratrol	142-153	heme oxygenase 1	Homo sapiens	49-52
26870816-3	2016	To limit the deleterious effects of excess ROS, certain gene promoters contain antioxidant response elements (ARE), e.g. the genes NQO-1 and HO-1.	Reactive Oxygen Species	43-46	heme oxygenase 1	Homo sapiens	141-145
26611539-0	2015	Brazilian green propolis water extract up-regulates the early expression level of HO-1 and accelerates Nrf2 after UVA irradiation.	Water	25-30	heme oxygenase 1	Homo sapiens	82-86
26600472-7	2015	We found that mercury increases oxidative stress (increased HO1 and NQO1 mRNA levels) and alters the cytoskeleton in the human endometrial Ishikawa cell line and to a lesser extent, in the "less-differentiated" human endometrial Hec-1b cells.	Mercury	14-21	heme oxygenase 1	Homo sapiens	60-63
26556982-7	2015	Although the underlying mechanisms are not well defined for most of the antibiotics, the pathways triggered for norfloxacin to induce such immunomodulatory effects involve the down-regulation of pro-inflammatory inducible nitric oxide synthase, cyclooxygenase-2, and NF-kappaB and the up-regulation of heme-oxygenase 1 and IL-10 expression.	Norfloxacin	112-123	heme oxygenase 1	Homo sapiens	302-318
26472707-8	2015	Results indicate that Cucurbitacins markedly promoted the activation of Nrf-2/ARE pathway-related downstream factors including NQO-1 and HO-1.	Cucurbitacins	22-35	heme oxygenase 1	Homo sapiens	137-141
26472707-9	2015	Furthermore, anti-neuroinflammatory effects of Cucurbitacins are attenuated in the knockdown of Nrf2, HO-1 and NQO-1 respectively.	Cucurbitacins	47-60	heme oxygenase 1	Homo sapiens	102-106
26884897-8	2015	HO-1 and its reaction products of heme degradation has been linked to cytoprotection, and as an inducible form of HO, serves a vital metabolic function as the rate-limiting step in the heme degradation pathway, and affords protection in models of liver I/R injury.	Heme	34-38	heme oxygenase 1	Homo sapiens	0-4
26884897-8	2015	HO-1 and its reaction products of heme degradation has been linked to cytoprotection, and as an inducible form of HO, serves a vital metabolic function as the rate-limiting step in the heme degradation pathway, and affords protection in models of liver I/R injury.	Heme	185-189	heme oxygenase 1	Homo sapiens	0-4
25847254-5	2015	In addition, 10-MDP induced activation of nuclear factor-E2-related factor 2 (Nrf2) and its target gene, haeme oxygenase-1 (HO-1).	methacryloyloxydecyl dihydrogen phosphate	13-19	heme oxygenase 1	Homo sapiens	105-122
25847254-5	2015	In addition, 10-MDP induced activation of nuclear factor-E2-related factor 2 (Nrf2) and its target gene, haeme oxygenase-1 (HO-1).	methacryloyloxydecyl dihydrogen phosphate	13-19	heme oxygenase 1	Homo sapiens	124-128
25847254-6	2015	We evaluated whether the effect of 10-MDP was related to the induction of HO-1 and found that treatment with a selective inhibitor of HO-1 reversed the production of 10-MDP-mediated pro-inflammatory cytokines and the inhibition of differentiation markers.	methacryloyloxydecyl dihydrogen phosphate	35-41	heme oxygenase 1	Homo sapiens	74-78
25847254-6	2015	We evaluated whether the effect of 10-MDP was related to the induction of HO-1 and found that treatment with a selective inhibitor of HO-1 reversed the production of 10-MDP-mediated pro-inflammatory cytokines and the inhibition of differentiation markers.	methacryloyloxydecyl dihydrogen phosphate	35-41	heme oxygenase 1	Homo sapiens	134-138
25847254-6	2015	We evaluated whether the effect of 10-MDP was related to the induction of HO-1 and found that treatment with a selective inhibitor of HO-1 reversed the production of 10-MDP-mediated pro-inflammatory cytokines and the inhibition of differentiation markers.	methacryloyloxydecyl dihydrogen phosphate	166-172	heme oxygenase 1	Homo sapiens	74-78
25847254-6	2015	We evaluated whether the effect of 10-MDP was related to the induction of HO-1 and found that treatment with a selective inhibitor of HO-1 reversed the production of 10-MDP-mediated pro-inflammatory cytokines and the inhibition of differentiation markers.	methacryloyloxydecyl dihydrogen phosphate	166-172	heme oxygenase 1	Homo sapiens	134-138
26351029-0	2015	Organic Nitrates in Heart Failure Revisited: Pentaerythritol Tetranitrate Induces Heme Oxygenase 1 to Protect the Myocardium.	organic nitrates	0-16	heme oxygenase 1	Homo sapiens	82-98
26456587-8	2015	Furthermore, SMXZF not only dose-dependently inhibited the phosphorylation of NF-kappaB, p50, p65 and IKKalpha/beta in TNF-alpha-treated EA.hy926 cells, but also regulated the Nrf2/HO-1 pathway in H2O2-treated PC12 cells.	smxzf	13-18	heme oxygenase 1	Homo sapiens	181-185
26324507-8	2015	Administering tin protoporphyrin IX dichloride (HO-1 inhibitor) or cobalt protoporphyrin (HO-1 inducer) into placental explants did not affect sFlt-1 or sENG secretion.	cobaltiprotoporphyrin	67-88	heme oxygenase 1	Homo sapiens	90-94
26351029-0	2015	Organic Nitrates in Heart Failure Revisited: Pentaerythritol Tetranitrate Induces Heme Oxygenase 1 to Protect the Myocardium.	Pentaerythritol Tetranitrate	45-73	heme oxygenase 1	Homo sapiens	82-98
26722274-0	2015	Knockdown of heme oxygenase-1 promotes apoptosis and autophagy and enhances the cytotoxicity of doxorubicin in breast cancer cells.	Doxorubicin	96-107	heme oxygenase 1	Homo sapiens	13-29
26227317-9	2015	Induction of DNA damage by mitoxantrone and etoposide repressed HO-1 transcription, whereas hydrogen peroxide and doxorubicin induced its expression.	Mitoxantrone	27-39	heme oxygenase 1	Homo sapiens	64-68
26227317-9	2015	Induction of DNA damage by mitoxantrone and etoposide repressed HO-1 transcription, whereas hydrogen peroxide and doxorubicin induced its expression.	Etoposide	44-53	heme oxygenase 1	Homo sapiens	64-68
26227317-10	2015	Xenograft studies showed that HO-1 regulation by doxorubicin also occurs in vivo.	Doxorubicin	49-60	heme oxygenase 1	Homo sapiens	30-34
26227317-11	2015	Immunofluorescence analysis revealed that BRCA1 overexpression and/or doxorubicin exposure induced the cytoplasmic retention of HO-1.	Doxorubicin	70-81	heme oxygenase 1	Homo sapiens	128-132
26722301-5	2015	In the present study, HO-1 was expressed in the human AML Kasumi-1, HL-60 and THP-1 cell lines, and HO-1 expression was regulated by Hemin (20 micromol/l) and ZnPPIX (10 micromol/l).	zinc protoporphyrin	159-165	heme oxygenase 1	Homo sapiens	22-26
26722301-5	2015	In the present study, HO-1 was expressed in the human AML Kasumi-1, HL-60 and THP-1 cell lines, and HO-1 expression was regulated by Hemin (20 micromol/l) and ZnPPIX (10 micromol/l).	zinc protoporphyrin	159-165	heme oxygenase 1	Homo sapiens	100-104
26722274-2	2015	In the present study, HMOX-1 was demonstrated to be overexpressed and able to be induced by doxorubicin in breast cancer cell lines.	Doxorubicin	92-103	heme oxygenase 1	Homo sapiens	22-28
26722274-3	2015	Knockdown of HMOX-1 using short interfering (si)RNA enhanced the cytotoxicity of doxorubicin in MDA-MB-231 and BT549 cells.	Doxorubicin	81-92	heme oxygenase 1	Homo sapiens	13-19
26722274-4	2015	Knockdown of HMOX-1 downregulated B cell lymphoma (Bcl)-2 and Bcl-extra large expression, and significantly enhanced doxorubicin-induced apoptosis in MDA-MB-231 and BT549 cells.	Doxorubicin	117-128	heme oxygenase 1	Homo sapiens	13-19
26722274-5	2015	Additionally, knockdown of HMOX-1 upregulated light chain 3B expression and markedly increased the accumulation of autophagic vacuoles in MDA-MB-231 and BT549 cells treated with doxorubicin.	Doxorubicin	178-189	heme oxygenase 1	Homo sapiens	27-33
26722274-7	2015	Therefore, HMOX-1 may represent a potential therapeutic target for enhancing the cytotoxicity and efficacy of doxorubicin during the treatment of breast cancer.	Doxorubicin	110-121	heme oxygenase 1	Homo sapiens	11-17
26147741-1	2015	Heme Oxygenase-1 and its product biliverdin/bilirubin have been demonstrated to protect against ischemia/reperfusion injury (IRI).	Biliverdine	33-43	heme oxygenase 1	Homo sapiens	0-16
26392237-1	2015	Heme oxygenase-1 (HO-1, hmox-1) catalyzes the rate-limiting step in the heme degradation processes.	Heme	72-76	heme oxygenase 1	Homo sapiens	0-22
26392237-1	2015	Heme oxygenase-1 (HO-1, hmox-1) catalyzes the rate-limiting step in the heme degradation processes.	Heme	72-76	heme oxygenase 1	Homo sapiens	24-30
26392237-2	2015	Out of three by-products of HO-1 activity, biliverdin, iron ions and carbon monoxide (CO), the latter was mostly shown to mediate many beneficial HO-1 effects, including protection against oxidative injury, regulation of apoptosis, modulation of inflammation as well as contribution to angiogenesis.	Biliverdine	43-53	heme oxygenase 1	Homo sapiens	146-150
26392237-2	2015	Out of three by-products of HO-1 activity, biliverdin, iron ions and carbon monoxide (CO), the latter was mostly shown to mediate many beneficial HO-1 effects, including protection against oxidative injury, regulation of apoptosis, modulation of inflammation as well as contribution to angiogenesis.	Iron	55-59	heme oxygenase 1	Homo sapiens	146-150
26392237-2	2015	Out of three by-products of HO-1 activity, biliverdin, iron ions and carbon monoxide (CO), the latter was mostly shown to mediate many beneficial HO-1 effects, including protection against oxidative injury, regulation of apoptosis, modulation of inflammation as well as contribution to angiogenesis.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	146-150
26392237-2	2015	Out of three by-products of HO-1 activity, biliverdin, iron ions and carbon monoxide (CO), the latter was mostly shown to mediate many beneficial HO-1 effects, including protection against oxidative injury, regulation of apoptosis, modulation of inflammation as well as contribution to angiogenesis.	Carbon Monoxide	86-88	heme oxygenase 1	Homo sapiens	146-150
26418896-5	2015	Application of CO, a product of HO-1 catalysis, increased levels of E-cadherin in the adherens junctions between cancer cells.	Carbon Monoxide	15-17	heme oxygenase 1	Homo sapiens	32-36
26510767-2	2015	Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation.	Heme	112-116	heme oxygenase 1	Homo sapiens	0-16
26510767-2	2015	Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation.	Heme	112-116	heme oxygenase 1	Homo sapiens	18-22
26510767-7	2015	Increasing HO-1 expression through adenoviral-mediated overexpression or induction with cobalt protoporphyrin (CoPP, a potent HO-1 inducer), pre- and postinfection, effectively inhibited BVDV replication.	cobaltiprotoporphyrin	88-109	heme oxygenase 1	Homo sapiens	11-15
26510767-7	2015	Increasing HO-1 expression through adenoviral-mediated overexpression or induction with cobalt protoporphyrin (CoPP, a potent HO-1 inducer), pre- and postinfection, effectively inhibited BVDV replication.	cobaltiprotoporphyrin	88-109	heme oxygenase 1	Homo sapiens	126-130
26510767-7	2015	Increasing HO-1 expression through adenoviral-mediated overexpression or induction with cobalt protoporphyrin (CoPP, a potent HO-1 inducer), pre- and postinfection, effectively inhibited BVDV replication.	cobaltiprotoporphyrin	111-115	heme oxygenase 1	Homo sapiens	11-15
26510767-7	2015	Increasing HO-1 expression through adenoviral-mediated overexpression or induction with cobalt protoporphyrin (CoPP, a potent HO-1 inducer), pre- and postinfection, effectively inhibited BVDV replication.	cobaltiprotoporphyrin	111-115	heme oxygenase 1	Homo sapiens	126-130
26186946-1	2015	The heme oxygenase-1 (HO-1)/carbon monoxide (CO) system induces mitochondrial biogenesis, but its biological impact in human skeletal muscle is uncertain.	Carbon Monoxide	45-47	heme oxygenase 1	Homo sapiens	4-20
26186946-1	2015	The heme oxygenase-1 (HO-1)/carbon monoxide (CO) system induces mitochondrial biogenesis, but its biological impact in human skeletal muscle is uncertain.	Carbon Monoxide	45-47	heme oxygenase 1	Homo sapiens	22-26
26493719-3	2015	Heme oxygenase-1 (HO-1; also known as Hsp32) is an inducible enzyme participating in heme degradation and involved in oxidative stress resistance.	Heme	85-89	heme oxygenase 1	Homo sapiens	0-16
26350099-5	2015	Furthermore, with the addition of N-acetylcysteine, a scavenger of reactive oxygen species (ROS), it was found that NGAL depletion was sufficient to cause apoptosis of lung adenocarcinoma cells by generating ROS through the inhibition of the nuclear factor E2-related factor 2/heme oxygenase-1 anti-oxidant pathway.	Acetylcysteine	34-50	heme oxygenase 1	Homo sapiens	277-293
26341012-12	2015	Plumbagin increased TrxR-1 and heme oxygenase (HO)-1 expression and pretreatment with NAC significantly attenuated the plumbagin-induced increase of TrxR-1 and HO-1 expression in HepG2 cells, LLC cells and SiHa cells.	Acetylcysteine	86-89	heme oxygenase 1	Homo sapiens	160-164
26493719-3	2015	Heme oxygenase-1 (HO-1; also known as Hsp32) is an inducible enzyme participating in heme degradation and involved in oxidative stress resistance.	Heme	85-89	heme oxygenase 1	Homo sapiens	18-22
26493719-3	2015	Heme oxygenase-1 (HO-1; also known as Hsp32) is an inducible enzyme participating in heme degradation and involved in oxidative stress resistance.	Heme	85-89	heme oxygenase 1	Homo sapiens	38-43
26291278-0	2015	Coordinated regulation of Nrf2 and histone H3 serine 10 phosphorylation in arsenite-activated transcription of the human heme oxygenase-1 gene.	Serine	46-52	heme oxygenase 1	Homo sapiens	121-137
26291278-8	2015	In response to arsenite, binding of Nrf2 to the HO-1 ARE preceded phosphorylation of H3S10 at the HO-1 ARE.	arsenite	15-23	heme oxygenase 1	Homo sapiens	48-52
26291278-0	2015	Coordinated regulation of Nrf2 and histone H3 serine 10 phosphorylation in arsenite-activated transcription of the human heme oxygenase-1 gene.	arsenite	75-83	heme oxygenase 1	Homo sapiens	121-137
26291278-8	2015	In response to arsenite, binding of Nrf2 to the HO-1 ARE preceded phosphorylation of H3S10 at the HO-1 ARE.	arsenite	15-23	heme oxygenase 1	Homo sapiens	98-102
26291278-4	2015	The environmental contaminant arsenite is a potent inducer of both HO-1 expression and phosphorylation of histone H3 serine 10 (H3S10); therefore, we investigated the relationships between Nrf2 and H3S10 phosphorylation in arsenite-induced, ARE-dependent, transcriptional activation of the human HO-1 gene.	arsenite	30-38	heme oxygenase 1	Homo sapiens	67-71
26291278-4	2015	The environmental contaminant arsenite is a potent inducer of both HO-1 expression and phosphorylation of histone H3 serine 10 (H3S10); therefore, we investigated the relationships between Nrf2 and H3S10 phosphorylation in arsenite-induced, ARE-dependent, transcriptional activation of the human HO-1 gene.	arsenite	30-38	heme oxygenase 1	Homo sapiens	296-300
26291278-8	2015	In response to arsenite, binding of Nrf2 to the HO-1 ARE preceded phosphorylation of H3S10 at the HO-1 ARE.	h3s10	85-90	heme oxygenase 1	Homo sapiens	48-52
26291278-8	2015	In response to arsenite, binding of Nrf2 to the HO-1 ARE preceded phosphorylation of H3S10 at the HO-1 ARE.	h3s10	85-90	heme oxygenase 1	Homo sapiens	98-102
26291278-5	2015	Arsenite increased phosphorylation of H3S10 both globally and at the HO-1 promoter concomitantly with HO-1 transcription in human HaCaT keratinocytes.	arsenite	0-8	heme oxygenase 1	Homo sapiens	69-73
26291278-9	2015	Furthermore, arsenite-mediated occupancy of phosphorylated H3S10 at the HO-1 ARE was decreased in Nrf2-deficient mouse embryonic fibroblasts.	arsenite	13-21	heme oxygenase 1	Homo sapiens	72-76
26291278-5	2015	Arsenite increased phosphorylation of H3S10 both globally and at the HO-1 promoter concomitantly with HO-1 transcription in human HaCaT keratinocytes.	h3s10	38-43	heme oxygenase 1	Homo sapiens	69-73
26291278-9	2015	Furthermore, arsenite-mediated occupancy of phosphorylated H3S10 at the HO-1 ARE was decreased in Nrf2-deficient mouse embryonic fibroblasts.	h3s10	59-64	heme oxygenase 1	Homo sapiens	72-76
26291278-10	2015	These results suggest the involvement of H3S10 phosphorylation in the Nrf2-ARE axis by proposing that Nrf2 may influence H3S10 phosphorylation at the HO-1 ARE and additional promoter regions.	h3s10	41-46	heme oxygenase 1	Homo sapiens	150-154
26291278-6	2015	Conversely, arsenite-induced H3S10 phosphorylation and HO-1 expression were blocked by N-acetylcysteine (NAC), the c-Jun N-terminal kinase (JNK) inhibitor SP600125, and JNK knockdown (siJNK).	arsenite	12-20	heme oxygenase 1	Homo sapiens	55-59
26291278-10	2015	These results suggest the involvement of H3S10 phosphorylation in the Nrf2-ARE axis by proposing that Nrf2 may influence H3S10 phosphorylation at the HO-1 ARE and additional promoter regions.	h3s10	121-126	heme oxygenase 1	Homo sapiens	150-154
26291278-11	2015	Our data highlights the complex interplay between Nrf2 and H3S10 phosphorylation in arsenite-activated HO-1 transcription.	h3s10	59-64	heme oxygenase 1	Homo sapiens	103-107
26291278-6	2015	Conversely, arsenite-induced H3S10 phosphorylation and HO-1 expression were blocked by N-acetylcysteine (NAC), the c-Jun N-terminal kinase (JNK) inhibitor SP600125, and JNK knockdown (siJNK).	Acetylcysteine	87-103	heme oxygenase 1	Homo sapiens	55-59
26291278-11	2015	Our data highlights the complex interplay between Nrf2 and H3S10 phosphorylation in arsenite-activated HO-1 transcription.	arsenite	84-92	heme oxygenase 1	Homo sapiens	103-107
26291278-6	2015	Conversely, arsenite-induced H3S10 phosphorylation and HO-1 expression were blocked by N-acetylcysteine (NAC), the c-Jun N-terminal kinase (JNK) inhibitor SP600125, and JNK knockdown (siJNK).	Acetylcysteine	105-108	heme oxygenase 1	Homo sapiens	55-59
26416516-8	2015	Terrein induced the induction of anti-oxidant molecules, copper/zinc-superoxide defence (Cu/ZnSOD), manganese superoxide dismutase (MnSOD) and heme oxygenase-1 (HO-1) in SIPS cells.	terrein	0-7	heme oxygenase 1	Homo sapiens	143-159
26416516-8	2015	Terrein induced the induction of anti-oxidant molecules, copper/zinc-superoxide defence (Cu/ZnSOD), manganese superoxide dismutase (MnSOD) and heme oxygenase-1 (HO-1) in SIPS cells.	terrein	0-7	heme oxygenase 1	Homo sapiens	161-165
26436888-8	2015	RESULTS: Treatment with 30 or 50 muM resveratrol reduced ROS production and HO-1 level induced by oxidative stress.	Resveratrol	37-48	heme oxygenase 1	Homo sapiens	76-80
26339767-5	2015	RECENT FINDINGS: Recent studies demonstrate that Hx-dependent uptake of extracellular heme leads to the deactivation of Bach1 repression leading to the transcriptional activation of antioxidant heme oxygenase-1 gene.	Heme	86-90	heme oxygenase 1	Homo sapiens	194-210
26206798-8	2015	HMOX1 rs743811 associated with chronic kidney disease stage (OR=3.0, P=0.0001) in the University of Illinois cohort and end-stage renal disease (OR=10.0, P=0.0003) in the Walk-Treatment of Pulmonary Hypertension and Sickle cell Disease with Sildenafil Therapy cohort.	Sildenafil Citrate	241-251	heme oxygenase 1	Homo sapiens	0-5
26043815-0	2015	Lipoic acid and N-acetylcysteine prevent ammonia-induced inflammatory response in C6 astroglial cells: The putative role of ERK and HO1 signaling pathways.	Thioctic Acid	0-11	heme oxygenase 1	Homo sapiens	132-135
25921464-5	2015	We showed that CORM-2-induced HO-1 protein and mRNA levels were inhibited by the inhibitor of c-Src (PP1 or SU6656), EGFR (AG1478), PI3K (LY294002), Akt (SH-5), JNK1/2 (SP600125), or p38 MAPK (SB202190) and transfection with siRNA of c-Src, EGFR, Akt, p38, JNK2, or Nrf2 in HTSMCs.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	138-146	heme oxygenase 1	Homo sapiens	30-34
25921464-5	2015	We showed that CORM-2-induced HO-1 protein and mRNA levels were inhibited by the inhibitor of c-Src (PP1 or SU6656), EGFR (AG1478), PI3K (LY294002), Akt (SH-5), JNK1/2 (SP600125), or p38 MAPK (SB202190) and transfection with siRNA of c-Src, EGFR, Akt, p38, JNK2, or Nrf2 in HTSMCs.	pyrazolanthrone	169-177	heme oxygenase 1	Homo sapiens	30-34
26141635-7	2015	Under normal conditions, fHb is effectively scavenged by the Hb-scavenging mechanism (HSM); this involves binding to haptoglobin (Hp), uptake via the Hb-scavenging receptor (CD163) on monocytes and metabolism by heme-oxygenase-1.	3-FLUORO-4-HYDROXYBENZOIC ACID	25-28	heme oxygenase 1	Homo sapiens	212-228
26929573-4	2015	MATERIALS AND METHODS: Protective ability of flavonoid-enriched (FE) fraction of clove was studied against UV-B induced cytotoxicity, anti-oxidant regulation, oxidative DNA damage, intracellular reactive oxygen species (ROS) generation, apoptotic morphological changes, and regulation of heme oxygenase-1 (HO-1) gene through nuclear factor E2-related factor 2 antioxidant response element (Nrf2 ARE) pathway.	Flavonoids	45-54	heme oxygenase 1	Homo sapiens	306-310
26929573-7	2015	CONCLUSION: The present study demonstrated for the first time that the FE fraction from clove could confer UV-B protection probably through the Nrf2-ARE pathway, which included the down-regulation of Nrf2 and HO-1.	Iron	71-73	heme oxygenase 1	Homo sapiens	209-213
25921464-1	2015	Carbon monoxide (CO), a reaction product of the cytoprotective heme oxygenase (HO)-1, displays an anti-inflammatory effect in various cellular injuries, but the precise mechanisms of HO-1 expression remain unknown.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	63-84
25921464-1	2015	Carbon monoxide (CO), a reaction product of the cytoprotective heme oxygenase (HO)-1, displays an anti-inflammatory effect in various cellular injuries, but the precise mechanisms of HO-1 expression remain unknown.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	183-187
25921464-1	2015	Carbon monoxide (CO), a reaction product of the cytoprotective heme oxygenase (HO)-1, displays an anti-inflammatory effect in various cellular injuries, but the precise mechanisms of HO-1 expression remain unknown.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	63-84
25921464-1	2015	Carbon monoxide (CO), a reaction product of the cytoprotective heme oxygenase (HO)-1, displays an anti-inflammatory effect in various cellular injuries, but the precise mechanisms of HO-1 expression remain unknown.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	183-187
25921464-5	2015	We showed that CORM-2-induced HO-1 protein and mRNA levels were inhibited by the inhibitor of c-Src (PP1 or SU6656), EGFR (AG1478), PI3K (LY294002), Akt (SH-5), JNK1/2 (SP600125), or p38 MAPK (SB202190) and transfection with siRNA of c-Src, EGFR, Akt, p38, JNK2, or Nrf2 in HTSMCs.	SU 6656	108-114	heme oxygenase 1	Homo sapiens	30-34
26185204-10	2015	Furthermore, activated ascaridole showed increased potential for induction of the Nrf2 target gene heme oxygenase 1 and upregulation of CD86 and CD54 on THP-1 cells, an established DC surrogate.	ascaridole	23-33	heme oxygenase 1	Homo sapiens	99-115
26043815-5	2015	LA and NAC prevented these effects by the modulation of ERK and HO1 pathways.	Acetylcysteine	7-10	heme oxygenase 1	Homo sapiens	64-67
26192096-0	2015	Involvement of the Nrf2/HO-1 signaling pathway in sulfuretin-induced protection against amyloid beta25-35 neurotoxicity.	sulfuretin	50-60	heme oxygenase 1	Homo sapiens	24-28
26277392-0	2015	Nitration of indoxyl sulfate facilitates its cytotoxicity in human renal proximal tubular cells via expression of heme oxygenase-1.	Indican	13-28	heme oxygenase 1	Homo sapiens	114-130
26277392-7	2015	Most importantly, however, as detected by immunofluorescence and Western blotting, 2-nitro-IS induces the expression of heme oxygenase-1 and thereby the formation of ROS; most probably through the Fenton reaction.	2-nitro	83-90	heme oxygenase 1	Homo sapiens	120-136
26277392-7	2015	Most importantly, however, as detected by immunofluorescence and Western blotting, 2-nitro-IS induces the expression of heme oxygenase-1 and thereby the formation of ROS; most probably through the Fenton reaction.	Reactive Oxygen Species	166-169	heme oxygenase 1	Homo sapiens	120-136
26192096-6	2015	We demonstrated that sulfuretin induces the expression of heme oxygenase-1 (HO-1), an anti-oxidant response gene.	sulfuretin	21-31	heme oxygenase 1	Homo sapiens	58-74
26192096-6	2015	We demonstrated that sulfuretin induces the expression of heme oxygenase-1 (HO-1), an anti-oxidant response gene.	sulfuretin	21-31	heme oxygenase 1	Homo sapiens	76-80
26143632-4	2015	Treatment of human adipocytes with cobalt protoporphyrin (CoPP) or hemin for 24-48 h increased HO-1 expression and activity without affecting adiponectin expression and secretion.	cobaltiprotoporphyrin	35-56	heme oxygenase 1	Homo sapiens	95-99
26192096-7	2015	Notably, we found that the neuroprotective effects of sulfuretin were diminished by an Nrf2 small interfering RNA (siRNA), the HO-1 inhibitor zinc protoporphyrin IX (ZnPP), as well as the PI3K/Akt inhibitor LY294002.	sulfuretin	54-64	heme oxygenase 1	Homo sapiens	127-131
26192096-8	2015	Taken together, these results indicated that sulfuretin protects neuronal cells from Abeta25-35-induced neurotoxicity through activation of Nrf/HO-1 and PI3K/Akt signaling pathways.	sulfuretin	45-55	heme oxygenase 1	Homo sapiens	144-148
26192096-9	2015	Our results also indicate that sulfuretin-induced induction of Nrf2-dependent HO-1 expression via the PI3K/Akt signaling pathway has preventive and/or therapeutic potential for the management of Alzheimer"s disease.	sulfuretin	31-41	heme oxygenase 1	Homo sapiens	78-82
26275128-0	2015	Novel Nrf2/ARE activator, trans-Coniferylaldehyde, induces a HO-1-mediated defense mechanism through a dual p38alpha/MAPKAPK-2 and PK-N3 signaling pathway.	coniferaldehyde	26-49	heme oxygenase 1	Homo sapiens	61-65
26275128-6	2015	The detoxifying/antioxidant genes activated by t-CA, especially heme oxygenase-1 (HO-1), were found to be involved in its cytoprotective effects against oxidative stress and cell injuries elicited by carcinogens tert-butylhydroperoxide and arecoline.	tert-Butylhydroperoxide	212-235	heme oxygenase 1	Homo sapiens	64-80
26275128-6	2015	The detoxifying/antioxidant genes activated by t-CA, especially heme oxygenase-1 (HO-1), were found to be involved in its cytoprotective effects against oxidative stress and cell injuries elicited by carcinogens tert-butylhydroperoxide and arecoline.	tert-Butylhydroperoxide	212-235	heme oxygenase 1	Homo sapiens	82-86
26275128-6	2015	The detoxifying/antioxidant genes activated by t-CA, especially heme oxygenase-1 (HO-1), were found to be involved in its cytoprotective effects against oxidative stress and cell injuries elicited by carcinogens tert-butylhydroperoxide and arecoline.	Arecoline	240-249	heme oxygenase 1	Homo sapiens	64-80
26275128-6	2015	The detoxifying/antioxidant genes activated by t-CA, especially heme oxygenase-1 (HO-1), were found to be involved in its cytoprotective effects against oxidative stress and cell injuries elicited by carcinogens tert-butylhydroperoxide and arecoline.	Arecoline	240-249	heme oxygenase 1	Homo sapiens	82-86
26445536-10	2015	In summary, AuNPs enhance the levels and nuclear translocation of the Nrf2 protein and Bach1 export/tyrosine phosphorylation, leading to Nrf2 binding to the HO-1 E2 enhancer promoter region to drive HO-1 expression in ECs.	Tyrosine	100-108	heme oxygenase 1	Homo sapiens	157-161
26445536-10	2015	In summary, AuNPs enhance the levels and nuclear translocation of the Nrf2 protein and Bach1 export/tyrosine phosphorylation, leading to Nrf2 binding to the HO-1 E2 enhancer promoter region to drive HO-1 expression in ECs.	Tyrosine	100-108	heme oxygenase 1	Homo sapiens	199-203
26143632-4	2015	Treatment of human adipocytes with cobalt protoporphyrin (CoPP) or hemin for 24-48 h increased HO-1 expression and activity without affecting adiponectin expression and secretion.	cobaltiprotoporphyrin	58-62	heme oxygenase 1	Homo sapiens	95-99
25917210-8	2015	Further, geraniin induced the expression of heme oxygenase-1 (HO-1), NAD(P)H quinone oxidoreductase-1 (NQO1) and level of glutathione (GSH) in a concentration- and time-dependent manner, and increased Nrf2 nuclear translocation.	Geraniin	9-17	heme oxygenase 1	Homo sapiens	44-60
26405158-0	2015	Heme oxygenase-1 accelerates erastin-induced ferroptotic cell death.	erastin	29-36	heme oxygenase 1	Homo sapiens	0-16
26405158-6	2015	Zinc protoporphyrin IX (ZnPP), a HO-1 inhibitor, prevented Erastin-triggered ferroptotic cancer cell death.	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	33-37
26405158-6	2015	Zinc protoporphyrin IX (ZnPP), a HO-1 inhibitor, prevented Erastin-triggered ferroptotic cancer cell death.	zinc protoporphyrin	24-28	heme oxygenase 1	Homo sapiens	33-37
26405158-6	2015	Zinc protoporphyrin IX (ZnPP), a HO-1 inhibitor, prevented Erastin-triggered ferroptotic cancer cell death.	erastin	59-66	heme oxygenase 1	Homo sapiens	33-37
26405158-7	2015	Furthermore, Erastin induced the protein and mRNA levels of HO-1 in HT-1080 fibrosarcoma cells.	erastin	13-20	heme oxygenase 1	Homo sapiens	60-64
26405158-10	2015	In addition, hemin and CORM accelerate the HO-1 expression in the presence of Erastin and increase membranous lipid peroxidation.	erastin	78-85	heme oxygenase 1	Homo sapiens	43-47
26405158-11	2015	Thus, HO-1 is an essential enzyme for iron-dependent lipid peroxidation during ferroptotic cell death.	Iron	38-42	heme oxygenase 1	Homo sapiens	6-10
26366056-8	2015	Finally, we showed curcumin A induced expression of HO-1 and decreased cell cycle progression of T cells.	curcumin a	19-29	heme oxygenase 1	Homo sapiens	52-56
25917210-8	2015	Further, geraniin induced the expression of heme oxygenase-1 (HO-1), NAD(P)H quinone oxidoreductase-1 (NQO1) and level of glutathione (GSH) in a concentration- and time-dependent manner, and increased Nrf2 nuclear translocation.	Geraniin	9-17	heme oxygenase 1	Homo sapiens	62-66
25917210-10	2015	However, inhibitors of PI3K/AKT and ERK1/2 (LY294002 or U0126) not only suppressed geraniin-induced nuclear translocation of Nrf2 but also abolished the expression of HO-1, NQO1 and GSH.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	44-52	heme oxygenase 1	Homo sapiens	167-171
25917210-10	2015	However, inhibitors of PI3K/AKT and ERK1/2 (LY294002 or U0126) not only suppressed geraniin-induced nuclear translocation of Nrf2 but also abolished the expression of HO-1, NQO1 and GSH.	U 0126	56-61	heme oxygenase 1	Homo sapiens	167-171
25917210-10	2015	However, inhibitors of PI3K/AKT and ERK1/2 (LY294002 or U0126) not only suppressed geraniin-induced nuclear translocation of Nrf2 but also abolished the expression of HO-1, NQO1 and GSH.	Geraniin	83-91	heme oxygenase 1	Homo sapiens	167-171
25917210-11	2015	CONCLUSIONS: These results demonstrated that geraniin induced Nrf2-mediated expression of antioxidant enzymes HO-1 and NQO1, presumably via PI3K/AKT and ERK1/2 signaling pathways, thereby protecting cells from H2O2-induced oxidative cell death.	Geraniin	45-53	heme oxygenase 1	Homo sapiens	110-114
25917210-11	2015	CONCLUSIONS: These results demonstrated that geraniin induced Nrf2-mediated expression of antioxidant enzymes HO-1 and NQO1, presumably via PI3K/AKT and ERK1/2 signaling pathways, thereby protecting cells from H2O2-induced oxidative cell death.	Hydrogen Peroxide	210-214	heme oxygenase 1	Homo sapiens	110-114
25977183-0	2015	Z-ligustilide ameliorated ultraviolet B-induced oxidative stress and inflammatory cytokine production in human keratinocytes through upregulation of Nrf2/HO-1 and suppression of NF-kappaB pathway.	ligustilide	0-13	heme oxygenase 1	Homo sapiens	154-158
26173399-4	2015	The inducible HO isoform (HO-1) has two functional genetic polymorphisms: (GT)n dinucleotide repeats and A(-413)T SNP (rs2071746), both of which can affect its promoter activity.	Dinucleoside Phosphates	80-92	heme oxygenase 1	Homo sapiens	26-30
26617752-13	2015	ATRA decreased anti-oxygen protein Nrf2 and HO-1, and increases inflammatory factors NF-kappaB and TNF-alpha.	Tretinoin	0-4	heme oxygenase 1	Homo sapiens	44-48
25977183-5	2015	Both silencing the nuclear factor E2-related factor 2 (Nrf2) and the supplement of tin protoporphyrin IX (SnPP), a haeme oxygenase-1 (HO-1) inhibitor, cancelled the inhibitory effect of Z-lig on UVB-induced ROS upregulation in NHEKs.	tin protoporphyrin IX	83-104	heme oxygenase 1	Homo sapiens	115-139
25977183-5	2015	Both silencing the nuclear factor E2-related factor 2 (Nrf2) and the supplement of tin protoporphyrin IX (SnPP), a haeme oxygenase-1 (HO-1) inhibitor, cancelled the inhibitory effect of Z-lig on UVB-induced ROS upregulation in NHEKs.	S-Nitroso-N-propionyl-D,L-penicillamine	106-110	heme oxygenase 1	Homo sapiens	115-139
25977183-5	2015	Both silencing the nuclear factor E2-related factor 2 (Nrf2) and the supplement of tin protoporphyrin IX (SnPP), a haeme oxygenase-1 (HO-1) inhibitor, cancelled the inhibitory effect of Z-lig on UVB-induced ROS upregulation in NHEKs.	ligustilide	186-191	heme oxygenase 1	Homo sapiens	115-139
25977183-8	2015	Taken together, these findings suggest that Z-lig can suppress UVB-induced ROS generation through Nrf2/HO-1 upregulation and inflammation by suppressing the NF-kappaB pathway, suggesting that Z-lig may be beneficial in protecting skin from UVB exposure.	ligustilide	44-49	heme oxygenase 1	Homo sapiens	103-107
25977183-8	2015	Taken together, these findings suggest that Z-lig can suppress UVB-induced ROS generation through Nrf2/HO-1 upregulation and inflammation by suppressing the NF-kappaB pathway, suggesting that Z-lig may be beneficial in protecting skin from UVB exposure.	Reactive Oxygen Species	75-78	heme oxygenase 1	Homo sapiens	103-107
25977183-8	2015	Taken together, these findings suggest that Z-lig can suppress UVB-induced ROS generation through Nrf2/HO-1 upregulation and inflammation by suppressing the NF-kappaB pathway, suggesting that Z-lig may be beneficial in protecting skin from UVB exposure.	ligustilide	192-197	heme oxygenase 1	Homo sapiens	103-107
26622665-11	2015	In addition, these results indicated that TET-dependent demethylation of the Nrf2 promoter upregulated Nrf2 and HO-1 expression, which induced cellular protection mechanisms, ultimately leading to drug resistance.	tetramethylenedisulfotetramine	42-45	heme oxygenase 1	Homo sapiens	112-116
26550306-11	2015	CONCLUSION: Sevoflurane preconditioning can reduce oxidative stress injury induced by OLV and protect lung tissue by increasing HO-1 expression in lung tissue.	Sevoflurane	12-23	heme oxygenase 1	Homo sapiens	128-132
26201059-7	2015	In the cardiovascular system, aspirin also acetylates eNOS with subsequent upregulation of NO formation and enhanced expression of the antioxidans heme-oxygenase-1.	Aspirin	30-37	heme oxygenase 1	Homo sapiens	147-163
25922869-1	2015	BACKGROUND: In vitro and animal studies indicate that statins increase heme oxygenase-1 gene (HMOX1) expression, which then, presumably, increases plasma bilirubin concentration.	Bilirubin	154-163	heme oxygenase 1	Homo sapiens	94-99
25922869-3	2015	We hypothesized that in patients with stable angina atorvastatin therapy (20 mg/day for 10 weeks) concomitantly increases total bilirubin concentration and HMOX1 expression, as assessed non-invasively by plasma analysis.	Atorvastatin	52-64	heme oxygenase 1	Homo sapiens	156-161
26071936-4	2015	We previously demonstrated that curcumin increased reactive oxygen species (ROS) formation and apoptosis in dermal fibroblasts, which could be prevented by pre-induction of the cytoprotective enzyme heme oxygenase (HO)-1.	Curcumin	32-40	heme oxygenase 1	Homo sapiens	199-220
26071936-4	2015	We previously demonstrated that curcumin increased reactive oxygen species (ROS) formation and apoptosis in dermal fibroblasts, which could be prevented by pre-induction of the cytoprotective enzyme heme oxygenase (HO)-1.	Reactive Oxygen Species	51-74	heme oxygenase 1	Homo sapiens	199-220
26071936-4	2015	We previously demonstrated that curcumin increased reactive oxygen species (ROS) formation and apoptosis in dermal fibroblasts, which could be prevented by pre-induction of the cytoprotective enzyme heme oxygenase (HO)-1.	Reactive Oxygen Species	76-79	heme oxygenase 1	Homo sapiens	199-220
25994789-6	2015	Active Nrf2 and the antioxidant enzyme heme oxygenase-1 (HO-1) increase at 3 h after tBHQ treatment.	2-tert-butylhydroquinone	85-89	heme oxygenase 1	Homo sapiens	39-55
25998388-5	2015	Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards.	Hemin	28-33	heme oxygenase 1	Homo sapiens	97-113
25998388-5	2015	Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards.	Hemin	28-33	heme oxygenase 1	Homo sapiens	115-119
25998388-5	2015	Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards.	Hemin	354-359	heme oxygenase 1	Homo sapiens	97-113
25998388-5	2015	Since the mode of action of hemin is both physiological and pharmacological through induction of heme oxygenase-1 (HO-1), an endogenous host protective response to an FDA-licensed therapeutic used to treat another disease, our study suggests an approach to developing novel, safe and effective therapeutic strategies for treating bone disorders, because hemin administration in humans has previously met required FDA safety standards.	Hemin	354-359	heme oxygenase 1	Homo sapiens	115-119
26309414-0	2015	Heme oxygenase-1 is a predictive biomarker for therapeutic targeting of advanced clear cell renal cell carcinoma treated with sorafenib or sunitinib.	Sorafenib	126-135	heme oxygenase 1	Homo sapiens	0-16
26309414-0	2015	Heme oxygenase-1 is a predictive biomarker for therapeutic targeting of advanced clear cell renal cell carcinoma treated with sorafenib or sunitinib.	Sunitinib	139-148	heme oxygenase 1	Homo sapiens	0-16
26309414-1	2015	BACKGROUND: We analyzed the expression of heme oxygenase-1 (HO-1) in patients undergoing radical nephrectomy for advanced clear cell renal cell carcinoma (CC-RCC) and evaluated the effects of the targeted therapies treated with sorafenib and sunitinib.	Sorafenib	228-237	heme oxygenase 1	Homo sapiens	42-58
26309414-1	2015	BACKGROUND: We analyzed the expression of heme oxygenase-1 (HO-1) in patients undergoing radical nephrectomy for advanced clear cell renal cell carcinoma (CC-RCC) and evaluated the effects of the targeted therapies treated with sorafenib and sunitinib.	Sorafenib	228-237	heme oxygenase 1	Homo sapiens	60-64
26309414-1	2015	BACKGROUND: We analyzed the expression of heme oxygenase-1 (HO-1) in patients undergoing radical nephrectomy for advanced clear cell renal cell carcinoma (CC-RCC) and evaluated the effects of the targeted therapies treated with sorafenib and sunitinib.	Sunitinib	242-251	heme oxygenase 1	Homo sapiens	42-58
26309414-1	2015	BACKGROUND: We analyzed the expression of heme oxygenase-1 (HO-1) in patients undergoing radical nephrectomy for advanced clear cell renal cell carcinoma (CC-RCC) and evaluated the effects of the targeted therapies treated with sorafenib and sunitinib.	Sunitinib	242-251	heme oxygenase 1	Homo sapiens	60-64
26309414-6	2015	In the low HO-1 level group, a higher tumor response rate and a longer survival time was achieved in patients who received sorafenib or sunitinib.	Sorafenib	123-132	heme oxygenase 1	Homo sapiens	11-15
26309414-6	2015	In the low HO-1 level group, a higher tumor response rate and a longer survival time was achieved in patients who received sorafenib or sunitinib.	Sunitinib	136-145	heme oxygenase 1	Homo sapiens	11-15
26309414-9	2015	Overall, HO-1 expression might be a useful biomarker for predicting the response to sunitinib and sorafenib for patients with metastatic CC-RCC.	Sunitinib	84-93	heme oxygenase 1	Homo sapiens	9-13
26309414-9	2015	Overall, HO-1 expression might be a useful biomarker for predicting the response to sunitinib and sorafenib for patients with metastatic CC-RCC.	Sorafenib	98-107	heme oxygenase 1	Homo sapiens	9-13
26163453-0	2015	Insight into the molecular mechanism of heme oxygenase-1 induction by docosahexaenoic acid in U937 cells.	Docosahexaenoic Acids	70-90	heme oxygenase 1	Homo sapiens	40-56
26163453-2	2015	To date, little is known about whether fatty acids can affect HO-1 induction.	Fatty Acids	39-50	heme oxygenase 1	Homo sapiens	62-66
26163453-3	2015	Here, we report the induction of HO-1 by docosahexaenoic acid (DHA) and the associated molecular mechanisms in human myelomonocytic lymphoma U937 cells.	Docosahexaenoic Acids	41-61	heme oxygenase 1	Homo sapiens	33-37
26163453-3	2015	Here, we report the induction of HO-1 by docosahexaenoic acid (DHA) and the associated molecular mechanisms in human myelomonocytic lymphoma U937 cells.	Docosahexaenoic Acids	63-66	heme oxygenase 1	Homo sapiens	33-37
26163453-4	2015	When U937 cells were treated with DHA, eicosapentaenoic acid, palmitic acid or oleic acid, DHA was the most effective inducer of HO-1.	Docosahexaenoic Acids	34-37	heme oxygenase 1	Homo sapiens	129-133
26163453-4	2015	When U937 cells were treated with DHA, eicosapentaenoic acid, palmitic acid or oleic acid, DHA was the most effective inducer of HO-1.	Eicosapentaenoic Acid	39-60	heme oxygenase 1	Homo sapiens	129-133
26163453-4	2015	When U937 cells were treated with DHA, eicosapentaenoic acid, palmitic acid or oleic acid, DHA was the most effective inducer of HO-1.	Palmitic Acid	62-75	heme oxygenase 1	Homo sapiens	129-133
26163453-4	2015	When U937 cells were treated with DHA, eicosapentaenoic acid, palmitic acid or oleic acid, DHA was the most effective inducer of HO-1.	Oleic Acid	79-89	heme oxygenase 1	Homo sapiens	129-133
26163453-4	2015	When U937 cells were treated with DHA, eicosapentaenoic acid, palmitic acid or oleic acid, DHA was the most effective inducer of HO-1.	Docosahexaenoic Acids	91-94	heme oxygenase 1	Homo sapiens	129-133
26163453-7	2015	The increase in HO-1 expression was significantly inhibited by U0126, an ERK1/2 inhibitor.	U 0126	63-68	heme oxygenase 1	Homo sapiens	16-20
26163453-8	2015	Nuclear translocation of nuclear factor erythroid 2-related factor 2 (Nrf-2) and its binding to the HO-1 promoter significantly increased upon DHA treatment.	Docosahexaenoic Acids	143-146	heme oxygenase 1	Homo sapiens	100-104
26163453-10	2015	Pretreatment with NAC dramatically inhibited the ERK1/2 activation, binding of Nrf-2 to antioxidant response elements (AREs) located in the HO-1 promoter and the induction of HO-1 by DHA.	Docosahexaenoic Acids	183-186	heme oxygenase 1	Homo sapiens	175-179
26163453-11	2015	In conclusion, DHA increased HO-1 expression in U937 cells via activation of ERK1/2 and increased Nrf-2 binding to ARE in the HO-1 promoter.	Docosahexaenoic Acids	15-18	heme oxygenase 1	Homo sapiens	29-33
26163453-11	2015	In conclusion, DHA increased HO-1 expression in U937 cells via activation of ERK1/2 and increased Nrf-2 binding to ARE in the HO-1 promoter.	Docosahexaenoic Acids	15-18	heme oxygenase 1	Homo sapiens	126-130
25994789-7	2015	Chelating intracellular free zinc with tetrakis-(2-pyridylmethyl)ethylenediamine (TPEN) during tBHQ exposure partially abrogates the tBHQ-induced activation of Nrf2 and HO-1 expression, while Keap1 is further decreased.	N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine	82-86	heme oxygenase 1	Homo sapiens	169-173
25994789-7	2015	Chelating intracellular free zinc with tetrakis-(2-pyridylmethyl)ethylenediamine (TPEN) during tBHQ exposure partially abrogates the tBHQ-induced activation of Nrf2 and HO-1 expression, while Keap1 is further decreased.	2-tert-butylhydroquinone	133-137	heme oxygenase 1	Homo sapiens	169-173
26270345-1	2015	Earlier observations indicate that free heme is selectively toxic to cells lacking heme oxygenase-1 (HO-1) but how this enzyme prevents heme toxicity remains unexplained.	Heme	40-44	heme oxygenase 1	Homo sapiens	83-99
26270345-1	2015	Earlier observations indicate that free heme is selectively toxic to cells lacking heme oxygenase-1 (HO-1) but how this enzyme prevents heme toxicity remains unexplained.	Heme	40-44	heme oxygenase 1	Homo sapiens	101-105
26270345-2	2015	Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induced cell death.	Heme	112-116	heme oxygenase 1	Homo sapiens	140-144
26270345-2	2015	Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induced cell death.	Heme	206-210	heme oxygenase 1	Homo sapiens	140-144
26270345-2	2015	Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induced cell death.	Heme	206-210	heme oxygenase 1	Homo sapiens	140-144
26270345-3	2015	However, it appears that the toxic effects of heme are exerted by "loose" (probably intralysosomal) iron because cytotoxic effects of heme are lessened by pre-incubation of HO-1 deficient cells with desferrioxamine (which localizes preferentially in the lysosomal compartment).	Heme	46-50	heme oxygenase 1	Homo sapiens	173-177
26270345-3	2015	However, it appears that the toxic effects of heme are exerted by "loose" (probably intralysosomal) iron because cytotoxic effects of heme are lessened by pre-incubation of HO-1 deficient cells with desferrioxamine (which localizes preferentially in the lysosomal compartment).	Iron	100-104	heme oxygenase 1	Homo sapiens	173-177
26270345-3	2015	However, it appears that the toxic effects of heme are exerted by "loose" (probably intralysosomal) iron because cytotoxic effects of heme are lessened by pre-incubation of HO-1 deficient cells with desferrioxamine (which localizes preferentially in the lysosomal compartment).	Heme	134-138	heme oxygenase 1	Homo sapiens	173-177
26270345-3	2015	However, it appears that the toxic effects of heme are exerted by "loose" (probably intralysosomal) iron because cytotoxic effects of heme are lessened by pre-incubation of HO-1 deficient cells with desferrioxamine (which localizes preferentially in the lysosomal compartment).	Deferoxamine	199-214	heme oxygenase 1	Homo sapiens	173-177
26270345-5	2015	Supporting the importance of endogenous oxidant production, both chemical and siRNA inhibition of catalase activity predisposes HO-1 deficient cells to heme-mediated killing.	Heme	152-156	heme oxygenase 1	Homo sapiens	128-132
26270345-6	2015	Importantly, it appears that HO-1 deficiency somehow blocks the induction of ferritin; control cells exposed to heme show ~10-fold increases in ferritin heavy chain expression whereas in heme-exposed HO-1 deficient cells ferritin expression is unchanged.	Heme	112-116	heme oxygenase 1	Homo sapiens	29-33
26270345-6	2015	Importantly, it appears that HO-1 deficiency somehow blocks the induction of ferritin; control cells exposed to heme show ~10-fold increases in ferritin heavy chain expression whereas in heme-exposed HO-1 deficient cells ferritin expression is unchanged.	Heme	187-191	heme oxygenase 1	Homo sapiens	29-33
26270345-7	2015	Finally, overexpression of ferritin H chain in HO-1 deficient cells completely prevents heme-induced cytotoxicity.	Heme	88-92	heme oxygenase 1	Homo sapiens	47-51
26270345-8	2015	Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	31-35
26270345-8	2015	Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	93-97
26270345-8	2015	Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	93-97
26270345-8	2015	Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	93-97
26208625-0	2015	How does binding of imidazole-based inhibitors to heme oxygenase-1 influence their conformation?	imidazole	20-29	heme oxygenase 1	Homo sapiens	50-66
26208625-3	2015	Imidazole-based analogues show effective and selective inhibitory potency of HO-1.	imidazole	0-9	heme oxygenase 1	Homo sapiens	77-81
26208625-6	2015	Molecular docking of imidazole-based analogues in the active site of HO-1 is in good agreement with the experimental structures.	imidazole	21-30	heme oxygenase 1	Homo sapiens	69-73
26208625-7	2015	Inhibitors interact with the heme cofactor and a hydrophobic pocket (Met34, Phe37, Val50, Leu147 and Phe214) in the HO-1 binding site.	Heme	29-33	heme oxygenase 1	Homo sapiens	116-120
25994789-6	2015	Active Nrf2 and the antioxidant enzyme heme oxygenase-1 (HO-1) increase at 3 h after tBHQ treatment.	2-tert-butylhydroquinone	85-89	heme oxygenase 1	Homo sapiens	57-61
25994789-7	2015	Chelating intracellular free zinc with tetrakis-(2-pyridylmethyl)ethylenediamine (TPEN) during tBHQ exposure partially abrogates the tBHQ-induced activation of Nrf2 and HO-1 expression, while Keap1 is further decreased.	SCHEMBL231091	39-80	heme oxygenase 1	Homo sapiens	169-173
26080289-7	2015	This resistance was due to an ability to cope with PENAO-induced oxidative stress, notably through heme oxygenase-1 induction, and a shift in metabolism towards glycolysis.	HH7VUN8QBQ	51-56	heme oxygenase 1	Homo sapiens	99-115
26041409-0	2015	Src/STAT3-dependent heme oxygenase-1 induction mediates chemoresistance of breast cancer cells to doxorubicin by promoting autophagy.	Doxorubicin	98-109	heme oxygenase 1	Homo sapiens	20-36
26041409-3	2015	In the present study, we found an induction of HO-1 expression in doxorubicin (DOX)-treated MDA-MB-231 human breast adenocarcinoma cells, which showed insensitivity to DOX treatment.	Doxorubicin	66-77	heme oxygenase 1	Homo sapiens	47-51
26041409-3	2015	In the present study, we found an induction of HO-1 expression in doxorubicin (DOX)-treated MDA-MB-231 human breast adenocarcinoma cells, which showed insensitivity to DOX treatment.	Doxorubicin	79-82	heme oxygenase 1	Homo sapiens	47-51
26041409-4	2015	Knockdown HO-1 expression dramatically upregulated the incidence of MDA-MB-231 cell death under DOX treatment, indicating that HO-1 functions as a critical contributor to drug resistance in MDA-MB-231 cells.	Doxorubicin	96-99	heme oxygenase 1	Homo sapiens	10-14
26041409-4	2015	Knockdown HO-1 expression dramatically upregulated the incidence of MDA-MB-231 cell death under DOX treatment, indicating that HO-1 functions as a critical contributor to drug resistance in MDA-MB-231 cells.	Doxorubicin	96-99	heme oxygenase 1	Homo sapiens	127-131
26041409-5	2015	We further observed that DOX exposure induced a cytoprotective autophagic flux in MDA-MB-231 cells, which was dependent on HO-1 induction.	Doxorubicin	25-28	heme oxygenase 1	Homo sapiens	123-127
26041409-8	2015	Therefore, we conclude that Src/STAT3-dependent HO-1 induction protects MDA-MB-231 breast cancer cells from DOX-induced death through promoting autophagy.	Doxorubicin	108-111	heme oxygenase 1	Homo sapiens	48-52
26041409-9	2015	In the following study, we further demonstrated the contribution of Src/STAT3/HO-1/autophagy pathway activation to DOX resistance in another breast cancer cell line, MDA-MB-468, which bears a similar phenotype to MDA-MB-231 cells.	Doxorubicin	115-118	heme oxygenase 1	Homo sapiens	78-82
26041409-10	2015	Therefore, activation of Src/STAT3/HO-1/autophagy signaling pathway might play a general role in protecting certain subtypes of breast cancer cells from DOX-induced cytotoxicity.	Doxorubicin	153-156	heme oxygenase 1	Homo sapiens	35-39
25881548-4	2015	Quercetin induced the nuclear translocation of Nrf2, along with the increased expression of the antioxidant responsive element (ARE)-dependent genes like catalytic or modify subunit of glutamate-cysteine ligase (GCLC/GCLM), and heme oxygenase-1 (HO-1).	Quercetin	0-9	heme oxygenase 1	Homo sapiens	228-244
25881548-4	2015	Quercetin induced the nuclear translocation of Nrf2, along with the increased expression of the antioxidant responsive element (ARE)-dependent genes like catalytic or modify subunit of glutamate-cysteine ligase (GCLC/GCLM), and heme oxygenase-1 (HO-1).	Quercetin	0-9	heme oxygenase 1	Homo sapiens	246-250
25881548-5	2015	In addition, the HO-1 inhibitor zinc protoporphyrin (ZnPP) and the GCL inhibitor L-buthionine-(S,R)-sulfoximine (BSO) both reduced the hepatoprotection induced by quercetin.	zinc protoporphyrin	32-51	heme oxygenase 1	Homo sapiens	17-21
25881548-5	2015	In addition, the HO-1 inhibitor zinc protoporphyrin (ZnPP) and the GCL inhibitor L-buthionine-(S,R)-sulfoximine (BSO) both reduced the hepatoprotection induced by quercetin.	zinc protoporphyrin	53-57	heme oxygenase 1	Homo sapiens	17-21
25881548-5	2015	In addition, the HO-1 inhibitor zinc protoporphyrin (ZnPP) and the GCL inhibitor L-buthionine-(S,R)-sulfoximine (BSO) both reduced the hepatoprotection induced by quercetin.	Quercetin	163-172	heme oxygenase 1	Homo sapiens	17-21
25981584-1	2015	Cobalt protoporphyrin (CoPP) is a metallo-protoporphyrin that works as a powerful inducer of heme oxigenase-1 (HO-1) in various tissues and cells.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	93-109
25981584-1	2015	Cobalt protoporphyrin (CoPP) is a metallo-protoporphyrin that works as a powerful inducer of heme oxigenase-1 (HO-1) in various tissues and cells.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	111-115
25981584-1	2015	Cobalt protoporphyrin (CoPP) is a metallo-protoporphyrin that works as a powerful inducer of heme oxigenase-1 (HO-1) in various tissues and cells.	cobaltiprotoporphyrin	23-27	heme oxygenase 1	Homo sapiens	93-109
25981584-1	2015	Cobalt protoporphyrin (CoPP) is a metallo-protoporphyrin that works as a powerful inducer of heme oxigenase-1 (HO-1) in various tissues and cells.	cobaltiprotoporphyrin	23-27	heme oxygenase 1	Homo sapiens	111-115
25981584-1	2015	Cobalt protoporphyrin (CoPP) is a metallo-protoporphyrin that works as a powerful inducer of heme oxigenase-1 (HO-1) in various tissues and cells.	metallo-protoporphyrin	34-56	heme oxygenase 1	Homo sapiens	93-109
25981584-1	2015	Cobalt protoporphyrin (CoPP) is a metallo-protoporphyrin that works as a powerful inducer of heme oxigenase-1 (HO-1) in various tissues and cells.	metallo-protoporphyrin	34-56	heme oxygenase 1	Homo sapiens	111-115
25881548-11	2015	In addition, SP600125 also decreased the increased mRNA and protein expression of GCLC, GCLM, and HO-1 induced by quercetin.	pyrazolanthrone	13-21	heme oxygenase 1	Homo sapiens	98-102
25881548-11	2015	In addition, SP600125 also decreased the increased mRNA and protein expression of GCLC, GCLM, and HO-1 induced by quercetin.	Quercetin	114-123	heme oxygenase 1	Homo sapiens	98-102
26241392-9	2015	Mechanistically, 4-AC blocked the increase of cellular ROS induced by oxidative stress, and upregulated NQO1 and HO-1 genes by stabilizing and inducing the nuclear translocation of NRF2 transcription factor.	4-hydroxyphenylacetate	17-21	heme oxygenase 1	Homo sapiens	113-117
26283888-0	2015	Arsenic Trioxide Activate Transcription of Heme Oxygenase-1 by Promoting Nuclear Translocation of NFE2L2.	Arsenic Trioxide	0-16	heme oxygenase 1	Homo sapiens	43-59
26283888-1	2015	In a previous study, we found that induced expression of Heme Oxygenase-1 (HO-1) is responsible for the resistance of human osteosarcoma MG63 cells to the chemotherapeutic agent arsenic trioxide (ATO).	Arsenic Trioxide	178-194	heme oxygenase 1	Homo sapiens	57-73
26283888-1	2015	In a previous study, we found that induced expression of Heme Oxygenase-1 (HO-1) is responsible for the resistance of human osteosarcoma MG63 cells to the chemotherapeutic agent arsenic trioxide (ATO).	Arsenic Trioxide	178-194	heme oxygenase 1	Homo sapiens	75-79
26283888-1	2015	In a previous study, we found that induced expression of Heme Oxygenase-1 (HO-1) is responsible for the resistance of human osteosarcoma MG63 cells to the chemotherapeutic agent arsenic trioxide (ATO).	Arsenic Trioxide	196-199	heme oxygenase 1	Homo sapiens	57-73
26283888-1	2015	In a previous study, we found that induced expression of Heme Oxygenase-1 (HO-1) is responsible for the resistance of human osteosarcoma MG63 cells to the chemotherapeutic agent arsenic trioxide (ATO).	Arsenic Trioxide	196-199	heme oxygenase 1	Homo sapiens	75-79
26283888-2	2015	The present study was aimed at investigating the molecular mechanisms underlying the induction of HO-1 that occurs after exposure of MG63 cells to ATO.	Arsenic Trioxide	147-150	heme oxygenase 1	Homo sapiens	98-102
26283888-3	2015	First, using RT-QPCT and Western-blot, we found that ATO strongly induced the expression of heme oxygenase-1 (HO-1) in these human osteosarcoma cells.	Arsenic Trioxide	53-56	heme oxygenase 1	Homo sapiens	92-108
26283888-3	2015	First, using RT-QPCT and Western-blot, we found that ATO strongly induced the expression of heme oxygenase-1 (HO-1) in these human osteosarcoma cells.	Arsenic Trioxide	53-56	heme oxygenase 1	Homo sapiens	110-114
26283888-4	2015	Then by analyzing HO-1 mRNA of MG63 cells exposed to ATO in the presence and absence of a transcription inhibitor Actinomycin-D (Act-D), we demonstrated that ATO activates HO-1 expression in MG63 cells by regulating the transcription of the gene.	Arsenic Trioxide	53-56	heme oxygenase 1	Homo sapiens	18-22
26283888-4	2015	Then by analyzing HO-1 mRNA of MG63 cells exposed to ATO in the presence and absence of a transcription inhibitor Actinomycin-D (Act-D), we demonstrated that ATO activates HO-1 expression in MG63 cells by regulating the transcription of the gene.	Arsenic Trioxide	53-56	heme oxygenase 1	Homo sapiens	172-176
26283888-4	2015	Then by analyzing HO-1 mRNA of MG63 cells exposed to ATO in the presence and absence of a transcription inhibitor Actinomycin-D (Act-D), we demonstrated that ATO activates HO-1 expression in MG63 cells by regulating the transcription of the gene.	Dactinomycin	114-127	heme oxygenase 1	Homo sapiens	172-176
26283888-4	2015	Then by analyzing HO-1 mRNA of MG63 cells exposed to ATO in the presence and absence of a transcription inhibitor Actinomycin-D (Act-D), we demonstrated that ATO activates HO-1 expression in MG63 cells by regulating the transcription of the gene.	Arsenic Trioxide	158-161	heme oxygenase 1	Homo sapiens	18-22
26283888-4	2015	Then by analyzing HO-1 mRNA of MG63 cells exposed to ATO in the presence and absence of a transcription inhibitor Actinomycin-D (Act-D), we demonstrated that ATO activates HO-1 expression in MG63 cells by regulating the transcription of the gene.	Arsenic Trioxide	158-161	heme oxygenase 1	Homo sapiens	172-176
26283888-6	2015	From these results we have concluded that transcription activation of HO-1 resulting from the nuclear translocation of NFE2L2 is the underlying molecular mechanism for its high induction, which, in turn, is responsible for the resistance of human osteosarcoma cells to ATO treatment.	Arsenic Trioxide	269-272	heme oxygenase 1	Homo sapiens	70-74
26082074-2	2015	In the present study, in order to elucidate the mechanisms responsible for the antioxidant activity of GPE, its effects on the expression of critical antioxidant enzymes, such as catalase (CAT), superoxide dismutase (SOD)1, heme oxygenase 1 (HO-1) and gamma-glutamylcysteine synthetase (GCS) were assessed in EA.hy926 and C2C12 cells.	gpe	103-106	heme oxygenase 1	Homo sapiens	224-240
26267493-0	2015	Effect of heat stress-induced production of mitochondrial reactive oxygen species on NADPH oxidase and heme oxygenase-1 mRNA levels in avian muscle cells.	Reactive Oxygen Species	58-81	heme oxygenase 1	Homo sapiens	103-119
26267493-6	2015	Addition of the superoxide scavenger 4-hydroxy TEMPO to the culture medium of heat-stressed cells restored mitochondrial superoxide and intracellular ROS levels as well as NOX4 and HO-1 mRNA levels to near-normal values.	Superoxides	16-26	heme oxygenase 1	Homo sapiens	181-185
26267493-6	2015	Addition of the superoxide scavenger 4-hydroxy TEMPO to the culture medium of heat-stressed cells restored mitochondrial superoxide and intracellular ROS levels as well as NOX4 and HO-1 mRNA levels to near-normal values.	TEMPOL-H	37-52	heme oxygenase 1	Homo sapiens	181-185
26267493-7	2015	We suggest that mitochondrial superoxide production could play an influential role in augmenting oxidative damage to avian muscle cells, possibly via the up-regulation of NOX4 and down-regulation of HO-1 in heat-stressed avian muscle cells.	Superoxides	30-40	heme oxygenase 1	Homo sapiens	199-203
25951827-9	2015	Genetic silencing of Nrf2 prevented the induction of HO-1 and mitochondrial biogenesis by cilostazol in HepG2 cells.	Cilostazol	90-100	heme oxygenase 1	Homo sapiens	53-57
26211586-0	2015	Cerium oxide nanoparticles alleviate oxidative stress and decreases Nrf-2/HO-1 in D-GALN/LPS induced hepatotoxicity.	ceric oxide	0-12	heme oxygenase 1	Homo sapiens	74-78
26211586-1	2015	Translocation of the master regulator of antioxidant-response element-driven antioxidant gene, nuclear factor erythroid 2 (Nrf-2) from the cytoplasm into the nucleus and triggering the transcription of hemoxygenase-1 (HO-1) to counteract the oxidative stress is a key feature in D-galactoseamine and lipopolysaccharide (D-GALN/LPS) induced hepatotoxicity.	d-galactoseamine	279-295	heme oxygenase 1	Homo sapiens	202-222
26088684-0	2015	Resveratrol Protects Hippocampal Astrocytes Against LPS-Induced Neurotoxicity Through HO-1, p38 and ERK Pathways.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	86-90
26088684-11	2015	Additionally, we demonstrated the involvement of NFkappaB, HO-1, p38 and ERK signaling pathways in the protective effect of resveratrol, providing the first mechanistic explanation for these effects in hippocampal astrocytes.	Resveratrol	124-135	heme oxygenase 1	Homo sapiens	59-63
26146841-3	2015	Eleven common mutations and polymorphisms across five bilirubin metabolism genes, namely those encoding UGT1A1, HMOX1, BLVRA, SLCO1B1 and SLCO1B3, were determined using the high resolution melt (HRM) assay or PCR-capillary electrophoresis analysis.	Bilirubin	54-63	heme oxygenase 1	Homo sapiens	112-117
26211586-2	2015	We mainly aimed to study the effect of cerium oxide (CeO2) nanoparticles on Nrf-2/HO-1 pathway whereas; it has previously shown to have an antioxidant effect in liver models.	ceric oxide	39-51	heme oxygenase 1	Homo sapiens	82-86
26211586-2	2015	We mainly aimed to study the effect of cerium oxide (CeO2) nanoparticles on Nrf-2/HO-1 pathway whereas; it has previously shown to have an antioxidant effect in liver models.	ceric oxide	53-57	heme oxygenase 1	Homo sapiens	82-86
26211586-3	2015	Administration of CeO2 nanoparticles significantly decreased the translocation of the cytoplasmic Nrf-2 with a concomitant decrement in the gene expression of HO-1 as it reveals a powerful antioxidative effect as indicated by the significant increase in the levels of glutathione (GSH), glutathione peroxidase (GPX1), glutathione reductase (GR), superoxide dismutase (SOD) and catalase.	Glutathione	268-279	heme oxygenase 1	Homo sapiens	159-163
26211586-3	2015	Administration of CeO2 nanoparticles significantly decreased the translocation of the cytoplasmic Nrf-2 with a concomitant decrement in the gene expression of HO-1 as it reveals a powerful antioxidative effect as indicated by the significant increase in the levels of glutathione (GSH), glutathione peroxidase (GPX1), glutathione reductase (GR), superoxide dismutase (SOD) and catalase.	Glutathione	281-284	heme oxygenase 1	Homo sapiens	159-163
25109682-0	2015	Monosodium urate crystals trigger Nrf2- and heme oxygenase-1-dependent inflammation in THP-1 cells.	Uric Acid	0-16	heme oxygenase 1	Homo sapiens	44-60
25109682-9	2015	MSU-induced IL-1beta secretion and NLRP3 inflammasome activation were inhibited by the knockdown of Nrf2 and via the HO-1 inhibitor zinc (II) protoporphyrin IX (ZnPP).	zinc;3-[7,12-bis(ethenyl)-18-(3-hydroperoxyprop-1-en-2-yl)-3,8,13,17-tetramethylporphyrin-21,23-diid-2-yl]propanoic acid	132-159	heme oxygenase 1	Homo sapiens	117-121
25109682-9	2015	MSU-induced IL-1beta secretion and NLRP3 inflammasome activation were inhibited by the knockdown of Nrf2 and via the HO-1 inhibitor zinc (II) protoporphyrin IX (ZnPP).	zinc protoporphyrin	161-165	heme oxygenase 1	Homo sapiens	117-121
25109682-10	2015	In addition, HO-1 inhibition increased the level of superoxide anion production and the consumption of glutathione.	Superoxides	52-68	heme oxygenase 1	Homo sapiens	13-17
25109682-10	2015	In addition, HO-1 inhibition increased the level of superoxide anion production and the consumption of glutathione.	Glutathione	103-114	heme oxygenase 1	Homo sapiens	13-17
25109682-11	2015	These findings suggest that Nrf2 and HO-1 mediate redox homeostasis and interact with pro-inflammatory factors in MSU-challenged THP-1 cells, thereby providing new insight into how MSU-induced gouty inflammation is mediated by specific mechanisms that are involved in the Nrf2/Ho-1 antioxidant signaling pathway.Cellular &amp; Molecular Immunology advance online publication, 11 August 2014; doi:10.1038/cmi.2014.65.	Uric Acid	114-117	heme oxygenase 1	Homo sapiens	37-41
25109682-11	2015	These findings suggest that Nrf2 and HO-1 mediate redox homeostasis and interact with pro-inflammatory factors in MSU-challenged THP-1 cells, thereby providing new insight into how MSU-induced gouty inflammation is mediated by specific mechanisms that are involved in the Nrf2/Ho-1 antioxidant signaling pathway.Cellular &amp; Molecular Immunology advance online publication, 11 August 2014; doi:10.1038/cmi.2014.65.	Uric Acid	114-117	heme oxygenase 1	Homo sapiens	277-281
25109682-11	2015	These findings suggest that Nrf2 and HO-1 mediate redox homeostasis and interact with pro-inflammatory factors in MSU-challenged THP-1 cells, thereby providing new insight into how MSU-induced gouty inflammation is mediated by specific mechanisms that are involved in the Nrf2/Ho-1 antioxidant signaling pathway.Cellular &amp; Molecular Immunology advance online publication, 11 August 2014; doi:10.1038/cmi.2014.65.	Adenosine Monophosphate	322-325	heme oxygenase 1	Homo sapiens	37-41
25820186-1	2015	BACKGROUND: Over-expression of the heme-degrading enzyme, heme oxygenase-1 (HO-1) promotes iron deposition, mitochondrial damage, and autophagy in astrocytes and enhances the vulnerability of nearby neuronal constituents to oxidative injury.	Heme	35-39	heme oxygenase 1	Homo sapiens	58-74
25820186-1	2015	BACKGROUND: Over-expression of the heme-degrading enzyme, heme oxygenase-1 (HO-1) promotes iron deposition, mitochondrial damage, and autophagy in astrocytes and enhances the vulnerability of nearby neuronal constituents to oxidative injury.	Heme	35-39	heme oxygenase 1	Homo sapiens	76-80
25820186-1	2015	BACKGROUND: Over-expression of the heme-degrading enzyme, heme oxygenase-1 (HO-1) promotes iron deposition, mitochondrial damage, and autophagy in astrocytes and enhances the vulnerability of nearby neuronal constituents to oxidative injury.	Iron	91-95	heme oxygenase 1	Homo sapiens	58-74
25820186-1	2015	BACKGROUND: Over-expression of the heme-degrading enzyme, heme oxygenase-1 (HO-1) promotes iron deposition, mitochondrial damage, and autophagy in astrocytes and enhances the vulnerability of nearby neuronal constituents to oxidative injury.	Iron	91-95	heme oxygenase 1	Homo sapiens	76-80
25820186-7	2015	CO and Fe were implicated in the HMOX1 effects, whereas bilirubin was inert or counteracted the HMOX1-related changes.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	33-38
25820186-7	2015	CO and Fe were implicated in the HMOX1 effects, whereas bilirubin was inert or counteracted the HMOX1-related changes.	Bilirubin	56-65	heme oxygenase 1	Homo sapiens	96-101
26011640-8	2015	Collectively, we found that microglial HO-1 and the generation of CO are essential for effective elimination of blood and heme after SAH that otherwise leads to neuronal injury and cognitive dysfunction.	Heme	122-126	heme oxygenase 1	Homo sapiens	39-43
25929446-7	2015	In addition, phloretin increased heme oxygenase-1 production in a concentration-dependent manner.	Phloretin	13-22	heme oxygenase 1	Homo sapiens	33-49
26595496-2	2015	Heme oxygenase-1(HO-1) metabolizes heme into biliverdin, bilirubin, carbon monoxide, and iron, our recent study showed that serum level of HO-1 was increased in stroke patients, yet the association of HO-1 level with risk of intracerebral hemorrhage (ICH) is poorly known.	Heme	35-39	heme oxygenase 1	Homo sapiens	0-16
26595496-2	2015	Heme oxygenase-1(HO-1) metabolizes heme into biliverdin, bilirubin, carbon monoxide, and iron, our recent study showed that serum level of HO-1 was increased in stroke patients, yet the association of HO-1 level with risk of intracerebral hemorrhage (ICH) is poorly known.	Biliverdine	45-55	heme oxygenase 1	Homo sapiens	0-16
26595496-2	2015	Heme oxygenase-1(HO-1) metabolizes heme into biliverdin, bilirubin, carbon monoxide, and iron, our recent study showed that serum level of HO-1 was increased in stroke patients, yet the association of HO-1 level with risk of intracerebral hemorrhage (ICH) is poorly known.	Bilirubin	57-66	heme oxygenase 1	Homo sapiens	0-16
26595496-2	2015	Heme oxygenase-1(HO-1) metabolizes heme into biliverdin, bilirubin, carbon monoxide, and iron, our recent study showed that serum level of HO-1 was increased in stroke patients, yet the association of HO-1 level with risk of intracerebral hemorrhage (ICH) is poorly known.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	0-16
26595496-2	2015	Heme oxygenase-1(HO-1) metabolizes heme into biliverdin, bilirubin, carbon monoxide, and iron, our recent study showed that serum level of HO-1 was increased in stroke patients, yet the association of HO-1 level with risk of intracerebral hemorrhage (ICH) is poorly known.	Iron	89-93	heme oxygenase 1	Homo sapiens	0-16
25815672-0	2015	Effects of Eicosapentaenoic Acid on the Cytoprotection Through Nrf2-Mediated Heme Oxygenase-1 in Human Endothelial Cells.	Eicosapentaenoic Acid	11-32	heme oxygenase 1	Homo sapiens	77-93
25815672-2	2015	The aim of this study was to investigate whether heme oxygenase-1 (HO-1) induction contributes to the cytoprotective effects of EPA in endothelial cells threatened with oxidative damage.	Eicosapentaenoic Acid	128-131	heme oxygenase 1	Homo sapiens	49-65
25815672-2	2015	The aim of this study was to investigate whether heme oxygenase-1 (HO-1) induction contributes to the cytoprotective effects of EPA in endothelial cells threatened with oxidative damage.	Eicosapentaenoic Acid	128-131	heme oxygenase 1	Homo sapiens	67-71
25804888-10	2015	Increased transcript expression of metallothioneins, MT1A and MT2A and the stress response genes HMOX1 (690%) and HIF1A (247%) occurred in CATLE cells possibly in adaptation to chronic arsenic exposure.	Arsenic	185-192	heme oxygenase 1	Homo sapiens	97-102
25815672-3	2015	In this study, we investigated the effect of EPA on the induction of HO-1 by NF-E2-related factor 2 (Nrf2) in human umbilical vein endothelial cells.	Eicosapentaenoic Acid	45-48	heme oxygenase 1	Homo sapiens	69-73
25815672-4	2015	In cells treated with low concentrations of EPA (10-25 muM), HO-1 expression increased in a time- and concentration-dependent manner.	Eicosapentaenoic Acid	44-47	heme oxygenase 1	Homo sapiens	61-65
25815672-5	2015	Additionally, EPA treatment increased Nrf2 nuclear translocation and antioxidant response element activity, leading to the upregulation of HO-1 expression.	Eicosapentaenoic Acid	14-17	heme oxygenase 1	Homo sapiens	139-143
25815672-7	2015	The reduction in cell death was reversed by treatment with zinc protoporphyrin, an inhibitor of HO-1, indicating that HO-1 contributed to the protective effect of EPA.	zinc protoporphyrin	59-78	heme oxygenase 1	Homo sapiens	96-100
25815672-7	2015	The reduction in cell death was reversed by treatment with zinc protoporphyrin, an inhibitor of HO-1, indicating that HO-1 contributed to the protective effect of EPA.	zinc protoporphyrin	59-78	heme oxygenase 1	Homo sapiens	118-122
25815672-7	2015	The reduction in cell death was reversed by treatment with zinc protoporphyrin, an inhibitor of HO-1, indicating that HO-1 contributed to the protective effect of EPA.	Eicosapentaenoic Acid	163-166	heme oxygenase 1	Homo sapiens	96-100
25815672-7	2015	The reduction in cell death was reversed by treatment with zinc protoporphyrin, an inhibitor of HO-1, indicating that HO-1 contributed to the protective effect of EPA.	Eicosapentaenoic Acid	163-166	heme oxygenase 1	Homo sapiens	118-122
25815672-8	2015	These data suggest that EPA protects against H(2)O(2)-induced oxidative stress in endothelial cells by activating Nrf2 and inducting HO-1 expression.	Eicosapentaenoic Acid	24-27	heme oxygenase 1	Homo sapiens	133-137
25815672-8	2015	These data suggest that EPA protects against H(2)O(2)-induced oxidative stress in endothelial cells by activating Nrf2 and inducting HO-1 expression.	Hydrogen Peroxide	45-53	heme oxygenase 1	Homo sapiens	133-137
25815690-9	2015	The results of the present study suggested that Pic may have the potential to prevent PA-induced impairment of insulin signaling and eNOS function, by inducing the expression of the anti-inflammatory and antioxidant, HO-1.	3,3',4,5'-tetrahydroxystilbene	48-51	heme oxygenase 1	Homo sapiens	217-221
25815690-9	2015	The results of the present study suggested that Pic may have the potential to prevent PA-induced impairment of insulin signaling and eNOS function, by inducing the expression of the anti-inflammatory and antioxidant, HO-1.	Palmitic Acid	86-88	heme oxygenase 1	Homo sapiens	217-221
25815690-0	2015	Resveratrol analog piceatannol restores the palmitic acid-induced impairment of insulin signaling and production of endothelial nitric oxide via activation of anti-inflammatory and antioxidative heme oxygenase-1 in human endothelial cells.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	195-211
25815690-0	2015	Resveratrol analog piceatannol restores the palmitic acid-induced impairment of insulin signaling and production of endothelial nitric oxide via activation of anti-inflammatory and antioxidative heme oxygenase-1 in human endothelial cells.	3,3',4,5'-tetrahydroxystilbene	19-30	heme oxygenase 1	Homo sapiens	195-211
25815690-0	2015	Resveratrol analog piceatannol restores the palmitic acid-induced impairment of insulin signaling and production of endothelial nitric oxide via activation of anti-inflammatory and antioxidative heme oxygenase-1 in human endothelial cells.	Palmitic Acid	44-57	heme oxygenase 1	Homo sapiens	195-211
26003724-0	2015	Ammonia-induced oxidative damage in neurons is prevented by resveratrol and lipoic acid with participation of heme oxygenase 1.	Ammonia	0-7	heme oxygenase 1	Homo sapiens	110-126
26003724-0	2015	Ammonia-induced oxidative damage in neurons is prevented by resveratrol and lipoic acid with participation of heme oxygenase 1.	Thioctic Acid	76-87	heme oxygenase 1	Homo sapiens	110-126
26003724-10	2015	Moreover, we showed that heme oxygenase 1 (HO1), a protein associated with protection against stress conditions, is involved in the beneficial effects of RSV and LA in cerebellar granule neurons.	Resveratrol	154-157	heme oxygenase 1	Homo sapiens	25-41
26003724-10	2015	Moreover, we showed that heme oxygenase 1 (HO1), a protein associated with protection against stress conditions, is involved in the beneficial effects of RSV and LA in cerebellar granule neurons.	Resveratrol	154-157	heme oxygenase 1	Homo sapiens	43-46
26132561-0	2015	Eriodictyol Protects Endothelial Cells against Oxidative Stress-Induced Cell Death through Modulating ERK/Nrf2/ARE-Dependent Heme Oxygenase-1 Expression.	eriodictyol	0-11	heme oxygenase 1	Homo sapiens	125-141
26132561-5	2015	In this study, human umbilical vein endothelial cells (HUVECs) treated with eriodictyol showed the upregulation of HO-1 through extracellular-regulated kinase (ERK)/nuclear factor erythroid 2-related factor 2 (Nrf2)/antioxidant response element (ARE) signaling pathways.	eriodictyol	76-87	heme oxygenase 1	Homo sapiens	115-119
26132561-8	2015	These data demonstrate that eriodictyol induces ERK/Nrf2/ARE-mediated HO-1 upregulation in human endothelial cells, which is directly associated with its vascular protection against oxidative stress-related endothelial injury, and propose that targeting the upregulation of HO-1 is a promising approach for therapeutic intervention in cardiovascular disease.	eriodictyol	28-39	heme oxygenase 1	Homo sapiens	70-74
26132561-8	2015	These data demonstrate that eriodictyol induces ERK/Nrf2/ARE-mediated HO-1 upregulation in human endothelial cells, which is directly associated with its vascular protection against oxidative stress-related endothelial injury, and propose that targeting the upregulation of HO-1 is a promising approach for therapeutic intervention in cardiovascular disease.	eriodictyol	28-39	heme oxygenase 1	Homo sapiens	274-278
25904702-6	2015	Our results demonstrated that pretreatment of hASCs with melatonin, 100 muM for 3 h, significantly increased their proliferation and their expression of prosurvival P-Erk1/2 and P-Akt, and of antioxidative enzymes catalase and heme oxygenase (HO)-1.	Melatonin	57-66	heme oxygenase 1	Homo sapiens	227-248
25978654-4	2015	In addition, NHDC induces the phase II antioxidant enzymes heme oxygenase 1 (HO-1) and NAD(P)H/quinone oxidoreductase 1 (NQO1) through the activation of the nuclear factor (erythroid-derived 2)-like 2 (Nrf2)/antioxidant response element (ARE) signaling.	neohesperidin dihydrochalcone	13-17	heme oxygenase 1	Homo sapiens	59-75
26110640-11	2015	Enhanced HO-1 expression in dh404 treated islets was confirmed by Western Blot assay.	dh404	28-33	heme oxygenase 1	Homo sapiens	9-13
26045540-3	2015	HO-1 converts the pro-oxidant, proinflammatory heme molecule into metabolites with antioxidant, anti-inflammatory, and proliferative activities.	Heme	47-51	heme oxygenase 1	Homo sapiens	0-4
26045540-4	2015	Previously published work has shown that KSHV-infected EC in vitro proliferate in response to free heme in a HO-1-dependent manner, thus implicating virus-enhanced HO-1 activity in KS tumorigenesis.	Heme	99-103	heme oxygenase 1	Homo sapiens	109-113
26045540-4	2015	Previously published work has shown that KSHV-infected EC in vitro proliferate in response to free heme in a HO-1-dependent manner, thus implicating virus-enhanced HO-1 activity in KS tumorigenesis.	Heme	99-103	heme oxygenase 1	Homo sapiens	164-168
26045540-12	2015	The detoxifying action of HO-1 is critical for the protection of cells exposed to high heme levels.	Heme	87-91	heme oxygenase 1	Homo sapiens	26-30
26045540-15	2015	Our previous work showed that KSHV-infected cells proliferate in response to heme and that this occurs in a HO-1-dependent manner.	Heme	77-81	heme oxygenase 1	Homo sapiens	108-112
26045540-16	2015	We therefore hypothesize that KSHV induction of HO-1 contributes to KS tumor development via heme metabolism and propose that HO-1 be evaluated as a therapeutic target for KS.	Heme	93-97	heme oxygenase 1	Homo sapiens	48-52
25932745-8	2015	Conversely, lycopene treatment enhanced heme oxygenase-1 (HO-1) gene expression through the activation of phosphoinositide 3-kinase (PI3K)/Akt pathway, followed by induction of the nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation; in addition, HO-1 silencing partially inhibited the repressive effects of lycopene on strain-induced ET-1 expression.	Lycopene	12-20	heme oxygenase 1	Homo sapiens	268-272
25615876-0	2015	Pretreatment with pPolyHb attenuates H2O2-induced endothelial cell injury through inhibition of JNK/p38 MAPK pathway by upregulation of heme oxygenase-1.	Hydrogen Peroxide	37-41	heme oxygenase 1	Homo sapiens	136-152
25615876-3	2015	The results showed that the pretreatment augmented heme oxygenase-1 (HO-1) expression, and at the same time, decreased the phosphorylation of JNK/p38 mitogen-activated protein kinase (MAPK) and intracellular ROS generation in H2O2-treated HUVECs.	ros	208-211	heme oxygenase 1	Homo sapiens	51-67
25615876-3	2015	The results showed that the pretreatment augmented heme oxygenase-1 (HO-1) expression, and at the same time, decreased the phosphorylation of JNK/p38 mitogen-activated protein kinase (MAPK) and intracellular ROS generation in H2O2-treated HUVECs.	ros	208-211	heme oxygenase 1	Homo sapiens	69-73
25615876-3	2015	The results showed that the pretreatment augmented heme oxygenase-1 (HO-1) expression, and at the same time, decreased the phosphorylation of JNK/p38 mitogen-activated protein kinase (MAPK) and intracellular ROS generation in H2O2-treated HUVECs.	Hydrogen Peroxide	226-230	heme oxygenase 1	Homo sapiens	51-67
25615876-3	2015	The results showed that the pretreatment augmented heme oxygenase-1 (HO-1) expression, and at the same time, decreased the phosphorylation of JNK/p38 mitogen-activated protein kinase (MAPK) and intracellular ROS generation in H2O2-treated HUVECs.	Hydrogen Peroxide	226-230	heme oxygenase 1	Homo sapiens	69-73
25615876-4	2015	Moreover, the inhibition of HO-1 expression by tin porphyrin (SnPP) abolished the protective effects of pPolyHb, which suggested that the cytoprotective effect of pPolyHb involves upregulating HO-1 and subsequently decreasing the phosphorylation of the JNK and p38 MAPK and ROS generation.	tin porphyrin	47-60	heme oxygenase 1	Homo sapiens	28-32
25615876-4	2015	Moreover, the inhibition of HO-1 expression by tin porphyrin (SnPP) abolished the protective effects of pPolyHb, which suggested that the cytoprotective effect of pPolyHb involves upregulating HO-1 and subsequently decreasing the phosphorylation of the JNK and p38 MAPK and ROS generation.	tin porphyrin	47-60	heme oxygenase 1	Homo sapiens	193-197
25615876-4	2015	Moreover, the inhibition of HO-1 expression by tin porphyrin (SnPP) abolished the protective effects of pPolyHb, which suggested that the cytoprotective effect of pPolyHb involves upregulating HO-1 and subsequently decreasing the phosphorylation of the JNK and p38 MAPK and ROS generation.	S-Nitroso-N-propionyl-D,L-penicillamine	62-66	heme oxygenase 1	Homo sapiens	28-32
25615876-4	2015	Moreover, the inhibition of HO-1 expression by tin porphyrin (SnPP) abolished the protective effects of pPolyHb, which suggested that the cytoprotective effect of pPolyHb involves upregulating HO-1 and subsequently decreasing the phosphorylation of the JNK and p38 MAPK and ROS generation.	S-Nitroso-N-propionyl-D,L-penicillamine	62-66	heme oxygenase 1	Homo sapiens	193-197
25615876-4	2015	Moreover, the inhibition of HO-1 expression by tin porphyrin (SnPP) abolished the protective effects of pPolyHb, which suggested that the cytoprotective effect of pPolyHb involves upregulating HO-1 and subsequently decreasing the phosphorylation of the JNK and p38 MAPK and ROS generation.	ros	274-277	heme oxygenase 1	Homo sapiens	28-32
25932745-0	2015	Lycopene inhibits cyclic strain-induced endothelin-1 expression through the suppression of reactive oxygen species generation and induction of heme oxygenase-1 in human umbilical vein endothelial cells.	Lycopene	0-8	heme oxygenase 1	Homo sapiens	143-159
25932745-8	2015	Conversely, lycopene treatment enhanced heme oxygenase-1 (HO-1) gene expression through the activation of phosphoinositide 3-kinase (PI3K)/Akt pathway, followed by induction of the nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation; in addition, HO-1 silencing partially inhibited the repressive effects of lycopene on strain-induced ET-1 expression.	Lycopene	12-20	heme oxygenase 1	Homo sapiens	40-56
25932745-8	2015	Conversely, lycopene treatment enhanced heme oxygenase-1 (HO-1) gene expression through the activation of phosphoinositide 3-kinase (PI3K)/Akt pathway, followed by induction of the nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation; in addition, HO-1 silencing partially inhibited the repressive effects of lycopene on strain-induced ET-1 expression.	Lycopene	12-20	heme oxygenase 1	Homo sapiens	58-62
25932745-8	2015	Conversely, lycopene treatment enhanced heme oxygenase-1 (HO-1) gene expression through the activation of phosphoinositide 3-kinase (PI3K)/Akt pathway, followed by induction of the nuclear factor erythroid 2-related factor 2 (Nrf2) nuclear translocation; in addition, HO-1 silencing partially inhibited the repressive effects of lycopene on strain-induced ET-1 expression.	Lycopene	329-337	heme oxygenase 1	Homo sapiens	58-62
25932745-9	2015	In summary, our study showed, for the first time, that lycopene inhibits cyclic strain-induced ET-1 gene expression through the suppression of ROS generation and induction of HO-1 in HUVECs.	Lycopene	55-63	heme oxygenase 1	Homo sapiens	175-179
26125799-1	2015	We evaluated the effects of down-regulated heme oxygenase (HO)-1 expression on the proliferation of the acute myelocytic leukemia Kasumi-1 cell line by using the HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX) in combination with daunorubicin (DNR), and evaluated the mechanism.	zinc protoporphyrin	177-199	heme oxygenase 1	Homo sapiens	43-64
26125799-1	2015	We evaluated the effects of down-regulated heme oxygenase (HO)-1 expression on the proliferation of the acute myelocytic leukemia Kasumi-1 cell line by using the HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX) in combination with daunorubicin (DNR), and evaluated the mechanism.	Daunorubicin	229-241	heme oxygenase 1	Homo sapiens	43-64
25714596-0	2015	Impact of Enhanced Production of Endogenous Heme Oxygenase-1 by Pitavastatin on Survival and Functional Activities of Bone Marrow-derived Mesenchymal Stem Cells.	pitavastatin	64-76	heme oxygenase 1	Homo sapiens	44-60
25714596-3	2015	We investigated the protective effect of statin-induced overexpression of HO-1 by examining changes in gene expression and function in MSCs after pitavastatin treatment.	pitavastatin	146-158	heme oxygenase 1	Homo sapiens	74-78
25714596-4	2015	The relative expression of the HO-1 and endothelial nitric oxide synthase genes in MSCs was significantly increased after treatment with pitavastatin (MSCs).	pitavastatin	137-149	heme oxygenase 1	Homo sapiens	31-35
25714596-9	2015	These results demonstrate that pitavastatin can enhance endogenous HO-1 expression in MSCs, which may protect the cells into the environment of oxidative stress with partial activation of endothelial nitric oxide synthase and Akt phosphorylation.	pitavastatin	31-43	heme oxygenase 1	Homo sapiens	67-71
25956277-1	2015	HO-1 gene encodes heme oxygenase-1 enzyme that catalyzes the oxidation of heme to carbon monoxide (CO).	Heme	18-22	heme oxygenase 1	Homo sapiens	0-4
26072076-0	2015	Protective effect of HO-1 transfection against ethanol-induced osteoblast damage.	Ethanol	47-54	heme oxygenase 1	Homo sapiens	21-25
26072076-2	2015	The aim of this study was to observe if HO-1 transfection could inhibit the damage of osteoblasts induced by ethanol.	Ethanol	109-116	heme oxygenase 1	Homo sapiens	40-44
26072076-8	2015	These results suggest that HO-1 plays a protective role in osteoblasts, and HO-1 transfection can effectively inhibit bone damage induced by ethanol.	Ethanol	141-148	heme oxygenase 1	Homo sapiens	76-80
25765514-8	2015	Among them, Hmox1, Bdkrb2, Adra2b, Ptgs2, Col1a2 and Tbxa2r are associated with endothelium-derived hyperpolarizing factor (EDHF).	endothelium-derived hyperpolarizing factor	80-122	heme oxygenase 1	Homo sapiens	12-17
25765514-8	2015	Among them, Hmox1, Bdkrb2, Adra2b, Ptgs2, Col1a2 and Tbxa2r are associated with endothelium-derived hyperpolarizing factor (EDHF).	edhf	124-128	heme oxygenase 1	Homo sapiens	12-17
25776458-0	2015	Myrosinase-treated glucoerucin is a potent inducer of the Nrf2 target gene heme oxygenase 1--studies in cultured HT-29 cells and mice.	glucoerucin	19-30	heme oxygenase 1	Homo sapiens	75-91
25956277-1	2015	HO-1 gene encodes heme oxygenase-1 enzyme that catalyzes the oxidation of heme to carbon monoxide (CO).	Carbon Monoxide	82-97	heme oxygenase 1	Homo sapiens	0-4
25633656-6	2015	The results of the present study demonstrated that the mRNA expression levels of HO-1 increased in a dose-dependent manner in the HepG2.2.15 cells, following exposure to 5-50 microM hemin.	Hemin	182-187	heme oxygenase 1	Homo sapiens	81-85
25751573-1	2015	BACKGROUND: Heme oxygenase 1 (HO1) catalyzes heme degradation, and offers protection for several organs, including the kidney.	Heme	45-49	heme oxygenase 1	Homo sapiens	12-28
25751573-1	2015	BACKGROUND: Heme oxygenase 1 (HO1) catalyzes heme degradation, and offers protection for several organs, including the kidney.	Heme	45-49	heme oxygenase 1	Homo sapiens	30-33
25956277-1	2015	HO-1 gene encodes heme oxygenase-1 enzyme that catalyzes the oxidation of heme to carbon monoxide (CO).	Carbon Monoxide	82-97	heme oxygenase 1	Homo sapiens	18-34
25956277-1	2015	HO-1 gene encodes heme oxygenase-1 enzyme that catalyzes the oxidation of heme to carbon monoxide (CO).	Carbon Monoxide	99-101	heme oxygenase 1	Homo sapiens	0-4
25956277-1	2015	HO-1 gene encodes heme oxygenase-1 enzyme that catalyzes the oxidation of heme to carbon monoxide (CO).	Carbon Monoxide	99-101	heme oxygenase 1	Homo sapiens	18-34
25956277-3	2015	A (GT) n dinucleotide repeat at HO-1 promoter is a polymorphic region and modulates gene transcription and associated with some of diseases.	Dinucleoside Phosphates	9-21	heme oxygenase 1	Homo sapiens	32-36
25849895-2	2015	Mammals contain two isoforms of this enzyme, HO2 and HO1, which share the same alpha-helical fold forming the catalytic core and heme binding site, as well as a membrane spanning helix at their C-termini.	Heme	129-133	heme oxygenase 1	Homo sapiens	53-56
25802333-0	2015	Induction of heme oxygenase-1 by Na+-H+ exchanger 1 protein plays a crucial role in imatinib-resistant chronic myeloid leukemia cells.	Imatinib Mesylate	84-92	heme oxygenase 1	Homo sapiens	13-29
25802333-3	2015	After treatment with the specific NHE1 inhibitor cariporide to decrease intracellular pH (pHi), the heme oxygenase-1 (HO-1) levels of the K562R cell line and cells from IM-insensitive CML patients decreased.	cariporide	49-59	heme oxygenase 1	Homo sapiens	100-116
26078725-10	2015	ROS scavenger N-acetyl-L-cysteine (NAC) blocked the autophagy process induced by 5cGy alpha particle, the upregulation of Nrf2 and HO-1, as well as the induced radio-resistance.	ros	0-3	heme oxygenase 1	Homo sapiens	131-135
26078725-11	2015	In conclusion, ROS elevation caused by LDIR promoted Autophagy/Nrf2-HO-1 and conferred radio-resistance in A549.	ros	15-18	heme oxygenase 1	Homo sapiens	68-72
25891083-13	2015	CONCLUSION: Curcumin inhibits appoptosin-induced apoptosis in SH-SY5Y cells by upregulating the expression of HO-1, reducing the production of intracellular heme and ROS, and preventing the DeltaPsim loss.	Curcumin	12-20	heme oxygenase 1	Homo sapiens	110-114
25941985-0	2015	Camptothecin suppresses expression of matrix metalloproteinase-9 and vascular endothelial growth factor in DU145 cells through PI3K/Akt-mediated inhibition of NF-kappaB activity and Nrf2-dependent induction of HO-1 expression.	Camptothecin	0-12	heme oxygenase 1	Homo sapiens	210-214
25795137-7	2015	Excess intracellular ROS induced by Dex significantly suppressed the expression levels of Nrf2 and the downstream effectors, HO1 and NQO1, but these changes could be reversed by I3C.	ros	21-24	heme oxygenase 1	Homo sapiens	125-128
25795137-7	2015	Excess intracellular ROS induced by Dex significantly suppressed the expression levels of Nrf2 and the downstream effectors, HO1 and NQO1, but these changes could be reversed by I3C.	Dexamethasone	36-39	heme oxygenase 1	Homo sapiens	125-128
25891083-0	2015	Curcumin inhibits appoptosin-induced apoptosis via upregulating heme oxygenase-1 expression in SH-SY5Y cells.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	64-80
25631293-6	2015	Moreover, DHEA stimulated the activation of Nrf2, which led to the expression of an antioxidant response gene, HO-1.	Dehydroepiandrosterone	10-14	heme oxygenase 1	Homo sapiens	111-115
25941985-6	2015	We further confirmed that CPT inhibits PMA-induced MMP-9 and VEGF expression by upregulating nuclear factor-erythroid related factor-2 (Nrf2)-mediated heme oxygenase-1 (HO-1) induction.	Tetradecanoylphorbol Acetate	39-42	heme oxygenase 1	Homo sapiens	151-167
25941985-6	2015	We further confirmed that CPT inhibits PMA-induced MMP-9 and VEGF expression by upregulating nuclear factor-erythroid related factor-2 (Nrf2)-mediated heme oxygenase-1 (HO-1) induction.	Tetradecanoylphorbol Acetate	39-42	heme oxygenase 1	Homo sapiens	169-173
25692285-0	2015	Anti-Inflammatory Activity of Butein and Luteolin Through Suppression of NFkappaB Activation and Induction of Heme Oxygenase-1.	butein	30-36	heme oxygenase 1	Homo sapiens	110-126
25744070-11	2015	Inhibition of HO-1 by tin protoporphyrin IX exacerbated autophagy and mitochondrial activity as well as cell viability in young cells.	tin protoporphyrin IX	22-43	heme oxygenase 1	Homo sapiens	14-18
25303683-4	2015	At 20% O2, DMF induced a stronger antioxidant response compared to 5% O2 as evidenced by a higher expression of heme oxygenase-1, NAD(P)H:quinone oxydoreductase-1 and superoxide dismutase-2.	Dimethyl Fumarate	11-14	heme oxygenase 1	Homo sapiens	112-189
25303683-4	2015	At 20% O2, DMF induced a stronger antioxidant response compared to 5% O2 as evidenced by a higher expression of heme oxygenase-1, NAD(P)H:quinone oxydoreductase-1 and superoxide dismutase-2.	Oxygen	70-72	heme oxygenase 1	Homo sapiens	112-189
25692285-7	2015	Additionally, the anti-inflammatory activities of butein and luteolin involved the induction of HO-1 expression, as confirmed by the zinc protoporphyrin (ZnPP) treatment (HO-1 selective inhibitor) and HO-1 small interfering (si)RNA system.	zinc protoporphyrin	133-152	heme oxygenase 1	Homo sapiens	96-100
25692285-7	2015	Additionally, the anti-inflammatory activities of butein and luteolin involved the induction of HO-1 expression, as confirmed by the zinc protoporphyrin (ZnPP) treatment (HO-1 selective inhibitor) and HO-1 small interfering (si)RNA system.	zinc protoporphyrin	154-158	heme oxygenase 1	Homo sapiens	96-100
25771143-0	2015	Rosuvastatin suppresses atrial tachycardia-induced cellular remodeling via Akt/Nrf2/heme oxygenase-1 pathway.	Rosuvastatin Calcium	0-12	heme oxygenase 1	Homo sapiens	84-100
25692285-8	2015	ZnPP-mediated downregulation and siRNA-mediated knockdown of HO-1 significantly abolished the inhibitory effects of butein and luteolin on the production of NO in LPS-induced macrophages.	butein	116-122	heme oxygenase 1	Homo sapiens	61-65
25771143-4	2015	Treatment of cultured atrium-derived myocytes (HL-1 cell line) with rosuvastatin enhanced HO-1 expression/activity and attenuated tachypacing-induced oxidative stress and myofibril degradation.	Rosuvastatin Calcium	68-80	heme oxygenase 1	Homo sapiens	90-94
25620054-5	2015	HO-1 expression and/or activity were inhibited by siRNA or tin protoporphyrin (Sn PPIX) and enhanced by an expression plasmid or cobalt protoporphyrin (CoPPIX).	tin protoporphyrin IX	59-77	heme oxygenase 1	Homo sapiens	0-4
25771143-5	2015	Heme oxygenase-1 inhibitors and small-interfering RNA for HO-1 blocked the inhibitory effect of rosuvastatin on tachypacing-stimulated changes, suggesting the crucial role of HO-1 in mediating the effect of rosuvastatin.	Rosuvastatin Calcium	96-108	heme oxygenase 1	Homo sapiens	58-62
25771143-5	2015	Heme oxygenase-1 inhibitors and small-interfering RNA for HO-1 blocked the inhibitory effect of rosuvastatin on tachypacing-stimulated changes, suggesting the crucial role of HO-1 in mediating the effect of rosuvastatin.	Rosuvastatin Calcium	96-108	heme oxygenase 1	Homo sapiens	175-179
25771143-5	2015	Heme oxygenase-1 inhibitors and small-interfering RNA for HO-1 blocked the inhibitory effect of rosuvastatin on tachypacing-stimulated changes, suggesting the crucial role of HO-1 in mediating the effect of rosuvastatin.	Rosuvastatin Calcium	207-219	heme oxygenase 1	Homo sapiens	58-62
25771143-5	2015	Heme oxygenase-1 inhibitors and small-interfering RNA for HO-1 blocked the inhibitory effect of rosuvastatin on tachypacing-stimulated changes, suggesting the crucial role of HO-1 in mediating the effect of rosuvastatin.	Rosuvastatin Calcium	207-219	heme oxygenase 1	Homo sapiens	175-179
25771143-7	2015	Furthermore, the involvement of Akt/Nrf2/HO-1 pathway in the antioxidant effect of rosuvastatin was documented in an ex vivo tachypacing model.	Rosuvastatin Calcium	83-95	heme oxygenase 1	Homo sapiens	41-45
25843086-3	2015	In this study, we found that the expression levels of Nrf2 and its target genes GCLC, HO-1, NQO1 were significantly higher in cisplatin-resistant A549 (A549/CDDP) cells than those in A549 cells, and this resistance was partially reversed by Nrf2 siRNA.	Cisplatin	126-135	heme oxygenase 1	Homo sapiens	86-90
25896339-4	2015	Following treatment with quercetin, analyses of the nuclear level of Nrf2, Nrf2 antioxidant response element-binding assay, Nrf2 promoter-luc assay, and RT-PCR toward the Nrf2-regulated gene, heme oxygenase-1, demonstrated that the induced Nrf2 is transcriptionally active.	Quercetin	25-34	heme oxygenase 1	Homo sapiens	192-208
25620054-5	2015	HO-1 expression and/or activity were inhibited by siRNA or tin protoporphyrin (Sn PPIX) and enhanced by an expression plasmid or cobalt protoporphyrin (CoPPIX).	tin protoporphyrin IX	79-86	heme oxygenase 1	Homo sapiens	0-4
25620054-5	2015	HO-1 expression and/or activity were inhibited by siRNA or tin protoporphyrin (Sn PPIX) and enhanced by an expression plasmid or cobalt protoporphyrin (CoPPIX).	cobaltiprotoporphyrin	129-150	heme oxygenase 1	Homo sapiens	0-4
25620054-5	2015	HO-1 expression and/or activity were inhibited by siRNA or tin protoporphyrin (Sn PPIX) and enhanced by an expression plasmid or cobalt protoporphyrin (CoPPIX).	coppix	152-158	heme oxygenase 1	Homo sapiens	0-4
25620054-7	2015	Inhibition of HO-1 enzymatic activity with SnPPIX and silencing of the HO-1 gene by siRNA enhanced DEP-induced ROS production, further decreased cell viability and increased expression of inflammatory and cell adhesion molecules.	tin protoporphyrin IX	43-49	heme oxygenase 1	Homo sapiens	14-18
25620054-7	2015	Inhibition of HO-1 enzymatic activity with SnPPIX and silencing of the HO-1 gene by siRNA enhanced DEP-induced ROS production, further decreased cell viability and increased expression of inflammatory and cell adhesion molecules.	ros	111-114	heme oxygenase 1	Homo sapiens	14-18
25620054-7	2015	Inhibition of HO-1 enzymatic activity with SnPPIX and silencing of the HO-1 gene by siRNA enhanced DEP-induced ROS production, further decreased cell viability and increased expression of inflammatory and cell adhesion molecules.	ros	111-114	heme oxygenase 1	Homo sapiens	71-75
25620054-8	2015	On the other hand, overexpression of the HO-1 gene by a pcDNA 3.1D/V5-HO-1 plasmid significantly mitigated ROS production, increased cell survival and decreased the expression of inflammatory genes.	ros	107-110	heme oxygenase 1	Homo sapiens	41-45
25620054-8	2015	On the other hand, overexpression of the HO-1 gene by a pcDNA 3.1D/V5-HO-1 plasmid significantly mitigated ROS production, increased cell survival and decreased the expression of inflammatory genes.	ros	107-110	heme oxygenase 1	Homo sapiens	70-74
25714994-5	2015	Ziram increased intracellular levels of zinc and copper, DMDC increased intracellular levels of only copper, and both dithiocarbamates enhanced oxidative injury evidenced by elevated levels of protein carbonyls and expression of heme oxygenase-1.	dithiocarbamates	118-134	heme oxygenase 1	Homo sapiens	229-245
24931165-1	2015	Heme oxygenase-1 (HO-1) is a heme-degrading enzyme anchored in the endoplasmic reticulum by a carboxyl-terminal transmembrane segment (TMS).	Heme	29-33	heme oxygenase 1	Homo sapiens	0-16
24931165-1	2015	Heme oxygenase-1 (HO-1) is a heme-degrading enzyme anchored in the endoplasmic reticulum by a carboxyl-terminal transmembrane segment (TMS).	Heme	29-33	heme oxygenase 1	Homo sapiens	18-22
25742418-5	2015	After translocation, Nrf2 subsequently binds to the antioxidant response element (ARE), up-regulated heme oxygenase-1 (HO-1), and NADH quinone oxidoreductase subunit 1 (NQO1), which may be considered as an antioxidative response to TCBQ-intoxication.	tetrachlorobenzoquinone	232-236	heme oxygenase 1	Homo sapiens	101-117
25875041-4	2015	The aim of the present study was to investigate whether EGCG could also inhibit PM2.5-induced oxidative stress by activating the nuclear factor E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway in human umbilical vein endothelial cells (HUVECs).	epigallocatechin gallate	56-60	heme oxygenase 1	Homo sapiens	171-187
25652453-0	2015	5-aminolevulinic acid combined with sodium ferrous citrate ameliorates H2O2-induced cardiomyocyte hypertrophy via activation of the MAPK/Nrf2/HO-1 pathway.	5-amino levulinic acid	0-21	heme oxygenase 1	Homo sapiens	142-146
25652453-0	2015	5-aminolevulinic acid combined with sodium ferrous citrate ameliorates H2O2-induced cardiomyocyte hypertrophy via activation of the MAPK/Nrf2/HO-1 pathway.	Ferromia	36-58	heme oxygenase 1	Homo sapiens	142-146
25652453-0	2015	5-aminolevulinic acid combined with sodium ferrous citrate ameliorates H2O2-induced cardiomyocyte hypertrophy via activation of the MAPK/Nrf2/HO-1 pathway.	Hydrogen Peroxide	71-75	heme oxygenase 1	Homo sapiens	142-146
25652453-3	2015	In this study, we investigated whether the heme precursor 5-aminolevulinic acid (5-ALA) with sodium ferrous citrate (SFC) could protect cardiomyocytes from H2O2-induced hypertrophy via modulation of HO-1 expression.	Heme	43-47	heme oxygenase 1	Homo sapiens	199-203
25652453-3	2015	In this study, we investigated whether the heme precursor 5-aminolevulinic acid (5-ALA) with sodium ferrous citrate (SFC) could protect cardiomyocytes from H2O2-induced hypertrophy via modulation of HO-1 expression.	5-amino levulinic acid	58-79	heme oxygenase 1	Homo sapiens	199-203
25652453-3	2015	In this study, we investigated whether the heme precursor 5-aminolevulinic acid (5-ALA) with sodium ferrous citrate (SFC) could protect cardiomyocytes from H2O2-induced hypertrophy via modulation of HO-1 expression.	5-amino levulinic acid	81-86	heme oxygenase 1	Homo sapiens	199-203
25652453-3	2015	In this study, we investigated whether the heme precursor 5-aminolevulinic acid (5-ALA) with sodium ferrous citrate (SFC) could protect cardiomyocytes from H2O2-induced hypertrophy via modulation of HO-1 expression.	SFC	117-120	heme oxygenase 1	Homo sapiens	199-203
25652453-13	2015	3) ERK1/2, p38, and SAPK/JNK signaling pathways were activated and modulate 5-ALA- and SFC-enhanced HO-1 expression.	5-amino levulinic acid	76-81	heme oxygenase 1	Homo sapiens	100-104
25652453-15	2015	In conclusion, our data suggest that 5-ALA and SFC protect HL-1 cells from H2O2-induced cardiac hypertrophy via activation of the MAPK/Nrf2/HO-1 signaling pathway.	5-amino levulinic acid	37-42	heme oxygenase 1	Homo sapiens	140-144
25652453-15	2015	In conclusion, our data suggest that 5-ALA and SFC protect HL-1 cells from H2O2-induced cardiac hypertrophy via activation of the MAPK/Nrf2/HO-1 signaling pathway.	Hydrogen Peroxide	75-79	heme oxygenase 1	Homo sapiens	140-144
25875041-8	2015	In addition, silencing Nrf2 abolished EGCG-induced Nrf2 and HO-1 upregulation and enhancement of cell viability.	epigallocatechin gallate	38-42	heme oxygenase 1	Homo sapiens	60-64
25875041-9	2015	The present study suggests that EGCG protects HUVECs from PM2.5-induced oxidative stress injury by upregulating Nrf2/HO-1 via activation of the p38 MAPK and the ERK1/2 signaling pathways.	epigallocatechin gallate	32-36	heme oxygenase 1	Homo sapiens	117-121
25875041-4	2015	The aim of the present study was to investigate whether EGCG could also inhibit PM2.5-induced oxidative stress by activating the nuclear factor E2-related factor 2 (Nrf2)/heme oxygenase-1 (HO-1) pathway in human umbilical vein endothelial cells (HUVECs).	epigallocatechin gallate	56-60	heme oxygenase 1	Homo sapiens	189-193
25875041-6	2015	Western blotting and PCR demonstrated that EGCG increased Nrf2 and HO-1 expression in HUVECs that had been exposed to PM2.5.	epigallocatechin gallate	43-47	heme oxygenase 1	Homo sapiens	67-71
28962395-8	2015	Our present experimental data support the notion that Cr(VI) caused mitochondrial damage, apoptosis, oxidative stress, and subsequently lead to a strong induction of HO1, GCLC and SOD2 via the Nrf-2 signaling pathway in hepatocytes.	Chromium	54-56	heme oxygenase 1	Homo sapiens	166-169
25807407-7	2015	RESULTS: Ketamine treatment dose-dependently attenuated the increased levels of proinflammatory mediators (HMGB1, nitric oxide, tumor necrosis factor alpha, and interleukin 1beta) and increased the HO-1 protein expression in LPS-activated macrophages.	Ketamine	9-17	heme oxygenase 1	Homo sapiens	198-202
25835394-0	2015	Heme oxygenase-1 protects corexit 9500A-induced respiratory epithelial injury across species.	corexit	26-33	heme oxygenase 1	Homo sapiens	0-16
25835394-5	2015	CE induced the expression of HO-1 as well as C-reactive protein (CRP) and NADPH oxidase 4 (NOX4), which are associated with ROS production.	ros	124-127	heme oxygenase 1	Homo sapiens	29-33
25835394-9	2015	Treatment with carbon monoxide releasing molecule-2 (CORM-2) significantly inhibited CE-induced ROS production, while the addition of HO-1 inhibitor, significantly increased CE-induced ROS production and apoptosis, suggesting a protective role of HO-1 or its reaction product, CO, in CE-induced apoptosis.	Carbon Monoxide	15-30	heme oxygenase 1	Homo sapiens	247-251
25835394-9	2015	Treatment with carbon monoxide releasing molecule-2 (CORM-2) significantly inhibited CE-induced ROS production, while the addition of HO-1 inhibitor, significantly increased CE-induced ROS production and apoptosis, suggesting a protective role of HO-1 or its reaction product, CO, in CE-induced apoptosis.	ros	185-188	heme oxygenase 1	Homo sapiens	134-138
25377066-6	2015	Moreover, we have revealed the PB treatment resulted in an increase in nuclear factor E2-related factor 2 (Nrf2) protein levels and subsequent activation of antioxidant response element (ARE) pathway genes of heme oxygenase-1 (HO-1) and gamma-glutamylcysteine synthetase (gamma-GCS) in SH-SY5Y cells.	pinocembrin	31-33	heme oxygenase 1	Homo sapiens	209-225
25595329-3	2015	It has been recently suggested that the heme-catabolizing enzyme heme oxygenase-1 is an essential component of the mesenchymal stromal cell-driven immune suppressive response.	Heme	40-44	heme oxygenase 1	Homo sapiens	65-81
25595329-4	2015	Because mesenchymal stromal cells upregulate indoleamine 2,3-dioxygenase expression on interferon-gamma priming and indoleamine 2,3-dioxygenase requires heme as a cofactor for optimal catabolic function, we investigated the potential antagonism of heme oxygenase-1 activity on indoleamine 2, 3-dioxygenase and the impact on mesenchymal stromal cell immune plasticity.	Heme	153-157	heme oxygenase 1	Homo sapiens	248-264
25667213-0	2015	Sofalcone upregulates the nuclear factor (erythroid-derived 2)-like 2/heme oxygenase-1 pathway, reduces soluble fms-like tyrosine kinase-1, and quenches endothelial dysfunction: potential therapeutic for preeclampsia.	sofalcone	0-9	heme oxygenase 1	Homo sapiens	70-86
25667213-5	2015	Sofalcone, a gastric antiulcer agent in clinical use, is known to induce HO-1 in gastric epithelium.	sofalcone	0-9	heme oxygenase 1	Homo sapiens	73-77
25667213-6	2015	We aimed to investigate whether sofalcone induces HO-1 and reduces sFlt-1 release from primary human placental and endothelial cells and blocks endothelial dysfunction in vitro.	sofalcone	32-41	heme oxygenase 1	Homo sapiens	50-54
25667213-9	2015	Sofalcone potently increased HO-1 mRNA and protein in both primary trophoblasts and human umbilical vein endothelial cells.	sofalcone	0-9	heme oxygenase 1	Homo sapiens	29-33
25667213-13	2015	These results indicate that in primary human tissues, sofalcone can potently activate antioxidant nuclear factor (erythroid-derived 2)-like 2/HO-1 pathway, decrease sFlt-1 production, and ameliorate endothelial dysfunction.	sofalcone	54-63	heme oxygenase 1	Homo sapiens	142-146
25653454-9	2015	The suppressive effect of HO-1 induction by protoporphyrin IX cobalt chloride (CoPP; a classical inducer of HO-1 expression) on PRRSV replication in MARC-145 cells and primary porcine alveolar macrophages could also be reversed by overexpression of miR-24-3p.	Protoporphyrin IX cobalt chloride	44-77	heme oxygenase 1	Homo sapiens	26-30
25653454-9	2015	The suppressive effect of HO-1 induction by protoporphyrin IX cobalt chloride (CoPP; a classical inducer of HO-1 expression) on PRRSV replication in MARC-145 cells and primary porcine alveolar macrophages could also be reversed by overexpression of miR-24-3p.	Protoporphyrin IX cobalt chloride	44-77	heme oxygenase 1	Homo sapiens	108-112
25653454-9	2015	The suppressive effect of HO-1 induction by protoporphyrin IX cobalt chloride (CoPP; a classical inducer of HO-1 expression) on PRRSV replication in MARC-145 cells and primary porcine alveolar macrophages could also be reversed by overexpression of miR-24-3p.	COPP protocol	79-83	heme oxygenase 1	Homo sapiens	26-30
25653454-9	2015	The suppressive effect of HO-1 induction by protoporphyrin IX cobalt chloride (CoPP; a classical inducer of HO-1 expression) on PRRSV replication in MARC-145 cells and primary porcine alveolar macrophages could also be reversed by overexpression of miR-24-3p.	COPP protocol	79-83	heme oxygenase 1	Homo sapiens	108-112
25652099-0	2015	Downregulation of HO-1 promoted apoptosis induced by decitabine via increasing p15INK4B promoter demethylation in myelodysplastic syndrome.	Decitabine	53-63	heme oxygenase 1	Homo sapiens	18-22
25652099-2	2015	In this study, heme oxygenase-1 (HO-1) was overexpressed in MDS cell line SKM-1, which was closely related to resistance to decitabine-induced apoptosis.	Decitabine	124-134	heme oxygenase 1	Homo sapiens	15-31
25652099-2	2015	In this study, heme oxygenase-1 (HO-1) was overexpressed in MDS cell line SKM-1, which was closely related to resistance to decitabine-induced apoptosis.	Decitabine	124-134	heme oxygenase 1	Homo sapiens	33-37
25652099-3	2015	We aimed to further investigate the role of HO-1 in apoptosis induced by low-dose decitabine in SKM-1 cells.	Decitabine	82-92	heme oxygenase 1	Homo sapiens	44-48
25652099-5	2015	In contrast, downregulation of HO-1 enhanced decitabine-induced apoptosis but reduced accumulation of the S phase in cell cycle.	Decitabine	45-55	heme oxygenase 1	Homo sapiens	31-35
25652099-12	2015	In conclusion, overexpression of HO-1 indicated resistance to demethylation of p15(INK4B) induced by decitabine.	Decitabine	101-111	heme oxygenase 1	Homo sapiens	33-37
25807407-0	2015	Ketamine reduces LPS-induced HMGB1 via activation of the Nrf2/HO-1 pathway and NF-kappaB suppression.	Ketamine	0-8	heme oxygenase 1	Homo sapiens	62-66
25807407-9	2015	In addition, the present study also demonstrated that ketamine induced HO-1 expression through the nuclear translocation of nuclear factor E2-related factor 2 in macrophages.	Ketamine	54-62	heme oxygenase 1	Homo sapiens	71-75
25807407-11	2015	CONCLUSION: Ketamine inhibits the release of HMGB1 in LPS-stimulated macrophages, and this effect is at least partly mediated by the activation of the Nrf2/HO-1 pathway and NF-kappaB suppression.	Ketamine	12-20	heme oxygenase 1	Homo sapiens	156-160
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Heme	95-99	heme oxygenase 1	Homo sapiens	0-16
25813625-9	2015	Taken together, these findings suggest that direct interaction of piperlongumine with Keap1 leads to the upregulation of Nrf2-mediated HO-1 expression, and HO-1 determines the differential response of breast normal cells and cancer cells to piperlongumine.	piperlonguminine	66-80	heme oxygenase 1	Homo sapiens	135-139
25813625-9	2015	Taken together, these findings suggest that direct interaction of piperlongumine with Keap1 leads to the upregulation of Nrf2-mediated HO-1 expression, and HO-1 determines the differential response of breast normal cells and cancer cells to piperlongumine.	piperlonguminine	241-255	heme oxygenase 1	Homo sapiens	156-160
25891728-6	2015	Immunohistochemistry and Western blot analysis data revealed that the FK506 treatment increased expression of heme oxygenase-1 (HO-1) in Jurkat cells in a dose-dependent manner.	Tacrolimus	70-75	heme oxygenase 1	Homo sapiens	110-126
25891728-6	2015	Immunohistochemistry and Western blot analysis data revealed that the FK506 treatment increased expression of heme oxygenase-1 (HO-1) in Jurkat cells in a dose-dependent manner.	Tacrolimus	70-75	heme oxygenase 1	Homo sapiens	128-132
25891728-7	2015	HO-1 expression was induced after 6 hours of treatment of FK506 to Jurkat cells, peaked at 24 hours, and then decreased after 48 hours.	Tacrolimus	58-63	heme oxygenase 1	Homo sapiens	0-4
25891728-8	2015	CONCLUSIONS: These results suggest that FK506 induces Nrf 2-driven transcriptional activation of the antioxidant response element by activating HO-1 and free radicals such as reactive oxygen species and nitric oxide.	Tacrolimus	40-45	heme oxygenase 1	Homo sapiens	144-148
25891728-8	2015	CONCLUSIONS: These results suggest that FK506 induces Nrf 2-driven transcriptional activation of the antioxidant response element by activating HO-1 and free radicals such as reactive oxygen species and nitric oxide.	Reactive Oxygen Species	175-198	heme oxygenase 1	Homo sapiens	144-148
25891728-8	2015	CONCLUSIONS: These results suggest that FK506 induces Nrf 2-driven transcriptional activation of the antioxidant response element by activating HO-1 and free radicals such as reactive oxygen species and nitric oxide.	Nitric Oxide	203-215	heme oxygenase 1	Homo sapiens	144-148
25813625-0	2015	Heme oxygenase-1 determines the differential response of breast cancer and normal cells to piperlongumine.	piperlonguminine	91-105	heme oxygenase 1	Homo sapiens	0-16
25813625-4	2015	Interestingly, this opposing effect of piperlongumine appears to be mediated by heme oxygenase-1 (HO-1).	piperlonguminine	39-53	heme oxygenase 1	Homo sapiens	80-96
25813625-4	2015	Interestingly, this opposing effect of piperlongumine appears to be mediated by heme oxygenase-1 (HO-1).	piperlonguminine	39-53	heme oxygenase 1	Homo sapiens	98-102
25813625-5	2015	Piperlongumine upregulated HO-1 expression through the activation of nuclear factor-erythroid-2-related factor-2 (Nrf2) signaling in both MCF-7 and MCF-10A cells.	piperlonguminine	0-14	heme oxygenase 1	Homo sapiens	27-31
25813625-6	2015	However, knockdown of HO-1 expression and pharmacological inhibition of its activity abolished the ability of piperlongumine to induce apoptosis in MCF-7 cells, whereas those promoted apoptosis in MCF-10A cells, indicating that HO-1 has anti-tumor functions in cancer cells but cytoprotective functions in normal cells.	piperlonguminine	110-124	heme oxygenase 1	Homo sapiens	22-26
25813625-6	2015	However, knockdown of HO-1 expression and pharmacological inhibition of its activity abolished the ability of piperlongumine to induce apoptosis in MCF-7 cells, whereas those promoted apoptosis in MCF-10A cells, indicating that HO-1 has anti-tumor functions in cancer cells but cytoprotective functions in normal cells.	piperlonguminine	110-124	heme oxygenase 1	Homo sapiens	228-232
25813625-7	2015	Moreover, it was found that piperlongumine-induced Nrf2 activation, HO-1 expression and cancer cell apoptosis are not dependent on the generation of reactive oxygen species.	piperlonguminine	28-42	heme oxygenase 1	Homo sapiens	68-72
25813625-8	2015	Instead, piperlongumine, which bears electrophilic alpha,beta-unsaturated carbonyl groups, appears to inactivate Kelch-like ECH-associated protein-1 (Keap1) through thiol modification, thereby activating the Nrf2/HO-1 pathway and subsequently upregulating HO-1 expression, which accounts for piperlongumine-induced apoptosis in cancer cells.	piperlonguminine	9-23	heme oxygenase 1	Homo sapiens	213-217
25813625-8	2015	Instead, piperlongumine, which bears electrophilic alpha,beta-unsaturated carbonyl groups, appears to inactivate Kelch-like ECH-associated protein-1 (Keap1) through thiol modification, thereby activating the Nrf2/HO-1 pathway and subsequently upregulating HO-1 expression, which accounts for piperlongumine-induced apoptosis in cancer cells.	piperlonguminine	9-23	heme oxygenase 1	Homo sapiens	256-260
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Heme	95-99	heme oxygenase 1	Homo sapiens	18-22
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Iron	117-121	heme oxygenase 1	Homo sapiens	0-16
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Iron	117-121	heme oxygenase 1	Homo sapiens	18-22
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Carbon Monoxide	123-138	heme oxygenase 1	Homo sapiens	0-16
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Carbon Monoxide	123-138	heme oxygenase 1	Homo sapiens	18-22
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Carbon Monoxide	140-142	heme oxygenase 1	Homo sapiens	0-16
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Carbon Monoxide	140-142	heme oxygenase 1	Homo sapiens	18-22
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Biliverdine	148-158	heme oxygenase 1	Homo sapiens	0-16
25885228-1	2015	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells.	Biliverdine	148-158	heme oxygenase 1	Homo sapiens	18-22
25885228-2	2015	In addition to its primary role in heme catabolism, HO-1 exhibits anti-oxidative and anti-inflammatory functions via the actions of biliverdin and CO, respectively.	Heme	35-39	heme oxygenase 1	Homo sapiens	52-56
25885228-2	2015	In addition to its primary role in heme catabolism, HO-1 exhibits anti-oxidative and anti-inflammatory functions via the actions of biliverdin and CO, respectively.	Biliverdine	132-142	heme oxygenase 1	Homo sapiens	52-56
25885228-2	2015	In addition to its primary role in heme catabolism, HO-1 exhibits anti-oxidative and anti-inflammatory functions via the actions of biliverdin and CO, respectively.	Carbon Monoxide	147-149	heme oxygenase 1	Homo sapiens	52-56
25686009-7	2015	Anthocyanin metabolites may therefore modulate vascular reactivity by inducing HO-1 and modulating NOX activity, resulting in reduced superoxide production and improved NO bioavailability.	Anthocyanins	0-11	heme oxygenase 1	Homo sapiens	79-83
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Heme	77-81	heme oxygenase 1	Homo sapiens	0-16
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Heme	77-81	heme oxygenase 1	Homo sapiens	18-22
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Iron	90-94	heme oxygenase 1	Homo sapiens	18-22
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Iron	90-94	heme oxygenase 1	Homo sapiens	0-16
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Carbon Monoxide	96-111	heme oxygenase 1	Homo sapiens	0-16
25769104-5	2015	Glutathione-S-transferase and Heme Oxygenase 1 mRNA levels are induced with ADE PM and reduced by DF and NAC.	Adenine	76-79	heme oxygenase 1	Homo sapiens	30-46
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Carbon Monoxide	96-111	heme oxygenase 1	Homo sapiens	18-22
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Biliverdine	116-126	heme oxygenase 1	Homo sapiens	0-16
25761244-1	2015	Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin.	Biliverdine	116-126	heme oxygenase 1	Homo sapiens	18-22
25761244-3	2015	In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions.	Iron	67-71	heme oxygenase 1	Homo sapiens	25-29
25761244-3	2015	In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions.	Iron	152-156	heme oxygenase 1	Homo sapiens	25-29
25761244-4	2015	Glial HO-1 expression may also impact neuroplasticity and cell survival by modulating brain sterol metabolism and the proteasomal degradation of neurotoxic proteins.	Sterols	92-98	heme oxygenase 1	Homo sapiens	6-10
25267105-12	2015	Besides, ES reduced TNF-alpha- and H2O2 -induced oxidative stress and in parallel induces anti-inflammatory haem oxygenase (HO)-1 expression.	sesamin	9-11	heme oxygenase 1	Homo sapiens	108-129
25592228-7	2015	Transfection with ATM induced expression of HO-1 which was mediated by PKC-delta and NF-kappaB in H2O2-treated MOCK cells.	Hydrogen Peroxide	98-102	heme oxygenase 1	Homo sapiens	44-48
26045831-0	2015	Effects of dexmedetomidine pretreatment on heme oxygenase-1 expression and oxidative stress during one-lung ventilation.	Dexmedetomidine	11-26	heme oxygenase 1	Homo sapiens	43-59
26045831-1	2015	PURPOSE: This study aimed to explore effects of dexmedetomidine pretreatment on heme oxygenase-1 (HO-1) expression and oxidative stress during one-lung ventilation (OLV) in lung cancer patients.	Dexmedetomidine	48-63	heme oxygenase 1	Homo sapiens	80-96
26045831-1	2015	PURPOSE: This study aimed to explore effects of dexmedetomidine pretreatment on heme oxygenase-1 (HO-1) expression and oxidative stress during one-lung ventilation (OLV) in lung cancer patients.	Dexmedetomidine	48-63	heme oxygenase 1	Homo sapiens	98-102
26045831-6	2015	Superoxide dismutase (SOD) activity and the expression level of HO-1 were higher in Dexmedetomidine group than in Control (P&lt;0.05).	Dexmedetomidine	84-99	heme oxygenase 1	Homo sapiens	64-68
26045831-7	2015	CONCLUSIONS: Dexmedetomidine pretreatment could upregulated expression of HO-1 in lung tissue and reduce oxidative stress and inflammation during OLV.	Dexmedetomidine	13-28	heme oxygenase 1	Homo sapiens	74-78
26045831-8	2015	Thus dexmedetomidine played a role in protecting lung injury by promoting HO-1 expression.	Dexmedetomidine	5-20	heme oxygenase 1	Homo sapiens	74-78
25585641-10	2015	Upregulation of p16 and changing of p16-relative cell cycle protein was observed after silencing HO-1 in AZA treated SKM-1 cells.	Azacitidine	105-108	heme oxygenase 1	Homo sapiens	97-101
25585641-12	2015	In vivo, silencing HO-1 inhibited SKM-1 cell growth induced by AZA in a NOD/SCID mouse model.	Azacitidine	63-66	heme oxygenase 1	Homo sapiens	19-23
25585641-13	2015	Silencing HO-1 sensitized SKM-1 cells toward AZA, which may be attributed to the influence of HO-1 on AZA-induced p16 demethylation.	Azacitidine	45-48	heme oxygenase 1	Homo sapiens	10-14
25585641-13	2015	Silencing HO-1 sensitized SKM-1 cells toward AZA, which may be attributed to the influence of HO-1 on AZA-induced p16 demethylation.	Azacitidine	45-48	heme oxygenase 1	Homo sapiens	94-98
25585641-13	2015	Silencing HO-1 sensitized SKM-1 cells toward AZA, which may be attributed to the influence of HO-1 on AZA-induced p16 demethylation.	Azacitidine	102-105	heme oxygenase 1	Homo sapiens	10-14
25585641-13	2015	Silencing HO-1 sensitized SKM-1 cells toward AZA, which may be attributed to the influence of HO-1 on AZA-induced p16 demethylation.	Azacitidine	102-105	heme oxygenase 1	Homo sapiens	94-98
25585641-14	2015	HO-1 may be one of the targets that enhance the therapeutic effects of AZA on MDS malignant transformation inspiring new treatment methods for high-risk and very high-risk MDS patients in clinical practice.	Azacitidine	71-74	heme oxygenase 1	Homo sapiens	0-4
25592228-8	2015	ZnPP, an HO-1 inhibitor, and transfection with HO-1 siRNA increased ROS levels and apoptosis, whereas hemin, an HO-1 activator, reduced ROS levels and apoptosis in H2O2-treated YZ5 cells.	zinc protoporphyrin	0-4	heme oxygenase 1	Homo sapiens	9-13
25592228-8	2015	ZnPP, an HO-1 inhibitor, and transfection with HO-1 siRNA increased ROS levels and apoptosis, whereas hemin, an HO-1 activator, reduced ROS levels and apoptosis in H2O2-treated YZ5 cells.	Reactive Oxygen Species	68-71	heme oxygenase 1	Homo sapiens	47-51
25592228-8	2015	ZnPP, an HO-1 inhibitor, and transfection with HO-1 siRNA increased ROS levels and apoptosis, whereas hemin, an HO-1 activator, reduced ROS levels and apoptosis in H2O2-treated YZ5 cells.	Reactive Oxygen Species	68-71	heme oxygenase 1	Homo sapiens	47-51
25592228-8	2015	ZnPP, an HO-1 inhibitor, and transfection with HO-1 siRNA increased ROS levels and apoptosis, whereas hemin, an HO-1 activator, reduced ROS levels and apoptosis in H2O2-treated YZ5 cells.	Hydrogen Peroxide	164-168	heme oxygenase 1	Homo sapiens	47-51
25592228-8	2015	ZnPP, an HO-1 inhibitor, and transfection with HO-1 siRNA increased ROS levels and apoptosis, whereas hemin, an HO-1 activator, reduced ROS levels and apoptosis in H2O2-treated YZ5 cells.	Hydrogen Peroxide	164-168	heme oxygenase 1	Homo sapiens	47-51
25592228-9	2015	Rottlerin, a PKC-delta inhibitor, inhibited NF-kappaB activation and HO-1 expression in H2O2-treated YZ5 cells.	rottlerin	0-9	heme oxygenase 1	Homo sapiens	69-73
25592228-9	2015	Rottlerin, a PKC-delta inhibitor, inhibited NF-kappaB activation and HO-1 expression in H2O2-treated YZ5 cells.	Hydrogen Peroxide	88-92	heme oxygenase 1	Homo sapiens	69-73
25592228-11	2015	In addition, transfection with p65 siRNA increased ROS levels and DNA fragmentation, but decreased HO-1 protein levels in H2O2-treated YZ5 cells.	Hydrogen Peroxide	122-126	heme oxygenase 1	Homo sapiens	99-103
25585641-0	2015	Silencing HO-1 sensitizes SKM-1 cells to apoptosis induced by low concentration 5-azacytidine through enhancing p16 demethylation.	Azacitidine	80-93	heme oxygenase 1	Homo sapiens	10-14
25585641-2	2015	We found that HO-1 was resistant to 5-azacytidine (AZA) treatment of myelodysplastic syndrome (MDS), and explored further the relative mechanisms.	Azacitidine	36-49	heme oxygenase 1	Homo sapiens	14-18
25585641-2	2015	We found that HO-1 was resistant to 5-azacytidine (AZA) treatment of myelodysplastic syndrome (MDS), and explored further the relative mechanisms.	Azacitidine	51-54	heme oxygenase 1	Homo sapiens	14-18
25585641-7	2015	HO-1 overexpression was observed in SKM-1 cells after AZA treatment comparing to other cell lines.	Azacitidine	54-57	heme oxygenase 1	Homo sapiens	0-4
25585641-9	2015	After HO-1 was silenced by lentivirus-mediated siRNA, the proliferation of SKM-1 cells was effectively inhibited by low concentration AZA, and the cell cycle was arrested in the G0/G1 phase.	Azacitidine	134-137	heme oxygenase 1	Homo sapiens	6-10
25471815-0	2015	alpha-Tocopherol protects renal cells from nicotine- or oleic acid-provoked oxidative stress via inducing heme oxygenase-1.	alpha-Tocopherol	0-16	heme oxygenase 1	Homo sapiens	106-122
25388553-2	2015	This study investigates the interaction between glucocorticoids or estrogens and GFs on the expression of heme oxygenase-1 (HO-1) and cyclin D1 in astrocyte cultures at 14 days treated for 48 or 60 hr with dexamethasone (DEX) or 48 hr with 17beta-estradiol (E2) alone or with GFs added only in the last 12 or 24 hr.	Dexamethasone	206-219	heme oxygenase 1	Homo sapiens	106-122
25388553-2	2015	This study investigates the interaction between glucocorticoids or estrogens and GFs on the expression of heme oxygenase-1 (HO-1) and cyclin D1 in astrocyte cultures at 14 days treated for 48 or 60 hr with dexamethasone (DEX) or 48 hr with 17beta-estradiol (E2) alone or with GFs added only in the last 12 or 24 hr.	Dexamethasone	221-224	heme oxygenase 1	Homo sapiens	106-122
25388553-2	2015	This study investigates the interaction between glucocorticoids or estrogens and GFs on the expression of heme oxygenase-1 (HO-1) and cyclin D1 in astrocyte cultures at 14 days treated for 48 or 60 hr with dexamethasone (DEX) or 48 hr with 17beta-estradiol (E2) alone or with GFs added only in the last 12 or 24 hr.	Estradiol	240-256	heme oxygenase 1	Homo sapiens	106-122
25388553-3	2015	Twelve- or twenty-four-hour epidermal growth factor (EGF) treatment significantly enhanced HO-1 expression in astrocyte cultures pretreated for 48 hr with DEX.	Dexamethasone	155-158	heme oxygenase 1	Homo sapiens	91-95
25471815-1	2015	Smoking and obesity increases renal oxidative stress via nicotine (NIC) or free fatty acid such as oleic acid (OA) but decreases levels of the vitamin E-derivative alpha-tocopherol (TOC), which has shown to stimulate the antioxidant system such as heme oxygenase-1 (HO-1).	Vitamin E	143-152	heme oxygenase 1	Homo sapiens	248-264
25471815-1	2015	Smoking and obesity increases renal oxidative stress via nicotine (NIC) or free fatty acid such as oleic acid (OA) but decreases levels of the vitamin E-derivative alpha-tocopherol (TOC), which has shown to stimulate the antioxidant system such as heme oxygenase-1 (HO-1).	Vitamin E	143-152	heme oxygenase 1	Homo sapiens	266-270
25471815-0	2015	alpha-Tocopherol protects renal cells from nicotine- or oleic acid-provoked oxidative stress via inducing heme oxygenase-1.	Nicotine	43-51	heme oxygenase 1	Homo sapiens	106-122
25471815-1	2015	Smoking and obesity increases renal oxidative stress via nicotine (NIC) or free fatty acid such as oleic acid (OA) but decreases levels of the vitamin E-derivative alpha-tocopherol (TOC), which has shown to stimulate the antioxidant system such as heme oxygenase-1 (HO-1).	alpha-Tocopherol	164-180	heme oxygenase 1	Homo sapiens	248-264
25471815-1	2015	Smoking and obesity increases renal oxidative stress via nicotine (NIC) or free fatty acid such as oleic acid (OA) but decreases levels of the vitamin E-derivative alpha-tocopherol (TOC), which has shown to stimulate the antioxidant system such as heme oxygenase-1 (HO-1).	alpha-Tocopherol	164-180	heme oxygenase 1	Homo sapiens	266-270
25471815-0	2015	alpha-Tocopherol protects renal cells from nicotine- or oleic acid-provoked oxidative stress via inducing heme oxygenase-1.	Oleic Acid	56-66	heme oxygenase 1	Homo sapiens	106-122
25471815-1	2015	Smoking and obesity increases renal oxidative stress via nicotine (NIC) or free fatty acid such as oleic acid (OA) but decreases levels of the vitamin E-derivative alpha-tocopherol (TOC), which has shown to stimulate the antioxidant system such as heme oxygenase-1 (HO-1).	alpha-Tocopherol	182-185	heme oxygenase 1	Homo sapiens	248-264
25471815-1	2015	Smoking and obesity increases renal oxidative stress via nicotine (NIC) or free fatty acid such as oleic acid (OA) but decreases levels of the vitamin E-derivative alpha-tocopherol (TOC), which has shown to stimulate the antioxidant system such as heme oxygenase-1 (HO-1).	alpha-Tocopherol	182-185	heme oxygenase 1	Homo sapiens	266-270
25659595-4	2015	In addition, increased heme oxygenase-1 (HMOX1) expression and non-toxic generation of superoxide were detected in the first 4 h. Regarding the effects on the UVB-induced toxicity, although the level of cyclobutane pyrimidine dimers in the keratinocytes pre-treated with zinc for 24 h was reduced 3 h after UVB irradiation, significantly enhanced superoxide generation was observed 10 h after UVB exposure in the zinc pre-exposed cells.	cyclobutane pyrimidine	203-225	heme oxygenase 1	Homo sapiens	41-46
25471815-3	2015	NIC- or OA-dependent production of reactive oxygen species (ROS) was determined in the presence or absence of various pharmacologic or genetic inhibitors that modulate HO-1 activation and enhancer elements in the HO-1 promoter such as the antioxidant response element (ARE) and the cAMP-response element (CRE) in renal proximal tubule cells (NRK52E).	Reactive Oxygen Species	35-58	heme oxygenase 1	Homo sapiens	168-172
25471815-3	2015	NIC- or OA-dependent production of reactive oxygen species (ROS) was determined in the presence or absence of various pharmacologic or genetic inhibitors that modulate HO-1 activation and enhancer elements in the HO-1 promoter such as the antioxidant response element (ARE) and the cAMP-response element (CRE) in renal proximal tubule cells (NRK52E).	Reactive Oxygen Species	35-58	heme oxygenase 1	Homo sapiens	213-217
25471815-3	2015	NIC- or OA-dependent production of reactive oxygen species (ROS) was determined in the presence or absence of various pharmacologic or genetic inhibitors that modulate HO-1 activation and enhancer elements in the HO-1 promoter such as the antioxidant response element (ARE) and the cAMP-response element (CRE) in renal proximal tubule cells (NRK52E).	Reactive Oxygen Species	60-63	heme oxygenase 1	Homo sapiens	168-172
25471815-3	2015	NIC- or OA-dependent production of reactive oxygen species (ROS) was determined in the presence or absence of various pharmacologic or genetic inhibitors that modulate HO-1 activation and enhancer elements in the HO-1 promoter such as the antioxidant response element (ARE) and the cAMP-response element (CRE) in renal proximal tubule cells (NRK52E).	Reactive Oxygen Species	60-63	heme oxygenase 1	Homo sapiens	213-217
25471815-5	2015	We found that pre- or posttreatment with TOC attenuated NIC- or OA-dependent ROS production that required HO-1 activation.	alpha-Tocopherol	41-44	heme oxygenase 1	Homo sapiens	106-110
25471815-5	2015	We found that pre- or posttreatment with TOC attenuated NIC- or OA-dependent ROS production that required HO-1 activation.	Reactive Oxygen Species	77-80	heme oxygenase 1	Homo sapiens	106-110
25471815-8	2015	Hence, vitamin E supplementation-via induction of the cytoprotective HO-1-may help to reduce renal oxidative stress imposed by smoking or obesity.	Vitamin E	7-16	heme oxygenase 1	Homo sapiens	69-73
26269017-1	2015	OBJECTIVE: To investigate the relationship between (GT)n polymorphism and esophageal cancer by analyzing the connection between microsatellite polymorphisms in the promoter of heme oxygenase-1 and the clinicopathological characteristics of esophageal squamous cell carcinoma (ESCC) in Han chinese population.	Nitrogen	15-16	heme oxygenase 1	Homo sapiens	176-192
25759595-5	2015	We found that PEMF treatment was followed by changes in the relative amount of messenger (m)RNAs encoding enzymes involved in heme catabolism and removal of reactive oxygen species, including an increase in heme oxygenase 1 and superoxide dismutase 3 mRNAs, in all cell types examined 2 hours after PEMF treatment.	pemf	14-18	heme oxygenase 1	Homo sapiens	207-223
26269017-5	2015	For in vitro experiments, the transient-transfection assay was performed to explore the correlation between different lengths of (GT)n repeats and promoter activity by assessing the promoter activities of HO-1 gene in cultured Ecal09 cells treated with H2O2 by analysis of cariance.	Hydrogen Peroxide	253-257	heme oxygenase 1	Homo sapiens	205-209
26269017-27	2015	In H2O treated control group, compared to (GT)26 and (GT)36, the basal promoter activities of HO-1 gene carrying (GT)16 repeat increased (F =41.	Water	3-6	heme oxygenase 1	Homo sapiens	94-98
25196646-0	2015	Modulation of heme oxygenase-1 by metalloporphyrins increases anti-viral T cell responses.	Metalloporphyrins	34-51	heme oxygenase 1	Homo sapiens	14-30
25541286-4	2015	Shikonin (0-1 muM) concentration-dependently induced heme oxygenase-1, glutamate cysteine ligase modifier subunit, catalase, superoxide dismutase 1, glutathione peroxidase 1, and glutathione reductase protein and mRNA expression and glutathione content via activation of the phosphatidylinositol 3-kinase (PI3K)/Akt/Nrf2 signaling pathway.	shikonin	0-8	heme oxygenase 1	Homo sapiens	53-69
25557764-8	2015	Thus an increase in Sirt4, Nrf2, Tfam, UCP1, eNOS, HO1 and STAT3 genes could profoundly affect mitochondrial function, cholesterol homeostasis, and fatty acid oxidation, suggesting that ASA could be beneficial beyond simply its ability to inhibit cyclooxygenase.	Cholesterol	119-130	heme oxygenase 1	Homo sapiens	51-54
25557764-8	2015	Thus an increase in Sirt4, Nrf2, Tfam, UCP1, eNOS, HO1 and STAT3 genes could profoundly affect mitochondrial function, cholesterol homeostasis, and fatty acid oxidation, suggesting that ASA could be beneficial beyond simply its ability to inhibit cyclooxygenase.	Fatty Acids	148-158	heme oxygenase 1	Homo sapiens	51-54
25557764-8	2015	Thus an increase in Sirt4, Nrf2, Tfam, UCP1, eNOS, HO1 and STAT3 genes could profoundly affect mitochondrial function, cholesterol homeostasis, and fatty acid oxidation, suggesting that ASA could be beneficial beyond simply its ability to inhibit cyclooxygenase.	Aspirin	186-189	heme oxygenase 1	Homo sapiens	51-54
25484350-5	2015	Treatment with tBHQ induced mRNA expression of the Nrf2 target genes HMOX-1, GCLC, and NQO1, and also increased NRF2 mRNA expression, albeit to a lesser extent than the other target genes.	2-tert-butylhydroquinone	15-19	heme oxygenase 1	Homo sapiens	69-75
25483558-10	2015	Whereas, treatment with zinc protoporphyrin IX (a HO-1 inhibitor) into the IPC+ischemia-operated groups did not preserve the IPC-mediated increase of HO-1 and lost beneficial effects of IPC by inhibiting ischemia-induced DNA damage and lipid peroxidation.	protoporphyrin IX	29-46	heme oxygenase 1	Homo sapiens	50-54
24744106-0	2015	Heme oxygenase-1 regulates cell proliferation via carbon monoxide-mediated inhibition of T-type Ca2+ channels.	Carbon Monoxide	50-65	heme oxygenase 1	Homo sapiens	0-16
25499849-4	2015	Microarray analysis of HaCaT cells revealed that 10-EZ-HODE and 12-ZE-HODE induced cellular antioxidant genes that are responsive to nuclear factor-erythroid 2 p45-related factor 2 (Nrf2), such as heme oxygenase-1 and glutathione synthesis enzymes.	10-ez-hode	49-59	heme oxygenase 1	Homo sapiens	197-213
25499849-4	2015	Microarray analysis of HaCaT cells revealed that 10-EZ-HODE and 12-ZE-HODE induced cellular antioxidant genes that are responsive to nuclear factor-erythroid 2 p45-related factor 2 (Nrf2), such as heme oxygenase-1 and glutathione synthesis enzymes.	12-ze-hode	64-74	heme oxygenase 1	Homo sapiens	197-213
25499849-4	2015	Microarray analysis of HaCaT cells revealed that 10-EZ-HODE and 12-ZE-HODE induced cellular antioxidant genes that are responsive to nuclear factor-erythroid 2 p45-related factor 2 (Nrf2), such as heme oxygenase-1 and glutathione synthesis enzymes.	Glutathione	218-229	heme oxygenase 1	Homo sapiens	197-213
25393640-10	2015	CONCLUSIONS: In a 2-months prospective pilot study, the addition of liraglutide to metformin resulted in improvement in oxidative stress as well as plasma ghrelin and HO-1 concentrations in patients with T2DM.	Metformin	83-92	heme oxygenase 1	Homo sapiens	167-171
25611090-5	2015	Furthermore, the cell-intrinsic and -extrinsic factors (namely, Spi-C, IRF8/4, heme oxygenase-1, and M-CSF) that regulate the development and survival of RPMs have been identified.	rpms	154-158	heme oxygenase 1	Homo sapiens	71-95
24744106-4	2015	Proliferation and [Ca(2+)]i levels were reduced to levels seen in non-transfected cells either by induction of HO-1 or exposure of cells to the HO-1 product, carbon monoxide (CO) (applied as the CO releasing molecule, CORM-3).	Carbon Monoxide	158-173	heme oxygenase 1	Homo sapiens	144-148
25593219-1	2015	Sulforaphane (SFN), one of the most important isothiocyanates in the human diet, is known to have chemo-preventive and antioxidant activities in different tissues via activation of nuclear factor erythroid 2-related factor 2 (Nrf2)-mediated induction of antioxidant/phase II enzymes, such as heme oxygenase-1 and NAD(P)H quinone oxidoreductase 1.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	292-345
25988128-8	2014	EGCG improved efficacy of cisplatin treatment in HeLa cells by regulating NFkappaB p65, COX-2, p-Akt, and p-mTOR pathways, whereas it increased the expression levels of Nrf2/HO-1 in combined therapy.	epigallocatechin gallate	0-4	heme oxygenase 1	Homo sapiens	174-178
25988128-8	2014	EGCG improved efficacy of cisplatin treatment in HeLa cells by regulating NFkappaB p65, COX-2, p-Akt, and p-mTOR pathways, whereas it increased the expression levels of Nrf2/HO-1 in combined therapy.	Cisplatin	26-35	heme oxygenase 1	Homo sapiens	174-178
25593219-1	2015	Sulforaphane (SFN), one of the most important isothiocyanates in the human diet, is known to have chemo-preventive and antioxidant activities in different tissues via activation of nuclear factor erythroid 2-related factor 2 (Nrf2)-mediated induction of antioxidant/phase II enzymes, such as heme oxygenase-1 and NAD(P)H quinone oxidoreductase 1.	sulforaphane	14-17	heme oxygenase 1	Homo sapiens	292-345
26303493-3	2015	HO-1 degrades heme to generate carbon monoxide (CO) along with Fe(2+) and biliverdin.	Heme	14-18	heme oxygenase 1	Homo sapiens	0-4
25574604-2	2015	We wanted to evaluate whether a functional polymorphism in the HMOX1 gene encoding heme oxygenase modifies risk of CRC or interacts with diet or lifestyle factors because this would identify heme or heme iron as a risk factor of CRC.	Heme	83-87	heme oxygenase 1	Homo sapiens	63-68
25574604-2	2015	We wanted to evaluate whether a functional polymorphism in the HMOX1 gene encoding heme oxygenase modifies risk of CRC or interacts with diet or lifestyle factors because this would identify heme or heme iron as a risk factor of CRC.	Heme	191-195	heme oxygenase 1	Homo sapiens	63-68
25574604-2	2015	We wanted to evaluate whether a functional polymorphism in the HMOX1 gene encoding heme oxygenase modifies risk of CRC or interacts with diet or lifestyle factors because this would identify heme or heme iron as a risk factor of CRC.	Iron	204-208	heme oxygenase 1	Homo sapiens	63-68
25610397-1	2014	The heme-degrading enzyme heme oxygenase-1 (HO-1) has cytoprotective, antioxidant, and anti-inflammatory properties.	Heme	4-8	heme oxygenase 1	Homo sapiens	26-42
25610397-1	2014	The heme-degrading enzyme heme oxygenase-1 (HO-1) has cytoprotective, antioxidant, and anti-inflammatory properties.	Heme	4-8	heme oxygenase 1	Homo sapiens	44-48
26303493-3	2015	HO-1 degrades heme to generate carbon monoxide (CO) along with Fe(2+) and biliverdin.	Carbon Monoxide	31-46	heme oxygenase 1	Homo sapiens	0-4
26303493-3	2015	HO-1 degrades heme to generate carbon monoxide (CO) along with Fe(2+) and biliverdin.	Carbon Monoxide	48-50	heme oxygenase 1	Homo sapiens	0-4
26303493-3	2015	HO-1 degrades heme to generate carbon monoxide (CO) along with Fe(2+) and biliverdin.	ammonium ferrous sulfate	63-69	heme oxygenase 1	Homo sapiens	0-4
26303493-3	2015	HO-1 degrades heme to generate carbon monoxide (CO) along with Fe(2+) and biliverdin.	Biliverdine	74-84	heme oxygenase 1	Homo sapiens	0-4
26295053-2	2015	We hypothesized that glutathione S-transferase (GST M1, T1, and P1), reactive oxygen species (ROS) related metabolic genes (NQO1, EPHX1, and HO-1), and DNA repair genes (XRCC1, XPD, hOGG1, and ATM) together may play a role in arsenic-induced skin carcinogenesis.	Reactive Oxygen Species	94-97	heme oxygenase 1	Homo sapiens	141-145
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Heme	55-59	heme oxygenase 1	Homo sapiens	0-16
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Heme	55-59	heme oxygenase 1	Homo sapiens	18-22
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Bilirubin	65-74	heme oxygenase 1	Homo sapiens	0-16
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Bilirubin	65-74	heme oxygenase 1	Homo sapiens	18-22
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Carbon Monoxide	76-91	heme oxygenase 1	Homo sapiens	0-16
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Carbon Monoxide	76-91	heme oxygenase 1	Homo sapiens	18-22
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Iron	97-101	heme oxygenase 1	Homo sapiens	0-16
25744452-1	2015	Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions.	Iron	97-101	heme oxygenase 1	Homo sapiens	18-22
25744452-3	2015	HO-1 is induced by its substrate heme and environmental factors including oxidative and heat stresses.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-4
25744452-6	2015	Based on a comparison of the results obtained with these cells, we found that nitric oxide (NO) was closely linked to the induction of HO-1.	Nitric Oxide	78-90	heme oxygenase 1	Homo sapiens	135-139
25744452-9	2015	N-Nitro-L-arginine methyl ester, an NO synthase inhibitor, reduced both HO-1 expression and NO production in LPS+IFN-gamma-treated JA-4 cells.	n-nitro-l-arginine methyl ester	0-31	heme oxygenase 1	Homo sapiens	72-76
25744452-12	2015	These results suggest that, among ROS, NO plays an important role in HO-1 induction in activated macrophages treated with LPS+IFN-gamma.	Reactive Oxygen Species	34-37	heme oxygenase 1	Homo sapiens	69-73
25661467-0	2015	High glucose promotes tumor invasion and increases metastasis-associated protein expression in human lung epithelial cells by upregulating heme oxygenase-1 via reactive oxygen species or the TGF-beta1/PI3K/Akt signaling pathway.	Glucose	5-12	heme oxygenase 1	Homo sapiens	139-155
25661467-0	2015	High glucose promotes tumor invasion and increases metastasis-associated protein expression in human lung epithelial cells by upregulating heme oxygenase-1 via reactive oxygen species or the TGF-beta1/PI3K/Akt signaling pathway.	Reactive Oxygen Species	160-183	heme oxygenase 1	Homo sapiens	139-155
25661467-1	2015	BACKGROUND: Growing evidence indicates that heme oxygenase-1 (HO-1) is up-regulated in malignancies and subsequently alters tumor aggressiveness and various cancer-related factors, such as high glucose (HG) levels.	Glucose	194-201	heme oxygenase 1	Homo sapiens	44-60
25661467-1	2015	BACKGROUND: Growing evidence indicates that heme oxygenase-1 (HO-1) is up-regulated in malignancies and subsequently alters tumor aggressiveness and various cancer-related factors, such as high glucose (HG) levels.	Glucose	194-201	heme oxygenase 1	Homo sapiens	62-66
25661467-2	2015	HO-1 expression can be induced when glucose concentrations are above 25 mM; however, the role of HO-1 in lung cancer patients with diabetes remains unknown.	Glucose	36-43	heme oxygenase 1	Homo sapiens	0-4
25661467-7	2015	RESULTS: HG treatment of A549 cells induced an increase in HO-1 expression, which was mediated by the HG-induced generation of reactive oxygen species (ROS) and transforming growth factor-beta1 (TGF-beta1) in a concentration- and time-dependent manner.	Reactive Oxygen Species	127-150	heme oxygenase 1	Homo sapiens	59-63
25661467-7	2015	RESULTS: HG treatment of A549 cells induced an increase in HO-1 expression, which was mediated by the HG-induced generation of reactive oxygen species (ROS) and transforming growth factor-beta1 (TGF-beta1) in a concentration- and time-dependent manner.	Reactive Oxygen Species	152-155	heme oxygenase 1	Homo sapiens	59-63
26159150-0	2015	Induction of Heme Oxygenase-1 by Sodium 9-Hydroxyltanshinone IIA Sulfonate Derivative Contributes to Inhibit LPS-Mediated Inflammatory Response in Macrophages.	sodium 9-hydroxyltanshinone iia sulfonate	33-74	heme oxygenase 1	Homo sapiens	13-29
26159150-6	2015	In addition, ZY-1A4 concentration- and time-dependently induced HO-1 expression associated with degradation of Kelch-like ECH-associated protein 1 (Keap1) and nuclear translocation of Nrf2, while the effect of ZY-1A4 was abolished by a phosphoinositide 3-kinase (PI3K) inhibitor LY294002.	zy-1a4	13-19	heme oxygenase 1	Homo sapiens	64-68
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	zy-1a4	161-167	heme oxygenase 1	Homo sapiens	46-50
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	zy-1a4	161-167	heme oxygenase 1	Homo sapiens	192-196
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	Carbon Monoxide	209-224	heme oxygenase 1	Homo sapiens	46-50
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	Carbon Monoxide	209-224	heme oxygenase 1	Homo sapiens	192-196
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	Bilirubin	229-238	heme oxygenase 1	Homo sapiens	46-50
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	Bilirubin	229-238	heme oxygenase 1	Homo sapiens	192-196
26159150-8	2015	Furthermore, the inhibitory effect of ZY-1A4 on LPS-induced iNOS expression and NO release was abolished by HO-1 siRNA or LY294002.	zy-1a4	38-44	heme oxygenase 1	Homo sapiens	108-112
26159150-6	2015	In addition, ZY-1A4 concentration- and time-dependently induced HO-1 expression associated with degradation of Kelch-like ECH-associated protein 1 (Keap1) and nuclear translocation of Nrf2, while the effect of ZY-1A4 was abolished by a phosphoinositide 3-kinase (PI3K) inhibitor LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	279-287	heme oxygenase 1	Homo sapiens	64-68
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	zinc protoporphyrin	56-78	heme oxygenase 1	Homo sapiens	46-50
26159150-7	2015	Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin.	zy- 1a4	116-123	heme oxygenase 1	Homo sapiens	46-50
26151294-0	2015	Edaravone protects rats and human pulmonary alveolar epithelial cells against hyperoxia injury: heme oxygenase-1 and PI3K/Akt pathway may be involved.	Edaravone	0-9	heme oxygenase 1	Homo sapiens	96-112
25874340-0	2015	Novel imidazole derivatives as heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2) inhibitors and their cytotoxic activity in human-derived cancer cell lines.	imidazole	6-15	heme oxygenase 1	Homo sapiens	31-47
25874340-0	2015	Novel imidazole derivatives as heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2) inhibitors and their cytotoxic activity in human-derived cancer cell lines.	imidazole	6-15	heme oxygenase 1	Homo sapiens	49-53
25874340-2	2015	In this work, novel imidazole derivatives were designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2).	imidazole	20-29	heme oxygenase 1	Homo sapiens	89-105
25874340-2	2015	In this work, novel imidazole derivatives were designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2).	imidazole	20-29	heme oxygenase 1	Homo sapiens	107-111
26495956-9	2015	qRT-PCR analysis confirmed significant upregulation of SULF2, IGF2, and HMOX1 in graft regions with PFA.	pfa	100-103	heme oxygenase 1	Homo sapiens	72-77
25527214-1	2015	Pegylated zinc protoporphyrin (PEG-ZnPP) is a water-soluble inhibitor of heme oxygenase-1.	zinc protoporphyrin	10-29	heme oxygenase 1	Homo sapiens	73-89
25527214-1	2015	Pegylated zinc protoporphyrin (PEG-ZnPP) is a water-soluble inhibitor of heme oxygenase-1.	pegylated zinc protoporphyrin	31-39	heme oxygenase 1	Homo sapiens	73-89
25527214-1	2015	Pegylated zinc protoporphyrin (PEG-ZnPP) is a water-soluble inhibitor of heme oxygenase-1.	Water	46-51	heme oxygenase 1	Homo sapiens	73-89
26151294-9	2015	CONCLUSIONS: This study indicates that edaravone protects rats and human pulmonary alveolar epithelial cells against hyperoxia-induced injury and the antioxidant effect may be related to upregulation of HO-1, which is regulated by PI3K/Akt pathway.	Edaravone	39-48	heme oxygenase 1	Homo sapiens	203-207
25084759-5	2015	The neuroprotective effect of agmatine was abolished by yohimbine (alpha2-adrenoceptor antagonist), ketanserin (5-HT2A receptor antagonist), LY294002 (PI3K inhibitor), PD98059 (MEK1/2 inhibitor), SnPP (HO-1 inhibitor), and cycloheximide (protein synthesis inhibitor).	Agmatine	30-38	heme oxygenase 1	Homo sapiens	202-206
25463280-1	2015	Heme oxygenase (HO)-1 is the inducible isoform of the heme-degrading enzyme HO, which is upregulated by multiple stress stimuli.	Heme	54-58	heme oxygenase 1	Homo sapiens	0-21
25185584-8	2015	Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death.	Hemin	48-53	heme oxygenase 1	Homo sapiens	13-29
25185584-8	2015	Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death.	Hemin	48-53	heme oxygenase 1	Homo sapiens	31-36
25185584-8	2015	Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death.	Hemin	48-53	heme oxygenase 1	Homo sapiens	37-41
25185584-8	2015	Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death.	chelerythrine	67-80	heme oxygenase 1	Homo sapiens	13-29
25185584-8	2015	Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death.	chelerythrine	67-80	heme oxygenase 1	Homo sapiens	31-36
25185584-8	2015	Induction of heme-oxygenase-1 (HMOX1/HO-1) with hemin also blocked chelerythrine-induced cell death.	chelerythrine	67-80	heme oxygenase 1	Homo sapiens	37-41
25553444-3	2015	Exposure to isoflurane decreased miR-155 and upregulated HIF-1 alpha and HO-1 mRNA and protein.	Isoflurane	12-22	heme oxygenase 1	Homo sapiens	73-77
25553444-6	2015	These results suggest that isoflurane posttreatment hr alleviates LPS-induced ALI and cell injury by triggering miR-155-HIF-1 alpha pathway, leading to upregulation of HO-1.	Isoflurane	27-37	heme oxygenase 1	Homo sapiens	168-172
25084759-6	2015	Agmatine increased Akt and ERK phosphorylation and induced the transcription factor Nrf2 and the proteins HO-1 and GCLc; induction of these proteins was prevented by yohimbine, ketanserin, LY294002, and PD98059.	Agmatine	0-8	heme oxygenase 1	Homo sapiens	106-119
25084759-6	2015	Agmatine increased Akt and ERK phosphorylation and induced the transcription factor Nrf2 and the proteins HO-1 and GCLc; induction of these proteins was prevented by yohimbine, ketanserin, LY294002, and PD98059.	Ketanserin	177-187	heme oxygenase 1	Homo sapiens	106-119
25084759-7	2015	In conclusion, agmatine affords neuroprotection against corticosterone effects by a mechanism that implicates Nrf2 induction via alpha2-adrenergic and 5-HT2A receptors, Akt and ERK pathways, and HO-1 and GCLc expression.	Agmatine	15-23	heme oxygenase 1	Homo sapiens	195-199
25084759-7	2015	In conclusion, agmatine affords neuroprotection against corticosterone effects by a mechanism that implicates Nrf2 induction via alpha2-adrenergic and 5-HT2A receptors, Akt and ERK pathways, and HO-1 and GCLc expression.	Corticosterone	56-70	heme oxygenase 1	Homo sapiens	195-199
25876966-0	2015	[The protein expression of heme oxygenase-1 and platelet endothelial cell adhesion molecules-1 in human coronary artery endothelial cell induced by zinc oxide nanoparticle].	Zinc Oxide	148-158	heme oxygenase 1	Homo sapiens	27-43
25405261-4	2015	There were major differences between the types of NMs; exposure to ZnO and Ag resulted in cytotoxicity and increased gene expression levels of HMOX1 and IL8.	Zinc Oxide	67-70	heme oxygenase 1	Homo sapiens	143-148
26161238-3	2015	Such protective phenomenon is reported to be implicated in decreasing the formation and reaction of reactive oxygen species and pro-nflammatory cytokines, as well as the mediation of a variety of intracellular signaling pathways, including the nitric oxide synthase, nicotinamide adenine dinucleotide phosphate oxidase, deacetylase sirtuin 1, mitogen-activated protein kinase, peroxisome proliferator-activated receptor-gamma coactivator 1 alpha, hemeoxygenase-1, and estrogen receptor-related pathways.	Reactive Oxygen Species	100-123	heme oxygenase 1	Homo sapiens	447-485
25926128-6	2015	In addition to a higher induction of the key cytoprotective gene heme oxygenase-1 (38.9-fold increase for CDDO-Im and 26.5-fold increase for CDDO-Me), CDDO-Im also induced greater expression of heat shock proteins (5.5-fold increase compared to 2.8-fold for CDDO-Me).	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	106-113	heme oxygenase 1	Homo sapiens	65-81
25926128-6	2015	In addition to a higher induction of the key cytoprotective gene heme oxygenase-1 (38.9-fold increase for CDDO-Im and 26.5-fold increase for CDDO-Me), CDDO-Im also induced greater expression of heat shock proteins (5.5-fold increase compared to 2.8-fold for CDDO-Me).	bardoxolone methyl	141-148	heme oxygenase 1	Homo sapiens	65-81
25926128-6	2015	In addition to a higher induction of the key cytoprotective gene heme oxygenase-1 (38.9-fold increase for CDDO-Im and 26.5-fold increase for CDDO-Me), CDDO-Im also induced greater expression of heat shock proteins (5.5-fold increase compared to 2.8-fold for CDDO-Me).	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	151-158	heme oxygenase 1	Homo sapiens	65-81
26689007-1	2015	Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin.	Heme	47-51	heme oxygenase 1	Homo sapiens	0-16
26689007-1	2015	Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin.	Heme	47-51	heme oxygenase 1	Homo sapiens	18-22
26689007-1	2015	Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin.	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	0-16
26689007-1	2015	Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin.	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	18-22
26689007-1	2015	Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin.	Biliverdine	106-116	heme oxygenase 1	Homo sapiens	0-16
26689007-1	2015	Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin.	Biliverdine	106-116	heme oxygenase 1	Homo sapiens	18-22
25876966-1	2015	OBJECTIVE: To explore the protein expression of heme oxygenase-1 (HO-1) and platelet endothelial cell adhesion molecules-1 (PECAM-1) in human coronary artery endothelial cells induced with Zinc Oxide Nanoparticle (ZnO-NPs).	Zinc Oxide	189-199	heme oxygenase 1	Homo sapiens	66-70
25876966-1	2015	OBJECTIVE: To explore the protein expression of heme oxygenase-1 (HO-1) and platelet endothelial cell adhesion molecules-1 (PECAM-1) in human coronary artery endothelial cells induced with Zinc Oxide Nanoparticle (ZnO-NPs).	Zinc Oxide	214-217	heme oxygenase 1	Homo sapiens	48-64
25876966-4	2015	Protein levels of HO-1 (ng/L) in each group were 0.041+-0.011, 0.512+-0.076, 0.906+-0.059, 1.062+-0.089 respectively after the stimulation of different concentrations of ZnO-NPs (0, 10, 20, 40microg/ml).	Zinc Oxide	170-173	heme oxygenase 1	Homo sapiens	18-22
25876966-1	2015	OBJECTIVE: To explore the protein expression of heme oxygenase-1 (HO-1) and platelet endothelial cell adhesion molecules-1 (PECAM-1) in human coronary artery endothelial cells induced with Zinc Oxide Nanoparticle (ZnO-NPs).	Zinc Oxide	189-199	heme oxygenase 1	Homo sapiens	48-64
25404134-3	2014	Here, we report that multiple nuclear-enriched eRNAs are transcribed from the regions adjacent to two human HO-1 enhancers (i.e. the distal E2 and proximal E1 enhancers), and some of these eRNAs are induced by the oxidative stress-causing reagent diethyl maleate (DEM).	diethyl maleate	247-262	heme oxygenase 1	Homo sapiens	108-112
25404134-4	2014	We demonstrated that the expression of one forward direction (5" to 3") eRNA transcribed from the human HO-1 E2 enhancer region (named human HO-1enhancer RNA E2-3; hereafter called eRNA E2-3) was induced by DEM in an NRF2-dependent manner in HeLa cells.	diethyl maleate	207-210	heme oxygenase 1	Homo sapiens	104-108
25236743-5	2014	Early DNFB induction of ATF4 positively modulates autophagy-related genes MAP1LC3B and ATG3 and stabilizes the transcription factor Nrf2, causing a strong induction of the HMOX1-detoxifying gene.	Dinitrofluorobenzene	6-10	heme oxygenase 1	Homo sapiens	172-177
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Heme	80-84	heme oxygenase 1	Homo sapiens	0-16
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Heme	80-84	heme oxygenase 1	Homo sapiens	18-22
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	0-16
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	18-22
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Iron	132-136	heme oxygenase 1	Homo sapiens	0-16
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Iron	132-136	heme oxygenase 1	Homo sapiens	18-22
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Biliverdine	142-152	heme oxygenase 1	Homo sapiens	0-16
25241054-1	2014	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin.	Biliverdine	142-152	heme oxygenase 1	Homo sapiens	18-22
25058038-1	2014	Carbon monoxide derived from the catalytic action of heme oxygenase-1 or carbon monoxide-releasing molecules (CORMs) has been found to potentially be an anticoagulant or procoagulant agent.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	53-69
25058038-1	2014	Carbon monoxide derived from the catalytic action of heme oxygenase-1 or carbon monoxide-releasing molecules (CORMs) has been found to potentially be an anticoagulant or procoagulant agent.	Carbon Monoxide	73-88	heme oxygenase 1	Homo sapiens	53-69
25501830-0	2014	Heme oxygenase-1 protects against Alzheimer"s amyloid-beta(1-42)-induced toxicity via carbon monoxide production.	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	0-16
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Heme	94-98	heme oxygenase 1	Homo sapiens	0-16
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Heme	94-98	heme oxygenase 1	Homo sapiens	18-22
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Biliverdine	102-112	heme oxygenase 1	Homo sapiens	0-16
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Biliverdine	102-112	heme oxygenase 1	Homo sapiens	18-22
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	ammonium ferrous sulfate	114-118	heme oxygenase 1	Homo sapiens	0-16
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	ammonium ferrous sulfate	114-118	heme oxygenase 1	Homo sapiens	18-22
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Carbon Monoxide	123-138	heme oxygenase 1	Homo sapiens	0-16
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Carbon Monoxide	123-138	heme oxygenase 1	Homo sapiens	18-22
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Carbon Monoxide	140-142	heme oxygenase 1	Homo sapiens	0-16
25501830-1	2014	Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO).	Carbon Monoxide	140-142	heme oxygenase 1	Homo sapiens	18-22
25111043-4	2014	Induction of the glial HMOX1 gene may lead to pathological brain iron deposition, intracellular oxidative damage, and bioenergetic failure in AD and other human CNS disorders such as PD and MS.	Iron	65-69	heme oxygenase 1	Homo sapiens	23-28
25231232-0	2014	Potential crosstalk of Ca2+-ROS-dependent mechanism involved in apoptosis of Kasumi-1 cells mediated by heme oxygenase-1 small interfering RNA.	ca2+-ros	23-31	heme oxygenase 1	Homo sapiens	104-120
25063314-3	2014	HO-1 expression was assessed in 215 formalin-fixed bladder cancer specimens by immunohistochemistry.	Formaldehyde	36-44	heme oxygenase 1	Homo sapiens	0-4
25227700-3	2014	To enhance intrainfarct graft viability, human embryonic stem cell-derived cardiomyocytes (hESC-CMs) were pretreated before implantation with cobalt protoporphyrin (CoPP), a pharmacologic inducer of cytoprotective heme oxygenase-1.	cobaltiprotoporphyrin	142-163	heme oxygenase 1	Homo sapiens	214-230
25437431-5	2014	Additional tests showed that BQ is also capable of inducing expression of NADPH oxidase1 (NOX1), and several other antioxidant enzymes or drug-metabolizing enzymes, including heme oxygenase 1 (HMOX1), superoxide dismutase (SOD), catalase and NAD(P)H dehydrogenase quinone 1 (NQO1).	quinone	29-31	heme oxygenase 1	Homo sapiens	175-191
25437431-5	2014	Additional tests showed that BQ is also capable of inducing expression of NADPH oxidase1 (NOX1), and several other antioxidant enzymes or drug-metabolizing enzymes, including heme oxygenase 1 (HMOX1), superoxide dismutase (SOD), catalase and NAD(P)H dehydrogenase quinone 1 (NQO1).	quinone	29-31	heme oxygenase 1	Homo sapiens	193-198
25262300-1	2014	OBJECTIVE: To explore the effects of variants in Uridine Diphosphate Glucuronosyl Transferase 1A1 (UGT1A1) and Heme Oxygenase-1 (HMOX1) on daily physiological bilirubin levels and bilirubin changes during the first week after birth in Chinese newborns.	Bilirubin	159-168	heme oxygenase 1	Homo sapiens	111-127
25262300-1	2014	OBJECTIVE: To explore the effects of variants in Uridine Diphosphate Glucuronosyl Transferase 1A1 (UGT1A1) and Heme Oxygenase-1 (HMOX1) on daily physiological bilirubin levels and bilirubin changes during the first week after birth in Chinese newborns.	Bilirubin	159-168	heme oxygenase 1	Homo sapiens	129-134
25262300-2	2014	Both UGT1A1 and HMOX1 code rate-limiting enzymes in the bilirubin metabolism pathway.	Bilirubin	56-65	heme oxygenase 1	Homo sapiens	16-21
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Ribavirin	0-9	heme oxygenase 1	Homo sapiens	109-125
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Ribavirin	0-9	heme oxygenase 1	Homo sapiens	127-132
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Heme	64-68	heme oxygenase 1	Homo sapiens	109-125
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Heme	64-68	heme oxygenase 1	Homo sapiens	127-132
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Carbon Monoxide	137-152	heme oxygenase 1	Homo sapiens	109-125
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Carbon Monoxide	137-152	heme oxygenase 1	Homo sapiens	127-132
25473172-9	2014	Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin).	Iron	179-183	heme oxygenase 1	Homo sapiens	127-132
25450364-12	2014	GABA treatment significantly impeded the ALA-mediated increase in the number of hemoglobinized cells as well as the induction of HBG, HBA, and HMOX1.	gamma-Aminobutyric Acid	0-4	heme oxygenase 1	Homo sapiens	143-148
25230250-6	2014	We also observed inductions (&gt;2 fold) of genes involved in eicosanoid biosynthesis (Pla2g4a, Pla2g4b, Ptgs2, Ptgis, Alox12, Alox15), heme metabolism (Hpx, Hmox1, Prdx1) and iron homeostasis (Hamp, Tf).	Eicosanoids	62-72	heme oxygenase 1	Homo sapiens	158-163
25450364-13	2014	Finally, small-interfering RNA-mediated knockdown of ALAS2 in HiDEP cells considerably decreased the expression of HBA, HBG, and HMOX1, and these expression levels were rescued with ALA treatment.	5-amino levulinic acid	53-56	heme oxygenase 1	Homo sapiens	129-134
24382006-3	2014	This may be, in part, explained by the high lung content of heme oxygenase-1 (HO-1), the rate-limiting enzyme in the degradation of heme and an important stress protein.	Heme	60-64	heme oxygenase 1	Homo sapiens	78-82
25224540-2	2014	The products of HO-1 enzymatic activity, biliverdin and carbon monoxide (CO), actively contribute to this protection, suggesting that exploitation of these cellular systems may offer new therapeutic avenues in a variety of diseases.	Biliverdine	41-51	heme oxygenase 1	Homo sapiens	16-20
25224540-2	2014	The products of HO-1 enzymatic activity, biliverdin and carbon monoxide (CO), actively contribute to this protection, suggesting that exploitation of these cellular systems may offer new therapeutic avenues in a variety of diseases.	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	16-20
25224540-2	2014	The products of HO-1 enzymatic activity, biliverdin and carbon monoxide (CO), actively contribute to this protection, suggesting that exploitation of these cellular systems may offer new therapeutic avenues in a variety of diseases.	Carbon Monoxide	73-75	heme oxygenase 1	Homo sapiens	16-20
25033992-6	2014	Thereafter, we introduce some information covering melatonin-related signaling pathways, including heme oxygenase-1 (HO-1), toll-like receptor (TLR), c-Jun N-terminal kinase (JNK), and so on.	Melatonin	51-60	heme oxygenase 1	Homo sapiens	99-115
25033992-6	2014	Thereafter, we introduce some information covering melatonin-related signaling pathways, including heme oxygenase-1 (HO-1), toll-like receptor (TLR), c-Jun N-terminal kinase (JNK), and so on.	Melatonin	51-60	heme oxygenase 1	Homo sapiens	117-121
25090972-7	2014	NADA enhances angiogenesis in endothelial vascular cells and promotes the expression of genes such as erythropoietin (EPO), vascular endothelial growth factor A (VEGFA), heme oxygenase 1 (HMOX-1), hexokinase 2 (HK2) and Bcl-2/E1B-nineteen kiloDalton interacting protein (BNIP3) in primary astrocytes.	arachidonyl dopamine	0-4	heme oxygenase 1	Homo sapiens	170-186
25090972-7	2014	NADA enhances angiogenesis in endothelial vascular cells and promotes the expression of genes such as erythropoietin (EPO), vascular endothelial growth factor A (VEGFA), heme oxygenase 1 (HMOX-1), hexokinase 2 (HK2) and Bcl-2/E1B-nineteen kiloDalton interacting protein (BNIP3) in primary astrocytes.	arachidonyl dopamine	0-4	heme oxygenase 1	Homo sapiens	188-194
23649983-8	2014	Also, treatment of the vapor samples with glutathione resulted in reduction in the Nrf2 activation and HO-1 induction, suggesting that electrophiles in vapor samples contribute to this Nrf2-dependent antioxidant or adaptive response.	Glutathione	42-53	heme oxygenase 1	Homo sapiens	103-107
24651515-0	2014	Delayed remote ischemic preconditioning produces an additive cardioprotection to sevoflurane postconditioning through an enhanced heme oxygenase 1 level partly via nuclear factor erythroid 2-related factor 2 nuclear translocation.	Sevoflurane	81-92	heme oxygenase 1	Homo sapiens	130-146
25175370-0	2014	Induction of heme oxygenase-1 expression protects articular chondrocytes against cilostazol-induced cellular senescence.	Cilostazol	81-91	heme oxygenase 1	Homo sapiens	13-29
25175370-5	2014	Cilostazol also significantly induced HO-1 expression, and the induction of HO-1 expression was affected by a significant increase in reactive oxygen species (ROS) production caused by cilostazol treatment.	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	38-42
25175370-5	2014	Cilostazol also significantly induced HO-1 expression, and the induction of HO-1 expression was affected by a significant increase in reactive oxygen species (ROS) production caused by cilostazol treatment.	Reactive Oxygen Species	134-157	heme oxygenase 1	Homo sapiens	76-80
25175370-5	2014	Cilostazol also significantly induced HO-1 expression, and the induction of HO-1 expression was affected by a significant increase in reactive oxygen species (ROS) production caused by cilostazol treatment.	Reactive Oxygen Species	159-162	heme oxygenase 1	Homo sapiens	76-80
25175370-5	2014	Cilostazol also significantly induced HO-1 expression, and the induction of HO-1 expression was affected by a significant increase in reactive oxygen species (ROS) production caused by cilostazol treatment.	Cilostazol	185-195	heme oxygenase 1	Homo sapiens	76-80
25175370-6	2014	Of note, pre-treatment with 3-morpholinosydnonimine hydrochloride (SIN-1), an inducer of HO-1 expression, markedly attenuated cilostazol-induced chondrocyte senescence, and thus, we examined whether HO-1 directly modulates chondrocyte senescence induced by cilostazol.	linsidomine	28-65	heme oxygenase 1	Homo sapiens	89-93
25175370-6	2014	Of note, pre-treatment with 3-morpholinosydnonimine hydrochloride (SIN-1), an inducer of HO-1 expression, markedly attenuated cilostazol-induced chondrocyte senescence, and thus, we examined whether HO-1 directly modulates chondrocyte senescence induced by cilostazol.	Cilostazol	126-136	heme oxygenase 1	Homo sapiens	89-93
25175370-6	2014	Of note, pre-treatment with 3-morpholinosydnonimine hydrochloride (SIN-1), an inducer of HO-1 expression, markedly attenuated cilostazol-induced chondrocyte senescence, and thus, we examined whether HO-1 directly modulates chondrocyte senescence induced by cilostazol.	Cilostazol	126-136	heme oxygenase 1	Homo sapiens	199-203
25175370-7	2014	The upregulation of HO-1 was found to suppress cilostazol-induced cellular senescence.	Cilostazol	47-57	heme oxygenase 1	Homo sapiens	20-24
25175370-8	2014	In addition, the inhibition of HO-1 activity with the iron chelator, desferrioxamine (DFO), or HO-1 siRNA increased cilostazol-induced chondrocyte senescence.	Iron	54-58	heme oxygenase 1	Homo sapiens	31-35
25175370-8	2014	In addition, the inhibition of HO-1 activity with the iron chelator, desferrioxamine (DFO), or HO-1 siRNA increased cilostazol-induced chondrocyte senescence.	Deferoxamine	69-84	heme oxygenase 1	Homo sapiens	31-35
25175370-8	2014	In addition, the inhibition of HO-1 activity with the iron chelator, desferrioxamine (DFO), or HO-1 siRNA increased cilostazol-induced chondrocyte senescence.	Deferoxamine	86-89	heme oxygenase 1	Homo sapiens	31-35
25175370-8	2014	In addition, the inhibition of HO-1 activity with the iron chelator, desferrioxamine (DFO), or HO-1 siRNA increased cilostazol-induced chondrocyte senescence.	Cilostazol	116-126	heme oxygenase 1	Homo sapiens	31-35
25175370-8	2014	In addition, the inhibition of HO-1 activity with the iron chelator, desferrioxamine (DFO), or HO-1 siRNA increased cilostazol-induced chondrocyte senescence.	Cilostazol	116-126	heme oxygenase 1	Homo sapiens	95-99
25172557-7	2014	In addition to its action on the reporter constructs, mRNA and protein levels of heme oxygenase 1, an endogenous target gene of Nrf2, was markedly upregulated by E2 both alone and in combination with tBHQ.	2-tert-butylhydroquinone	200-204	heme oxygenase 1	Homo sapiens	81-97
24762402-1	2014	The length polymorphism of guanosine thymidine dinucleotide repeats in the heme oxygenase-1 gene promoter is associated with cardiovascular events and mortality in high-risk populations.	guanosine thymidine dinucleotide	27-59	heme oxygenase 1	Homo sapiens	75-91
24762402-4	2014	We analyzed the allelic frequencies of guanosine thymidine dinucleotide repeats in the heme oxygenase-1 gene promoter in 386 patients with coronary artery disease recruited from January 1999 to July 2001 and followed until August 31, 2012.	guanosine thymidine dinucleotide	39-71	heme oxygenase 1	Homo sapiens	87-103
24762402-10	2014	In conclusion, a greater number of guanosine thymidine dinucleotide repeats in the heme oxygenase-1 gene promoter is associated with higher risk for CKD, cardiovascular events, and mortality among patients with coronary artery disease.	guanosine thymidine dinucleotide	35-67	heme oxygenase 1	Homo sapiens	83-99
24651515-9	2014	Hence, we conclude that DRIPC may produce an additive cardioprotection to SPoC through an enhanced HO-1 expression partly via Nrf2 translocation.	dripc	24-29	heme oxygenase 1	Homo sapiens	99-103
24968709-0	2014	Epigallocatechin-3-gallate (EGCG) protects skin cells from ionizing radiation via heme oxygenase-1 (HO-1) overexpression.	epigallocatechin gallate	0-26	heme oxygenase 1	Homo sapiens	82-98
24968709-0	2014	Epigallocatechin-3-gallate (EGCG) protects skin cells from ionizing radiation via heme oxygenase-1 (HO-1) overexpression.	epigallocatechin gallate	0-26	heme oxygenase 1	Homo sapiens	100-104
24968709-0	2014	Epigallocatechin-3-gallate (EGCG) protects skin cells from ionizing radiation via heme oxygenase-1 (HO-1) overexpression.	epigallocatechin gallate	28-32	heme oxygenase 1	Homo sapiens	82-98
24968709-0	2014	Epigallocatechin-3-gallate (EGCG) protects skin cells from ionizing radiation via heme oxygenase-1 (HO-1) overexpression.	epigallocatechin gallate	28-32	heme oxygenase 1	Homo sapiens	100-104
24968709-9	2014	Furthermore, EGCG induced the expression of the cytoprotective molecule heme oxygenase-1 (HO-1) in a dose-dependent manner via transcriptional activation.	epigallocatechin gallate	13-17	heme oxygenase 1	Homo sapiens	72-88
24968709-9	2014	Furthermore, EGCG induced the expression of the cytoprotective molecule heme oxygenase-1 (HO-1) in a dose-dependent manner via transcriptional activation.	epigallocatechin gallate	13-17	heme oxygenase 1	Homo sapiens	90-94
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	tin protoporphyrin IX	52-70	heme oxygenase 1	Homo sapiens	37-41
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	tin protoporphyrin IX	52-70	heme oxygenase 1	Homo sapiens	37-41
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	tin protoporphyrin IX	72-78	heme oxygenase 1	Homo sapiens	37-41
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	tin protoporphyrin IX	72-78	heme oxygenase 1	Homo sapiens	37-41
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	epigallocatechin gallate	112-116	heme oxygenase 1	Homo sapiens	0-4
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	epigallocatechin gallate	112-116	heme oxygenase 1	Homo sapiens	37-41
24968709-10	2014	HO-1 knockdown or treatment with the HO-1 inhibitor tin protoporphyrin (SnPPIX) reversed the protective role of EGCG, indicating an important role for HO-1.	epigallocatechin gallate	112-116	heme oxygenase 1	Homo sapiens	37-41
25036905-2	2014	In this study, we hypothesized that the expression of heme oxygenase-1 determined by the number of guanidinium thiocyanate (GT) repeats can influence the occurrence of acute pancreatitis.	Guanidine	99-110	heme oxygenase 1	Homo sapiens	54-70
25036905-2	2014	In this study, we hypothesized that the expression of heme oxygenase-1 determined by the number of guanidinium thiocyanate (GT) repeats can influence the occurrence of acute pancreatitis.	thiocyanate	111-122	heme oxygenase 1	Homo sapiens	54-70
25156196-11	2014	It was also demonstrated that HO-1 is modulated by NO, as shown by experiments performed in the presence of an NO donor (sodium nitroprusside), an NO scavenger (2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide), or an NO synthesis inhibitor (N-nitro-l-arginine methyl ester, NAME).	Nitroprusside	121-141	heme oxygenase 1	Homo sapiens	30-34
25213834-4	2014	Knockdown of Nrf2 by siRNA (siNrf2) targeting caused additional refractoriness of HO-1 protein induction to a second UVA or heme treatment and this treatment also further enhanced cell damage by a second dose of UVA radiation.	Heme	124-128	heme oxygenase 1	Homo sapiens	82-86
25156196-11	2014	It was also demonstrated that HO-1 is modulated by NO, as shown by experiments performed in the presence of an NO donor (sodium nitroprusside), an NO scavenger (2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide), or an NO synthesis inhibitor (N-nitro-l-arginine methyl ester, NAME).	1,3-dihydroxy-4,4,5,5-tetramethyl-2-(4-carboxyphenyl)tetrahydroimidazole	161-227	heme oxygenase 1	Homo sapiens	30-34
25156196-11	2014	It was also demonstrated that HO-1 is modulated by NO, as shown by experiments performed in the presence of an NO donor (sodium nitroprusside), an NO scavenger (2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide), or an NO synthesis inhibitor (N-nitro-l-arginine methyl ester, NAME).	n-nitro-l-arginine methyl ester	259-290	heme oxygenase 1	Homo sapiens	30-34
25190803-8	2014	The mammalian target of rapamycin complex 2 (mTORC2) inhibitor, AZD2014, ablated XBP1u or HDAC3 or disturbed flow-mediated Akt1 phosphorylation, Nrf2 nuclear translocation, and HO-1 expression.	vistusertib	64-71	heme oxygenase 1	Homo sapiens	177-181
25105464-6	2014	Treatment with CDDO-Me increased the gene expression of NQO1 (P = 0.04) and decreased the expression of HO-1 (P = 0.03) in PBMCs from patients with septic shock.	bardoxolone methyl	15-22	heme oxygenase 1	Homo sapiens	104-108
25169430-4	2014	Co-treatment with 100muM sesamin for 12h up-regulated the HO-1 protein level increased by LPS; however, HO-1 mRNA was unaffected.	sesamin	25-32	heme oxygenase 1	Homo sapiens	58-62
25223958-0	2014	Upregulation of both heme oxygenase-1 and ATPase inhibitory factor 1 renders tumoricidal activity by synthetic flavonoids via depleting cellular ATP.	Flavonoids	111-121	heme oxygenase 1	Homo sapiens	21-37
25169430-5	2014	Sesamin delayed the reversal, by the protein synthesis inhibitor cycloheximide (1muM), of the LPS-induced increase of HO-1 protein level.	sesamin	0-7	heme oxygenase 1	Homo sapiens	118-122
25223958-8	2014	To gain a physiological significance, we treated the synthetic flavonoids in colon cancer cells, HT29 and HCT116 cells and confirmed that overexpression of both HO-1 and ATPIF1 was critical for tumor cell death with an impaired mitochondrial energetics.	Flavonoids	63-73	heme oxygenase 1	Homo sapiens	161-165
25169430-10	2014	Co-treatment with sesamin decreased ubiquitinated HO-1 protein accumulation by MG-132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	79-85	heme oxygenase 1	Homo sapiens	50-54
25169430-12	2014	These findings suggest that sesamin disturbs the degradation of HO-1 protein through inhibiting its ubiquitination, resulting in HO-1 protein up-regulation.	sesamin	28-35	heme oxygenase 1	Homo sapiens	64-68
25169430-5	2014	Sesamin delayed the reversal, by the protein synthesis inhibitor cycloheximide (1muM), of the LPS-induced increase of HO-1 protein level.	Cycloheximide	65-78	heme oxygenase 1	Homo sapiens	118-122
25169430-12	2014	These findings suggest that sesamin disturbs the degradation of HO-1 protein through inhibiting its ubiquitination, resulting in HO-1 protein up-regulation.	sesamin	28-35	heme oxygenase 1	Homo sapiens	129-133
25169430-8	2014	To clarify the mechanisms that underlie the up-regulation of HO-1 protein level by sesamin, the human embryonic kidney (HEK) 293T cell line transfected with Flag-tagged HO-1 was used.	sesamin	83-90	heme oxygenase 1	Homo sapiens	61-65
25169430-9	2014	A proteasome inhibitor, MG-132 (10muM), stabilized HO-1 protein in HEK 293T cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	24-30	heme oxygenase 1	Homo sapiens	51-55
25169430-10	2014	Co-treatment with sesamin decreased ubiquitinated HO-1 protein accumulation by MG-132.	sesamin	18-25	heme oxygenase 1	Homo sapiens	50-54
24499676-4	2014	In addition, the transduced PEP-1-HO-1 inhibited generation of reactive oxygen species (ROS) and cell death caused by 1-methyl-4-phenylpyridinium ion (MPP+).	Reactive Oxygen Species	63-86	heme oxygenase 1	Homo sapiens	34-38
25325059-8	2014	Induction of heme oxygenase-1, which can be attained with phase 2 inducer phytochemicals such as lipoic acid and green tea catechins, promotes reverse cholesterol transport in macrophages and inhibits atherogenesis in rodents, likely due to, in large part, NF-kappaB antagonism.	Thioctic Acid	97-108	heme oxygenase 1	Homo sapiens	13-29
25325059-8	2014	Induction of heme oxygenase-1, which can be attained with phase 2 inducer phytochemicals such as lipoic acid and green tea catechins, promotes reverse cholesterol transport in macrophages and inhibits atherogenesis in rodents, likely due to, in large part, NF-kappaB antagonism.	Catechin	123-132	heme oxygenase 1	Homo sapiens	13-29
25325059-8	2014	Induction of heme oxygenase-1, which can be attained with phase 2 inducer phytochemicals such as lipoic acid and green tea catechins, promotes reverse cholesterol transport in macrophages and inhibits atherogenesis in rodents, likely due to, in large part, NF-kappaB antagonism.	Cholesterol	151-162	heme oxygenase 1	Homo sapiens	13-29
25086213-2	2014	Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation.	Heme	112-116	heme oxygenase 1	Homo sapiens	0-16
25086213-2	2014	Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation.	Heme	112-116	heme oxygenase 1	Homo sapiens	18-22
25341814-0	2014	Atorvastatin Attenuates TNF-alpha Production via Heme Oxygenase-1 Pathway in LPS-stimulated RAW264.7 Macrophages.	Atorvastatin	0-12	heme oxygenase 1	Homo sapiens	49-65
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	Atorvastatin	76-88	heme oxygenase 1	Homo sapiens	4-8
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	Atorvastatin	76-88	heme oxygenase 1	Homo sapiens	22-26
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	Atorvastatin	111-123	heme oxygenase 1	Homo sapiens	4-8
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	Atorvastatin	111-123	heme oxygenase 1	Homo sapiens	22-26
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	SB 203580	152-160	heme oxygenase 1	Homo sapiens	4-8
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	SB 203580	152-160	heme oxygenase 1	Homo sapiens	22-26
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	165-172	heme oxygenase 1	Homo sapiens	4-8
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	165-172	heme oxygenase 1	Homo sapiens	22-26
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	Atorvastatin	111-123	heme oxygenase 1	Homo sapiens	4-8
25341814-7	2014	The HO-1 activity and HO-1 expression level were significantly higher after atorvastatin treatment than before atorvastatin treatment and attenuated by SB203580 and PD98059 but not by SP600125, suggesting that the ERK and p38 mitogen-activated protein kinase (MAPK) pathways participate in regulating the above-mentioned effects of atorvastatin.	Atorvastatin	111-123	heme oxygenase 1	Homo sapiens	22-26
25341814-8	2014	Moreover, the HO-1 activity suppressed by SnPP or the HO-1 expression inhibited by siRNA significantly attenuated the effect of atorvastatin on TNF-alpha expression and production in LPS-stimulated macrophages.	Atorvastatin	128-140	heme oxygenase 1	Homo sapiens	14-18
25341814-8	2014	Moreover, the HO-1 activity suppressed by SnPP or the HO-1 expression inhibited by siRNA significantly attenuated the effect of atorvastatin on TNF-alpha expression and production in LPS-stimulated macrophages.	Atorvastatin	128-140	heme oxygenase 1	Homo sapiens	54-58
25341814-9	2014	CONCLUSION: Atorvastatin can attenuate LPS-induced TNF-alpha expression and production by activating HO-1 via the ERK and p38 MAPK pathways, suggesting that atorvastatin can be used in treatment of inflammatory diseases such as sepsis, especially in those with atherosclerotic diseases.	Atorvastatin	12-24	heme oxygenase 1	Homo sapiens	101-105
25341814-9	2014	CONCLUSION: Atorvastatin can attenuate LPS-induced TNF-alpha expression and production by activating HO-1 via the ERK and p38 MAPK pathways, suggesting that atorvastatin can be used in treatment of inflammatory diseases such as sepsis, especially in those with atherosclerotic diseases.	Atorvastatin	157-169	heme oxygenase 1	Homo sapiens	101-105
24934751-0	2014	AP-1 activation attenuates the arsenite-induced apoptotic response in human bronchial epithelial cells by up-regulating HO-1 expression.	arsenite	31-39	heme oxygenase 1	Homo sapiens	120-124
24934751-4	2014	Here, we show that a significant induction of HO-1 expression is present in human bronchial epithelial cells (Beas-2B) treated with lethal doses of arsenite treatment.	arsenite	148-156	heme oxygenase 1	Homo sapiens	46-50
24934751-6	2014	As expected, HO-1 RNAi knockdown, or ERK/AP1 inhibition, renders the Beas-2B cells more sensitive to arsenite damage.	arsenite	101-109	heme oxygenase 1	Homo sapiens	13-17
24934751-7	2014	Our data thus suggest that transcriptional upregulation of HO-1 expression via a putative ERK/AP-1 pathway constitutes an inherent mechanism by which arsenite-induced apoptosis is attenuated.	arsenite	150-158	heme oxygenase 1	Homo sapiens	59-63
24499676-4	2014	In addition, the transduced PEP-1-HO-1 inhibited generation of reactive oxygen species (ROS) and cell death caused by 1-methyl-4-phenylpyridinium ion (MPP+).	Reactive Oxygen Species	88-91	heme oxygenase 1	Homo sapiens	34-38
24499676-4	2014	In addition, the transduced PEP-1-HO-1 inhibited generation of reactive oxygen species (ROS) and cell death caused by 1-methyl-4-phenylpyridinium ion (MPP+).	1-Methyl-4-phenylpyridinium	118-149	heme oxygenase 1	Homo sapiens	34-38
24499676-4	2014	In addition, the transduced PEP-1-HO-1 inhibited generation of reactive oxygen species (ROS) and cell death caused by 1-methyl-4-phenylpyridinium ion (MPP+).	mangion-purified polysaccharide (Candida albicans)	151-155	heme oxygenase 1	Homo sapiens	34-38
24732176-3	2014	Such investigation could be important, as iron and carbon monoxide are two of the products of heme catabolism via heme oxygenase-1, an enzyme upregulated in a variety of disease states associated with thrombophilia.	Iron	42-46	heme oxygenase 1	Homo sapiens	114-130
24732176-3	2014	Such investigation could be important, as iron and carbon monoxide are two of the products of heme catabolism via heme oxygenase-1, an enzyme upregulated in a variety of disease states associated with thrombophilia.	Carbon Monoxide	51-66	heme oxygenase 1	Homo sapiens	114-130
24732176-3	2014	Such investigation could be important, as iron and carbon monoxide are two of the products of heme catabolism via heme oxygenase-1, an enzyme upregulated in a variety of disease states associated with thrombophilia.	Heme	94-98	heme oxygenase 1	Homo sapiens	114-130
25150395-0	2014	Up-regulation of heme oxygenase-1 expression modulates reactive oxygen species level during the cryopreservation of human seminiferous tubules.	Reactive Oxygen Species	55-78	heme oxygenase 1	Homo sapiens	17-33
25150395-13	2014	The ROS level was negatively correlated with HO-1 expression.	Reactive Oxygen Species	4-7	heme oxygenase 1	Homo sapiens	45-49
25023856-2	2014	Described here are studies of tyrosyl radical formation reactions that occur after oxidizing Fe(III)(Por) to Fe(IV)=O(Por( +)) in human heme oxygenase isoform-1 (hHO-1) and the structurally homologous protein from Corynebacterium diphtheriae (cdHO).	Tyrosyl radical	30-45	heme oxygenase 1	Homo sapiens	162-167
24993616-7	2014	Furthermore, sulforaphane was observed to activate endoplasmic reticulum (ER) stress and the nuclear factor-E2-related factor-2 (Nrf2) signaling pathway, as demonstrated by the upregulation of ER stress-related proteins, including glucose-regulated protein 78 and C/EBP-homologous protein, and the accumulation of phosphorylated Nrf2 proteins in the nucleus and induction of heme oxygenase-1 expression, respectively.	sulforaphane	13-25	heme oxygenase 1	Homo sapiens	375-391
26461289-4	2014	Sulforaphane (SFN) is an isothiocyanate present in cruciferous vegetables that can induce antioxidant defence enzymes such as heme oxygenase-1 (HO-1) and peroxiredoxin-1 (Prx-1).	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	126-142
26461289-4	2014	Sulforaphane (SFN) is an isothiocyanate present in cruciferous vegetables that can induce antioxidant defence enzymes such as heme oxygenase-1 (HO-1) and peroxiredoxin-1 (Prx-1).	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	144-148
26461289-4	2014	Sulforaphane (SFN) is an isothiocyanate present in cruciferous vegetables that can induce antioxidant defence enzymes such as heme oxygenase-1 (HO-1) and peroxiredoxin-1 (Prx-1).	sulforaphane	14-17	heme oxygenase 1	Homo sapiens	126-142
26461289-4	2014	Sulforaphane (SFN) is an isothiocyanate present in cruciferous vegetables that can induce antioxidant defence enzymes such as heme oxygenase-1 (HO-1) and peroxiredoxin-1 (Prx-1).	sulforaphane	14-17	heme oxygenase 1	Homo sapiens	144-148
26461289-4	2014	Sulforaphane (SFN) is an isothiocyanate present in cruciferous vegetables that can induce antioxidant defence enzymes such as heme oxygenase-1 (HO-1) and peroxiredoxin-1 (Prx-1).	isothiocyanic acid	25-39	heme oxygenase 1	Homo sapiens	126-142
26461289-4	2014	Sulforaphane (SFN) is an isothiocyanate present in cruciferous vegetables that can induce antioxidant defence enzymes such as heme oxygenase-1 (HO-1) and peroxiredoxin-1 (Prx-1).	isothiocyanic acid	25-39	heme oxygenase 1	Homo sapiens	144-148
25091622-0	2014	Tussilagone inhibits dendritic cell functions via induction of heme oxygenase-1.	tussilagone	0-11	heme oxygenase 1	Homo sapiens	63-79
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	tussilagone	40-43	heme oxygenase 1	Homo sapiens	54-70
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	tussilagone	40-43	heme oxygenase 1	Homo sapiens	72-76
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	Heme	54-58	heme oxygenase 1	Homo sapiens	72-76
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	Carbon Monoxide	138-153	heme oxygenase 1	Homo sapiens	54-70
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	Carbon Monoxide	138-153	heme oxygenase 1	Homo sapiens	72-76
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	Bilirubin	158-167	heme oxygenase 1	Homo sapiens	54-70
25091622-5	2014	As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin.	Bilirubin	158-167	heme oxygenase 1	Homo sapiens	72-76
25091622-6	2014	HO-1 inhibitor reversed the inhibitory activity of TUS in DCs.	tussilagone	51-54	heme oxygenase 1	Homo sapiens	0-4
25091622-7	2014	In conclusion, this study suggests that TUS inhibits DC function through the induction of HO-1.	tussilagone	40-43	heme oxygenase 1	Homo sapiens	90-94
25091623-5	2014	However, 3-DSC-mediated HO-1 induction was completely blocked by treatment with cycloheximide, a translational inhibitor, or rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR).	Cycloheximide	80-93	heme oxygenase 1	Homo sapiens	24-28
25091623-5	2014	However, 3-DSC-mediated HO-1 induction was completely blocked by treatment with cycloheximide, a translational inhibitor, or rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR).	Sirolimus	125-134	heme oxygenase 1	Homo sapiens	24-28
25202977-6	2014	HO-1 siRNA knockdown and HO enzymatic inhibition in HIV-infected macrophages increased supernatant glutamate and neurotoxicity.	Glutamic Acid	99-108	heme oxygenase 1	Homo sapiens	0-4
25202977-7	2014	In contrast, increasing HO-1 expression through siRNA derepression or with nonselective pharmacologic inducers, including the CNS-penetrating drug dimethyl fumarate (DMF), decreased supernatant glutamate and neurotoxicity.	Dimethyl Fumarate	147-164	heme oxygenase 1	Homo sapiens	24-28
25202977-7	2014	In contrast, increasing HO-1 expression through siRNA derepression or with nonselective pharmacologic inducers, including the CNS-penetrating drug dimethyl fumarate (DMF), decreased supernatant glutamate and neurotoxicity.	Dimethyl Fumarate	166-169	heme oxygenase 1	Homo sapiens	24-28
25202977-7	2014	In contrast, increasing HO-1 expression through siRNA derepression or with nonselective pharmacologic inducers, including the CNS-penetrating drug dimethyl fumarate (DMF), decreased supernatant glutamate and neurotoxicity.	Glutamic Acid	194-203	heme oxygenase 1	Homo sapiens	24-28
25023856-2	2014	Described here are studies of tyrosyl radical formation reactions that occur after oxidizing Fe(III)(Por) to Fe(IV)=O(Por( +)) in human heme oxygenase isoform-1 (hHO-1) and the structurally homologous protein from Corynebacterium diphtheriae (cdHO).	ferric sulfate	93-100	heme oxygenase 1	Homo sapiens	162-167
25023856-2	2014	Described here are studies of tyrosyl radical formation reactions that occur after oxidizing Fe(III)(Por) to Fe(IV)=O(Por( +)) in human heme oxygenase isoform-1 (hHO-1) and the structurally homologous protein from Corynebacterium diphtheriae (cdHO).	fe(iv)	109-115	heme oxygenase 1	Homo sapiens	162-167
25023856-3	2014	Site-directed mutagenesis on hHO-1 probes the reduction of Fe(IV)=O(Por( +)) by tyrosine residues within 11 A of the prosthetic group.	Tyrosine	80-88	heme oxygenase 1	Homo sapiens	29-34
24734887-6	2014	We found that NAC significantly increased Nrf2 and downstream HO-1 expression.	Acetylcysteine	14-17	heme oxygenase 1	Homo sapiens	62-66
25037998-5	2014	In vitro, caffeic acid increases the nuclear/cytosolic Nrf2 ratio and the mRNA expression of the downstream antioxidant enzymes, Upsilon-glutamyl cysteine synthetase, glutathione peroxidase, glutathione reductase, and heme oxygenase-1, by activating the JNK/p38 pathway in Int-407 cells.	caffeic acid	10-22	heme oxygenase 1	Homo sapiens	218-234
25093998-0	2014	Effects of aspirin &amp; simvastatin and aspirin, simvastatin, &amp; lipoic acid on heme oxygenase-1 in healthy human subjects.	Aspirin	41-48	heme oxygenase 1	Homo sapiens	84-100
25093998-0	2014	Effects of aspirin &amp; simvastatin and aspirin, simvastatin, &amp; lipoic acid on heme oxygenase-1 in healthy human subjects.	Adenosine Monophosphate	64-67	heme oxygenase 1	Homo sapiens	84-100
25093998-0	2014	Effects of aspirin &amp; simvastatin and aspirin, simvastatin, &amp; lipoic acid on heme oxygenase-1 in healthy human subjects.	Thioctic Acid	69-80	heme oxygenase 1	Homo sapiens	84-100
25093998-3	2014	However, the only drugs (i.e., hemin and heme arginate) which pharmacologically upregulate HO-1 in humans are expensive and can only be administered intravenously.	Hemin	31-36	heme oxygenase 1	Homo sapiens	91-95
25093998-3	2014	However, the only drugs (i.e., hemin and heme arginate) which pharmacologically upregulate HO-1 in humans are expensive and can only be administered intravenously.	heme arginate	41-54	heme oxygenase 1	Homo sapiens	91-95
25093998-4	2014	Our aims were to compare the effects of placebo, aspirin, and simvastatin alone, and with alpha-lipoic acid, on HO-1 protein concentration and activity in humans.	Simvastatin	62-73	heme oxygenase 1	Homo sapiens	112-116
25093998-4	2014	Our aims were to compare the effects of placebo, aspirin, and simvastatin alone, and with alpha-lipoic acid, on HO-1 protein concentration and activity in humans.	Thioctic Acid	90-107	heme oxygenase 1	Homo sapiens	112-116
25309329-5	2014	The isoform HMOX1 is highly inducible in response to reactive oxygen species, which induce an increase in BBB permeability and impair its pathophysiology.	Reactive Oxygen Species	53-76	heme oxygenase 1	Homo sapiens	12-17
25355252-5	2014	Compared with the control group, the serum HO-1 was significantly increased at 6, 12, 24, 48 h after the heart valve replacement surgery in both the RIPerC and RIPostC groups (P&lt;0.05); the SCr, BUN, urinary NGAL and serum iron values were decreased at 6, 12, 24, 48 h after the heart valve replacement surgery in both the RIPerC and RIPostC groups (P&gt;0.05).	Iron	225-229	heme oxygenase 1	Homo sapiens	43-47
25107906-5	2014	This regulation of Nrf2 post-induction by nuclear HO-1 is important for the preferential transcription of phase II detoxification enzymes such as NQO1 as well as glucose-6-phosphate dehydrogenase (G6PDH), a regulator of the pentose phosphate pathway.	Pentosephosphates	224-241	heme oxygenase 1	Homo sapiens	50-54
25272046-0	2014	Long-term aerobic exercise protects against cisplatin-induced nephrotoxicity by modulating the expression of IL-6 and HO-1.	Cisplatin	44-53	heme oxygenase 1	Homo sapiens	118-122
25148906-4	2014	Further analysis using gene microarray showed that 6S upregulated the expression of Nrf2 target genes (AKR1B10, FTL, GGTLA4, and HMOX1) in HCT-116 cells.	S 6	51-53	heme oxygenase 1	Homo sapiens	129-134
24954650-7	2014	HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO).	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4
25182732-5	2014	The collective application of polyunsaturated fatty acids (PUFAs) and irradiation significantly changed the expression of EGR1, TNF-alpha, NOTCH1, c-MYC, TP53, HMOX1, AKR1C1, NQO1, while up-regulation of GADD45A, EGR1, GRP78, DDIT3, c-MYC, FOSL1 were recorded both in response to PUFA treatment or irradiation alone.	Fatty Acids, Unsaturated	30-57	heme oxygenase 1	Homo sapiens	160-165
24954650-7	2014	HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO).	Biliverdine	25-35	heme oxygenase 1	Homo sapiens	0-4
24954650-7	2014	HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO).	Iron	37-41	heme oxygenase 1	Homo sapiens	0-4
24954650-7	2014	HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO).	Carbon Monoxide	46-61	heme oxygenase 1	Homo sapiens	0-4
24954650-7	2014	HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO).	Carbon Monoxide	63-65	heme oxygenase 1	Homo sapiens	0-4
24998495-0	2014	Andrographolide inhibits TNFalpha-induced ICAM-1 expression via suppression of NADPH oxidase activation and induction of HO-1 and GCLM expression through the PI3K/Akt/Nrf2 and PI3K/Akt/AP-1 pathways in human endothelial cells.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	121-125
24998495-7	2014	Andrographolide induced the gene expression of heme oxygenase 1 (HO-1) and glutamate cysteine ligase modifier subunit (GCLM) in a time-dependent manner.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	47-63
24998495-7	2014	Andrographolide induced the gene expression of heme oxygenase 1 (HO-1) and glutamate cysteine ligase modifier subunit (GCLM) in a time-dependent manner.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	65-69
24998495-11	2014	The mechanism underlying the up-regulation of HO-1 and GCLM by andrographolide was dependent on the PI3K/Akt pathway, and both the Nrf2 and AP-1 transcriptional factors were involved.	andrographolide	63-78	heme oxygenase 1	Homo sapiens	46-50
24998495-12	2014	Our results suggest that andrographolide attenuates TNFalpha-induced ICAM-1 expression at least partially through suppression of NADPH oxidase activation and induction of HO-1 and GCLM expression, which is PI3K/Akt pathway-dependent.	andrographolide	25-40	heme oxygenase 1	Homo sapiens	171-175
24970682-9	2014	Metformin reduced heme oxygenase-1 and superoxide dismutase 2 but upregulated catalase expression in MCF-7 cells.	Metformin	0-9	heme oxygenase 1	Homo sapiens	18-34
24568186-0	2014	15-deoxy-Delta12,14-prostaglandin J2 induces p53 expression through Nrf2-mediated upregulation of heme oxygenase-1 in human breast cancer cells.	14-prostaglandin j2	17-36	heme oxygenase 1	Homo sapiens	98-114
25072782-3	2014	CO is a byproduct of heme degradation mediated by heme oxygenase (HO-1).	Heme	21-25	heme oxygenase 1	Homo sapiens	66-70
24568186-3	2014	In the present work, we investigated the effects of HO-1 on the expression of p53 induced by 15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ2) in human breast cancer (MCF-7) cells.	9-deoxy-delta-9-prostaglandin D2	115-131	heme oxygenase 1	Homo sapiens	52-56
24568186-4	2014	Treatment of MCF-7 cells with 15d-PGJ2 led to time-dependent increases in the expression of p53 as well as HO-1.	15-deoxy-delta(12,14)-prostaglandin J2	30-38	heme oxygenase 1	Homo sapiens	107-111
24568186-5	2014	Upregulation of p53 expression by 15d-PGJ2 was abrogated by si-RNA knock-down of HO-1.	15-deoxy-delta(12,14)-prostaglandin J2	34-42	heme oxygenase 1	Homo sapiens	81-85
24568186-8	2014	We speculated that iron, a by-product of HO-1-catalyzed reactions, could mediate 15d-PGJ2-induced p53 expression.	Iron	19-23	heme oxygenase 1	Homo sapiens	41-45
24568186-8	2014	We speculated that iron, a by-product of HO-1-catalyzed reactions, could mediate 15d-PGJ2-induced p53 expression.	15-deoxy-delta(12,14)-prostaglandin J2	81-89	heme oxygenase 1	Homo sapiens	41-45
24568186-10	2014	Iron released from heme by HO-1 activity is mostly in the Fe(2+) form.	Iron	0-4	heme oxygenase 1	Homo sapiens	27-31
24568186-10	2014	Iron released from heme by HO-1 activity is mostly in the Fe(2+) form.	Heme	19-23	heme oxygenase 1	Homo sapiens	27-31
24568186-10	2014	Iron released from heme by HO-1 activity is mostly in the Fe(2+) form.	ammonium ferrous sulfate	58-64	heme oxygenase 1	Homo sapiens	27-31
24932697-0	2014	Gastrodin protects against MPP(+)-induced oxidative stress by up regulates heme oxygenase-1 expression through p38 MAPK/Nrf2 pathway in human dopaminergic cells.	gastrodin	0-9	heme oxygenase 1	Homo sapiens	75-91
24932697-8	2014	And the increase in HO-1 expression was correlated with the protective effect of gastrodin against MPP(+)-induced injury.	gastrodin	81-90	heme oxygenase 1	Homo sapiens	20-24
24932697-8	2014	And the increase in HO-1 expression was correlated with the protective effect of gastrodin against MPP(+)-induced injury.	mangion-purified polysaccharide (Candida albicans)	99-105	heme oxygenase 1	Homo sapiens	20-24
24932697-9	2014	Because the inhibitor of HO-1 activity, ZnPP reversed the protective effect of gastrodin against MPP(+)-induced cell death.	zinc protoporphyrin	40-44	heme oxygenase 1	Homo sapiens	25-29
24932697-9	2014	Because the inhibitor of HO-1 activity, ZnPP reversed the protective effect of gastrodin against MPP(+)-induced cell death.	gastrodin	79-88	heme oxygenase 1	Homo sapiens	25-29
24932697-10	2014	We also demonstrated that the specific p38 MAPK inhibitor, SB203580, concentration-dependently blocked on gastrodin-induced HO-1 expression, and meanwhile SB203580 reversed the protective effect of gastrodin against MPP(+)-induced cell death.	SB 203580	59-67	heme oxygenase 1	Homo sapiens	124-128
24932697-11	2014	Taken together, these findings suggest that gastrodin can induce HO-1 expression through activation of p38 MAPK/Nrf2 signaling pathway, thereby protecting the SH-SY5Y cells from MPP(+)-induced oxidative cell death.	gastrodin	44-53	heme oxygenase 1	Homo sapiens	65-69
24963040-3	2014	Here, we report that subablative bone marrow transplantation (BMT) has a curative effect for disease in Hmox1(-/-) animals as a result of restoration of heme recycling by repopulation of the tissues with wild-type macrophages.	Heme	153-157	heme oxygenase 1	Homo sapiens	104-109
24963040-6	2014	These cells, identified as Kupffer cells with high levels of Hmox1 expression, persisted months after transient engraftment of the donor bone marrow and were responsible for the full restoration of heme-recycling ability in Hmox1(-/-) mice and reversing Hmox1-deficient phenotype.	Heme	198-202	heme oxygenase 1	Homo sapiens	224-229
24718901-8	2014	WA demonstrated induction of N-acetyl-L-cysteine-repressible oxidative stress as measured directly and through a subsequent heat shock response with HSP32 and HSP70 upregulation and decreased HSF1.	Acetylcysteine	29-48	heme oxygenase 1	Homo sapiens	149-154
24662764-3	2014	Our previous study showed that the nuclear factor E2-related factor 2-antioxidant response element (Nrf2-ARE) pathway and its downstream antioxidant enzyme heme oxygenase-1 (HO-1) are crucial for melanocytes to cope with H2O2-induced oxidative damage.	Hydrogen Peroxide	221-225	heme oxygenase 1	Homo sapiens	156-172
24662764-3	2014	Our previous study showed that the nuclear factor E2-related factor 2-antioxidant response element (Nrf2-ARE) pathway and its downstream antioxidant enzyme heme oxygenase-1 (HO-1) are crucial for melanocytes to cope with H2O2-induced oxidative damage.	Hydrogen Peroxide	221-225	heme oxygenase 1	Homo sapiens	174-178
24662764-5	2014	We found that vitiligo melanocytes exhibited hypersensitivity to H2O2-induced oxidative injury because of reduced Nrf2 nuclear translocation and transcriptional activity, which led to decreased HO-1 expression and aberrant redox balance.	Hydrogen Peroxide	65-69	heme oxygenase 1	Homo sapiens	194-198
25371895-0	2014	Sildenafil Inhibits Advanced Glycation End Products-induced sFlt-1 Release Through Upregulation of Heme Oxygenase-1.	Sildenafil Citrate	0-10	heme oxygenase 1	Homo sapiens	99-115
25371895-8	2014	CONCLUSION: These results strongly suggest that sildenafil citrate inhibits sFlt-1 release and ROS production in cells treated with AGEs-BSA through upregulation of the HO-1 expression in JEG-3 cells.	Sildenafil Citrate	48-66	heme oxygenase 1	Homo sapiens	169-173
25176212-6	2014	The reactive oxygen species were detected in the HO-1-overexpression HEK293T cells and the normal cells after the adding of hydrogen peroxide.	Reactive Oxygen Species	4-27	heme oxygenase 1	Homo sapiens	49-53
25176212-6	2014	The reactive oxygen species were detected in the HO-1-overexpression HEK293T cells and the normal cells after the adding of hydrogen peroxide.	Hydrogen Peroxide	124-141	heme oxygenase 1	Homo sapiens	49-53
25176212-9	2014	The reactive oxygen species in the HO-1-overexpression HEK293T cells and human umbilical vein endothelial cells decreased obviously after exposure to hydrogen peroxide.	Reactive Oxygen Species	4-27	heme oxygenase 1	Homo sapiens	35-39
25176212-9	2014	The reactive oxygen species in the HO-1-overexpression HEK293T cells and human umbilical vein endothelial cells decreased obviously after exposure to hydrogen peroxide.	Hydrogen Peroxide	150-167	heme oxygenase 1	Homo sapiens	35-39
25317018-3	2014	To regulate hemeoxygenase-1 (HO-1) expression, the cells were treated CoCl2 or HO-1 siRNA.	cobaltous chloride	70-75	heme oxygenase 1	Homo sapiens	12-33
24997245-11	2014	Furthermore, alpha-iso-cubebenol stimulated the expression of multiple antioxidant response genes (NQO-1 and HO-1).	alpha-iso-cubebenol	13-32	heme oxygenase 1	Homo sapiens	109-113
25136316-7	2014	In addition, curcumin with its versatile activities modulated the expression of many oxidative stress-regulating genes such as PDGF, VEGF, IGFBP-2, HO1, SOD2, and GPX1.	Curcumin	13-21	heme oxygenase 1	Homo sapiens	148-151
25019514-7	2014	Bach1 has an endogenous ligand, heme, that inhibits Bach1 binding to ARE, thus allowing Nrf2-mediated gene expression including that of heme-oxygenase-1 (HMOX1), a well described target of Bach1 repression.	Heme	32-36	heme oxygenase 1	Homo sapiens	136-152
25068294-8	2014	Antioxidant proteins including heme oxygenase-1 and peroxiredoxin-2 levels were also increased in retinal AC under high glucose conditions through nuclear localization of transcription factor nuclear factor-erythroid 2-related factor-2.	Glucose	120-127	heme oxygenase 1	Homo sapiens	31-47
25019514-7	2014	Bach1 has an endogenous ligand, heme, that inhibits Bach1 binding to ARE, thus allowing Nrf2-mediated gene expression including that of heme-oxygenase-1 (HMOX1), a well described target of Bach1 repression.	Heme	32-36	heme oxygenase 1	Homo sapiens	154-159
25007817-0	2014	Nrf2-mediated HO-1 induction coupled with the ERK signaling pathway contributes to indirect antioxidant capacity of caffeic acid phenethyl ester in HepG2 cells.	caffeic acid phenethyl ester	116-144	heme oxygenase 1	Homo sapiens	14-18
25170436-7	2014	Results showed a significant increase in the expression of NRF2-responsive genes, GCLC, HMOX1, NQO1, after 1 muM Cd x 1 muM B[a]P co-exposure.	Cadmium	113-115	heme oxygenase 1	Homo sapiens	88-93
24981859-3	2014	NO suppresses the pathogenesis of ECM via a mechanism involving (1) the transcription factor nuclear factor erythroid 2-related factor 2 (NRF-2), (2) induction of heme oxygenase-1 (HO-1), and (3) CO production via heme catabolism by HO-1.	Heme	163-167	heme oxygenase 1	Homo sapiens	181-185
25007817-4	2014	Treatment with ERK inhibitor U126 completely suppressed CAPE-induced ERK phosphorylation and HO-1 expression, but it only partly inhibited CAPE-induced Nrf2 accumulation and ARE promoter.	3-Bromo-2-fluorotoluene	29-33	heme oxygenase 1	Homo sapiens	93-97
25007817-4	2014	Treatment with ERK inhibitor U126 completely suppressed CAPE-induced ERK phosphorylation and HO-1 expression, but it only partly inhibited CAPE-induced Nrf2 accumulation and ARE promoter.	caffeic acid phenethyl ester	56-60	heme oxygenase 1	Homo sapiens	93-97
25007817-6	2014	From the overall results it is proposed that the indirect antioxidant activity of CAPE against oxidative stress in HepG2 cells is partially attributed to induction of HO-1, which is regulated by Kelch-like erythroid-cell-derived protein with CNC homology (ECH)-associated protein 1 (Keap1)-independent Nrf2 activation relying on post-translational phosphorylation of ERK.	caffeic acid phenethyl ester	82-86	heme oxygenase 1	Homo sapiens	167-171
24594225-4	2014	RESULTS: 17-Oxo-DHA was a strong inducer of the anti-oxidant response promoting Nrf2 nuclear accumulation, leading to the expression of heme oxygenase 1 and more than doubling glutathione levels.	(4Z,7Z,10Z,13Z,15E,19Z)-17-Oxodocosahexaenoic acid	9-19	heme oxygenase 1	Homo sapiens	136-152
24703885-2	2014	We previously reported that caffeic acid phenethyl ester (CAPE), a plant-derived polyphenolic compound, protected human umbilical vein endothelial cells (HUVEC) from menadione-induced oxidative stress and that this cytoprotective effect was correlated with the capacity to induce heme oxygenase-1 (HMOX1) and its protein product, a phase II cytoprotective enzyme.	caffeic acid phenethyl ester	28-56	heme oxygenase 1	Homo sapiens	280-296
24703885-2	2014	We previously reported that caffeic acid phenethyl ester (CAPE), a plant-derived polyphenolic compound, protected human umbilical vein endothelial cells (HUVEC) from menadione-induced oxidative stress and that this cytoprotective effect was correlated with the capacity to induce heme oxygenase-1 (HMOX1) and its protein product, a phase II cytoprotective enzyme.	caffeic acid phenethyl ester	28-56	heme oxygenase 1	Homo sapiens	298-303
24703885-2	2014	We previously reported that caffeic acid phenethyl ester (CAPE), a plant-derived polyphenolic compound, protected human umbilical vein endothelial cells (HUVEC) from menadione-induced oxidative stress and that this cytoprotective effect was correlated with the capacity to induce heme oxygenase-1 (HMOX1) and its protein product, a phase II cytoprotective enzyme.	caffeic acid phenethyl ester	58-62	heme oxygenase 1	Homo sapiens	280-296
24703885-2	2014	We previously reported that caffeic acid phenethyl ester (CAPE), a plant-derived polyphenolic compound, protected human umbilical vein endothelial cells (HUVEC) from menadione-induced oxidative stress and that this cytoprotective effect was correlated with the capacity to induce heme oxygenase-1 (HMOX1) and its protein product, a phase II cytoprotective enzyme.	caffeic acid phenethyl ester	58-62	heme oxygenase 1	Homo sapiens	298-303
24703885-6	2014	In addition to potent up-regulation of HMOX1, heat shock proteins (HSP) were also found to be highly induced by CDDO-Im in HUVEC.	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	112-119	heme oxygenase 1	Homo sapiens	39-44
24613679-8	2014	RESULTS: rHx-bound heme induced the expression of HO-1 and decreased the level of Bach1 protein.	rhx	9-12	heme oxygenase 1	Homo sapiens	50-54
24613679-8	2014	RESULTS: rHx-bound heme induced the expression of HO-1 and decreased the level of Bach1 protein.	Heme	19-23	heme oxygenase 1	Homo sapiens	50-54
24613679-9	2014	CPZ inhibited the induction of the HO-1 expression by rHx-bound heme.	Chlorpromazine	0-3	heme oxygenase 1	Homo sapiens	35-39
24613679-9	2014	CPZ inhibited the induction of the HO-1 expression by rHx-bound heme.	rhx	54-57	heme oxygenase 1	Homo sapiens	35-39
24613679-9	2014	CPZ inhibited the induction of the HO-1 expression by rHx-bound heme.	Heme	64-68	heme oxygenase 1	Homo sapiens	35-39
24613679-10	2014	CONCLUSION: rHx-bound heme was internalized into the cells via endocytosis, resulting in HO-1 expression and inactivation of Bach1.	rhx	12-15	heme oxygenase 1	Homo sapiens	89-93
24613679-10	2014	CONCLUSION: rHx-bound heme was internalized into the cells via endocytosis, resulting in HO-1 expression and inactivation of Bach1.	Heme	22-26	heme oxygenase 1	Homo sapiens	89-93
24613679-11	2014	GENERAL SIGNIFICANCE: The Bach1-dependent repression of the HO-1 expression is under the control of the Hx-dependent uptake of extracellular heme.	Heme	141-145	heme oxygenase 1	Homo sapiens	60-64
24613679-2	2014	Heme also induces the expression of genes such as heme oxygenase-1 (HO-1) by inactivating the transcription repressor Bach1 through direct binding.	Heme	0-4	heme oxygenase 1	Homo sapiens	50-66
24613679-2	2014	Heme also induces the expression of genes such as heme oxygenase-1 (HO-1) by inactivating the transcription repressor Bach1 through direct binding.	Heme	0-4	heme oxygenase 1	Homo sapiens	68-72
24613679-3	2014	However, the source of heme for the regulation of the Bach1-HO-1 axis has been unclear.	Heme	23-27	heme oxygenase 1	Homo sapiens	60-64
25022355-7	2014	Also, SR decreased Ca(2+) and ROS, mitochondrial membrane potential, dysfunction, and increased glutathione, NAD(P)H dehydrogenase and heme oxygenase-1.	Strontium	6-8	heme oxygenase 1	Homo sapiens	135-151
24509340-2	2014	Colon and pancreas tumor cells have an increase in hemeoxygenase-1 (HO-1) activity, the endogenous enzyme responsible for carbon monoxide production.	Carbon Monoxide	122-137	heme oxygenase 1	Homo sapiens	51-72
24879794-6	2014	Exogenous hemin induced Treg polarization in purified T cell/monocyte cocultures from healthy volunteers through the monocyte anti-inflammatory heme-degrading enzyme heme oxygenase-1.	Hemin	10-15	heme oxygenase 1	Homo sapiens	166-182
24859911-12	2014	This is probably due to the enhancement of oxidative stress and cellular apoptosis induced by frequent glucose swings through the inhibition of Nrf2/HO-1 pathway.	Glucose	103-110	heme oxygenase 1	Homo sapiens	149-153
24742817-6	2014	Increased O2(-) levels promote ERK phosphorylation (approx sixfold compared to control; P &lt; 0.001) and downstream transcriptional increase of several genes: HMOX1 (P &lt; 0.05), involved in the protection of chemical reactive species; MDR1 (P &lt; 0.01), responsible for the efflux of xenobiotics in the cell; and CD83 (P &lt; 0.05), a DC maturation marker.	Superoxides	10-12	heme oxygenase 1	Homo sapiens	160-165
24799610-4	2014	Individuals with the long allele of a guanine-thymine (GTn) microsatellite repeat located in the promoter region of HMOX1 have a higher risk of cardiometabolic diseases compared with those with the short allele.	guanine-thymine	38-53	heme oxygenase 1	Homo sapiens	116-121
24799610-4	2014	Individuals with the long allele of a guanine-thymine (GTn) microsatellite repeat located in the promoter region of HMOX1 have a higher risk of cardiometabolic diseases compared with those with the short allele.	Nitroglycerin	55-58	heme oxygenase 1	Homo sapiens	116-121
24670329-5	2014	We and others have demonstrated that heme oxygenase-1 can modulate production of reactive oxygen species, both in vivo and in vitro, from NADPH oxidase, a major enzymatic source of reactive oxygen species generation in the vascular wall.	Reactive Oxygen Species	81-104	heme oxygenase 1	Homo sapiens	37-53
24670329-5	2014	We and others have demonstrated that heme oxygenase-1 can modulate production of reactive oxygen species, both in vivo and in vitro, from NADPH oxidase, a major enzymatic source of reactive oxygen species generation in the vascular wall.	Reactive Oxygen Species	181-204	heme oxygenase 1	Homo sapiens	37-53
24879794-6	2014	Exogenous hemin induced Treg polarization in purified T cell/monocyte cocultures from healthy volunteers through the monocyte anti-inflammatory heme-degrading enzyme heme oxygenase-1.	Heme	144-148	heme oxygenase 1	Homo sapiens	166-182
26104642-6	2014	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	72-87	heme oxygenase 1	Homo sapiens	29-45
24673378-0	2014	Guanosine protects C6 astroglial cells against azide-induced oxidative damage: a putative role of heme oxygenase 1.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	98-114
24673378-8	2014	Guanosine strongly prevented these effects, protecting glial cells against azide-induced cytotoxicity and modulating glial, oxidative and inflammatory responses through the activation of the heme oxygenase 1 pathway.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	191-207
24673378-12	2014	Guanosine prevented these effects through the HO1 signaling pathway, thus our findings support the antioxidant effects of guanosine.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	46-49
24673378-12	2014	Guanosine prevented these effects through the HO1 signaling pathway, thus our findings support the antioxidant effects of guanosine.	Guanosine	122-131	heme oxygenase 1	Homo sapiens	46-49
24788892-5	2014	Therefore, the present study assessed the inhibitory effect of PEITC on K562 cells and whether HO-1 facilitated cell apoptosis and ROS generation.	Reactive Oxygen Species	131-134	heme oxygenase 1	Homo sapiens	95-99
24788892-8	2014	The results of the present study suggest that PEITC may be a potential anti-tumor compound for CML therapy, and that HO-1 has a critical function in PEITC-induced apoptosis and ROS generation.	phenethyl isothiocyanate	149-154	heme oxygenase 1	Homo sapiens	117-121
24788892-8	2014	The results of the present study suggest that PEITC may be a potential anti-tumor compound for CML therapy, and that HO-1 has a critical function in PEITC-induced apoptosis and ROS generation.	Reactive Oxygen Species	177-180	heme oxygenase 1	Homo sapiens	117-121
24676542-0	2014	Heme oxygenase-1 silencing increases the sensitivity of human osteosarcoma MG63 cells to arsenic trioxide.	Arsenic Trioxide	89-105	heme oxygenase 1	Homo sapiens	0-16
24676542-2	2014	Our previous study regarding the effects of ATO on mesenchymal-derived human osteosarcoma MG63 cells showed that heme oxygenase-1 (HO-1) was strongly induced upon treatment with ATO.	Arsenic Trioxide	44-47	heme oxygenase 1	Homo sapiens	113-129
24676542-2	2014	Our previous study regarding the effects of ATO on mesenchymal-derived human osteosarcoma MG63 cells showed that heme oxygenase-1 (HO-1) was strongly induced upon treatment with ATO.	Arsenic Trioxide	44-47	heme oxygenase 1	Homo sapiens	131-135
24676542-2	2014	Our previous study regarding the effects of ATO on mesenchymal-derived human osteosarcoma MG63 cells showed that heme oxygenase-1 (HO-1) was strongly induced upon treatment with ATO.	Arsenic Trioxide	178-181	heme oxygenase 1	Homo sapiens	113-129
24676542-2	2014	Our previous study regarding the effects of ATO on mesenchymal-derived human osteosarcoma MG63 cells showed that heme oxygenase-1 (HO-1) was strongly induced upon treatment with ATO.	Arsenic Trioxide	178-181	heme oxygenase 1	Homo sapiens	131-135
24676542-3	2014	The present study sought to investigate the effect of silencing HO-1 on the sensitivity of osteosarcoma cells to ATO to determine the potential for therapeutic applications.	Arsenic Trioxide	113-116	heme oxygenase 1	Homo sapiens	64-68
24676542-6	2014	shRNA-mediated interference prevented the induction of HO-1, increased cell death, and increased intracellular ROS levels in MG63 cells upon treatment with ATO.	Arsenic Trioxide	156-159	heme oxygenase 1	Homo sapiens	55-59
24676542-7	2014	Silencing HO-1 increased the susceptibility of MG63 cells to the chemotherapeutic drug ATO by enhancing intracellular accumulation of ROS.	Reactive Oxygen Species	134-137	heme oxygenase 1	Homo sapiens	10-14
24676542-8	2014	Our results suggest that the inhibition of HO-1 could improve the outcome of osteosarcoma treated with ATO.	Arsenic Trioxide	103-106	heme oxygenase 1	Homo sapiens	43-47
26104642-6	2014	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	29-45
26104642-6	2014	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	47-51
26104642-6	2014	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	72-87	heme oxygenase 1	Homo sapiens	47-51
24530428-9	2014	In the case of DP41, the production of O2(-) radicals was followed by an up-regulation of Nrf2, HO-1, phospho-eIF2alpha and ATF4.	o2(-) radicals	39-53	heme oxygenase 1	Homo sapiens	96-100
24792517-4	2014	Although hemin was able to induce HO-1 in a dose dependent manner, a specific HO-1 inhibitor, Sn-PPIX, was unable to interfere with the effect of hemin on Caco-2 cells.	Hemin	9-14	heme oxygenase 1	Homo sapiens	34-38
24792517-4	2014	Although hemin was able to induce HO-1 in a dose dependent manner, a specific HO-1 inhibitor, Sn-PPIX, was unable to interfere with the effect of hemin on Caco-2 cells.	sn-ppix	94-101	heme oxygenase 1	Homo sapiens	78-82
24958774-4	2014	In a stable isotope labeling by amino acids in cell culture-based proteomics screen, we identified HO-1 (heme oxygenase-1), the rate-limiting enzyme in the degradation of heme to biliverdin, as a novel SPP substrate.	Heme	105-109	heme oxygenase 1	Homo sapiens	99-103
24958774-4	2014	In a stable isotope labeling by amino acids in cell culture-based proteomics screen, we identified HO-1 (heme oxygenase-1), the rate-limiting enzyme in the degradation of heme to biliverdin, as a novel SPP substrate.	Biliverdine	179-189	heme oxygenase 1	Homo sapiens	99-103
24958774-4	2014	In a stable isotope labeling by amino acids in cell culture-based proteomics screen, we identified HO-1 (heme oxygenase-1), the rate-limiting enzyme in the degradation of heme to biliverdin, as a novel SPP substrate.	Biliverdine	179-189	heme oxygenase 1	Homo sapiens	105-121
24927633-0	2014	Upregulation of heme oxygenase-1 in colorectal cancer patients with increased circulation carbon monoxide levels, potentially affects chemotherapeutic sensitivity.	Carbon Monoxide	90-105	heme oxygenase 1	Homo sapiens	16-32
24927633-1	2014	BACKGROUND: Heme oxygenase-1 (HO-1) and its major product carbon monoxide (CO) are known to be involved in the development and progression of many tumors.	Carbon Monoxide	58-73	heme oxygenase 1	Homo sapiens	12-28
24927633-1	2014	BACKGROUND: Heme oxygenase-1 (HO-1) and its major product carbon monoxide (CO) are known to be involved in the development and progression of many tumors.	Carbon Monoxide	58-73	heme oxygenase 1	Homo sapiens	30-34
24927633-1	2014	BACKGROUND: Heme oxygenase-1 (HO-1) and its major product carbon monoxide (CO) are known to be involved in the development and progression of many tumors.	Carbon Monoxide	75-77	heme oxygenase 1	Homo sapiens	12-28
24927633-1	2014	BACKGROUND: Heme oxygenase-1 (HO-1) and its major product carbon monoxide (CO) are known to be involved in the development and progression of many tumors.	Carbon Monoxide	75-77	heme oxygenase 1	Homo sapiens	30-34
24927633-9	2014	In parallel with HO-1 expression, circulation CO levels in CRC patients also significantly accelerated.	Carbon Monoxide	46-48	heme oxygenase 1	Homo sapiens	17-21
24927633-10	2014	Moreover, HO-1 expression/induction also related to the chemosensitivity of colon cells; HO inhibitor zinc protoporphyrin significantly increased cytotoxicities of THP (i.e., 2.6 - 5.3 folds compared to cells without zinc protoporphyrin treatment).	zinc protoporphyrin	102-121	heme oxygenase 1	Homo sapiens	10-14
24927633-10	2014	Moreover, HO-1 expression/induction also related to the chemosensitivity of colon cells; HO inhibitor zinc protoporphyrin significantly increased cytotoxicities of THP (i.e., 2.6 - 5.3 folds compared to cells without zinc protoporphyrin treatment).	pirarubicin	164-167	heme oxygenase 1	Homo sapiens	10-14
24927633-10	2014	Moreover, HO-1 expression/induction also related to the chemosensitivity of colon cells; HO inhibitor zinc protoporphyrin significantly increased cytotoxicities of THP (i.e., 2.6 - 5.3 folds compared to cells without zinc protoporphyrin treatment).	zinc protoporphyrin	217-236	heme oxygenase 1	Homo sapiens	10-14
24041027-2	2014	We sought to determine the role of NO, heme oxygenase-1 (HO-1), and its reaction product (carbon monoxide [CO]) in the induction of mitochondrial biogenesis by the natural antioxidant resveratrol.	Resveratrol	184-195	heme oxygenase 1	Homo sapiens	39-55
24041027-2	2014	We sought to determine the role of NO, heme oxygenase-1 (HO-1), and its reaction product (carbon monoxide [CO]) in the induction of mitochondrial biogenesis by the natural antioxidant resveratrol.	Resveratrol	184-195	heme oxygenase 1	Homo sapiens	57-61
24041027-6	2014	Cobalt protoporphyrin (CoPP)-IX, an HO-1 inducing agent, stimulated mitochondrial biogenesis in HepG2 cells, which could be reversed by the CO scavenger hemoglobin.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	36-40
24041027-6	2014	Cobalt protoporphyrin (CoPP)-IX, an HO-1 inducing agent, stimulated mitochondrial biogenesis in HepG2 cells, which could be reversed by the CO scavenger hemoglobin.	cobaltiprotoporphyrin	23-27	heme oxygenase 1	Homo sapiens	36-40
24041027-9	2014	The natural antioxidant resveratrol induced mitochondrial biogenesis in HepG2 cells, in a manner dependent on NO biosynthesis, cGMP synthesis, Nrf2-dependent HO-1 activation, and endogenous CO production.	Resveratrol	24-35	heme oxygenase 1	Homo sapiens	158-162
24959672-6	2014	In addition, urate markedly up-regulated the transcription and protein expression of gamma-glutamate-cysteine ligase catalytic subunit (gamma-GCLC) and heme oxygenase-1 (HO-1), both of which are controlled by Nrf2 activity.	Uric Acid	13-18	heme oxygenase 1	Homo sapiens	152-168
24768191-2	2014	Niacin directly activates both GPR-109A in leukocytes and the heme oxygenase-1 pathway, promoting strong anti-inflammatory and antioxidative effects, as well as induces immediate production of prostaglandin D2, leading to endothelial vasodilation.	Niacin	0-6	heme oxygenase 1	Homo sapiens	62-78
24458266-7	2014	HO-1 concentrations also positively correlated with random plasma glucose, circulating glycosylated hemoglobin, and low-density lipoprotein levels.	Glucose	66-73	heme oxygenase 1	Homo sapiens	0-4
24458266-8	2014	Moreover, patients with coincident TB and T2DM exhibited increased plasma levels of TIMP-4 and elevated peripheral blood neutrophil counts, which, when considered together with HO-1, resulted in increased power to discriminate individuals with active TB with and without T2DM.	Terbium	35-37	heme oxygenase 1	Homo sapiens	177-181
24610348-5	2014	In addition, DHF induced the activation of extracellular signal-regulated kinase (ERK), while U0126 (a specific pharmacological inhibitor of ERK kinase) abrogated DHF-activated Nrf2 and HO-1 expression.	dhf	163-166	heme oxygenase 1	Homo sapiens	186-190
24943970-0	2014	The relationship between anticancer effect of metformin and the transcriptional regulation of certain genes (CHOP, CAV-1, HO-1, SGK-1 and Par-4) on MCF-7 cell line.	Metformin	46-55	heme oxygenase 1	Homo sapiens	122-126
24610348-0	2014	Effect of 7, 8-dihydroxyflavone on the up-regulation of Nrf2-mediated heme oxygenase-1 expression in hamster lung fibroblasts.	6,7-dihydroxyflavone	10-31	heme oxygenase 1	Homo sapiens	70-86
24442713-0	2014	Angiotensin II-derived reactive oxygen species promote angiogenesis in human late endothelial progenitor cells through heme oxygenase-1 via ERK1/2 and AKT/PI3K pathways.	Reactive Oxygen Species	23-46	heme oxygenase 1	Homo sapiens	119-135
24442713-4	2014	Ang II-derived ROS could also upregulate heme oxygenase-1 (HO-1) expression, and treating late EPCs with HO-1 small interfering RNA or heme oxygenase inhibitor (HO inhibitor) could inhibit Ang II-induced tube formation and increase ROS level and apoptosis rate.	Reactive Oxygen Species	15-18	heme oxygenase 1	Homo sapiens	41-57
24442713-4	2014	Ang II-derived ROS could also upregulate heme oxygenase-1 (HO-1) expression, and treating late EPCs with HO-1 small interfering RNA or heme oxygenase inhibitor (HO inhibitor) could inhibit Ang II-induced tube formation and increase ROS level and apoptosis rate.	Reactive Oxygen Species	15-18	heme oxygenase 1	Homo sapiens	59-63
24442713-4	2014	Ang II-derived ROS could also upregulate heme oxygenase-1 (HO-1) expression, and treating late EPCs with HO-1 small interfering RNA or heme oxygenase inhibitor (HO inhibitor) could inhibit Ang II-induced tube formation and increase ROS level and apoptosis rate.	Reactive Oxygen Species	232-235	heme oxygenase 1	Homo sapiens	105-109
24442713-5	2014	In addition, PD98059 and LY294002 pretreatment attenuated Ang II-induced HO-1 expression.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	13-20	heme oxygenase 1	Homo sapiens	73-77
24442713-5	2014	In addition, PD98059 and LY294002 pretreatment attenuated Ang II-induced HO-1 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	25-33	heme oxygenase 1	Homo sapiens	73-77
24442713-6	2014	Accordingly, Ang II-derived ROS could promote angiogenesis in late EPCs by inducing HO-1 expression via ERK1/2 and AKT/PI3K pathways, and we believe HO-1 might be a promising intervention target in EPCs due to its potent proangiogenic, antioxidant, and antiapoptosis potentials.	Reactive Oxygen Species	28-31	heme oxygenase 1	Homo sapiens	84-88
24442713-6	2014	Accordingly, Ang II-derived ROS could promote angiogenesis in late EPCs by inducing HO-1 expression via ERK1/2 and AKT/PI3K pathways, and we believe HO-1 might be a promising intervention target in EPCs due to its potent proangiogenic, antioxidant, and antiapoptosis potentials.	Reactive Oxygen Species	28-31	heme oxygenase 1	Homo sapiens	149-153
24610348-1	2014	The cytoprotective mechanism of 7, 8-dihydroxyflavone (DHF) against oxidative stress-induced cell damage with respect to its stimulatory effect on the expression of heme oxygenase-1 (HO-1), a potent antioxidant enzyme, was investigated in the present study.	6,7-dihydroxyflavone	32-53	heme oxygenase 1	Homo sapiens	165-181
24610348-1	2014	The cytoprotective mechanism of 7, 8-dihydroxyflavone (DHF) against oxidative stress-induced cell damage with respect to its stimulatory effect on the expression of heme oxygenase-1 (HO-1), a potent antioxidant enzyme, was investigated in the present study.	6,7-dihydroxyflavone	32-53	heme oxygenase 1	Homo sapiens	183-187
24610348-1	2014	The cytoprotective mechanism of 7, 8-dihydroxyflavone (DHF) against oxidative stress-induced cell damage with respect to its stimulatory effect on the expression of heme oxygenase-1 (HO-1), a potent antioxidant enzyme, was investigated in the present study.	dhf	55-58	heme oxygenase 1	Homo sapiens	165-181
24610348-1	2014	The cytoprotective mechanism of 7, 8-dihydroxyflavone (DHF) against oxidative stress-induced cell damage with respect to its stimulatory effect on the expression of heme oxygenase-1 (HO-1), a potent antioxidant enzyme, was investigated in the present study.	dhf	55-58	heme oxygenase 1	Homo sapiens	183-187
24610348-2	2014	Up-regulation of HO-1 expression by DHF was both dose and time dependent in lung fibroblast V79-4 cells.	dhf	36-39	heme oxygenase 1	Homo sapiens	17-21
24610348-3	2014	DHF also increased the protein expression level of the transcription factor nuclear factor erythroid-2-related factor 2 (Nrf2), and induced the translocation of Nrf2 from the cytosol into the nucleus, leading to elevated HO-1 expression.	dhf	0-3	heme oxygenase 1	Homo sapiens	221-225
24610348-4	2014	The siNrf2 RNA-transfection attenuated HO-1 expression induced by DHF treatment.	dhf	66-69	heme oxygenase 1	Homo sapiens	39-43
24610348-5	2014	In addition, DHF induced the activation of extracellular signal-regulated kinase (ERK), while U0126 (a specific pharmacological inhibitor of ERK kinase) abrogated DHF-activated Nrf2 and HO-1 expression.	U 0126	94-99	heme oxygenase 1	Homo sapiens	186-190
24610348-6	2014	This suggests that DHF increased the levels of Nrf2 and HO-1 via ERK-dependent pathways.	dhf	19-22	heme oxygenase 1	Homo sapiens	56-60
24610348-8	2014	Taken together, these results demonstrate that DHF protected cells from oxidative stress via the activation of an ERK/Nrf2/HO-1 signaling pathway.	dhf	47-50	heme oxygenase 1	Homo sapiens	123-127
24415199-5	2014	Our study demonstrated that DMSO pretreatment showed a cytoprotective effect against H2 O2 -induced oxidative damage (impaired cell viability, increased apopototic cells rate and caspase-3 level, and increased release of LDH and CK) and this process is partially mediated by HO-1 upregulation.	Dimethyl Sulfoxide	28-32	heme oxygenase 1	Homo sapiens	275-279
24415199-0	2014	Dimethyl sulfoxide attenuates hydrogen peroxide-induced injury in cardiomyocytes via heme oxygenase-1.	Dimethyl Sulfoxide	0-18	heme oxygenase 1	Homo sapiens	85-101
24415199-5	2014	Our study demonstrated that DMSO pretreatment showed a cytoprotective effect against H2 O2 -induced oxidative damage (impaired cell viability, increased apopototic cells rate and caspase-3 level, and increased release of LDH and CK) and this process is partially mediated by HO-1 upregulation.	Hydrogen Peroxide	85-90	heme oxygenase 1	Homo sapiens	275-279
24415199-0	2014	Dimethyl sulfoxide attenuates hydrogen peroxide-induced injury in cardiomyocytes via heme oxygenase-1.	Hydrogen Peroxide	30-47	heme oxygenase 1	Homo sapiens	85-101
24415199-6	2014	Furthermore, our data showed that the activation of p38 MAPK and Nrf2 translocation are involved in the HO-1 upregulation induced by DMSO.	Dimethyl Sulfoxide	133-137	heme oxygenase 1	Homo sapiens	104-108
24415199-2	2014	Our former study showed that DMSO is able to induce heme oxygenase-1 (HO-1) expression in endothelial cells, which is a potent antioxidant enzyme.	Dimethyl Sulfoxide	29-33	heme oxygenase 1	Homo sapiens	52-68
24415199-7	2014	This study reports for the first time that the cytoprotective effect of DMSO in cardiomyocytes is partially mediated by HO-1, which may further explain the mechanisms by which DMSO exerts cardioprotection on H2 O2 injury.	Dimethyl Sulfoxide	72-76	heme oxygenase 1	Homo sapiens	120-124
24415199-2	2014	Our former study showed that DMSO is able to induce heme oxygenase-1 (HO-1) expression in endothelial cells, which is a potent antioxidant enzyme.	Dimethyl Sulfoxide	29-33	heme oxygenase 1	Homo sapiens	70-74
24415199-3	2014	In this study, we hypothesized that the antioxidant effects of DMSO in cardiomyocytes are mediated or partially mediated by increased HO-1 expression.	Dimethyl Sulfoxide	63-67	heme oxygenase 1	Homo sapiens	134-138
24415199-7	2014	This study reports for the first time that the cytoprotective effect of DMSO in cardiomyocytes is partially mediated by HO-1, which may further explain the mechanisms by which DMSO exerts cardioprotection on H2 O2 injury.	Dimethyl Sulfoxide	176-180	heme oxygenase 1	Homo sapiens	120-124
24415199-7	2014	This study reports for the first time that the cytoprotective effect of DMSO in cardiomyocytes is partially mediated by HO-1, which may further explain the mechanisms by which DMSO exerts cardioprotection on H2 O2 injury.	Hydrogen Peroxide	208-213	heme oxygenase 1	Homo sapiens	120-124
24500083-8	2014	Moreover, a regulatory role of ROS for HO-1 regulation in these cells is demonstrated by studies with the antioxidant N-acetylcysteine and exogenous hydrogenperoxide.	Reactive Oxygen Species	31-34	heme oxygenase 1	Homo sapiens	39-43
24413982-8	2014	Treatment with resveratrol and genipin up-regulated NQO1 and HMOX1 expression and reduced oxidative stress in patients" lymphoblastoid cells.	Resveratrol	15-26	heme oxygenase 1	Homo sapiens	61-66
24413982-8	2014	Treatment with resveratrol and genipin up-regulated NQO1 and HMOX1 expression and reduced oxidative stress in patients" lymphoblastoid cells.	genipin	31-38	heme oxygenase 1	Homo sapiens	61-66
24977002-1	2014	BACKGROUND: There is a reverse relationship between serum bilirubin level and incidence of stroke, heme oxygenase-1 (HO-1) can catalyze heme into bilirubin, it is unknown the association of HO-1 level with risk of stroke.	Heme	99-103	heme oxygenase 1	Homo sapiens	117-121
24977002-1	2014	BACKGROUND: There is a reverse relationship between serum bilirubin level and incidence of stroke, heme oxygenase-1 (HO-1) can catalyze heme into bilirubin, it is unknown the association of HO-1 level with risk of stroke.	Bilirubin	146-155	heme oxygenase 1	Homo sapiens	99-115
24977002-1	2014	BACKGROUND: There is a reverse relationship between serum bilirubin level and incidence of stroke, heme oxygenase-1 (HO-1) can catalyze heme into bilirubin, it is unknown the association of HO-1 level with risk of stroke.	Bilirubin	146-155	heme oxygenase 1	Homo sapiens	117-121
24412540-6	2014	Resveratrol decreases intracellular ROS production, most likely by mechanisms involving NMDA, AMPA/KA, intracellular Ca(2+) and the heme oxygenase 1 (HO1) pathway, and prevents mitochondrial dysfunction and impairments in Na(+)K(+)-ATPase and GS activity after glutamate activation.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	132-148
24412540-6	2014	Resveratrol decreases intracellular ROS production, most likely by mechanisms involving NMDA, AMPA/KA, intracellular Ca(2+) and the heme oxygenase 1 (HO1) pathway, and prevents mitochondrial dysfunction and impairments in Na(+)K(+)-ATPase and GS activity after glutamate activation.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	150-153
24412540-6	2014	Resveratrol decreases intracellular ROS production, most likely by mechanisms involving NMDA, AMPA/KA, intracellular Ca(2+) and the heme oxygenase 1 (HO1) pathway, and prevents mitochondrial dysfunction and impairments in Na(+)K(+)-ATPase and GS activity after glutamate activation.	Reactive Oxygen Species	36-39	heme oxygenase 1	Homo sapiens	132-148
24736402-3	2014	To improve early graft survival, hESC-CMs were pretreated with cobalt protoporphyrin (CoPP), a transcriptional activator of cytoprotective heme oxygenase-1 (HO-1).	cobaltiprotoporphyrin	63-84	heme oxygenase 1	Homo sapiens	139-155
24736402-3	2014	To improve early graft survival, hESC-CMs were pretreated with cobalt protoporphyrin (CoPP), a transcriptional activator of cytoprotective heme oxygenase-1 (HO-1).	cobaltiprotoporphyrin	63-84	heme oxygenase 1	Homo sapiens	157-161
24736402-3	2014	To improve early graft survival, hESC-CMs were pretreated with cobalt protoporphyrin (CoPP), a transcriptional activator of cytoprotective heme oxygenase-1 (HO-1).	cobaltiprotoporphyrin	86-90	heme oxygenase 1	Homo sapiens	139-155
24736402-3	2014	To improve early graft survival, hESC-CMs were pretreated with cobalt protoporphyrin (CoPP), a transcriptional activator of cytoprotective heme oxygenase-1 (HO-1).	cobaltiprotoporphyrin	86-90	heme oxygenase 1	Homo sapiens	157-161
24736402-5	2014	Compared with PBS-pretreated cells, CoPP-pretreated hESC-CM preparations exhibited higher levels of HO-1 expression, Akt phosphorylation, and vascular endothelial growth factor production, with reduced apoptosis, and a 30% decrease in intracellular reactive oxygen species.	cobaltiprotoporphyrin	36-40	heme oxygenase 1	Homo sapiens	100-104
24500083-8	2014	Moreover, a regulatory role of ROS for HO-1 regulation in these cells is demonstrated by studies with the antioxidant N-acetylcysteine and exogenous hydrogenperoxide.	Acetylcysteine	118-134	heme oxygenase 1	Homo sapiens	39-43
24500083-8	2014	Moreover, a regulatory role of ROS for HO-1 regulation in these cells is demonstrated by studies with the antioxidant N-acetylcysteine and exogenous hydrogenperoxide.	Hydrogen Peroxide	149-165	heme oxygenase 1	Homo sapiens	39-43
24801208-0	2014	Matrix conditions and KLF2-dependent induction of heme oxygenase-1 modulate inhibition of HCV replication by fluvastatin.	Fluvastatin	109-120	heme oxygenase 1	Homo sapiens	50-66
24622883-5	2014	DFO and PHEN downregulated Grp78, Grp94, and MRP1 expressions and upregulated CHOP and HO-1 expressions.	Deferoxamine	0-3	heme oxygenase 1	Homo sapiens	87-91
24622883-8	2014	We determined that the reduction of increased Grp78, Grp94, HO-1, and MRP1 expressions, which appears to inhibit the chemotherapeutic effect of TSA, through the combination with DFO or PHEN will contribute to the anticancer effect.	trichostatin A	144-147	heme oxygenase 1	Homo sapiens	60-64
24622883-8	2014	We determined that the reduction of increased Grp78, Grp94, HO-1, and MRP1 expressions, which appears to inhibit the chemotherapeutic effect of TSA, through the combination with DFO or PHEN will contribute to the anticancer effect.	Deferoxamine	178-181	heme oxygenase 1	Homo sapiens	60-64
24862399-8	2014	The Pearson correlation analysis showed that HO-1, HO-2, and HO activity were negatively associated with waist circumference (P&lt;.05), body mass index (P&lt;.05), triglycerides (P&lt;.05) and positively with HDL-C (P&lt;.05).	Triglycerides	165-178	heme oxygenase 1	Homo sapiens	45-49
24862399-13	2014	CONCLUSION: Alteration of serum triglycerides and HDL-C significantly impairs HO-1 and HO-2 levels in benign prostatic hyperplasia patients.	Triglycerides	32-45	heme oxygenase 1	Homo sapiens	78-82
24857917-0	2014	The cytoprotective effect of sulfuretin against tert-butyl hydroperoxide-induced hepatotoxicity through Nrf2/ARE and JNK/ERK MAPK-mediated heme oxygenase-1 expression.	sulfuretin	29-39	heme oxygenase 1	Homo sapiens	139-155
24857917-0	2014	The cytoprotective effect of sulfuretin against tert-butyl hydroperoxide-induced hepatotoxicity through Nrf2/ARE and JNK/ERK MAPK-mediated heme oxygenase-1 expression.	tert-Butylhydroperoxide	48-72	heme oxygenase 1	Homo sapiens	139-155
24832131-5	2014	Interestingly, during the initiation of lateral root primordia, IAA is a potent inducer of endogenous H 2S and CO, which is produced by L-cysteine desulfhydrase (LCD) and heme oxygenase-1 (HO-1), respectively.	indoleacetic acid	64-67	heme oxygenase 1	Homo sapiens	171-187
24832131-5	2014	Interestingly, during the initiation of lateral root primordia, IAA is a potent inducer of endogenous H 2S and CO, which is produced by L-cysteine desulfhydrase (LCD) and heme oxygenase-1 (HO-1), respectively.	indoleacetic acid	64-67	heme oxygenase 1	Homo sapiens	189-193
24832131-5	2014	Interestingly, during the initiation of lateral root primordia, IAA is a potent inducer of endogenous H 2S and CO, which is produced by L-cysteine desulfhydrase (LCD) and heme oxygenase-1 (HO-1), respectively.	Hydrogen Sulfide	102-106	heme oxygenase 1	Homo sapiens	171-187
24832131-5	2014	Interestingly, during the initiation of lateral root primordia, IAA is a potent inducer of endogenous H 2S and CO, which is produced by L-cysteine desulfhydrase (LCD) and heme oxygenase-1 (HO-1), respectively.	Hydrogen Sulfide	102-106	heme oxygenase 1	Homo sapiens	189-193
24832131-5	2014	Interestingly, during the initiation of lateral root primordia, IAA is a potent inducer of endogenous H 2S and CO, which is produced by L-cysteine desulfhydrase (LCD) and heme oxygenase-1 (HO-1), respectively.	Carbon Monoxide	111-113	heme oxygenase 1	Homo sapiens	171-187
24832131-5	2014	Interestingly, during the initiation of lateral root primordia, IAA is a potent inducer of endogenous H 2S and CO, which is produced by L-cysteine desulfhydrase (LCD) and heme oxygenase-1 (HO-1), respectively.	Carbon Monoxide	111-113	heme oxygenase 1	Homo sapiens	189-193
24622883-8	2014	We determined that the reduction of increased Grp78, Grp94, HO-1, and MRP1 expressions, which appears to inhibit the chemotherapeutic effect of TSA, through the combination with DFO or PHEN will contribute to the anticancer effect.	Phenanthrolines	185-189	heme oxygenase 1	Homo sapiens	60-64
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Curcumin	12-20	heme oxygenase 1	Homo sapiens	47-63
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Curcumin	12-20	heme oxygenase 1	Homo sapiens	65-69
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Hemin	26-31	heme oxygenase 1	Homo sapiens	47-63
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Hemin	26-31	heme oxygenase 1	Homo sapiens	65-69
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Porphyrins	123-132	heme oxygenase 1	Homo sapiens	47-63
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Porphyrins	123-132	heme oxygenase 1	Homo sapiens	65-69
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Chlorophyll	137-148	heme oxygenase 1	Homo sapiens	47-63
24830678-7	2014	We compared curcumin with hemin, an agonist of heme oxygenase-1 (HO-1), which significantly affects only one KEGG pathway, porphyrin and chlorophyll metabolism (adjusted p = 1.5x10-5).	Chlorophyll	137-148	heme oxygenase 1	Homo sapiens	65-69
24830678-10	2014	Selective inhibition of HO-1 completely blocked the action of hemin but not that of curcumin, suggesting simultaneous multi-pathway intervention by curcumin.	Curcumin	148-156	heme oxygenase 1	Homo sapiens	24-28
24819505-4	2014	Overexpression of Nrf2 or HO-1 resulted in upregulation of TP in NCI-H292 cells, an effect mimicked by treatment with an antioxidant N-acetylcysteine and partially reversed by HO-1 knockdown.	Acetylcysteine	133-149	heme oxygenase 1	Homo sapiens	26-30
24553299-8	2014	Using an in vitro model, we found that HO-1 induction, using cobalt protoporphyrin, stimulates cytotrophoblast beta-ENaC expression by 1.5- and 1.8-fold (10 and 50 muM).	cobaltiprotoporphyrin	61-82	heme oxygenase 1	Homo sapiens	39-43
24413553-2	2014	In addition to increased thrombin generation via tumor release of tissue factor-bearing microparticles and hyperfibrinogenemia, brain tumors and surrounding normal brain likely generate endogenous carbon monoxide (CO) via the hemeoxygenase-1 (HO-1) system.	Carbon Monoxide	197-212	heme oxygenase 1	Homo sapiens	226-247
24413553-2	2014	In addition to increased thrombin generation via tumor release of tissue factor-bearing microparticles and hyperfibrinogenemia, brain tumors and surrounding normal brain likely generate endogenous carbon monoxide (CO) via the hemeoxygenase-1 (HO-1) system.	Carbon Monoxide	214-216	heme oxygenase 1	Homo sapiens	226-247
24180257-7	2014	Further, heme is an important component of a number of metabolic enzymes, and, therefore, HO-1 plays an important role in the modulation of cellular bioenergetics.	Heme	9-13	heme oxygenase 1	Homo sapiens	90-94
24743738-8	2014	The siRNA- or shRNA-mediated knockdown of Nrf2 or HO-1 significantly suppressed cancer cell viability and tumor growth in vitro and in vivo, resulting in enhanced 5-FU sensitivity.	Fluorouracil	163-167	heme oxygenase 1	Homo sapiens	50-54
24743738-12	2014	These results suggested that the mechanism underlying the acquisition of 5-FU resistance in CRC involves the upregulation of Nrf2 and HO-1 expression via epigenetic modifications of DNA demethylation.	Fluorouracil	73-77	heme oxygenase 1	Homo sapiens	134-138
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Heme	47-51	heme oxygenase 1	Homo sapiens	14-30
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Heme	47-51	heme oxygenase 1	Homo sapiens	32-36
24583029-3	2014	Hemin, a commercial preparation of heme, is used as an iron donor or heme oxygenase 1 (HO-1) inducer, and has been shown to provide antiviral activity in many studies.	Hemin	0-5	heme oxygenase 1	Homo sapiens	69-85
24583029-3	2014	Hemin, a commercial preparation of heme, is used as an iron donor or heme oxygenase 1 (HO-1) inducer, and has been shown to provide antiviral activity in many studies.	Hemin	0-5	heme oxygenase 1	Homo sapiens	87-91
24583029-7	2014	In addition, after treatment with Protoporphyrin IX zinc (II) (ZnPP) or Sn (IV) Protoporphyrin IX dichloride (SnPP), inhibitors of HO-1, the inhibition of viral replication by hemin was partially reversed.	protoporphyrin ix dichloride	80-108	heme oxygenase 1	Homo sapiens	131-135
24553817-0	2014	Maslinic acid protects vascular smooth muscle cells from oxidative stress through Akt/Nrf2/HO-1 pathway.	maslinic acid	0-13	heme oxygenase 1	Homo sapiens	91-95
24553817-5	2014	Wortmannin suppression of Akt was able to abolish HO-1 upregulation in VSMCs, suggesting the requirement of Akt activation for MA effect on HO-1.	Wortmannin	0-10	heme oxygenase 1	Homo sapiens	50-54
24553817-5	2014	Wortmannin suppression of Akt was able to abolish HO-1 upregulation in VSMCs, suggesting the requirement of Akt activation for MA effect on HO-1.	Wortmannin	0-10	heme oxygenase 1	Homo sapiens	140-144
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Biliverdine	55-65	heme oxygenase 1	Homo sapiens	14-30
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Biliverdine	55-65	heme oxygenase 1	Homo sapiens	32-36
24180287-7	2014	Moreover, the potential for heme catabolism end products, such as carbon monoxide, to amplify the HMOX1 stress response should be considered.	Carbon Monoxide	66-81	heme oxygenase 1	Homo sapiens	98-103
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Carbon Monoxide	67-82	heme oxygenase 1	Homo sapiens	14-30
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Carbon Monoxide	67-82	heme oxygenase 1	Homo sapiens	32-36
24180608-1	2014	SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin.	Heme	112-116	heme oxygenase 1	Homo sapiens	88-92
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	ammonium ferrous sulfate	88-95	heme oxygenase 1	Homo sapiens	14-30
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	ammonium ferrous sulfate	88-95	heme oxygenase 1	Homo sapiens	32-36
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Heme	144-148	heme oxygenase 1	Homo sapiens	14-30
24180608-1	2014	SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	88-92
24053682-1	2014	SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism.	Heme	144-148	heme oxygenase 1	Homo sapiens	32-36
24053682-2	2014	HO-1 via heme removal and degradation products acts as a cytoprotective, anti-inflammatory, immunomodulatory, and proangiogenic protein, regulating also a cell cycle.	Heme	9-13	heme oxygenase 1	Homo sapiens	0-4
24180608-1	2014	SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin.	Carbon Monoxide	137-139	heme oxygenase 1	Homo sapiens	88-92
24180608-1	2014	SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin.	Biliverdine	162-172	heme oxygenase 1	Homo sapiens	88-92
24124891-5	2014	While heme catabolism by heme oxygenase-1 (HO-1) prevents programmed cell death, this cytoprotective effect requires the co-expression of ferritin H (heart/heavy) chain (FTH), which controls the pro-oxidant effect of labile Fe released from the protoporphyrin IX ring of heme.	Heme	6-10	heme oxygenase 1	Homo sapiens	25-41
24131232-1	2014	SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Heme	90-94	heme oxygenase 1	Homo sapiens	31-35
24131232-1	2014	SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	100-115	heme oxygenase 1	Homo sapiens	31-35
24131232-1	2014	SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	117-119	heme oxygenase 1	Homo sapiens	31-35
24131232-1	2014	SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Iron	122-126	heme oxygenase 1	Homo sapiens	31-35
24131232-1	2014	SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Biliverdine	132-142	heme oxygenase 1	Homo sapiens	31-35
24131232-1	2014	SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Bilirubin	179-188	heme oxygenase 1	Homo sapiens	31-35
24131232-5	2014	Moreover, therapeutic delivery of HO-1 products CO, biliverdin, and bilirubin has been shown to have favorable effects, notably on endothelial cells and in animal models of vascular disease.	Biliverdine	52-62	heme oxygenase 1	Homo sapiens	34-38
24131232-5	2014	Moreover, therapeutic delivery of HO-1 products CO, biliverdin, and bilirubin has been shown to have favorable effects, notably on endothelial cells and in animal models of vascular disease.	Bilirubin	68-77	heme oxygenase 1	Homo sapiens	34-38
24341409-1	2014	Not only double, Janus face, but numerous appearances characterize heme oxygenase-1 (HO-1), an inducible enzyme which main role is to degrade heme.	Heme	67-71	heme oxygenase 1	Homo sapiens	85-89
24147608-6	2014	The importance of HO-1 in MP is emphasized by their expression of specific receptors that primarily function to ingest heme-containing substrate and deliver it to HO-1.	Heme	119-123	heme oxygenase 1	Homo sapiens	18-22
24413389-0	2014	Crucial role of heme oxygenase-1 in the sensitivity of acute myeloid leukemia cell line Kasumi-1 to ursolic acid.	ursolic acid	100-112	heme oxygenase 1	Homo sapiens	16-32
24700716-2	2014	They focus on a key enzyme involved in heme catabolism, heme oxygenase 1 (HO-1), which, ironically, has been poorly investigated in erythroid cells, the largest pool of heme-containing cells.	Heme	39-43	heme oxygenase 1	Homo sapiens	56-72
24700716-2	2014	They focus on a key enzyme involved in heme catabolism, heme oxygenase 1 (HO-1), which, ironically, has been poorly investigated in erythroid cells, the largest pool of heme-containing cells.	Heme	39-43	heme oxygenase 1	Homo sapiens	74-78
24413389-4	2014	HO-1 in Kasumi-1 cells was upregulated by being treated with low-dose rather than high-dose UA.	ursolic acid	92-94	heme oxygenase 1	Homo sapiens	0-4
24413389-5	2014	Inhibition of HO-1 by zinc protoporphyrin (ZnPP) IX sensitized Kasumi-1 cells to UA, and the apoptotic rate was close to that induced by Ara-C (P&lt;0.01).	zinc protoporphyrin	22-41	heme oxygenase 1	Homo sapiens	14-18
24413389-5	2014	Inhibition of HO-1 by zinc protoporphyrin (ZnPP) IX sensitized Kasumi-1 cells to UA, and the apoptotic rate was close to that induced by Ara-C (P&lt;0.01).	zinc protoporphyrin	43-47	heme oxygenase 1	Homo sapiens	14-18
24413389-5	2014	Inhibition of HO-1 by zinc protoporphyrin (ZnPP) IX sensitized Kasumi-1 cells to UA, and the apoptotic rate was close to that induced by Ara-C (P&lt;0.01).	ursolic acid	81-83	heme oxygenase 1	Homo sapiens	14-18
24413389-7	2014	After silencing HO-1 by siRNA transfection with lentivirus, the cells" proliferation induced by UA was increased as it was by Ara-C.	ursolic acid	96-98	heme oxygenase 1	Homo sapiens	16-20
24413389-7	2014	After silencing HO-1 by siRNA transfection with lentivirus, the cells" proliferation induced by UA was increased as it was by Ara-C.	Cytarabine	126-131	heme oxygenase 1	Homo sapiens	16-20
24413389-10	2014	AML-M2 can feasibly be treated by target-inhibiting HO-1 that enhances the antileukemia effects of UA in vitro and in vivo.	ursolic acid	99-101	heme oxygenase 1	Homo sapiens	52-56
24503931-0	2014	7,8-Dihydroxyflavone protects human keratinocytes against oxidative stress-induced cell damage via the ERK and PI3K/Akt-mediated Nrf2/HO-1 signaling pathways.	6,7-dihydroxyflavone	0-20	heme oxygenase 1	Homo sapiens	134-138
24847330-3	2014	HO-1 degrades heme but increases in experimental models of AKI.	Heme	14-18	heme oxygenase 1	Homo sapiens	0-4
24588654-6	2014	Moreover, treatment of NHEKs with Z-Ligustilide increased reactive oxygen species (ROS) and L-N-acetylcysteine (L-NAC, an antioxidant) attenuated Z-ligustilide-induced Nrf2 nuclear translocation and HO-1 expression.	ligustilide	34-47	heme oxygenase 1	Homo sapiens	199-203
24588654-6	2014	Moreover, treatment of NHEKs with Z-Ligustilide increased reactive oxygen species (ROS) and L-N-acetylcysteine (L-NAC, an antioxidant) attenuated Z-ligustilide-induced Nrf2 nuclear translocation and HO-1 expression.	Acetylcysteine	92-110	heme oxygenase 1	Homo sapiens	199-203
24588654-6	2014	Moreover, treatment of NHEKs with Z-Ligustilide increased reactive oxygen species (ROS) and L-N-acetylcysteine (L-NAC, an antioxidant) attenuated Z-ligustilide-induced Nrf2 nuclear translocation and HO-1 expression.	Acetylcysteine	112-117	heme oxygenase 1	Homo sapiens	199-203
24588654-6	2014	Moreover, treatment of NHEKs with Z-Ligustilide increased reactive oxygen species (ROS) and L-N-acetylcysteine (L-NAC, an antioxidant) attenuated Z-ligustilide-induced Nrf2 nuclear translocation and HO-1 expression.	ligustilide	146-159	heme oxygenase 1	Homo sapiens	199-203
24380881-0	2014	HO-1 up-regulation: a key point in high-risk neuroblastoma resistance to bortezomib.	Bortezomib	73-83	heme oxygenase 1	Homo sapiens	0-4
24380881-3	2014	We have shown that MYCN amplified HTLA-230 cells were slightly sensitive to BTZ treatment, due to the activation of Nrf2 that led to an impressive up-regulation of HO-1.	Bortezomib	76-79	heme oxygenase 1	Homo sapiens	164-168
24380881-5	2014	The inhibition of HO-1 activity obtained by Zinc (II) protoprophyrin IX (ZnPPIX) was able to significantly increase the pro-apoptotic effect of BTZ in a p53- and p21-independent way.	zinc (ii) protoprophyrin ix	44-71	heme oxygenase 1	Homo sapiens	18-22
24380881-5	2014	The inhibition of HO-1 activity obtained by Zinc (II) protoprophyrin IX (ZnPPIX) was able to significantly increase the pro-apoptotic effect of BTZ in a p53- and p21-independent way.	zinc protoporphyrin	73-79	heme oxygenase 1	Homo sapiens	18-22
24380881-5	2014	The inhibition of HO-1 activity obtained by Zinc (II) protoprophyrin IX (ZnPPIX) was able to significantly increase the pro-apoptotic effect of BTZ in a p53- and p21-independent way.	Bortezomib	144-147	heme oxygenase 1	Homo sapiens	18-22
24486344-0	2014	Salvianolic acid A protects RPE cells against oxidative stress through activation of Nrf2/HO-1 signaling.	salvianolic acid A	0-18	heme oxygenase 1	Homo sapiens	90-94
24486344-7	2014	Both Nrf2 and HO-1 were required for Sal A-mediated cytoprotective effect, as Nrf2/HO-1 inhibition abolished Sal A-induced beneficial effects against H2O2.	salvianolic acid A	37-42	heme oxygenase 1	Homo sapiens	14-18
24486344-7	2014	Both Nrf2 and HO-1 were required for Sal A-mediated cytoprotective effect, as Nrf2/HO-1 inhibition abolished Sal A-induced beneficial effects against H2O2.	salvianolic acid A	37-42	heme oxygenase 1	Homo sapiens	83-87
24486344-7	2014	Both Nrf2 and HO-1 were required for Sal A-mediated cytoprotective effect, as Nrf2/HO-1 inhibition abolished Sal A-induced beneficial effects against H2O2.	salvianolic acid A	109-114	heme oxygenase 1	Homo sapiens	83-87
24486344-7	2014	Both Nrf2 and HO-1 were required for Sal A-mediated cytoprotective effect, as Nrf2/HO-1 inhibition abolished Sal A-induced beneficial effects against H2O2.	Hydrogen Peroxide	150-154	heme oxygenase 1	Homo sapiens	83-87
24486344-8	2014	Meanwhile, the PI3K/Akt/mTORC1 chemical inhibitors not only suppressed Sal A-induced Nrf2/HO-1 activation, but also eliminated its cytoprotective effect in RPE cells.	salvianolic acid A	71-76	heme oxygenase 1	Homo sapiens	90-94
24486344-9	2014	These observations suggest that Sal A activates the Nrf2/HO-1 axis in RPE cells and protects against oxidative stress via activation of Akt/mTORC1 signaling.	salvianolic acid A	32-37	heme oxygenase 1	Homo sapiens	57-61
24503931-7	2014	Taken together, the results suggested that DHF activates ERK- and Akt-Nrf2 signaling cascades in HaCaT cells, leading to the upregulation of HO-1 and cytoprotection against oxidative stress.	6,7-dihydroxyflavone	43-46	heme oxygenase 1	Homo sapiens	141-145
24503931-1	2014	This study investigated the effect of 7,8-dihydroxyflavone (DHF) on the expression and activity of heme oxygenase-1 (HO-1), an enzyme with potent antioxidant properties, as well as the molecular mechanisms involved.	6,7-dihydroxyflavone	38-58	heme oxygenase 1	Homo sapiens	99-115
24503931-1	2014	This study investigated the effect of 7,8-dihydroxyflavone (DHF) on the expression and activity of heme oxygenase-1 (HO-1), an enzyme with potent antioxidant properties, as well as the molecular mechanisms involved.	6,7-dihydroxyflavone	38-58	heme oxygenase 1	Homo sapiens	117-121
24503931-1	2014	This study investigated the effect of 7,8-dihydroxyflavone (DHF) on the expression and activity of heme oxygenase-1 (HO-1), an enzyme with potent antioxidant properties, as well as the molecular mechanisms involved.	6,7-dihydroxyflavone	60-63	heme oxygenase 1	Homo sapiens	99-115
24503931-1	2014	This study investigated the effect of 7,8-dihydroxyflavone (DHF) on the expression and activity of heme oxygenase-1 (HO-1), an enzyme with potent antioxidant properties, as well as the molecular mechanisms involved.	6,7-dihydroxyflavone	60-63	heme oxygenase 1	Homo sapiens	117-121
24503931-2	2014	DHF markedly upregulated HO-1 mRNA and protein expression in human keratinocytes (HaCaT cells), resulting in increased HO-1 activity.	6,7-dihydroxyflavone	0-3	heme oxygenase 1	Homo sapiens	25-29
24503931-2	2014	DHF markedly upregulated HO-1 mRNA and protein expression in human keratinocytes (HaCaT cells), resulting in increased HO-1 activity.	6,7-dihydroxyflavone	0-3	heme oxygenase 1	Homo sapiens	119-123
24503931-3	2014	DHF also increased the protein level of transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2), which regulates HO-1 expression by binding to the antioxidant response element (ARE) within the HO-1 gene promoter, in a time-dependent manner.	6,7-dihydroxyflavone	0-3	heme oxygenase 1	Homo sapiens	129-133
24503931-3	2014	DHF also increased the protein level of transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2), which regulates HO-1 expression by binding to the antioxidant response element (ARE) within the HO-1 gene promoter, in a time-dependent manner.	6,7-dihydroxyflavone	0-3	heme oxygenase 1	Homo sapiens	209-213
24503931-5	2014	DHF activated extracellular-regulated kinase (ERK) and protein kinase B (PKB, Akt) in keratinocytes, while the ERK and Akt inhibitors attenuated DHF-enhanced Nrf2 and HO-1 expression.	6,7-dihydroxyflavone	145-148	heme oxygenase 1	Homo sapiens	167-171
24503931-6	2014	DHF also protected the keratinocytes against hydrogen peroxide- and ultraviolet B-induced oxidative damage, while HO-1, ERK and Akt inhibitors markedly suppressed DHF-mediated cytoprotection.	6,7-dihydroxyflavone	163-166	heme oxygenase 1	Homo sapiens	114-118
25371888-5	2014	qRT-PCR and Western blot analyses showed that diazoxide up-regulated the heme oxygenase-1 (HO-1) expression.	Diazoxide	46-55	heme oxygenase 1	Homo sapiens	73-89
25371888-5	2014	qRT-PCR and Western blot analyses showed that diazoxide up-regulated the heme oxygenase-1 (HO-1) expression.	Diazoxide	46-55	heme oxygenase 1	Homo sapiens	91-95
25371888-8	2014	CONCLUSION: These results, taken together, strongly suggest that up-regulation of the HO-1 expression is the crucial mechanism responsible for the diazoxide-induced inhibition of the sFlt-1 release and ROS production under hypoxia.	Reactive Oxygen Species	202-205	heme oxygenase 1	Homo sapiens	86-90
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	cobaltiprotoporphyrin	30-51	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	cobaltiprotoporphyrin	53-57	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Bilirubin	93-102	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Bilirubin	93-102	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Diazoxide	112-121	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Diazoxide	112-121	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Diazoxide	112-121	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Reactive Oxygen Species	152-175	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Reactive Oxygen Species	152-175	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Reactive Oxygen Species	152-175	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Reactive Oxygen Species	177-180	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Reactive Oxygen Species	177-180	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Reactive Oxygen Species	177-180	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	zinc protoporphyrin	235-257	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	zinc protoporphyrin	235-257	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	zinc protoporphyrin	235-257	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	zinc protoporphyrin	259-266	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	zinc protoporphyrin	259-266	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	zinc protoporphyrin	259-266	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Diazoxide	294-303	heme oxygenase 1	Homo sapiens	17-21
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Diazoxide	294-303	heme oxygenase 1	Homo sapiens	88-92
25371888-6	2014	In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide.	Diazoxide	294-303	heme oxygenase 1	Homo sapiens	88-92
25371888-8	2014	CONCLUSION: These results, taken together, strongly suggest that up-regulation of the HO-1 expression is the crucial mechanism responsible for the diazoxide-induced inhibition of the sFlt-1 release and ROS production under hypoxia.	Diazoxide	147-156	heme oxygenase 1	Homo sapiens	86-90
24399465-7	2014	TQ treatments caused increased levels of reactive oxygen species (ROS) and mRNAs of oxidative stress-related genes, NQO1 and HO-1.	thymoquinone	0-2	heme oxygenase 1	Homo sapiens	125-129
24633012-1	2014	Haem oxygenase (HO)-1/carbon monoxide (CO) protects cancer cells from oxidative stress, but the gas-responsive signalling mechanisms remain unknown.	Cobalt	39-41	heme oxygenase 1	Homo sapiens	0-21
24681888-5	2014	Heme inhibits the transcriptional repressor activity of Bach1, resulting in the derepression of its target genes, such as globin in erythroid cells and heme oxygenase-1 in diverse cell types.	Heme	0-4	heme oxygenase 1	Homo sapiens	152-168
24651442-0	2014	Heme oxygenase-1 derived carbon monoxide permits maturation of myeloid cells.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
24690955-2	2014	Bilirubin is produced by heme oxygenase-1 (HO-1), catalyzed by UDP-glucuronosyltransferase (UGT1A1), and has potential as an antioxidant.	Bilirubin	0-9	heme oxygenase 1	Homo sapiens	25-41
24690955-2	2014	Bilirubin is produced by heme oxygenase-1 (HO-1), catalyzed by UDP-glucuronosyltransferase (UGT1A1), and has potential as an antioxidant.	Bilirubin	0-9	heme oxygenase 1	Homo sapiens	43-47
24355171-9	2014	TQ also generated reactive oxygen species (ROS) and pretreatment with N-acetyl cysteine (NAC) abrogated TQ-induced ROS accumulation, Akt and AMPKalpha activation, Nrf2 nuclear localization, the ARE-luciferase activity, and HO-1 expression in HaCaT cells.	Acetylcysteine	70-87	heme oxygenase 1	Homo sapiens	223-227
24681707-5	2014	Two Hsp32-targeting drugs, pegylated zinc protoporphyrine (PEG-ZnPP) and styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP), induced apoptosis and growth arrest in the BCR/ABL1+ cell lines, in Ph- lymphoblastic cell lines and in primary Ph+ and Ph- ALL cells.	zinc protoporphyrine	37-57	heme oxygenase 1	Homo sapiens	4-9
24681707-5	2014	Two Hsp32-targeting drugs, pegylated zinc protoporphyrine (PEG-ZnPP) and styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP), induced apoptosis and growth arrest in the BCR/ABL1+ cell lines, in Ph- lymphoblastic cell lines and in primary Ph+ and Ph- ALL cells.	peg-znpp	59-67	heme oxygenase 1	Homo sapiens	4-9
24681707-5	2014	Two Hsp32-targeting drugs, pegylated zinc protoporphyrine (PEG-ZnPP) and styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP), induced apoptosis and growth arrest in the BCR/ABL1+ cell lines, in Ph- lymphoblastic cell lines and in primary Ph+ and Ph- ALL cells.	2-Butenedioic acid (2Z)-, polymer with ethenylbenzene	73-92	heme oxygenase 1	Homo sapiens	4-9
24681707-5	2014	Two Hsp32-targeting drugs, pegylated zinc protoporphyrine (PEG-ZnPP) and styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP), induced apoptosis and growth arrest in the BCR/ABL1+ cell lines, in Ph- lymphoblastic cell lines and in primary Ph+ and Ph- ALL cells.	zinc protoporphyrin	63-67	heme oxygenase 1	Homo sapiens	4-9
24681707-5	2014	Two Hsp32-targeting drugs, pegylated zinc protoporphyrine (PEG-ZnPP) and styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP), induced apoptosis and growth arrest in the BCR/ABL1+ cell lines, in Ph- lymphoblastic cell lines and in primary Ph+ and Ph- ALL cells.	sma-znpp	120-128	heme oxygenase 1	Homo sapiens	4-9
24681707-7	2014	In Ph+ ALL, major growth-inhibitory effects of the Hsp32-targeting drugs were observed in imatinib-sensitive and imatinib-resistant cells.	Imatinib Mesylate	90-98	heme oxygenase 1	Homo sapiens	51-56
24681707-7	2014	In Ph+ ALL, major growth-inhibitory effects of the Hsp32-targeting drugs were observed in imatinib-sensitive and imatinib-resistant cells.	Imatinib Mesylate	113-121	heme oxygenase 1	Homo sapiens	51-56
24681707-8	2014	Hsp32-targeting drugs were found to synergize with imatinib, nilotinib, and bendamustine in producing growth inhibition and apoptosis in Ph+ ALL cells.	Imatinib Mesylate	51-59	heme oxygenase 1	Homo sapiens	0-5
24681707-8	2014	Hsp32-targeting drugs were found to synergize with imatinib, nilotinib, and bendamustine in producing growth inhibition and apoptosis in Ph+ ALL cells.	nilotinib	61-70	heme oxygenase 1	Homo sapiens	0-5
24681707-8	2014	Hsp32-targeting drugs were found to synergize with imatinib, nilotinib, and bendamustine in producing growth inhibition and apoptosis in Ph+ ALL cells.	Bendamustine Hydrochloride	76-88	heme oxygenase 1	Homo sapiens	0-5
24681707-9	2014	A siRNA against Hsp32 was found to inhibit growth and survival of ALL cells and to synergize with imatinib in suppressing the growth of ALL cells.	Imatinib Mesylate	98-106	heme oxygenase 1	Homo sapiens	16-21
24355171-0	2014	Thymoquinone induces heme oxygenase-1 expression in HaCaT cells via Nrf2/ARE activation: Akt and AMPKalpha as upstream targets.	thymoquinone	0-12	heme oxygenase 1	Homo sapiens	21-37
24355171-9	2014	TQ also generated reactive oxygen species (ROS) and pretreatment with N-acetyl cysteine (NAC) abrogated TQ-induced ROS accumulation, Akt and AMPKalpha activation, Nrf2 nuclear localization, the ARE-luciferase activity, and HO-1 expression in HaCaT cells.	thymoquinone	0-2	heme oxygenase 1	Homo sapiens	223-227
24659985-2	2014	The expression of the heme catabolizing enzyme encoded by this gene, namely HO-1, is required to successfully support reproductive events.	Heme	22-26	heme oxygenase 1	Homo sapiens	76-80
24659985-9	2014	In vitro, HO-1 protein levels in AN3 cells augmented after the addition of physiological concentrations of progesterone and estradiol, which confirmed our in vivo observations.	Progesterone	107-119	heme oxygenase 1	Homo sapiens	10-14
24659985-9	2014	In vitro, HO-1 protein levels in AN3 cells augmented after the addition of physiological concentrations of progesterone and estradiol, which confirmed our in vivo observations.	Estradiol	124-133	heme oxygenase 1	Homo sapiens	10-14
24355171-9	2014	TQ also generated reactive oxygen species (ROS) and pretreatment with N-acetyl cysteine (NAC) abrogated TQ-induced ROS accumulation, Akt and AMPKalpha activation, Nrf2 nuclear localization, the ARE-luciferase activity, and HO-1 expression in HaCaT cells.	Acetylcysteine	89-92	heme oxygenase 1	Homo sapiens	223-227
24365205-8	2014	HO-1 increased autophagy, and HO-1 reduced I/R-induced calcium overload in hepatocytes and prevented calpain 2 activation both in vivo and in vitro.	Calcium	55-62	heme oxygenase 1	Homo sapiens	30-34
24355171-9	2014	TQ also generated reactive oxygen species (ROS) and pretreatment with N-acetyl cysteine (NAC) abrogated TQ-induced ROS accumulation, Akt and AMPKalpha activation, Nrf2 nuclear localization, the ARE-luciferase activity, and HO-1 expression in HaCaT cells.	thymoquinone	104-106	heme oxygenase 1	Homo sapiens	223-227
24355171-10	2014	Taken together, TQ induces HO-1 expression in HaCaT cells by activating Nrf2 through ROS-mediated phosphorylation of Akt and AMPKalpha.	Reactive Oxygen Species	85-88	heme oxygenase 1	Homo sapiens	27-31
24407487-4	2014	The (GT)n and (TA)n dinucleotide variations in heme oxygenase 1 (HMOX1) and bilirubin UDP-glucuronosyl transferase (UGT1A1) gene promoters were determined by fragment analysis.	Dinucleoside Phosphates	20-32	heme oxygenase 1	Homo sapiens	47-63
24637794-1	2014	Heme oxygenase-1 (HO-1) and its enzymatic by-product carbon monoxide (CO) have emerged as important regulators of acute and chronic inflammation.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	0-16
24637794-1	2014	Heme oxygenase-1 (HO-1) and its enzymatic by-product carbon monoxide (CO) have emerged as important regulators of acute and chronic inflammation.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	18-22
24637794-1	2014	Heme oxygenase-1 (HO-1) and its enzymatic by-product carbon monoxide (CO) have emerged as important regulators of acute and chronic inflammation.	Carbon Monoxide	70-72	heme oxygenase 1	Homo sapiens	0-16
24637794-1	2014	Heme oxygenase-1 (HO-1) and its enzymatic by-product carbon monoxide (CO) have emerged as important regulators of acute and chronic inflammation.	Carbon Monoxide	70-72	heme oxygenase 1	Homo sapiens	18-22
24407487-4	2014	The (GT)n and (TA)n dinucleotide variations in heme oxygenase 1 (HMOX1) and bilirubin UDP-glucuronosyl transferase (UGT1A1) gene promoters were determined by fragment analysis.	Dinucleoside Phosphates	20-32	heme oxygenase 1	Homo sapiens	65-70
23972718-4	2014	On the vascular side, the upregulation of carbon monoxide CO, metabolite of heme oxygenase-1 (HO-1; by inhibiting soluble Flt-1, SFlt-1, and soluble endoglin, SEng, release), explains the very promising protective and potentially therapeutic effect of pravastatin in preeclampsia and the paradoxical strong protective effect of cigarette smoking on preeclampsia.	Carbon Monoxide	42-57	heme oxygenase 1	Homo sapiens	76-92
23972718-4	2014	On the vascular side, the upregulation of carbon monoxide CO, metabolite of heme oxygenase-1 (HO-1; by inhibiting soluble Flt-1, SFlt-1, and soluble endoglin, SEng, release), explains the very promising protective and potentially therapeutic effect of pravastatin in preeclampsia and the paradoxical strong protective effect of cigarette smoking on preeclampsia.	Carbon Monoxide	42-57	heme oxygenase 1	Homo sapiens	94-98
23972718-4	2014	On the vascular side, the upregulation of carbon monoxide CO, metabolite of heme oxygenase-1 (HO-1; by inhibiting soluble Flt-1, SFlt-1, and soluble endoglin, SEng, release), explains the very promising protective and potentially therapeutic effect of pravastatin in preeclampsia and the paradoxical strong protective effect of cigarette smoking on preeclampsia.	Carbon Monoxide	58-60	heme oxygenase 1	Homo sapiens	76-92
23972718-4	2014	On the vascular side, the upregulation of carbon monoxide CO, metabolite of heme oxygenase-1 (HO-1; by inhibiting soluble Flt-1, SFlt-1, and soluble endoglin, SEng, release), explains the very promising protective and potentially therapeutic effect of pravastatin in preeclampsia and the paradoxical strong protective effect of cigarette smoking on preeclampsia.	Carbon Monoxide	58-60	heme oxygenase 1	Homo sapiens	94-98
23972718-4	2014	On the vascular side, the upregulation of carbon monoxide CO, metabolite of heme oxygenase-1 (HO-1; by inhibiting soluble Flt-1, SFlt-1, and soluble endoglin, SEng, release), explains the very promising protective and potentially therapeutic effect of pravastatin in preeclampsia and the paradoxical strong protective effect of cigarette smoking on preeclampsia.	Pravastatin	252-263	heme oxygenase 1	Homo sapiens	76-92
23972718-4	2014	On the vascular side, the upregulation of carbon monoxide CO, metabolite of heme oxygenase-1 (HO-1; by inhibiting soluble Flt-1, SFlt-1, and soluble endoglin, SEng, release), explains the very promising protective and potentially therapeutic effect of pravastatin in preeclampsia and the paradoxical strong protective effect of cigarette smoking on preeclampsia.	Pravastatin	252-263	heme oxygenase 1	Homo sapiens	94-98
24642709-0	2014	Capsaicin ameliorates cisplatin-induced renal injury through induction of heme oxygenase-1.	Capsaicin	0-9	heme oxygenase 1	Homo sapiens	74-90
24642709-0	2014	Capsaicin ameliorates cisplatin-induced renal injury through induction of heme oxygenase-1.	Cisplatin	22-31	heme oxygenase 1	Homo sapiens	74-90
24642709-4	2014	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in the heme metabolism, has been implicated in a various cellular processes, such as inflammatory injury and anti-oxidant/oxidant homeostasis.	Heme	57-61	heme oxygenase 1	Homo sapiens	0-16
24642709-4	2014	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in the heme metabolism, has been implicated in a various cellular processes, such as inflammatory injury and anti-oxidant/oxidant homeostasis.	Heme	57-61	heme oxygenase 1	Homo sapiens	18-22
24642709-9	2014	We also found that capsaicin induces HO-1 expression in kidney tissues and HK-2 cells.	Capsaicin	19-28	heme oxygenase 1	Homo sapiens	37-41
24642709-10	2014	Notably, the protective effects of capsaicin were completely abrogated by treatment with either the HO inhibitor ZnPP IX or HO-1 knockdown in HK-2 cells.	Capsaicin	35-44	heme oxygenase 1	Homo sapiens	124-128
24642709-11	2014	These results suggest that capsaicin has protective effects against cisplatin-induced renal dysfunction through induction of HO-1 as well as inhibition oxidative stress and inflammation.	Capsaicin	27-36	heme oxygenase 1	Homo sapiens	125-129
24642709-11	2014	These results suggest that capsaicin has protective effects against cisplatin-induced renal dysfunction through induction of HO-1 as well as inhibition oxidative stress and inflammation.	Cisplatin	68-77	heme oxygenase 1	Homo sapiens	125-129
24361488-0	2014	Nrf2/ARE pathway activation, HO-1 and NQO1 induction by polychlorinated biphenyl quinone is associated with reactive oxygen species and PI3K/AKT signaling.	polychlorinated biphenyl quinone	56-88	heme oxygenase 1	Homo sapiens	29-33
24503248-2	2014	The Hmox1/carbon monoxide (CO) pathway inhibits soluble Flt-1 (sFlt-1) and soluble Endoglin (sEng).	Carbon Monoxide	10-25	heme oxygenase 1	Homo sapiens	4-9
24503248-2	2014	The Hmox1/carbon monoxide (CO) pathway inhibits soluble Flt-1 (sFlt-1) and soluble Endoglin (sEng).	Cobalt	27-29	heme oxygenase 1	Homo sapiens	4-9
24623202-10	2014	The TAT-HO-1 attenuated the generation of reactive oxygen species and decreased HaCaT cell radiosensitivity to irradiation.	Reactive Oxygen Species	42-65	heme oxygenase 1	Homo sapiens	8-12
24361488-4	2014	In the present study, we found that exposure to PCB29-pQ resulted in a significant increase in Nrf2 and Keap1 expression in total protein, as well as the Nrf2 targeting genes, including NQO1 and HO-1.	2,3,5-trichloro-6-phenyl-(1,4)benzoquinone	48-56	heme oxygenase 1	Homo sapiens	195-199
24533775-1	2014	BACKGROUND: Previously, we reported that menadione activated rat, native heme oxygenase-2 (HO-2) and human recombinant heme oxygenase-2 selectively; it did not activate spleen, microsomal heme oxygenase-1.	Vitamin K 3	41-50	heme oxygenase 1	Homo sapiens	188-204
24361488-8	2014	Additionally, PCB29-pQ treatment led to significant up-regulation of the mRNA level of antioxidant enzymes, NQO1 and HO-1, in a concentration-dependent manner.	2,3,5-trichloro-6-phenyl-(1,4)benzoquinone	14-22	heme oxygenase 1	Homo sapiens	117-121
24361488-11	2014	Pretreatment with LY294002, a specific inhibitor of phosphatidylinositol 3-kinase (PI3K), suppressed the phosphorylation of AKT and inhibited PCB29-pQ induced Nrf2/HO-1 activation, meanwhile, GSK-3beta expression was increased accordingly.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	18-26	heme oxygenase 1	Homo sapiens	164-168
24361488-11	2014	Pretreatment with LY294002, a specific inhibitor of phosphatidylinositol 3-kinase (PI3K), suppressed the phosphorylation of AKT and inhibited PCB29-pQ induced Nrf2/HO-1 activation, meanwhile, GSK-3beta expression was increased accordingly.	2,3,5-trichloro-6-phenyl-(1,4)benzoquinone	142-150	heme oxygenase 1	Homo sapiens	164-168
24361900-0	2014	Nitric oxide sets off an antioxidant response in adrenal cells: involvement of sGC and Nrf2 in HO-1 induction.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	95-99
24361900-2	2014	In adrenal cells, HO-1 induction by ACTH exerts a modulatory effect on steroid production as well.	Steroids	71-78	heme oxygenase 1	Homo sapiens	18-22
24361900-3	2014	As nitric oxide (NO) has been also regarded as an autocrine/paracrine modulator of adrenal steroidogenesis we sought to study the effects of NO on the induction of HO-1 and the mechanism involved.	Nitric Oxide	3-15	heme oxygenase 1	Homo sapiens	164-168
24361900-4	2014	We hereby analyzed the time and dose-dependent effect of a NO-donor (DETA/NO) on HO-1 induction in a murine adrenocortical cell line.	DEET	69-73	heme oxygenase 1	Homo sapiens	81-85
24361900-8	2014	We finally show that the effects of the NO-donor are reproduced by a permeable analog of cGMP and that a soluble guanylate cyclase specific inhibitor blocked both the induction of HO-1 by NO and the nuclear translocation of Nrf2.	Cyclic GMP	89-93	heme oxygenase 1	Homo sapiens	180-184
24516582-7	2014	Interestingly, the most affected biological pathway by both 2 or 12 hrs of iAs exposure were the Nrf2-Keap1 pathway, represented by the highly up-regulated HMOX1 transcript, which is transcriptionally regulated by the transcription factor Nrf2.	4-Iodoacetamidosalicylic acid	75-78	heme oxygenase 1	Homo sapiens	156-161
24516582-10	2014	Since HMOX1 expression increased early (20 min) and was responsive to low iAs concentrations (0.1 microM), this gene could be a suitable early biomarker for iAs exposure.	4-Iodoacetamidosalicylic acid	74-77	heme oxygenase 1	Homo sapiens	6-11
24516582-10	2014	Since HMOX1 expression increased early (20 min) and was responsive to low iAs concentrations (0.1 microM), this gene could be a suitable early biomarker for iAs exposure.	4-Iodoacetamidosalicylic acid	157-160	heme oxygenase 1	Homo sapiens	6-11
23852531-0	2014	Hydrogen sulfide induces heme oxygenase-1 in human kidney cells.	Hydrogen Sulfide	0-16	heme oxygenase 1	Homo sapiens	25-41
23852531-2	2014	The aim of this study was to investigate if H2S effects the expression of the antioxidant enzyme heme oxygenase-1 (HO-1) in human kidney cells.	Hydrogen Sulfide	44-47	heme oxygenase 1	Homo sapiens	97-113
23852531-2	2014	The aim of this study was to investigate if H2S effects the expression of the antioxidant enzyme heme oxygenase-1 (HO-1) in human kidney cells.	Hydrogen Sulfide	44-47	heme oxygenase 1	Homo sapiens	115-119
23852531-5	2014	There was a significant increase in HO-1 expression after treatment with the H2S donors in both mesangial and podocyte cells.	Hydrogen Sulfide	77-80	heme oxygenase 1	Homo sapiens	36-40
23852531-6	2014	These results suggest that H2S has a role in the regulation of HO-1 expression, and the ability to upregulate this antioxidant enzyme maybe a potential mechanism by which H2S exerts its protective effects.	Hydrogen Sulfide	27-30	heme oxygenase 1	Homo sapiens	63-67
23852531-6	2014	These results suggest that H2S has a role in the regulation of HO-1 expression, and the ability to upregulate this antioxidant enzyme maybe a potential mechanism by which H2S exerts its protective effects.	Hydrogen Sulfide	171-174	heme oxygenase 1	Homo sapiens	63-67
24396429-5	2014	Correlation analysis showed that the expression levels of HO-1 protein were positively correlated with the HO-1 mRNA expression levels (r=0.680; P=0.000), and the levels of ROS (r=0.572; P=0.000) and MDA (r=0.614; P=0.000).	Reactive Oxygen Species	173-176	heme oxygenase 1	Homo sapiens	58-62
24396429-6	2014	HO-1 mRNA expression levels were found to positively correlate with the levels of MDA (r=0.451; P=0.010) and fasting plasma glucose (FPG; r=0.337; P=0.039).	Glucose	124-131	heme oxygenase 1	Homo sapiens	0-4
24396429-7	2014	Partial correlation analysis demonstrated that, after removing the effects of body mass index, FPG and 2-h plasma glucose, HO-1 protein expression levels were positively correlated with the levels of HO-1 mRNA expression (r=0.611; P=0.005), ROS (r=0.526; P=0.021) and MDA (r=0.519; P=0.015).	Reactive Oxygen Species	241-244	heme oxygenase 1	Homo sapiens	123-127
24396429-7	2014	Partial correlation analysis demonstrated that, after removing the effects of body mass index, FPG and 2-h plasma glucose, HO-1 protein expression levels were positively correlated with the levels of HO-1 mRNA expression (r=0.611; P=0.005), ROS (r=0.526; P=0.021) and MDA (r=0.519; P=0.015).	Reactive Oxygen Species	241-244	heme oxygenase 1	Homo sapiens	200-204
24396429-8	2014	These findings indicate that pregnant females with GDM may be protected against oxidative injury due to the induction of adaptive and compensatory expression of HO-1 to guard against oxidative stress induced by high glucose levels.	Glucose	216-223	heme oxygenase 1	Homo sapiens	161-165
24451142-0	2014	Resveratrol partially prevents rotenone-induced neurotoxicity in dopaminergic SH-SY5Y cells through induction of heme oxygenase-1 dependent autophagy.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	113-129
23934646-0	2014	Neuroprotection by monocarbonyl dimethoxycurcumin C: ameliorating the toxicity of mutant TDP-43 via HO-1.	monocarbonyl dimethoxycurcumin c	19-51	heme oxygenase 1	Homo sapiens	100-104
23934646-9	2014	Znpp, which is known an inhibitor of HO-1, dramatically interfered with the function of Compound C. In addition, Compound C was tested in vivo, and HO-1 was significantly upregulated at the hippocampus.	zinc protoporphyrin	0-4	heme oxygenase 1	Homo sapiens	37-41
23934646-9	2014	Znpp, which is known an inhibitor of HO-1, dramatically interfered with the function of Compound C. In addition, Compound C was tested in vivo, and HO-1 was significantly upregulated at the hippocampus.	zinc protoporphyrin	0-4	heme oxygenase 1	Homo sapiens	148-152
24489685-3	2014	Among the three organosulfur compounds, DATS was found to be most potent in inducing heme oxygenase-1 (HO-1) and NAD(P)H: quinone oxidoreductase-1 (NQO1) in human gastric epithelial (AGS) cells.	dats	40-44	heme oxygenase 1	Homo sapiens	85-101
24302760-7	2014	Tan treatment induced the phosphorylation and nuclear translocation of Nrf2 and subsequently increased the expression of HO-1, and these effects were abolished by the specific ERK inhibitors, PD98059 and U0126.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	192-199	heme oxygenase 1	Homo sapiens	121-125
24302760-7	2014	Tan treatment induced the phosphorylation and nuclear translocation of Nrf2 and subsequently increased the expression of HO-1, and these effects were abolished by the specific ERK inhibitors, PD98059 and U0126.	U 0126	204-209	heme oxygenase 1	Homo sapiens	121-125
24302760-8	2014	Moreover, HO-1 small interfering RNA or zinc protoporphyrin (a HO-1 inhibitor) abrogated Tan-mediated suppression of lipid accumulation in macrophages.	zinc protoporphyrin	40-59	heme oxygenase 1	Homo sapiens	63-67
24302760-9	2014	Our current findings demonstrate that a novel HO-1-dependent mechanism is involved in the regulation of cholesterol balance by Tan.	Cholesterol	104-115	heme oxygenase 1	Homo sapiens	46-50
24355260-2	2014	Of interest, patients with lung tumors have been noted to have an increase in endogenous carbon monoxide production via upregulation of hemeoxygenase-1 activity.	Carbon Monoxide	89-104	heme oxygenase 1	Homo sapiens	136-151
24095978-4	2014	HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron.	Heme	59-63	heme oxygenase 1	Homo sapiens	0-4
24095978-4	2014	HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron.	Biliverdine	127-140	heme oxygenase 1	Homo sapiens	0-4
24095978-4	2014	HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron.	bilirubin-ix	152-164	heme oxygenase 1	Homo sapiens	0-4
24095978-4	2014	HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron.	Carbon Monoxide	226-241	heme oxygenase 1	Homo sapiens	0-4
24095978-4	2014	HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron.	Carbon Monoxide	243-245	heme oxygenase 1	Homo sapiens	0-4
24095978-4	2014	HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron.	ferrous iron	251-263	heme oxygenase 1	Homo sapiens	0-4
24434148-10	2014	NADPH oxidase inhibitor Apocynin and superoxide scavenger N-acetyl-cysteine (NAC) significantly attenuated EI-stimulated expression of OKL38 and HO-1.	acetovanillone	24-32	heme oxygenase 1	Homo sapiens	145-149
24434148-10	2014	NADPH oxidase inhibitor Apocynin and superoxide scavenger N-acetyl-cysteine (NAC) significantly attenuated EI-stimulated expression of OKL38 and HO-1.	Superoxides	37-47	heme oxygenase 1	Homo sapiens	145-149
24434148-10	2014	NADPH oxidase inhibitor Apocynin and superoxide scavenger N-acetyl-cysteine (NAC) significantly attenuated EI-stimulated expression of OKL38 and HO-1.	Acetylcysteine	58-75	heme oxygenase 1	Homo sapiens	145-149
24434148-10	2014	NADPH oxidase inhibitor Apocynin and superoxide scavenger N-acetyl-cysteine (NAC) significantly attenuated EI-stimulated expression of OKL38 and HO-1.	Acetylcysteine	77-80	heme oxygenase 1	Homo sapiens	145-149
24434148-10	2014	NADPH oxidase inhibitor Apocynin and superoxide scavenger N-acetyl-cysteine (NAC) significantly attenuated EI-stimulated expression of OKL38 and HO-1.	aziridine	107-109	heme oxygenase 1	Homo sapiens	145-149
24300974-0	2014	Gambogic acid synergistically potentiates cisplatin-induced apoptosis in non-small-cell lung cancer through suppressing NF-kappaB and MAPK/HO-1 signalling.	gambogic acid	0-13	heme oxygenase 1	Homo sapiens	139-143
24451142-0	2014	Resveratrol partially prevents rotenone-induced neurotoxicity in dopaminergic SH-SY5Y cells through induction of heme oxygenase-1 dependent autophagy.	Rotenone	31-39	heme oxygenase 1	Homo sapiens	113-129
24300974-0	2014	Gambogic acid synergistically potentiates cisplatin-induced apoptosis in non-small-cell lung cancer through suppressing NF-kappaB and MAPK/HO-1 signalling.	Cisplatin	42-51	heme oxygenase 1	Homo sapiens	139-143
24300974-8	2014	Importantly, it was found that, followed by CDDP treatment, GA could inhibit NF-kappaB and mitogen-activated protein kinase (MAPK)/heme oxygenase-1 (HO-1) signalling pathways, which have been validated to reduce ROS release and confer CDDP resistance.	Cisplatin	44-48	heme oxygenase 1	Homo sapiens	131-147
24451142-9	2014	Further, rotenone reduced heme oxygenase-1 (HO-1) expression, whereas resveratrol increased HO-1 expression.	Rotenone	9-17	heme oxygenase 1	Homo sapiens	26-42
24300974-8	2014	Importantly, it was found that, followed by CDDP treatment, GA could inhibit NF-kappaB and mitogen-activated protein kinase (MAPK)/heme oxygenase-1 (HO-1) signalling pathways, which have been validated to reduce ROS release and confer CDDP resistance.	Cisplatin	44-48	heme oxygenase 1	Homo sapiens	149-153
24451142-9	2014	Further, rotenone reduced heme oxygenase-1 (HO-1) expression, whereas resveratrol increased HO-1 expression.	Rotenone	9-17	heme oxygenase 1	Homo sapiens	44-48
24300974-8	2014	Importantly, it was found that, followed by CDDP treatment, GA could inhibit NF-kappaB and mitogen-activated protein kinase (MAPK)/heme oxygenase-1 (HO-1) signalling pathways, which have been validated to reduce ROS release and confer CDDP resistance.	gambogic acid	60-62	heme oxygenase 1	Homo sapiens	131-147
24300974-8	2014	Importantly, it was found that, followed by CDDP treatment, GA could inhibit NF-kappaB and mitogen-activated protein kinase (MAPK)/heme oxygenase-1 (HO-1) signalling pathways, which have been validated to reduce ROS release and confer CDDP resistance.	gambogic acid	60-62	heme oxygenase 1	Homo sapiens	149-153
24451142-9	2014	Further, rotenone reduced heme oxygenase-1 (HO-1) expression, whereas resveratrol increased HO-1 expression.	Resveratrol	70-81	heme oxygenase 1	Homo sapiens	92-96
24300974-8	2014	Importantly, it was found that, followed by CDDP treatment, GA could inhibit NF-kappaB and mitogen-activated protein kinase (MAPK)/heme oxygenase-1 (HO-1) signalling pathways, which have been validated to reduce ROS release and confer CDDP resistance.	Reactive Oxygen Species	212-215	heme oxygenase 1	Homo sapiens	149-153
24300974-8	2014	Importantly, it was found that, followed by CDDP treatment, GA could inhibit NF-kappaB and mitogen-activated protein kinase (MAPK)/heme oxygenase-1 (HO-1) signalling pathways, which have been validated to reduce ROS release and confer CDDP resistance.	Cisplatin	235-239	heme oxygenase 1	Homo sapiens	149-153
24300974-10	2014	Moreover, our results indicated that the combination of CDDP and GA exerted increased antitumour effects on A549 xenograft models through inhibiting NF-kappaB, HO-1, and subsequently inducing apoptosis.	Cisplatin	56-60	heme oxygenase 1	Homo sapiens	160-164
24300974-10	2014	Moreover, our results indicated that the combination of CDDP and GA exerted increased antitumour effects on A549 xenograft models through inhibiting NF-kappaB, HO-1, and subsequently inducing apoptosis.	gambogic acid	65-67	heme oxygenase 1	Homo sapiens	160-164
24300974-11	2014	CONCLUSION: Gambogic acid sensitises lung cancer cells to CDDP in vitro and in vivo in NSCLC through inactivation of NF-kappaB and MAPK/HO-1 signalling pathways, providing a rationale for the combined use of CDDP and GA in lung cancer chemotherapy.	gambogic acid	12-25	heme oxygenase 1	Homo sapiens	136-140
24451142-10	2014	Pharmacological inhibition of HO-1 abolished resveratrol-mediated autophagy and neuroprotection.	Resveratrol	45-56	heme oxygenase 1	Homo sapiens	30-34
24451142-11	2014	Notably, the effects of a pharmacological inducer of HO-1 were similar to those of resveratrol, and protected against rotenone-induced cell death in an autophagy-dependent manner, validating the hypothesis of HO-1 dependent autophagy in preventing neuronal death in the in vitro PD model.	Rotenone	118-126	heme oxygenase 1	Homo sapiens	53-57
24451142-11	2014	Notably, the effects of a pharmacological inducer of HO-1 were similar to those of resveratrol, and protected against rotenone-induced cell death in an autophagy-dependent manner, validating the hypothesis of HO-1 dependent autophagy in preventing neuronal death in the in vitro PD model.	Rotenone	118-126	heme oxygenase 1	Homo sapiens	209-213
24451142-12	2014	Collectively, our findings suggest that resveratrol induces HO-1 expression and prevents dopaminergic cell death by regulating autophagic flux; thus protecting against rotenone-induced neuronal apoptosis.	Resveratrol	40-51	heme oxygenase 1	Homo sapiens	60-64
24183966-8	2014	HO-1 may also contribute to the iron accumulation in neurons, but its mechanism needs to be further investigated.	Iron	32-36	heme oxygenase 1	Homo sapiens	0-4
24035224-6	2014	In addition, sauchinone induced heme oxygenase (HO)-1 expression through nuclear translocation of nuclear factor E2-related factor 2 in HUVEC.	sauchinone	13-23	heme oxygenase 1	Homo sapiens	32-53
24239896-4	2014	The induction of HO-1 was associated with an increase in NF-E2-related factor-2 (Nrf2) activity and reactive oxygen species (ROS).	Reactive Oxygen Species	100-123	heme oxygenase 1	Homo sapiens	17-21
24239896-4	2014	The induction of HO-1 was associated with an increase in NF-E2-related factor-2 (Nrf2) activity and reactive oxygen species (ROS).	Reactive Oxygen Species	125-128	heme oxygenase 1	Homo sapiens	17-21
24239896-6	2014	In addition, the CM-mediated induction of HO-1 and activation of Nrf2 was abolished by acetylcysteine.	Acetylcysteine	87-101	heme oxygenase 1	Homo sapiens	42-46
24239896-9	2014	Thus, induction of HO-1 via the ROS-Nrf2 pathway counteracts the anti-proliferative and inflammatory actions of CM.	Reactive Oxygen Species	32-35	heme oxygenase 1	Homo sapiens	19-23
24239896-3	2014	We found that three distinct CM, including high-osmolar (diatrizoate), low-osmolar (iopamidol), and iso-osmolar (iodixanol), stimulated the expression of HO-1 protein and mRNA.	Diatrizoate	57-68	heme oxygenase 1	Homo sapiens	154-158
24239896-3	2014	We found that three distinct CM, including high-osmolar (diatrizoate), low-osmolar (iopamidol), and iso-osmolar (iodixanol), stimulated the expression of HO-1 protein and mRNA.	Iopamidol	84-93	heme oxygenase 1	Homo sapiens	154-158
24239896-3	2014	We found that three distinct CM, including high-osmolar (diatrizoate), low-osmolar (iopamidol), and iso-osmolar (iodixanol), stimulated the expression of HO-1 protein and mRNA.	iodixanol	113-122	heme oxygenase 1	Homo sapiens	154-158
24089372-3	2014	Heme arginate (HA), a HO-1 inducer, is a promising, translatable, preconditioning agent.	heme arginate	0-13	heme oxygenase 1	Homo sapiens	22-26
24126012-0	2014	Mechanistic study on the biological effects of silver and gold nanoparticles in Caco-2 cells--induction of the Nrf2/HO-1 pathway by high concentrations of silver nanoparticles.	Silver	47-53	heme oxygenase 1	Homo sapiens	116-120
24126012-0	2014	Mechanistic study on the biological effects of silver and gold nanoparticles in Caco-2 cells--induction of the Nrf2/HO-1 pathway by high concentrations of silver nanoparticles.	Silver	155-161	heme oxygenase 1	Homo sapiens	116-120
24126012-5	2014	Furthermore, siRNA silencing of Nrf2 transcripts significantly reduced the AgNP-induced HO-1 mRNA induction, suggesting a key role for Nrf2 in the control of HO-1 expression.	agnp	75-79	heme oxygenase 1	Homo sapiens	88-92
24126012-5	2014	Furthermore, siRNA silencing of Nrf2 transcripts significantly reduced the AgNP-induced HO-1 mRNA induction, suggesting a key role for Nrf2 in the control of HO-1 expression.	agnp	75-79	heme oxygenase 1	Homo sapiens	158-162
24089372-3	2014	Heme arginate (HA), a HO-1 inducer, is a promising, translatable, preconditioning agent.	heme arginate	15-17	heme oxygenase 1	Homo sapiens	22-26
23861314-6	2014	Interestingly, protoporphyrin-IX, a competitive inhibitor of HO-1 activity, partly attenuated the inhibitory effects of Res and Pic (but not TMS) on TNF-alpha and IL-1beta production, suggesting that suppression of TNF-alpha and IL-1beta production correlates at least in part with HO-1 expression.	protoporphyrin IX	15-32	heme oxygenase 1	Homo sapiens	61-65
25344086-4	2014	HO-1 along with its reaction products bilirubin and CO are protective against ischemia-induced injury (myocardial infarction, ischemia-reperfusion (IR)-injury and post-infarct structural remodelling).	Bilirubin	38-47	heme oxygenase 1	Homo sapiens	0-4
25344086-4	2014	HO-1 along with its reaction products bilirubin and CO are protective against ischemia-induced injury (myocardial infarction, ischemia-reperfusion (IR)-injury and post-infarct structural remodelling).	Carbon Monoxide	52-54	heme oxygenase 1	Homo sapiens	0-4
23861314-6	2014	Interestingly, protoporphyrin-IX, a competitive inhibitor of HO-1 activity, partly attenuated the inhibitory effects of Res and Pic (but not TMS) on TNF-alpha and IL-1beta production, suggesting that suppression of TNF-alpha and IL-1beta production correlates at least in part with HO-1 expression.	protoporphyrin IX	15-32	heme oxygenase 1	Homo sapiens	282-286
24592391-0	2014	Human pharmacokinetics of high dose oral curcumin and its effect on heme oxygenase-1 expression in healthy male subjects.	Curcumin	41-49	heme oxygenase 1	Homo sapiens	68-84
24060752-5	2014	RESULTS: The sulforaphane treatment activated Nrf2, increased levels of the Nrf2 target heme oxygenase-1 and subsequently lowered oxidant stress as shown by the decline in lipid peroxidation and 3-nitrotyrosine protein adducts and an increase in GSH levels after the acute ethanol treatment.	sulforaphane	13-25	heme oxygenase 1	Homo sapiens	88-104
25273386-8	2014	Tryptanthrin also up-regulated the expression of the heme oxygenase 1 and glutamate-cysteine ligase catalytic subunits, which are representative target genes of Nrf2.	tryptanthrine	0-12	heme oxygenase 1	Homo sapiens	53-69
24592391-3	2014	We investigated the inducibility of HO-1 by orally administered curcumin in healthy male subjects and its correlation with the GT length polymorphism.	Curcumin	64-72	heme oxygenase 1	Homo sapiens	36-40
24117426-0	2014	Andrographolide exerts anti-hepatitis C virus activity by up-regulating haeme oxygenase-1 via the p38 MAPK/Nrf2 pathway in human hepatoma cells.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	72-89
24117426-7	2014	Andrographolide up-regulated the expression of haeme oxygenase-1 (HO-1), leading to increased amounts of its metabolite biliverdin, which was found to suppress HCV replication by promoting the antiviral IFN responses and inhibiting NS3/4A protease activity.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	47-64
24117426-9	2014	Andrographolide activated p38 MAPK phosphorylation, which stimulated nuclear factor erythroid 2-related factor 2 (Nrf2)-mediated HO-1 expression, and this was found to be associated with its anti-HCV activity.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	129-133
24117426-10	2014	CONCLUSIONS AND IMPLICATIONS: Our results demonstrate that andrographolide has the potential to control HCV replication and suggest that targeting the Nrf2-HO-1 signalling pathway might be a promising strategy for drug development.	andrographolide	59-74	heme oxygenase 1	Homo sapiens	156-160
24117426-7	2014	Andrographolide up-regulated the expression of haeme oxygenase-1 (HO-1), leading to increased amounts of its metabolite biliverdin, which was found to suppress HCV replication by promoting the antiviral IFN responses and inhibiting NS3/4A protease activity.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	66-70
24117426-7	2014	Andrographolide up-regulated the expression of haeme oxygenase-1 (HO-1), leading to increased amounts of its metabolite biliverdin, which was found to suppress HCV replication by promoting the antiviral IFN responses and inhibiting NS3/4A protease activity.	Biliverdine	120-130	heme oxygenase 1	Homo sapiens	47-64
24117426-7	2014	Andrographolide up-regulated the expression of haeme oxygenase-1 (HO-1), leading to increased amounts of its metabolite biliverdin, which was found to suppress HCV replication by promoting the antiviral IFN responses and inhibiting NS3/4A protease activity.	Biliverdine	120-130	heme oxygenase 1	Homo sapiens	66-70
24117426-8	2014	Significantly, these antiviral effects were attenuated by an HO-1-specific inhibitor or HO-1 gene knockdown, indicating that HO-1 contributed to the anti-HCV activity of andrographolide.	andrographolide	170-185	heme oxygenase 1	Homo sapiens	61-65
24117426-8	2014	Significantly, these antiviral effects were attenuated by an HO-1-specific inhibitor or HO-1 gene knockdown, indicating that HO-1 contributed to the anti-HCV activity of andrographolide.	andrographolide	170-185	heme oxygenase 1	Homo sapiens	88-92
24117426-8	2014	Significantly, these antiviral effects were attenuated by an HO-1-specific inhibitor or HO-1 gene knockdown, indicating that HO-1 contributed to the anti-HCV activity of andrographolide.	andrographolide	170-185	heme oxygenase 1	Homo sapiens	88-92
24766133-3	2014	During the last decade, different strategies such as pharmacologic or gene therapy modulation of heme oxygenase-1 (HO-1) and the administration of its metabolic product, carbon monoxide (CO), have been shown to display beneficial immunoregulatory and cytoprotective properties.	Carbon Monoxide	187-189	heme oxygenase 1	Homo sapiens	97-113
25146616-14	2014	According to progression of CML, HO-1 expression level in CML patients increased from CP (0.009 5+-0.017 6) to AP (0.028 0+-0.055 7) and then to BP (0.276 7 +- 0.447 0).	Benzo(a)pyrene	145-147	heme oxygenase 1	Homo sapiens	33-37
24655000-7	2014	The water-soluble forms of the HO-1 inhibitor Zinc protoporphyrin (ZnPP) have seemed promising in different in-vivo models, in which it has induced growth arrest in tumour cells with few, if any, side effects.	Water	4-9	heme oxygenase 1	Homo sapiens	31-35
24655000-7	2014	The water-soluble forms of the HO-1 inhibitor Zinc protoporphyrin (ZnPP) have seemed promising in different in-vivo models, in which it has induced growth arrest in tumour cells with few, if any, side effects.	zinc protoporphyrin	46-65	heme oxygenase 1	Homo sapiens	31-35
24655000-7	2014	The water-soluble forms of the HO-1 inhibitor Zinc protoporphyrin (ZnPP) have seemed promising in different in-vivo models, in which it has induced growth arrest in tumour cells with few, if any, side effects.	zinc protoporphyrin	67-71	heme oxygenase 1	Homo sapiens	31-35
24934350-0	2014	Salvianolic acid B inhibits atherogenesis of vascular cells through induction of Nrf2-dependent heme oxygenase-1.	salvianolic acid B	0-18	heme oxygenase 1	Homo sapiens	96-112
24934350-4	2014	METHODS AND RESULTS: Treatment of vascular smooth muscle cells with Sal B effectively inhibited platelet-derived growth factor (PDGF)-induced cell proliferation and migration, and markedly increased heme oxygenase-1 (HO-1) expression.	salvianolic acid B	68-73	heme oxygenase 1	Homo sapiens	199-215
24934350-4	2014	METHODS AND RESULTS: Treatment of vascular smooth muscle cells with Sal B effectively inhibited platelet-derived growth factor (PDGF)-induced cell proliferation and migration, and markedly increased heme oxygenase-1 (HO-1) expression.	salvianolic acid B	68-73	heme oxygenase 1	Homo sapiens	217-221
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Heme	70-74	heme oxygenase 1	Homo sapiens	88-92
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Biliverdine	165-175	heme oxygenase 1	Homo sapiens	70-86
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Biliverdine	165-175	heme oxygenase 1	Homo sapiens	88-92
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Iron	187-191	heme oxygenase 1	Homo sapiens	70-86
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Iron	187-191	heme oxygenase 1	Homo sapiens	88-92
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Carbon Monoxide	207-222	heme oxygenase 1	Homo sapiens	70-86
24934350-7	2014	Knockdown of HO-1 expression by siRNA abolished the effects of Sal B in vascular cells and prevented the inhibition of proliferation, migration, and inflammation in HO-1-deficient cells.	salvianolic acid B	63-68	heme oxygenase 1	Homo sapiens	13-17
24934350-9	2014	CONCLUSIONS: We conclude that Sal B exerts antiatherogenic effects by inhibiting the proliferation, migration, and inflammation of vascular cells through induction of HO-1 via Nrf2 activation.	salvianolic acid B	30-35	heme oxygenase 1	Homo sapiens	167-171
24275768-1	2014	PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide.	Carbon Monoxide	207-222	heme oxygenase 1	Homo sapiens	88-92
24766133-3	2014	During the last decade, different strategies such as pharmacologic or gene therapy modulation of heme oxygenase-1 (HO-1) and the administration of its metabolic product, carbon monoxide (CO), have been shown to display beneficial immunoregulatory and cytoprotective properties.	Carbon Monoxide	187-189	heme oxygenase 1	Homo sapiens	115-119
25530680-7	2014	We report that Mox-LDL inhibits endothelial cell motility and tubulogenesis through an increase in miR-22 and heme oxygenase 1 expression.	mox-ldl	15-22	heme oxygenase 1	Homo sapiens	110-126
25762501-7	2014	We also show that ER stress combined with inflammation synergistically upregulated the expression of the iron carrier protein NGAL and the stress-inducible heme degrading enzyme heme oxygenase-1 (HO-1) leading to iron liberation.	Heme	156-160	heme oxygenase 1	Homo sapiens	178-194
25762501-7	2014	We also show that ER stress combined with inflammation synergistically upregulated the expression of the iron carrier protein NGAL and the stress-inducible heme degrading enzyme heme oxygenase-1 (HO-1) leading to iron liberation.	Iron	213-217	heme oxygenase 1	Homo sapiens	178-194
24763872-0	2014	Cytoprotective effect of beta-lapachone by inducing heme oxygenase-1 expression and AMP-activated protein kinase activation in human endothelial cells.	beta-lapachone	25-39	heme oxygenase 1	Homo sapiens	52-68
24763872-11	2014	Cytoprotection by BL was almost completely abolished by CC and DC and partly by SnPP, a competitive inhibitor of HO-1.	S-Nitroso-N-propionyl-D,L-penicillamine	80-84	heme oxygenase 1	Homo sapiens	113-117
25386047-0	2014	Epigallocatechin gallate attenuates proliferation and oxidative stress in human vascular smooth muscle cells induced by interleukin-1beta via heme oxygenase-1.	epigallocatechin gallate	0-24	heme oxygenase 1	Homo sapiens	142-158
25386047-3	2014	This study aimed to elucidate the effects of the most active green tea catechin derivative, (-)-epigallocatechin-3-gallate (EGCG), in human aortic smooth muscle cells (HASMCs), focusing particularly on the role of a potent anti-inflammatory and antioxidative enzyme heme oxygenase-1 (HO-1).	epigallocatechin gallate	92-122	heme oxygenase 1	Homo sapiens	266-282
25386047-3	2014	This study aimed to elucidate the effects of the most active green tea catechin derivative, (-)-epigallocatechin-3-gallate (EGCG), in human aortic smooth muscle cells (HASMCs), focusing particularly on the role of a potent anti-inflammatory and antioxidative enzyme heme oxygenase-1 (HO-1).	epigallocatechin gallate	92-122	heme oxygenase 1	Homo sapiens	284-288
25386047-3	2014	This study aimed to elucidate the effects of the most active green tea catechin derivative, (-)-epigallocatechin-3-gallate (EGCG), in human aortic smooth muscle cells (HASMCs), focusing particularly on the role of a potent anti-inflammatory and antioxidative enzyme heme oxygenase-1 (HO-1).	epigallocatechin gallate	124-128	heme oxygenase 1	Homo sapiens	266-282
25386047-3	2014	This study aimed to elucidate the effects of the most active green tea catechin derivative, (-)-epigallocatechin-3-gallate (EGCG), in human aortic smooth muscle cells (HASMCs), focusing particularly on the role of a potent anti-inflammatory and antioxidative enzyme heme oxygenase-1 (HO-1).	epigallocatechin gallate	124-128	heme oxygenase 1	Homo sapiens	284-288
25386047-4	2014	We found that pretreatment of EGCG dose- and time-dependently induced HO-1 protein levels in HASMCs.	epigallocatechin gallate	30-34	heme oxygenase 1	Homo sapiens	70-74
25386047-6	2014	The HO-1 inducer CoPPIX decreased IL-1beta-induced cell proliferation, whereas the HO-1 enzyme inhibitor ZnPPIX significantly reversed EGCG-caused growth inhibition in IL-1beta-treated HASMCs.	coppix	17-23	heme oxygenase 1	Homo sapiens	4-8
25386047-6	2014	The HO-1 inducer CoPPIX decreased IL-1beta-induced cell proliferation, whereas the HO-1 enzyme inhibitor ZnPPIX significantly reversed EGCG-caused growth inhibition in IL-1beta-treated HASMCs.	zinc protoporphyrin	105-111	heme oxygenase 1	Homo sapiens	83-87
25386047-6	2014	The HO-1 inducer CoPPIX decreased IL-1beta-induced cell proliferation, whereas the HO-1 enzyme inhibitor ZnPPIX significantly reversed EGCG-caused growth inhibition in IL-1beta-treated HASMCs.	epigallocatechin gallate	135-139	heme oxygenase 1	Homo sapiens	83-87
25386047-6	2014	The HO-1 inducer CoPPIX decreased IL-1beta-induced cell proliferation, whereas the HO-1 enzyme inhibitor ZnPPIX significantly reversed EGCG-caused growth inhibition in IL-1beta-treated HASMCs.	hasmcs	185-191	heme oxygenase 1	Homo sapiens	83-87
25386047-8	2014	These results suggest that EGCG might serve as a complementary and alternative medicine in the treatment of these pathologies by inducing HO-1 expression and subsequently decreasing VSMC proliferation.	epigallocatechin gallate	27-31	heme oxygenase 1	Homo sapiens	138-142
24220687-10	2014	We also demonstrated that sanguinarine induced HO-1 expression, and that the inhibition of MMP-9 and COX-2 expression and the enzymatic activity of sanguinarine were abrogated by siRNA-mediated knockdown of HO-1 expression.	sanguinarine	26-38	heme oxygenase 1	Homo sapiens	47-51
24447094-0	2014	PPARalpha activation sensitizes cancer cells to epigallocatechin-3-gallate (EGCG) treatment via suppressing heme oxygenase-1.	epigallocatechin gallate	48-74	heme oxygenase 1	Homo sapiens	108-124
24447094-0	2014	PPARalpha activation sensitizes cancer cells to epigallocatechin-3-gallate (EGCG) treatment via suppressing heme oxygenase-1.	epigallocatechin gallate	76-80	heme oxygenase 1	Homo sapiens	108-124
24447094-6	2014	The PPARalpha agonist clofibrate blocked cytoprotective heme oxygenase-1 (HO-1) induction and sensitized multiple types of cancer cells to EGCG-induced cell death.	Clofibrate	22-32	heme oxygenase 1	Homo sapiens	56-72
24447094-6	2014	The PPARalpha agonist clofibrate blocked cytoprotective heme oxygenase-1 (HO-1) induction and sensitized multiple types of cancer cells to EGCG-induced cell death.	Clofibrate	22-32	heme oxygenase 1	Homo sapiens	74-78
24447094-7	2014	Conversely, the PPARalpha inhibitor G6471 and PPARalpha siRNA increased HO-1 expression.	g6471	36-41	heme oxygenase 1	Homo sapiens	72-76
24447094-9	2014	Moreover, cell death induced by EGCG plus clofibrate was partially reversed by HO-1 overexpression in PANC1 cells.	epigallocatechin gallate	32-36	heme oxygenase 1	Homo sapiens	79-83
24447094-9	2014	Moreover, cell death induced by EGCG plus clofibrate was partially reversed by HO-1 overexpression in PANC1 cells.	Clofibrate	42-52	heme oxygenase 1	Homo sapiens	79-83
24447094-10	2014	These results indicate that PPARalpha is a direct and negative regulator of HO-1 induced by EGCG and confers cell susceptibility to EGCG.	epigallocatechin gallate	92-96	heme oxygenase 1	Homo sapiens	76-80
24447094-10	2014	These results indicate that PPARalpha is a direct and negative regulator of HO-1 induced by EGCG and confers cell susceptibility to EGCG.	epigallocatechin gallate	132-136	heme oxygenase 1	Homo sapiens	76-80
25150313-0	2014	MiR-200c sensitizes clear-cell renal cell carcinoma cells to sorafenib and imatinib by targeting heme oxygenase-1.	Imatinib Mesylate	75-83	heme oxygenase 1	Homo sapiens	97-113
25150313-5	2014	We provided evidences to elucidate that miR-200c could sensitize ccRCC cells to sorafenib or imatinib to inhibit cell proliferation, at least partly by targeting HO-1.	Sorafenib	80-89	heme oxygenase 1	Homo sapiens	162-166
25150313-5	2014	We provided evidences to elucidate that miR-200c could sensitize ccRCC cells to sorafenib or imatinib to inhibit cell proliferation, at least partly by targeting HO-1.	Imatinib Mesylate	93-101	heme oxygenase 1	Homo sapiens	162-166
24220687-0	2014	Sanguinarine inhibits invasiveness and the MMP-9 and COX-2 expression in TPA-induced breast cancer cells by inducing HO-1 expression.	sanguinarine	0-12	heme oxygenase 1	Homo sapiens	117-121
24220687-0	2014	Sanguinarine inhibits invasiveness and the MMP-9 and COX-2 expression in TPA-induced breast cancer cells by inducing HO-1 expression.	Tetradecanoylphorbol Acetate	73-76	heme oxygenase 1	Homo sapiens	117-121
24220687-4	2014	In the present study, we investigated the anti-invasive mechanism of sanguinarine by focusing on its role in inducing HO-1 in breast cancer cells.	sanguinarine	69-81	heme oxygenase 1	Homo sapiens	118-122
24220687-10	2014	We also demonstrated that sanguinarine induced HO-1 expression, and that the inhibition of MMP-9 and COX-2 expression and the enzymatic activity of sanguinarine were abrogated by siRNA-mediated knockdown of HO-1 expression.	sanguinarine	26-38	heme oxygenase 1	Homo sapiens	207-211
24220687-10	2014	We also demonstrated that sanguinarine induced HO-1 expression, and that the inhibition of MMP-9 and COX-2 expression and the enzymatic activity of sanguinarine were abrogated by siRNA-mediated knockdown of HO-1 expression.	sanguinarine	148-160	heme oxygenase 1	Homo sapiens	207-211
24220687-11	2014	Thus, knockdown of endogenous HO-1 decreased TPA-induced cell invasion.	Tetradecanoylphorbol Acetate	45-48	heme oxygenase 1	Homo sapiens	30-34
24220687-12	2014	Overall, the results of the present study demonstrate that HO-1 plays a pivotal role in the anti-invasive response of sanguinarine in TPA-stimulated breast cancer cells.	sanguinarine	118-130	heme oxygenase 1	Homo sapiens	59-63
25136403-5	2014	HO-1 isoform has been extensively studied mainly by its ability to respond to cellular stresses such as hemin, nitric oxide donors, oxidative damage, hypoxia, hyperthermia, and heavy metals, between others.	Hemin	104-109	heme oxygenase 1	Homo sapiens	0-4
25136403-5	2014	HO-1 isoform has been extensively studied mainly by its ability to respond to cellular stresses such as hemin, nitric oxide donors, oxidative damage, hypoxia, hyperthermia, and heavy metals, between others.	Nitric Oxide	111-123	heme oxygenase 1	Homo sapiens	0-4
24220687-12	2014	Overall, the results of the present study demonstrate that HO-1 plays a pivotal role in the anti-invasive response of sanguinarine in TPA-stimulated breast cancer cells.	Tetradecanoylphorbol Acetate	134-137	heme oxygenase 1	Homo sapiens	59-63
24854244-7	2014	Similarly, lysophosphatidic acid (LPA) induced TGF-beta expression and decreased HO-1 expression in human lung fibroblasts.	lysophosphatidic acid	11-32	heme oxygenase 1	Homo sapiens	81-85
24854244-7	2014	Similarly, lysophosphatidic acid (LPA) induced TGF-beta expression and decreased HO-1 expression in human lung fibroblasts.	lysophosphatidic acid	34-37	heme oxygenase 1	Homo sapiens	81-85
24145726-2	2013	Of interest, patients with breast cancer have been noted to have an increase in endogenous carbon monoxide production via upregulation of heme oxygenase-1 activity.	Carbon Monoxide	91-106	heme oxygenase 1	Homo sapiens	138-154
25462065-8	2014	HO-1 mRNA expression was measured as a downstream marker of response to oxidative stress induced by Zn(2+) exposure.	Zinc	100-103	heme oxygenase 1	Homo sapiens	0-4
25462065-10	2014	Compartment-directed catalase expression blunted Zn(2+)-induced elevations in cytosolic EGSH and the increased expression of HO-1 mRNA levels.	Zinc	49-51	heme oxygenase 1	Homo sapiens	125-129
24211270-1	2014	Heme oxygenase (HO)-1 is an oxidative stress-response enzyme which catalyzes the degradation of heme into bilirubin, ferric ion, and carbon monoxide (CO).	Heme	96-100	heme oxygenase 1	Homo sapiens	0-21
24211270-1	2014	Heme oxygenase (HO)-1 is an oxidative stress-response enzyme which catalyzes the degradation of heme into bilirubin, ferric ion, and carbon monoxide (CO).	Bilirubin	106-115	heme oxygenase 1	Homo sapiens	0-21
24211270-1	2014	Heme oxygenase (HO)-1 is an oxidative stress-response enzyme which catalyzes the degradation of heme into bilirubin, ferric ion, and carbon monoxide (CO).	Ferric enterobactin ion	117-123	heme oxygenase 1	Homo sapiens	0-21
24211270-1	2014	Heme oxygenase (HO)-1 is an oxidative stress-response enzyme which catalyzes the degradation of heme into bilirubin, ferric ion, and carbon monoxide (CO).	Carbon Monoxide	133-148	heme oxygenase 1	Homo sapiens	0-21
24211270-1	2014	Heme oxygenase (HO)-1 is an oxidative stress-response enzyme which catalyzes the degradation of heme into bilirubin, ferric ion, and carbon monoxide (CO).	Carbon Monoxide	150-152	heme oxygenase 1	Homo sapiens	0-21
24428990-4	2014	The activities of the heme oxygenase-1 (HO-1) and NAD (P) H: quinone oxidoreductase 1 (NQO-1) in cells and the superoxide dismutase (SOD) and catalase (CAT) in supernatant, as well as malondialdehyde (MDA) content, were measured by enzyme-linked immunosorbent assay.	Malondialdehyde	184-199	heme oxygenase 1	Homo sapiens	40-44
24428990-4	2014	The activities of the heme oxygenase-1 (HO-1) and NAD (P) H: quinone oxidoreductase 1 (NQO-1) in cells and the superoxide dismutase (SOD) and catalase (CAT) in supernatant, as well as malondialdehyde (MDA) content, were measured by enzyme-linked immunosorbent assay.	Malondialdehyde	201-204	heme oxygenase 1	Homo sapiens	40-44
25593981-5	2014	Within few hours of application, disulfiram caused irreversible cell damage associated with pronounced induction of the inducible heat shock proteins HSP70, HSP40, and HSP32.	Disulfiram	33-43	heme oxygenase 1	Homo sapiens	168-173
24564601-2	2014	Although they do not share the same mechanisms, membrane glycosphingolipids (GSL) and the antioxidant enzyme heme oxygenase-1 (HMOX1) both act against the pro-oxidative effect of TBA.	tba	179-182	heme oxygenase 1	Homo sapiens	109-125
24564601-2	2014	Although they do not share the same mechanisms, membrane glycosphingolipids (GSL) and the antioxidant enzyme heme oxygenase-1 (HMOX1) both act against the pro-oxidative effect of TBA.	tba	179-182	heme oxygenase 1	Homo sapiens	127-132
24145726-9	2013	Future investigation of the role played by heme oxygenase-1-derived carbon monoxide in the pathogenesis of breast cancer-related thrombophilia is warranted.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	43-59
23954820-5	2013	Moreover, treatments of PQ strongly inhibited the expression of Nrf2 and the downstream effectors, HO1 and NQO1.	Paraquat	24-26	heme oxygenase 1	Homo sapiens	99-102
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Heme	84-88	heme oxygenase 1	Homo sapiens	0-16
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Heme	84-88	heme oxygenase 1	Homo sapiens	18-23
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	0-16
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	18-23
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	0-16
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	18-23
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Iron	130-134	heme oxygenase 1	Homo sapiens	0-16
23939757-1	2013	Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions.	Iron	130-134	heme oxygenase 1	Homo sapiens	18-23
23418094-0	2013	Caffeoylserotonin protects human keratinocyte HaCaT cells against H2 O2 -induced oxidative stress and apoptosis through upregulation of HO-1 expression via activation of the PI3K/Akt/Nrf2 pathway.	N-caffeoylserotonin	0-17	heme oxygenase 1	Homo sapiens	136-140
23418094-0	2013	Caffeoylserotonin protects human keratinocyte HaCaT cells against H2 O2 -induced oxidative stress and apoptosis through upregulation of HO-1 expression via activation of the PI3K/Akt/Nrf2 pathway.	Hydrogen Peroxide	66-71	heme oxygenase 1	Homo sapiens	136-140
23418094-10	2013	These results demonstrate that CaS protects against oxidative stress-induced keratinocyte cell death in part through the activation of Nrf2-mediated HO-1 induction via the PI3K/Akt and/or PKC pathways, but not MAPK signaling.	cas	31-34	heme oxygenase 1	Homo sapiens	149-153
24167056-5	2013	Among the differentially expressed proteins, heme oxygenase-1 (HO-1) was found in the sunitinib and imatinib mesylate treatment groups, which possibly acts as a specific target for synthetic lethality in combinational treatment.	Sunitinib	86-95	heme oxygenase 1	Homo sapiens	45-61
24167056-5	2013	Among the differentially expressed proteins, heme oxygenase-1 (HO-1) was found in the sunitinib and imatinib mesylate treatment groups, which possibly acts as a specific target for synthetic lethality in combinational treatment.	Sunitinib	86-95	heme oxygenase 1	Homo sapiens	63-67
24167056-5	2013	Among the differentially expressed proteins, heme oxygenase-1 (HO-1) was found in the sunitinib and imatinib mesylate treatment groups, which possibly acts as a specific target for synthetic lethality in combinational treatment.	Imatinib Mesylate	100-108	heme oxygenase 1	Homo sapiens	45-61
24167056-5	2013	Among the differentially expressed proteins, heme oxygenase-1 (HO-1) was found in the sunitinib and imatinib mesylate treatment groups, which possibly acts as a specific target for synthetic lethality in combinational treatment.	Imatinib Mesylate	100-108	heme oxygenase 1	Homo sapiens	63-67
24260155-7	2013	The pretreatment of cells with specific ER inhibitors or PI3K/Akt (ICI182,780 and LY294002) increased Nrf2, HO-1, and NQO1 protein, impaired nuclear translocation of HA-Nrf2, and decreased ARE-luciferase activity.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	82-90	heme oxygenase 1	Homo sapiens	108-112
23580157-7	2013	Fluticasone propionate did not modify intracellular ROS production, GSH and HDCA-2 but reduced Nrf2 and HO-1 in CSE-stimulated 16-HBE.	Fluticasone	0-22	heme oxygenase 1	Homo sapiens	104-108
23580157-8	2013	Carbocysteine reduced ROS production and increased GSH, HO-1, Nrf2 and HDAC-2 nuclear expression/activity in CSE-stimulated cells and was more effective than fluticasone propionate in modulating the CSE-mediated effects.	Carbocysteine	0-13	heme oxygenase 1	Homo sapiens	56-60
24121491-2	2013	Carbon monoxide (CO), one of the products of the cytoprotective molecule heme oxygenase-1 (HO-1) in cancer cells, has been implicated in carcinogenesis and therapeutic resistance.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	73-89
24121491-2	2013	Carbon monoxide (CO), one of the products of the cytoprotective molecule heme oxygenase-1 (HO-1) in cancer cells, has been implicated in carcinogenesis and therapeutic resistance.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	91-95
24121491-2	2013	Carbon monoxide (CO), one of the products of the cytoprotective molecule heme oxygenase-1 (HO-1) in cancer cells, has been implicated in carcinogenesis and therapeutic resistance.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	73-89
24121491-2	2013	Carbon monoxide (CO), one of the products of the cytoprotective molecule heme oxygenase-1 (HO-1) in cancer cells, has been implicated in carcinogenesis and therapeutic resistance.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	91-95
23877636-1	2013	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in bilirubin metabolism, and its genetic variant may modulate hyperbilirubinemia risk in neonates.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	0-16
23877636-1	2013	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in bilirubin metabolism, and its genetic variant may modulate hyperbilirubinemia risk in neonates.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	18-22
24772975-6	2013	The Grp78, MTJ1 and HMOX1 gene expression increased with the administration of 1 microM dex.	Dexamethasone	88-91	heme oxygenase 1	Homo sapiens	20-25
24772975-9	2013	The increase in Grp78, Grp94, HMOX1 and MTJ1 gene expression was greater in groups in which dex was administered in combination with PBA than in groups in which dex was administered alone.	Dexamethasone	92-95	heme oxygenase 1	Homo sapiens	30-35
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	Heme	36-40	heme oxygenase 1	Homo sapiens	0-16
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	Heme	36-40	heme oxygenase 1	Homo sapiens	18-22
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	Carbon Monoxide	44-59	heme oxygenase 1	Homo sapiens	0-16
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	Carbon Monoxide	44-59	heme oxygenase 1	Homo sapiens	18-22
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	ammonium ferrous sulfate	61-68	heme oxygenase 1	Homo sapiens	0-16
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	ammonium ferrous sulfate	61-68	heme oxygenase 1	Homo sapiens	18-22
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	Biliverdine	78-88	heme oxygenase 1	Homo sapiens	0-16
24323422-7	2013	Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin.	Biliverdine	78-88	heme oxygenase 1	Homo sapiens	18-22
24323422-8	2013	CO activates cGMP to promote vasodilation, and biliverdin is converted to bilirubin which can serve as an anti-oxidant, both of which may contribute to the reported protective role of HO-1 in cerebral ischemia and subarachnoid hemorrhage.	Biliverdine	47-57	heme oxygenase 1	Homo sapiens	184-188
24323422-8	2013	CO activates cGMP to promote vasodilation, and biliverdin is converted to bilirubin which can serve as an anti-oxidant, both of which may contribute to the reported protective role of HO-1 in cerebral ischemia and subarachnoid hemorrhage.	Bilirubin	74-83	heme oxygenase 1	Homo sapiens	184-188
24323422-9	2013	However, ferrous ion can react with hydrogen peroxide to produce pro-oxidant hydroxyl radicals which may explain the harmful role of HO-1 in intracerebral hemorrhage.	ammonium ferrous sulfate	9-20	heme oxygenase 1	Homo sapiens	133-137
24323422-9	2013	However, ferrous ion can react with hydrogen peroxide to produce pro-oxidant hydroxyl radicals which may explain the harmful role of HO-1 in intracerebral hemorrhage.	Hydrogen Peroxide	36-53	heme oxygenase 1	Homo sapiens	133-137
24323422-9	2013	However, ferrous ion can react with hydrogen peroxide to produce pro-oxidant hydroxyl radicals which may explain the harmful role of HO-1 in intracerebral hemorrhage.	Hydroxyl Radical	77-94	heme oxygenase 1	Homo sapiens	133-137
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Heme	99-103	heme oxygenase 1	Homo sapiens	0-16
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Heme	99-103	heme oxygenase 1	Homo sapiens	18-22
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	0-16
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	18-22
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Carbon Monoxide	126-129	heme oxygenase 1	Homo sapiens	0-16
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Carbon Monoxide	126-129	heme oxygenase 1	Homo sapiens	18-22
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	ammonium ferrous sulfate	131-137	heme oxygenase 1	Homo sapiens	0-16
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	ammonium ferrous sulfate	131-137	heme oxygenase 1	Homo sapiens	18-22
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Biliverdine	144-154	heme oxygenase 1	Homo sapiens	0-16
23852701-1	2013	Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin.	Biliverdine	144-154	heme oxygenase 1	Homo sapiens	18-22
23836589-8	2013	Both heme oxygenase 1 (HO-1) and nuclear factor erythroid 2-related factor 2 (Nrf2) knockdown attenuated the isothiocyanate inhibition of oxLDL-induced ROS production, kappaB-reporter activity, and adhesion molecule expression.	isothiocyanic acid	109-123	heme oxygenase 1	Homo sapiens	5-21
23426167-7	2013	Inhibition of HO-1 increases the toxicity of ATO, but has no effect on Dar-induced apoptosis.	Arsenic Trioxide	45-48	heme oxygenase 1	Homo sapiens	14-18
24201221-3	2013	HMOX1 is the rate-limiting enzyme of heme degradation, and the heme breakdown products, CO, Fe, and bilirubin, are considered to be biologically active metabolites with direct or indirect antioxidant and anti-inflammatory properties.	Heme	37-41	heme oxygenase 1	Homo sapiens	0-5
23845594-6	2013	In human corneal epithelial cells in culture, addition of 4-HNE or 9-nitrooleic acid, a reactive nitrolipid formed during nitrosative stress, caused a time-dependent induction of HO-1 mRNA and protein; maximal responses were evident after 10h with 30 muM 4-HNE or 6h with 10 muM 9-nitrooleic acid.	4-hydroxy-2-nonenal	58-63	heme oxygenase 1	Homo sapiens	179-183
24179613-2	2013	HO-1, a stress-responsive enzyme that catabolizes heme into carbon monoxide (CO), biliverdin and iron, has previously been shown to protect grafts from ischemia/reperfusion and rejection.	Heme	50-54	heme oxygenase 1	Homo sapiens	0-4
24179613-2	2013	HO-1, a stress-responsive enzyme that catabolizes heme into carbon monoxide (CO), biliverdin and iron, has previously been shown to protect grafts from ischemia/reperfusion and rejection.	Carbon Monoxide	60-75	heme oxygenase 1	Homo sapiens	0-4
24179613-2	2013	HO-1, a stress-responsive enzyme that catabolizes heme into carbon monoxide (CO), biliverdin and iron, has previously been shown to protect grafts from ischemia/reperfusion and rejection.	Carbon Monoxide	77-79	heme oxygenase 1	Homo sapiens	0-4
24179613-2	2013	HO-1, a stress-responsive enzyme that catabolizes heme into carbon monoxide (CO), biliverdin and iron, has previously been shown to protect grafts from ischemia/reperfusion and rejection.	Biliverdine	82-92	heme oxygenase 1	Homo sapiens	0-4
24179613-2	2013	HO-1, a stress-responsive enzyme that catabolizes heme into carbon monoxide (CO), biliverdin and iron, has previously been shown to protect grafts from ischemia/reperfusion and rejection.	Iron	97-101	heme oxygenase 1	Homo sapiens	0-4
24179613-5	2013	More specifically, the CO derived from HO-1-mediated heme catabolism has been shown to be involved in the regulation of inflammation; furthermore, administration of low concentrations of exogenous CO has a protective effect against inflammation.	Heme	53-57	heme oxygenase 1	Homo sapiens	39-43
23845594-6	2013	In human corneal epithelial cells in culture, addition of 4-HNE or 9-nitrooleic acid, a reactive nitrolipid formed during nitrosative stress, caused a time-dependent induction of HO-1 mRNA and protein; maximal responses were evident after 10h with 30 muM 4-HNE or 6h with 10 muM 9-nitrooleic acid.	nitrolipid	97-107	heme oxygenase 1	Homo sapiens	179-183
23845594-6	2013	In human corneal epithelial cells in culture, addition of 4-HNE or 9-nitrooleic acid, a reactive nitrolipid formed during nitrosative stress, caused a time-dependent induction of HO-1 mRNA and protein; maximal responses were evident after 10h with 30 muM 4-HNE or 6h with 10 muM 9-nitrooleic acid.	4-hydroxy-2-nonenal	255-260	heme oxygenase 1	Homo sapiens	179-183
23845594-6	2013	In human corneal epithelial cells in culture, addition of 4-HNE or 9-nitrooleic acid, a reactive nitrolipid formed during nitrosative stress, caused a time-dependent induction of HO-1 mRNA and protein; maximal responses were evident after 10h with 30 muM 4-HNE or 6h with 10 muM 9-nitrooleic acid.	10-nitro-oleic acid	67-84	heme oxygenase 1	Homo sapiens	179-183
23845594-6	2013	In human corneal epithelial cells in culture, addition of 4-HNE or 9-nitrooleic acid, a reactive nitrolipid formed during nitrosative stress, caused a time-dependent induction of HO-1 mRNA and protein; maximal responses were evident after 10h with 30 muM 4-HNE or 6h with 10 muM 9-nitrooleic acid.	6H	264-266	heme oxygenase 1	Homo sapiens	179-183
24075775-0	2013	Docosahexaenoic acid (DHA)-induced heme oxygenase-1 attenuates cytotoxic effects of DHA in vascular smooth muscle cells.	Docosahexaenoic Acids	0-20	heme oxygenase 1	Homo sapiens	35-51
23845594-6	2013	In human corneal epithelial cells in culture, addition of 4-HNE or 9-nitrooleic acid, a reactive nitrolipid formed during nitrosative stress, caused a time-dependent induction of HO-1 mRNA and protein; maximal responses were evident after 10h with 30 muM 4-HNE or 6h with 10 muM 9-nitrooleic acid.	10-nitro-oleic acid	279-296	heme oxygenase 1	Homo sapiens	179-183
24052896-3	2013	A known regulator of the oxidative stress response is the heat shock protein, heme-oxygenase 1 (HO-1), which is induced by cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	123-147	heme oxygenase 1	Homo sapiens	78-94
24052896-3	2013	A known regulator of the oxidative stress response is the heat shock protein, heme-oxygenase 1 (HO-1), which is induced by cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	149-153	heme oxygenase 1	Homo sapiens	78-94
23816986-0	2013	The activation of HO-1/Nrf-2 contributes to the protective effects of diallyl disulfide (DADS) against ethanol-induced oxidative stress.	diallyl disulfide	70-87	heme oxygenase 1	Homo sapiens	18-22
23816986-0	2013	The activation of HO-1/Nrf-2 contributes to the protective effects of diallyl disulfide (DADS) against ethanol-induced oxidative stress.	diallyl disulfide	89-93	heme oxygenase 1	Homo sapiens	18-22
23816986-0	2013	The activation of HO-1/Nrf-2 contributes to the protective effects of diallyl disulfide (DADS) against ethanol-induced oxidative stress.	Ethanol	103-110	heme oxygenase 1	Homo sapiens	18-22
23816986-12	2013	CONCLUSION: These results demonstrate that DADS could induce the activation of HO-1/Nrf-2 pathway, which may contribute to the protective effects of DADS against ethanol-induced liver injury.	diallyl disulfide	43-47	heme oxygenase 1	Homo sapiens	79-83
23816986-12	2013	CONCLUSION: These results demonstrate that DADS could induce the activation of HO-1/Nrf-2 pathway, which may contribute to the protective effects of DADS against ethanol-induced liver injury.	diallyl disulfide	149-153	heme oxygenase 1	Homo sapiens	79-83
23816986-12	2013	CONCLUSION: These results demonstrate that DADS could induce the activation of HO-1/Nrf-2 pathway, which may contribute to the protective effects of DADS against ethanol-induced liver injury.	Ethanol	162-169	heme oxygenase 1	Homo sapiens	79-83
24075775-0	2013	Docosahexaenoic acid (DHA)-induced heme oxygenase-1 attenuates cytotoxic effects of DHA in vascular smooth muscle cells.	Docosahexaenoic Acids	22-25	heme oxygenase 1	Homo sapiens	35-51
24075775-0	2013	Docosahexaenoic acid (DHA)-induced heme oxygenase-1 attenuates cytotoxic effects of DHA in vascular smooth muscle cells.	Docosahexaenoic Acids	84-87	heme oxygenase 1	Homo sapiens	35-51
24075775-3	2013	In the present study we examined the impact of heme oxygenase (HO)-1, induced by DHA, on DHA-induced oxidative stress, UPR, cell proliferation and apoptosis in hPASMC.	Docosahexaenoic Acids	81-84	heme oxygenase 1	Homo sapiens	47-68
24075775-3	2013	In the present study we examined the impact of heme oxygenase (HO)-1, induced by DHA, on DHA-induced oxidative stress, UPR, cell proliferation and apoptosis in hPASMC.	Docosahexaenoic Acids	89-92	heme oxygenase 1	Homo sapiens	47-68
23932761-6	2013	Consistent with this view, high expression alleles of the major enzymatic source of bilirubin, heme oxygenase-1 (HO-1), do associate with decreased vascular risk in the majority of studies that have addressed this issue, and increased plasma bilirubin has been reported in carriers of these alleles.	Bilirubin	84-93	heme oxygenase 1	Homo sapiens	95-111
23347118-4	2013	EXPERIMENTAL APPROACH: The aim of this study was to analyse the effects of AEA or FAAH inhibition by the URB597 inhibitor or FAAH/siRNA on the activation of Nrf2-ARE signalling pathway and heme oxygenase-1 (HO-1) induction and transcription.	aea	75-78	heme oxygenase 1	Homo sapiens	189-205
23347118-4	2013	EXPERIMENTAL APPROACH: The aim of this study was to analyse the effects of AEA or FAAH inhibition by the URB597 inhibitor or FAAH/siRNA on the activation of Nrf2-ARE signalling pathway and heme oxygenase-1 (HO-1) induction and transcription.	aea	75-78	heme oxygenase 1	Homo sapiens	207-211
23347118-7	2013	We found that inhibition of FAAH by the URB597 inhibitor induced antioxidant HO-1 in breast cancer cells and MCF-10A cells.	cyclohexyl carbamic acid 3'-carbamoylbiphenyl-3-yl ester	40-46	heme oxygenase 1	Homo sapiens	77-81
23347118-9	2013	Furthermore, URB597, AEA and siRNA-FAAH treatments induced the nuclear translocation of Nrf2, while siRNA-Nrf2 treatment and Keap1 expression blocked AEA, URB597 and si-FAAH from activation of ARE reporter and HO-1 induction.	cyclohexyl carbamic acid 3'-carbamoylbiphenyl-3-yl ester	13-19	heme oxygenase 1	Homo sapiens	210-214
23347118-9	2013	Furthermore, URB597, AEA and siRNA-FAAH treatments induced the nuclear translocation of Nrf2, while siRNA-Nrf2 treatment and Keap1 expression blocked AEA, URB597 and si-FAAH from activation of ARE reporter and HO-1 induction.	aea	150-153	heme oxygenase 1	Homo sapiens	210-214
23347118-9	2013	Furthermore, URB597, AEA and siRNA-FAAH treatments induced the nuclear translocation of Nrf2, while siRNA-Nrf2 treatment and Keap1 expression blocked AEA, URB597 and si-FAAH from activation of ARE reporter and HO-1 induction.	cyclohexyl carbamic acid 3'-carbamoylbiphenyl-3-yl ester	155-161	heme oxygenase 1	Homo sapiens	210-214
23347118-11	2013	CONCLUSIONS AND IMPLICATIONS: These data uncovered a novel mechanism by which inhibition of FAAH or exposure to AEA induced HO-1 transcripts and implicating AEA and FAAH as direct modifiers in signalling mediated activation of Nrf2-HO-1 pathway, independent of cannabinoid receptors.	aea	112-115	heme oxygenase 1	Homo sapiens	124-128
23347118-11	2013	CONCLUSIONS AND IMPLICATIONS: These data uncovered a novel mechanism by which inhibition of FAAH or exposure to AEA induced HO-1 transcripts and implicating AEA and FAAH as direct modifiers in signalling mediated activation of Nrf2-HO-1 pathway, independent of cannabinoid receptors.	aea	112-115	heme oxygenase 1	Homo sapiens	232-236
23347118-11	2013	CONCLUSIONS AND IMPLICATIONS: These data uncovered a novel mechanism by which inhibition of FAAH or exposure to AEA induced HO-1 transcripts and implicating AEA and FAAH as direct modifiers in signalling mediated activation of Nrf2-HO-1 pathway, independent of cannabinoid receptors.	aea	157-160	heme oxygenase 1	Homo sapiens	124-128
23347118-11	2013	CONCLUSIONS AND IMPLICATIONS: These data uncovered a novel mechanism by which inhibition of FAAH or exposure to AEA induced HO-1 transcripts and implicating AEA and FAAH as direct modifiers in signalling mediated activation of Nrf2-HO-1 pathway, independent of cannabinoid receptors.	aea	157-160	heme oxygenase 1	Homo sapiens	232-236
23813560-3	2013	This study assessed the association between the length of guanosine thymidine dinucleotide repeats in the heme oxygenase-1 gene microsatellite promoter and cardiovascular events and mortality among hemodialysis patients.	guanosine thymidine dinucleotide	58-90	heme oxygenase 1	Homo sapiens	106-122
23813560-5	2013	The allelic frequencies of the length of guanosine thymidine dinucleotide repeats (the S allele represents shorter [&lt;27] repeats, and the L allele represents longer [&gt;= 27] repeats) in the heme oxygenase-1 gene promoter were analyzed in 1080 unrelated chronic hemodialysis patients and 365 healthy controls for distribution comparison.	guanosine thymidine dinucleotide	41-73	heme oxygenase 1	Homo sapiens	195-211
23813560-12	2013	CONCLUSIONS: Chronic hemodialysis patients with longer lengths of guanosine thymidine dinucleotide repeats in the heme oxygenase-1 gene promoter exhibit higher inflammation and oxidative stress.	guanosine thymidine dinucleotide	66-98	heme oxygenase 1	Homo sapiens	114-130
22593043-3	2013	We found that the endogenous expression of Nrf2 as well as its target proteins heme oxygenase-1 (HO-1), NADP(H):quinone oxidoreductase (NQO) in MCF-7/DOX cells was higher than that in MCF-7 cells.	Doxorubicin	150-153	heme oxygenase 1	Homo sapiens	79-95
22593043-3	2013	We found that the endogenous expression of Nrf2 as well as its target proteins heme oxygenase-1 (HO-1), NADP(H):quinone oxidoreductase (NQO) in MCF-7/DOX cells was higher than that in MCF-7 cells.	Doxorubicin	150-153	heme oxygenase 1	Homo sapiens	97-101
22593043-4	2013	Tert-butylhydroquinone treatment increased the expression Nrf2, HO-1, and NQO-1, and enhanced resistance of MCF-7 cells to DOX.	2-tert-butylhydroquinone	0-22	heme oxygenase 1	Homo sapiens	64-68
23872045-4	2013	The mRNA expression levels of detoxifying, NQO1, HO-1, GSTA1, MT-1, and HSP70, were significantly decreased in all heavy metal-exposed group as compared to control group.	Metals	121-126	heme oxygenase 1	Homo sapiens	49-53
23759444-4	2013	Xenon exposure enhanced the expression of heat-shock protein 70 (HSP-70) and heme oxygenase 1 (HO-1) and promoted cell survival after hypothermia-hypoxia insult in human proximal tubular (HK-2) cells, which was abolished by HSP-70 or HO-1 siRNA.	Xenon	0-5	heme oxygenase 1	Homo sapiens	77-93
23759444-4	2013	Xenon exposure enhanced the expression of heat-shock protein 70 (HSP-70) and heme oxygenase 1 (HO-1) and promoted cell survival after hypothermia-hypoxia insult in human proximal tubular (HK-2) cells, which was abolished by HSP-70 or HO-1 siRNA.	Xenon	0-5	heme oxygenase 1	Homo sapiens	95-99
23759444-4	2013	Xenon exposure enhanced the expression of heat-shock protein 70 (HSP-70) and heme oxygenase 1 (HO-1) and promoted cell survival after hypothermia-hypoxia insult in human proximal tubular (HK-2) cells, which was abolished by HSP-70 or HO-1 siRNA.	Xenon	0-5	heme oxygenase 1	Homo sapiens	234-238
23850497-1	2013	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that is induced by intraplaque hemorrhage and degrades free heme and releases ferrous iron, which is rapidly sequestered by ferritin.	Heme	111-115	heme oxygenase 1	Homo sapiens	0-16
23850497-1	2013	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that is induced by intraplaque hemorrhage and degrades free heme and releases ferrous iron, which is rapidly sequestered by ferritin.	Heme	111-115	heme oxygenase 1	Homo sapiens	18-22
23850497-1	2013	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that is induced by intraplaque hemorrhage and degrades free heme and releases ferrous iron, which is rapidly sequestered by ferritin.	Iron	137-141	heme oxygenase 1	Homo sapiens	0-16
23850497-1	2013	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that is induced by intraplaque hemorrhage and degrades free heme and releases ferrous iron, which is rapidly sequestered by ferritin.	Iron	137-141	heme oxygenase 1	Homo sapiens	18-22
23932761-6	2013	Consistent with this view, high expression alleles of the major enzymatic source of bilirubin, heme oxygenase-1 (HO-1), do associate with decreased vascular risk in the majority of studies that have addressed this issue, and increased plasma bilirubin has been reported in carriers of these alleles.	Bilirubin	242-251	heme oxygenase 1	Homo sapiens	95-111
24003391-12	2013	CONCLUSIONS: AKAP plays an important role in PGE2 regulation of COX-2 expression, and the suppression of HO-1 by PGE2-cAMP-PKA-AKAP signaling helps potentiate the LPS-induced COX-2 expression through a positive feedback loop in RAW 264.7 macrophages.	Dinoprostone	113-117	heme oxygenase 1	Homo sapiens	105-109
23824679-0	2013	Role of HO-1 in the arsenite-induced neurotoxicity in primary cultured cortical neurons.	arsenite	20-28	heme oxygenase 1	Homo sapiens	8-12
23824679-1	2013	In the present study, the role of heme oxygenase (HO)-1 in sodium arsenite (arsenite)-induced neurotoxicity was investigated using primary cultured cortical neurons.	sodium arsenite	59-74	heme oxygenase 1	Homo sapiens	34-55
23824679-1	2013	In the present study, the role of heme oxygenase (HO)-1 in sodium arsenite (arsenite)-induced neurotoxicity was investigated using primary cultured cortical neurons.	arsenite	66-74	heme oxygenase 1	Homo sapiens	34-55
23824679-5	2013	Western blot assay showed that arsenite significantly increased HO-1 levels, a redox-regulated protein.	arsenite	31-39	heme oxygenase 1	Homo sapiens	64-68
23824679-6	2013	Co-incubation with glutathione (10 mM) attenuated arsenite-induced HO-1 elevation and caspase 3 activation, suggesting that oxidative stress is involved in the arsenite-induced neurotoxicity.	Glutathione	19-30	heme oxygenase 1	Homo sapiens	67-71
23824679-6	2013	Co-incubation with glutathione (10 mM) attenuated arsenite-induced HO-1 elevation and caspase 3 activation, suggesting that oxidative stress is involved in the arsenite-induced neurotoxicity.	arsenite	50-58	heme oxygenase 1	Homo sapiens	67-71
23824679-7	2013	The neurotoxic effects of inorganic arsenics were compared; arsenite was more potent than arsenate in inducing HO-1 expression and caspase 3 activation.	arsenite	60-68	heme oxygenase 1	Homo sapiens	111-115
23824679-7	2013	The neurotoxic effects of inorganic arsenics were compared; arsenite was more potent than arsenate in inducing HO-1 expression and caspase 3 activation.	arsenic acid	90-98	heme oxygenase 1	Homo sapiens	111-115
23824679-9	2013	HO-1 siRNA transfection was employed to prevent arsenite-induced HO-1 elevation.	arsenite	48-56	heme oxygenase 1	Homo sapiens	0-4
24003391-5	2013	METHODS: We explored the involvement of HO-1 on PGE2 regulation of LPS-induced COX-2 expression in RAW 264.7 macrophages.	Dinoprostone	48-52	heme oxygenase 1	Homo sapiens	40-44
24003391-10	2013	In addition, HO-1 induction by the HO activator copper protoporphyrin suppressed LPS-induced COX-2 expression, which was restored by the addition of exogenous PGE2.	Copper	48-54	heme oxygenase 1	Homo sapiens	13-17
24003391-10	2013	In addition, HO-1 induction by the HO activator copper protoporphyrin suppressed LPS-induced COX-2 expression, which was restored by the addition of exogenous PGE2.	protoporphyrin IX	55-69	heme oxygenase 1	Homo sapiens	13-17
24003391-10	2013	In addition, HO-1 induction by the HO activator copper protoporphyrin suppressed LPS-induced COX-2 expression, which was restored by the addition of exogenous PGE2.	Dinoprostone	159-163	heme oxygenase 1	Homo sapiens	13-17
23824679-9	2013	HO-1 siRNA transfection was employed to prevent arsenite-induced HO-1 elevation.	arsenite	48-56	heme oxygenase 1	Homo sapiens	65-69
23824679-10	2013	At the same time, arsenite-induced caspase 3 activation and neuronal death were attenuated in the HO-1 siRNA-transfected cells.	arsenite	18-26	heme oxygenase 1	Homo sapiens	98-102
23824679-11	2013	Taken together, HO-1 appears to be neuroprotective in the arsenite-induced neurotoxicity in primary cultured cortical neurons.	arsenite	58-66	heme oxygenase 1	Homo sapiens	16-20
23824679-12	2013	In addition to antioxidants, HO-1 elevation may be a neuroprotective strategy for arsenite-induced neurotoxicity.	arsenite	82-90	heme oxygenase 1	Homo sapiens	29-33
24046187-0	2013	S-adenosyl methionine prevents endothelial dysfunction by inducing heme oxygenase-1 in vascular endothelial cells.	Sulfur	0-1	heme oxygenase 1	Homo sapiens	67-83
24046187-0	2013	S-adenosyl methionine prevents endothelial dysfunction by inducing heme oxygenase-1 in vascular endothelial cells.	S-Adenosylmethionine	2-21	heme oxygenase 1	Homo sapiens	67-83
24003391-12	2013	CONCLUSIONS: AKAP plays an important role in PGE2 regulation of COX-2 expression, and the suppression of HO-1 by PGE2-cAMP-PKA-AKAP signaling helps potentiate the LPS-induced COX-2 expression through a positive feedback loop in RAW 264.7 macrophages.	Cyclic AMP	118-122	heme oxygenase 1	Homo sapiens	105-109
23617628-6	2013	Carbon monoxide was a mediator of HMOX1 effects on proliferation, migration, and miR-378 expression.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	34-39
23867390-1	2013	A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2).	1,2,4-triazole	60-74	heme oxygenase 1	Homo sapiens	129-145
23867390-0	2013	Evaluation of novel aryloxyalkyl derivatives of imidazole and 1,2,4-triazole as heme oxygenase-1 (HO-1) inhibitors and their antitumor properties.	imidazole	48-57	heme oxygenase 1	Homo sapiens	80-96
23867390-1	2013	A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2).	1,2,4-triazole	60-74	heme oxygenase 1	Homo sapiens	147-151
23867390-0	2013	Evaluation of novel aryloxyalkyl derivatives of imidazole and 1,2,4-triazole as heme oxygenase-1 (HO-1) inhibitors and their antitumor properties.	imidazole	48-57	heme oxygenase 1	Homo sapiens	98-102
23867390-2	2013	Some of these compounds were found to be good inhibitors of HO-1, in particular those carrying an imidazole moiety as azolyl group and a 3-bromo or 4-iodophenyl as aryl moiety.	imidazole	98-107	heme oxygenase 1	Homo sapiens	60-64
23867390-0	2013	Evaluation of novel aryloxyalkyl derivatives of imidazole and 1,2,4-triazole as heme oxygenase-1 (HO-1) inhibitors and their antitumor properties.	1,2,4-triazole	62-76	heme oxygenase 1	Homo sapiens	80-96
22609818-0	2013	Genetic polymorphisms of HO-1 and COX-1 are associated with aspirin resistance defined by light transmittance aggregation in Chinese Han patients.	Aspirin	60-67	heme oxygenase 1	Homo sapiens	25-29
23867390-0	2013	Evaluation of novel aryloxyalkyl derivatives of imidazole and 1,2,4-triazole as heme oxygenase-1 (HO-1) inhibitors and their antitumor properties.	1,2,4-triazole	62-76	heme oxygenase 1	Homo sapiens	98-102
23867390-1	2013	A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2).	imidazole	46-55	heme oxygenase 1	Homo sapiens	129-145
23867390-1	2013	A novel series of aryloxyalkyl derivatives of imidazole and 1,2,4-triazole, 17-31, was designed and synthesized as inhibitors of heme oxygenase-1 (HO-1) and heme oxygenase-2 (HO-2).	imidazole	46-55	heme oxygenase 1	Homo sapiens	147-151
23817544-2	2013	Of interest, thyroid cancer cell lines can have upregulation of the carbon monoxide-producing enzyme, hemeoxygenase-1.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	102-117
23817544-5	2013	This initial observation serves as a rationale to further investigate the role played by hemeoxygenase-1 upregulation in the setting of cancers associated with increased endogenous carbon monoxide production.	Carbon Monoxide	181-196	heme oxygenase 1	Homo sapiens	89-104
22609818-1	2013	BACKGROUND: Cyclooxygenase 1 (COX-1), COX-2, and HO-1 are involved in the process of aspirin"s effect.	Aspirin	85-92	heme oxygenase 1	Homo sapiens	49-53
22609818-10	2013	HO-1 rs2071746 (-413A&gt;T) is associated with AR.	Argon	47-49	heme oxygenase 1	Homo sapiens	0-4
25337552-3	2013	In the present study, the cytoprotective effects of morin (3,5,7,2",4"-pentahydroxyflavone), in terms of HO-1 enzyme, against the oxidative stress and its involved mechanisms was elucidated.	morin	59-90	heme oxygenase 1	Homo sapiens	105-109
23712098-0	2013	Lucidone protects human skin keratinocytes against free radical-induced oxidative damage and inflammation through the up-regulation of HO-1/Nrf2 antioxidant genes and down-regulation of NF-kappaB signaling pathway.	lucidone	0-8	heme oxygenase 1	Homo sapiens	135-139
23729024-0	2013	Effectiveness of miltefosine treatment in targeting anti-leishmanial HO-1/Nrf-2-mediated oxidative responses in visceral leishmaniasis patients.	miltefosine	17-28	heme oxygenase 1	Homo sapiens	69-73
23729024-3	2013	We aimed to investigate the role of miltefosine in regulating HO-1/Nrf-2-mediated oxidative responses in visceral leishmaniasis (VL) patients in vivo and in vitro.	miltefosine	36-47	heme oxygenase 1	Homo sapiens	62-66
23729024-7	2013	The in vitro HO-1/Nrf-2-dependent anti-leishmanial effect of miltefosine was assessed by the use of specific inhibitors/inducers and subsequent microscopic measurement of parasite killing and Th1/Th2 cytokine regulation by ELISA.	miltefosine	61-72	heme oxygenase 1	Homo sapiens	13-17
23729024-8	2013	RESULTS: Increased levels of transcript and serum HO-1, Nrf-2 nuclear translocation, serum bilirubin, GPx and SOD activity in untreated VL patients were reversed after miltefosine chemotherapy.	miltefosine	168-179	heme oxygenase 1	Homo sapiens	50-54
23729024-9	2013	The effectiveness of miltefosine for positive induction of ROS via NADPH correlated with a decrease in HO-1/ERK/Nrf-2-dependent parasite load.	miltefosine	21-32	heme oxygenase 1	Homo sapiens	103-107
23729024-9	2013	The effectiveness of miltefosine for positive induction of ROS via NADPH correlated with a decrease in HO-1/ERK/Nrf-2-dependent parasite load.	Reactive Oxygen Species	59-62	heme oxygenase 1	Homo sapiens	103-107
23729024-9	2013	The effectiveness of miltefosine for positive induction of ROS via NADPH correlated with a decrease in HO-1/ERK/Nrf-2-dependent parasite load.	NADP	67-72	heme oxygenase 1	Homo sapiens	103-107
23729024-10	2013	Furthermore, HO-1 blockade by miltefosine led to suppression of interleukin-10 and transforming growth factor-beta, but enhanced interleukin-12 and tumour necrosis factor-alpha production, in VL patients.	miltefosine	30-41	heme oxygenase 1	Homo sapiens	13-17
23712098-0	2013	Lucidone protects human skin keratinocytes against free radical-induced oxidative damage and inflammation through the up-regulation of HO-1/Nrf2 antioxidant genes and down-regulation of NF-kappaB signaling pathway.	Free Radicals	51-63	heme oxygenase 1	Homo sapiens	135-139
23712098-3	2013	Notably, the antioxidant potential of lucidone was directly correlated with the increased expression of an antioxidant gene, heme oxygenase 1 (HO-1), which was followed by the augmentation of the nuclear translocation and transcriptional activation of NF-E2-related factor-2 (Nrf2), with or without AAPH.	lucidone	38-46	heme oxygenase 1	Homo sapiens	125-141
23712098-3	2013	Notably, the antioxidant potential of lucidone was directly correlated with the increased expression of an antioxidant gene, heme oxygenase 1 (HO-1), which was followed by the augmentation of the nuclear translocation and transcriptional activation of NF-E2-related factor-2 (Nrf2), with or without AAPH.	lucidone	38-46	heme oxygenase 1	Homo sapiens	143-147
25337552-9	2013	HO-1 inhibitor ZnPP attenuated the protective effect of morin against H2O2-induced cytotoxicity.	zinc protoporphyrin	15-19	heme oxygenase 1	Homo sapiens	0-4
25337552-9	2013	HO-1 inhibitor ZnPP attenuated the protective effect of morin against H2O2-induced cytotoxicity.	Hydrogen Peroxide	70-74	heme oxygenase 1	Homo sapiens	0-4
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Heme	60-64	heme oxygenase 1	Homo sapiens	0-16
23661026-0	2013	Overexpression of Smad7 suppressed ROS/MMP9-dependent collagen synthesis through regulation of heme oxygenase-1.	Reactive Oxygen Species	35-38	heme oxygenase 1	Homo sapiens	95-111
23661026-6	2013	Further investigation showed that Smad7 regulated NADPH-mediated ROS production through activating Heme oxygenase-1 (HO-1).	NADP	50-55	heme oxygenase 1	Homo sapiens	99-115
23661026-6	2013	Further investigation showed that Smad7 regulated NADPH-mediated ROS production through activating Heme oxygenase-1 (HO-1).	NADP	50-55	heme oxygenase 1	Homo sapiens	117-121
23661026-6	2013	Further investigation showed that Smad7 regulated NADPH-mediated ROS production through activating Heme oxygenase-1 (HO-1).	Reactive Oxygen Species	65-68	heme oxygenase 1	Homo sapiens	99-115
23661026-6	2013	Further investigation showed that Smad7 regulated NADPH-mediated ROS production through activating Heme oxygenase-1 (HO-1).	Reactive Oxygen Species	65-68	heme oxygenase 1	Homo sapiens	117-121
23661026-8	2013	Knockdown of HO-1 in Smad7-overexpressed cardiac fibroblasts or cells pretreated with SnPP IX, a competitive inhibitor of HO-1 activity, resulted in increased productions of ROS and NADPH p47(phox), and abolished the inhibitory effects of Smad7 on MMP9 activity and collagen expression.	tin protoporphyrin IX	86-93	heme oxygenase 1	Homo sapiens	13-17
23661026-8	2013	Knockdown of HO-1 in Smad7-overexpressed cardiac fibroblasts or cells pretreated with SnPP IX, a competitive inhibitor of HO-1 activity, resulted in increased productions of ROS and NADPH p47(phox), and abolished the inhibitory effects of Smad7 on MMP9 activity and collagen expression.	tin protoporphyrin IX	86-93	heme oxygenase 1	Homo sapiens	122-126
23661026-8	2013	Knockdown of HO-1 in Smad7-overexpressed cardiac fibroblasts or cells pretreated with SnPP IX, a competitive inhibitor of HO-1 activity, resulted in increased productions of ROS and NADPH p47(phox), and abolished the inhibitory effects of Smad7 on MMP9 activity and collagen expression.	Reactive Oxygen Species	174-177	heme oxygenase 1	Homo sapiens	13-17
23707609-9	2013	The inactivation of AMPK by siRNA, DN-AMPK or the pharmacological AMPK inhibitor compound C, revealed that metformin reduced HO-1 expression in an AMPK-independent manner.	Metformin	107-116	heme oxygenase 1	Homo sapiens	125-129
23661026-8	2013	Knockdown of HO-1 in Smad7-overexpressed cardiac fibroblasts or cells pretreated with SnPP IX, a competitive inhibitor of HO-1 activity, resulted in increased productions of ROS and NADPH p47(phox), and abolished the inhibitory effects of Smad7 on MMP9 activity and collagen expression.	4-ethoxymethylene-2-phenyl-2-oxazoline-5-one	192-196	heme oxygenase 1	Homo sapiens	13-17
23707609-0	2013	Metformin inhibits heme oxygenase-1 expression in cancer cells through inactivation of Raf-ERK-Nrf2 signaling and AMPK-independent pathways.	Metformin	0-9	heme oxygenase 1	Homo sapiens	19-35
23707609-4	2013	In this study, we tested the hypothesis that the anti-tumor effects of metformin are mediated by suppression of HO-1 expression in cancer cells.	Metformin	71-80	heme oxygenase 1	Homo sapiens	112-116
23707609-5	2013	Our results indicate that metformin strongly suppresses HO-1 mRNA and protein expression in human hepatic carcinoma HepG2, cervical cancer HeLa, and non-small-cell lung cancer A549 cells.	Metformin	26-35	heme oxygenase 1	Homo sapiens	56-60
23878198-8	2013	Overexpression of PtGR-1 in HEK293T cells promoted nitroalkene metabolism to inactive nitroalkanes, an effect that abrogated the Nrf2-dependent induction of heme oxygenase-1 expression by nitro-oleic acid.	nitro-oleic acid	188-204	heme oxygenase 1	Homo sapiens	157-173
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Heme	60-64	heme oxygenase 1	Homo sapiens	18-22
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Heme	60-64	heme oxygenase 1	Homo sapiens	207-211
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Biliverdine	128-138	heme oxygenase 1	Homo sapiens	0-16
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Biliverdine	128-138	heme oxygenase 1	Homo sapiens	18-22
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Biliverdine	128-138	heme oxygenase 1	Homo sapiens	207-211
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Iron	167-171	heme oxygenase 1	Homo sapiens	0-16
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Iron	167-171	heme oxygenase 1	Homo sapiens	18-22
23714423-2	2013	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme.	Iron	167-171	heme oxygenase 1	Homo sapiens	207-211
23720344-2	2013	Interestingly, the antioxidant enzyme heme oxygenase-1 (HO-1) is not present in the mitochondria despite the fact that the organelle is the site of heme synthesis and contains multiple heme proteins.	Heme	38-42	heme oxygenase 1	Homo sapiens	56-60
23720344-2	2013	Interestingly, the antioxidant enzyme heme oxygenase-1 (HO-1) is not present in the mitochondria despite the fact that the organelle is the site of heme synthesis and contains multiple heme proteins.	Heme	148-152	heme oxygenase 1	Homo sapiens	56-60
23720344-9	2013	Furthermore, decrement in production of tricarboxylic acid cycle intermediates following hypoxia was significantly mitigated in Mito-HO-1 cells.	Tricarboxylic Acids	40-58	heme oxygenase 1	Homo sapiens	133-137
23720344-10	2013	These data suggest that specific mitochondrially targeted HO-1 under acute pathological conditions may have beneficial effects, but the selective advantage of long-term expression is constrained by a negative impact on the synthesis of heme-containing mitochondrial proteins.	Heme	236-240	heme oxygenase 1	Homo sapiens	58-62
23707273-0	2013	Peroxisome proliferator-activated receptor-gamma agonist rosiglitazone attenuates inflammatory pain through the induction of heme oxygenase-1 in macrophages.	Rosiglitazone	57-70	heme oxygenase 1	Homo sapiens	125-141
23615401-8	2013	HO-1 end products, such as carbon monoxide, free iron and bilirubin, suppressed the TPA-induced MMP-9 mRNA and protein expression, enzyme activity, migration and invasion in MCF-7 cells.	Carbon Monoxide	27-42	heme oxygenase 1	Homo sapiens	0-4
23615401-8	2013	HO-1 end products, such as carbon monoxide, free iron and bilirubin, suppressed the TPA-induced MMP-9 mRNA and protein expression, enzyme activity, migration and invasion in MCF-7 cells.	Iron	49-53	heme oxygenase 1	Homo sapiens	0-4
23615401-8	2013	HO-1 end products, such as carbon monoxide, free iron and bilirubin, suppressed the TPA-induced MMP-9 mRNA and protein expression, enzyme activity, migration and invasion in MCF-7 cells.	Bilirubin	58-67	heme oxygenase 1	Homo sapiens	0-4
23615401-8	2013	HO-1 end products, such as carbon monoxide, free iron and bilirubin, suppressed the TPA-induced MMP-9 mRNA and protein expression, enzyme activity, migration and invasion in MCF-7 cells.	Tetradecanoylphorbol Acetate	84-87	heme oxygenase 1	Homo sapiens	0-4
23615401-9	2013	Furthermore, TPA-induced extracellular signal-regulated kinase (ERK) 1/2 and Akt phosphorylation and the DNA binding activity of activator protein-1 (AP-1) and nuclear factor-kappa B (NF-kappaB) were attenuated by pretreatment with AP and HO-1 end products.	Tetradecanoylphorbol Acetate	13-16	heme oxygenase 1	Homo sapiens	239-243
23615401-11	2013	Additionally, induction of HO-1 expression is at least partially involved in the inhibition of TPA-induced MMP-9 activation and cell migration in MCF-7 cells by AP.	Tetradecanoylphorbol Acetate	95-98	heme oxygenase 1	Homo sapiens	27-31
23624303-0	2013	Immuno-spin trapping of heme-induced protein radicals: Implications for heme oxygenase-1 induction and heme degradation.	Heme	24-28	heme oxygenase 1	Homo sapiens	72-88
23624303-3	2013	Heme is known to induce heme oxygenase-1(HO-1) expression, and the extent of induction depends on the ratio of albumin to heme in plasma.	Heme	0-4	heme oxygenase 1	Homo sapiens	24-40
23732814-3	2013	Therefore, we generated mice with cardiac-specific, tamoxifen (TAM)-inducible overexpression of a human HO-1 (hHO-1) transgene (myosin heavy chain (MHC)-HO-1 mice) by breeding mice with cardiac-specific expression of a TAM-inducible Cre recombinase (MHC-Cre mice), with mice containing an hHO-1 transgene preceded by a floxed-stop signal.	Tamoxifen	52-61	heme oxygenase 1	Homo sapiens	104-126
23732814-3	2013	Therefore, we generated mice with cardiac-specific, tamoxifen (TAM)-inducible overexpression of a human HO-1 (hHO-1) transgene (myosin heavy chain (MHC)-HO-1 mice) by breeding mice with cardiac-specific expression of a TAM-inducible Cre recombinase (MHC-Cre mice), with mice containing an hHO-1 transgene preceded by a floxed-stop signal.	Tamoxifen	52-61	heme oxygenase 1	Homo sapiens	104-108
23732814-3	2013	Therefore, we generated mice with cardiac-specific, tamoxifen (TAM)-inducible overexpression of a human HO-1 (hHO-1) transgene (myosin heavy chain (MHC)-HO-1 mice) by breeding mice with cardiac-specific expression of a TAM-inducible Cre recombinase (MHC-Cre mice), with mice containing an hHO-1 transgene preceded by a floxed-stop signal.	Tamoxifen	63-66	heme oxygenase 1	Homo sapiens	104-126
23977989-0	2013	Curcumin ameliorates TNF-alpha-induced ICAM-1 expression and subsequent THP-1 adhesiveness via the induction of heme oxygenase-1 in the HaCaT cells.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	112-128
23977989-3	2013	Curcumin induced expression of heme oxygenase-1 (HO-1) in the human keratinocyte cell line HaCaT.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	31-47
23977989-3	2013	Curcumin induced expression of heme oxygenase-1 (HO-1) in the human keratinocyte cell line HaCaT.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	49-53
23977989-5	2013	Curcumin suppressed TNF-alpha- induced ICAM-1 expression and subsequent monocyte adhesion, which were reversed by the addition of tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, or HO-1 knockdown using siRNA.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	184-188
23977989-5	2013	Curcumin suppressed TNF-alpha- induced ICAM-1 expression and subsequent monocyte adhesion, which were reversed by the addition of tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, or HO-1 knockdown using siRNA.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	193-197
23977989-5	2013	Curcumin suppressed TNF-alpha- induced ICAM-1 expression and subsequent monocyte adhesion, which were reversed by the addition of tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, or HO-1 knockdown using siRNA.	tin protoporphyrin IX	130-151	heme oxygenase 1	Homo sapiens	184-188
23977989-5	2013	Curcumin suppressed TNF-alpha- induced ICAM-1 expression and subsequent monocyte adhesion, which were reversed by the addition of tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, or HO-1 knockdown using siRNA.	S-Nitroso-N-propionyl-D,L-penicillamine	153-157	heme oxygenase 1	Homo sapiens	184-188
23977989-7	2013	These results suggest that curcumin may exert its anti-inflammatory activity by suppressing the TNF-alpha-induced ICAM-1 expression and subsequent monocyte adhesion via expression of HO-1 in the keratinocytes.	Curcumin	27-35	heme oxygenase 1	Homo sapiens	183-187
23671274-2	2013	Here, we report regulation of T-type Ca(2+) channels by carbon monoxide (CO) a HO-1 by-product.	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	79-83
23732814-3	2013	Therefore, we generated mice with cardiac-specific, tamoxifen (TAM)-inducible overexpression of a human HO-1 (hHO-1) transgene (myosin heavy chain (MHC)-HO-1 mice) by breeding mice with cardiac-specific expression of a TAM-inducible Cre recombinase (MHC-Cre mice), with mice containing an hHO-1 transgene preceded by a floxed-stop signal.	Tamoxifen	63-66	heme oxygenase 1	Homo sapiens	104-108
24059059-0	2013	[The effect of heme oxygenase-1 on BMSCs damaged by high-concentration glucose].	Glucose	71-78	heme oxygenase 1	Homo sapiens	15-31
24059059-1	2013	This investigation was aimed to explore whether over-expression of 27heme oxygenase-1 (HO-1) could protect bone marrow mesenchymal stem cells(BMSCs)against injury induced by high-concentration glucose.	Glucose	193-200	heme oxygenase 1	Homo sapiens	69-85
21809430-5	2013	Our results showed that intracellular ROS were both dose- and time-dependent induced by inorganic arsenic; Cellular Nrf2 protein levels increased rapidly after 2 h of exposure, elevated significantly at 6 h, and reached the maximum at 12 h. The endogenous Nrf2-regulated downstream HO-1 mRNA and protein were also induced dramatically and lasted for as long as 24 h. In addition, intracellular GSH levels elevated in consistent with Nrf2 activation.	Reactive Oxygen Species	38-41	heme oxygenase 1	Homo sapiens	282-286
25206471-8	2013	Western blot and real-time PCR analysis showed that the Braintone-containing serum increased the levels of hypoxia-inducible factor 1alpha mRNA and protein, heme oxygenase-1 protein and vascular endothelial growth factor mRNA in oxygen-glucose deprived human umbilical vein endothelial cells.	braintone	56-65	heme oxygenase 1	Homo sapiens	157-173
25206471-8	2013	Western blot and real-time PCR analysis showed that the Braintone-containing serum increased the levels of hypoxia-inducible factor 1alpha mRNA and protein, heme oxygenase-1 protein and vascular endothelial growth factor mRNA in oxygen-glucose deprived human umbilical vein endothelial cells.	oxygen-glucose	229-243	heme oxygenase 1	Homo sapiens	157-173
23238643-7	2013	We demonstrated that early stage of exposure to IH-induced oxidative and inflammatory stresses leading to acceleration of cell apoptosis via NF-kappaB and Nrf2/HO-1 pathways in endothelial cells, suggesting the potential mechanisms for IH-induced vascular pathogenesis, in resemblance to OSA.	Ile-His	48-50	heme oxygenase 1	Homo sapiens	160-164
23238643-7	2013	We demonstrated that early stage of exposure to IH-induced oxidative and inflammatory stresses leading to acceleration of cell apoptosis via NF-kappaB and Nrf2/HO-1 pathways in endothelial cells, suggesting the potential mechanisms for IH-induced vascular pathogenesis, in resemblance to OSA.	Ile-His	236-238	heme oxygenase 1	Homo sapiens	160-164
23892599-6	2013	MgNPs-Fe3O4 induced the expression of heme oxygenase-1 at a concentration of 1 mug/mL, and in a dose-dependent manner.	mgnps	0-5	heme oxygenase 1	Homo sapiens	38-54
23892599-6	2013	MgNPs-Fe3O4 induced the expression of heme oxygenase-1 at a concentration of 1 mug/mL, and in a dose-dependent manner.	ferryl iron	6-11	heme oxygenase 1	Homo sapiens	38-54
23583297-6	2013	In contrast, DIM+SFN or TCDD+SFN induced NQO1 and HMOX1 mRNA expression to levels higher than SFN alone, which was prevented by RNAi-mediated knockdown of AHR.	dim+sfn	13-20	heme oxygenase 1	Homo sapiens	50-55
23583297-6	2013	In contrast, DIM+SFN or TCDD+SFN induced NQO1 and HMOX1 mRNA expression to levels higher than SFN alone, which was prevented by RNAi-mediated knockdown of AHR.	Polychlorinated Dibenzodioxins	24-28	heme oxygenase 1	Homo sapiens	50-55
23583297-6	2013	In contrast, DIM+SFN or TCDD+SFN induced NQO1 and HMOX1 mRNA expression to levels higher than SFN alone, which was prevented by RNAi-mediated knockdown of AHR.	sulforaphane	17-20	heme oxygenase 1	Homo sapiens	50-55
23583297-6	2013	In contrast, DIM+SFN or TCDD+SFN induced NQO1 and HMOX1 mRNA expression to levels higher than SFN alone, which was prevented by RNAi-mediated knockdown of AHR.	sulforaphane	29-32	heme oxygenase 1	Homo sapiens	50-55
23583297-7	2013	DIM+SFN but not TCDD+SFN also induced recruitment of ERalpha to NQO1 and HMOX1.	dim+sfn	0-7	heme oxygenase 1	Homo sapiens	73-78
23893806-5	2013	Peripheral blood mononuclear cells isolated from asthmatic patients and healthy controls were co-cultured with human bone marrow mesenchymal stem cells which were pretreated with Hemin (the revulsive of Heme Oxygenase-1), Protoporphyrin IX zinc (the inhibitor of Heme Oxygenase-1) and saline.	Hemin	179-184	heme oxygenase 1	Homo sapiens	203-219
23893806-5	2013	Peripheral blood mononuclear cells isolated from asthmatic patients and healthy controls were co-cultured with human bone marrow mesenchymal stem cells which were pretreated with Hemin (the revulsive of Heme Oxygenase-1), Protoporphyrin IX zinc (the inhibitor of Heme Oxygenase-1) and saline.	Hemin	179-184	heme oxygenase 1	Homo sapiens	263-279
23893806-6	2013	The expression of Heme Oxygenase-1 in MSCs was enhanced by Hemin and inhibited by Protoporphyrin  zinc in vitro.	Hemin	59-64	heme oxygenase 1	Homo sapiens	18-34
23893806-6	2013	The expression of Heme Oxygenase-1 in MSCs was enhanced by Hemin and inhibited by Protoporphyrin  zinc in vitro.	zinc protoporphyrin	82-102	heme oxygenase 1	Homo sapiens	18-34
23406266-8	2013	Induction of HO-1 by CoPP (cobalt protoporphyrin IX) reversed these IL-1beta actions.	cobaltiprotoporphyrin	21-25	heme oxygenase 1	Homo sapiens	13-17
23406266-8	2013	Induction of HO-1 by CoPP (cobalt protoporphyrin IX) reversed these IL-1beta actions.	cobaltiprotoporphyrin	27-51	heme oxygenase 1	Homo sapiens	13-17
21809430-0	2013	Sodium arsenite induced reactive oxygen species generation, nuclear factor (erythroid-2 related) factor 2 activation, heme oxygenase-1 expression, and glutathione elevation in Chang human hepatocytes.	sodium arsenite	0-15	heme oxygenase 1	Homo sapiens	118-134
21809430-5	2013	Our results showed that intracellular ROS were both dose- and time-dependent induced by inorganic arsenic; Cellular Nrf2 protein levels increased rapidly after 2 h of exposure, elevated significantly at 6 h, and reached the maximum at 12 h. The endogenous Nrf2-regulated downstream HO-1 mRNA and protein were also induced dramatically and lasted for as long as 24 h. In addition, intracellular GSH levels elevated in consistent with Nrf2 activation.	Arsenic	98-105	heme oxygenase 1	Homo sapiens	282-286
24152841-7	2013	Furthermore; iNOS and HO-1 expression and cytokines plasma levels were significantly higher in patients with ACHF as compared to controls group.	achf	109-113	heme oxygenase 1	Homo sapiens	22-26
23184650-0	2013	Akt/Nrf2 activated upregulation of heme oxygenase-1 involves in the role of Rg1 against ferrous iron-induced neurotoxicity in SK-N-SH cells.	Iron	96-100	heme oxygenase 1	Homo sapiens	35-51
23536331-10	2013	DJ-1 knockout astrocytes showed blunted ability to increase the expression of cellular protective mechanisms against oxidative stress mediated via Nrf-2 and HO-1 in response to exposure to 6-OHDA.	Oxidopamine	189-195	heme oxygenase 1	Homo sapiens	157-161
23184650-0	2013	Akt/Nrf2 activated upregulation of heme oxygenase-1 involves in the role of Rg1 against ferrous iron-induced neurotoxicity in SK-N-SH cells.	sk-n	126-130	heme oxygenase 1	Homo sapiens	35-51
24024172-5	2013	Interference with the supply of glucose or the pentose phosphate pathway and NADPH generation not only hampers Nrf2-mediated detoxification of reactive oxygen species on the enzyme level but also Nrf2-initiated expression of antioxidant defense proteins, such as glutathione reductase and heme-oxygenase1.	Glucose	32-39	heme oxygenase 1	Homo sapiens	289-304
22933385-0	2013	Sanguisorbae radix protects against 6-hydroxydopamine-induced neurotoxicity by regulating NADPH oxidase and NF-E2-related factor-2/heme oxygenase-1 expressions.	Oxidopamine	36-53	heme oxygenase 1	Homo sapiens	131-147
22933385-2	2013	The major mechanisms of protection against ROS-induced stress are inhibiting expression of ROS generating genes such as NADPH oxidase (NOX) and increasing expression of endogenous antioxidant genes such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	43-46	heme oxygenase 1	Homo sapiens	206-222
22933385-2	2013	The major mechanisms of protection against ROS-induced stress are inhibiting expression of ROS generating genes such as NADPH oxidase (NOX) and increasing expression of endogenous antioxidant genes such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	43-46	heme oxygenase 1	Homo sapiens	224-228
22933385-6	2013	SRE also abolished 6-OHDA-induced ROS by inhibiting NOX expression and by inducing HO-1 expression via NF-E2-related factor-2 activation.	Oxidopamine	19-25	heme oxygenase 1	Homo sapiens	83-87
24024172-5	2013	Interference with the supply of glucose or the pentose phosphate pathway and NADPH generation not only hampers Nrf2-mediated detoxification of reactive oxygen species on the enzyme level but also Nrf2-initiated expression of antioxidant defense proteins, such as glutathione reductase and heme-oxygenase1.	NADP	77-82	heme oxygenase 1	Homo sapiens	289-304
24024172-5	2013	Interference with the supply of glucose or the pentose phosphate pathway and NADPH generation not only hampers Nrf2-mediated detoxification of reactive oxygen species on the enzyme level but also Nrf2-initiated expression of antioxidant defense proteins, such as glutathione reductase and heme-oxygenase1.	Reactive Oxygen Species	143-166	heme oxygenase 1	Homo sapiens	289-304
23840483-4	2013	Since heme molecules are essential for the NADPH oxidase maturation and activity, we therefore investigated the consequences of the modulation of Heme oxygenase-1 (HO-1), the limiting enzyme in heme catabolism, on the IL-1beta signaling pathway and more specifically on Nox4 activity.	Heme	6-10	heme oxygenase 1	Homo sapiens	164-168
24024172-5	2013	Interference with the supply of glucose or the pentose phosphate pathway and NADPH generation not only hampers Nrf2-mediated detoxification of reactive oxygen species on the enzyme level but also Nrf2-initiated expression of antioxidant defense proteins, such as glutathione reductase and heme-oxygenase1.	Pentosephosphates	47-64	heme oxygenase 1	Homo sapiens	289-304
23840483-8	2013	Therefore, the downregulation of Nox4 activity by HO-1 induction appeared to be mediated by carbon monoxide (CO) generated from the heme degradation process.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	50-54
23840483-8	2013	Therefore, the downregulation of Nox4 activity by HO-1 induction appeared to be mediated by carbon monoxide (CO) generated from the heme degradation process.	Carbon Monoxide	109-111	heme oxygenase 1	Homo sapiens	50-54
23840483-8	2013	Therefore, the downregulation of Nox4 activity by HO-1 induction appeared to be mediated by carbon monoxide (CO) generated from the heme degradation process.	Heme	132-136	heme oxygenase 1	Homo sapiens	50-54
23604711-5	2013	The induction of HO-1 was preceded by a rise in reactive oxygen species (ROS) and Nrf2 protein expression.	Reactive Oxygen Species	48-71	heme oxygenase 1	Homo sapiens	17-21
23604711-5	2013	The induction of HO-1 was preceded by a rise in reactive oxygen species (ROS) and Nrf2 protein expression.	Reactive Oxygen Species	73-76	heme oxygenase 1	Homo sapiens	17-21
23604711-7	2013	In addition, the strain-mediated induction of HO-1 and activation of Nrf2 was abolished by the antioxidant N-acetyl-l-cysteine.	Acetylcysteine	107-126	heme oxygenase 1	Homo sapiens	46-50
23604711-10	2013	In conclusion, the present study demonstrates that a hemodynamically relevant level of cyclic strain stimulates HO-1 gene expression in ECs via the ROS-Nrf2 signaling pathway to inhibit EC death.	Reactive Oxygen Species	148-151	heme oxygenase 1	Homo sapiens	112-116
23665328-6	2013	Treatment of cells with HO-1 inhibitor SnPP IX (tin protoporphyrin IX) attenuated the LPS-mediated responses, HIV-1 replication and secretion of MIP1alpha, MIP1beta, and LD78beta chemokines with little change in surface CCR-5 expression.	tin protoporphyrin IX	39-46	heme oxygenase 1	Homo sapiens	24-28
23583009-7	2013	Ethanol-stimulated (100mM) CYP2E1 upregulation was suppressed by quercetin but further enhanced by HO-1 inhibition with resultant heme accumulation.	Heme	130-134	heme oxygenase 1	Homo sapiens	99-103
23583009-9	2013	CO donor dose-dependently inactivated CYP2E1 of ethanol-incubated microsome, which was mimicked by HO-1 substrate but abolished by CO scavenger.	Ethanol	48-55	heme oxygenase 1	Homo sapiens	99-103
23583009-10	2013	Thus, CYP2E1-mediated ethanol hepatotoxicity was alleviated by quercetin through HO-1 induction.	Ethanol	22-29	heme oxygenase 1	Homo sapiens	81-85
23583009-10	2013	Thus, CYP2E1-mediated ethanol hepatotoxicity was alleviated by quercetin through HO-1 induction.	Quercetin	63-72	heme oxygenase 1	Homo sapiens	81-85
23583009-2	2013	However, the precise mechanism by which quercetin counteracts CYP2E1-mediated ethanol hepatotoxicity through HO-1 system is still remained unclear.	Quercetin	40-49	heme oxygenase 1	Homo sapiens	109-113
23583009-2	2013	However, the precise mechanism by which quercetin counteracts CYP2E1-mediated ethanol hepatotoxicity through HO-1 system is still remained unclear.	Ethanol	78-85	heme oxygenase 1	Homo sapiens	109-113
23583009-5	2013	Our data showed that chronic ethanol over-activated CYP2E1 but suppressed HO-1 with concurrent hepatic oxidative damage, which was partially normalized by quercetin (100mg/kg.bw.).	Ethanol	29-36	heme oxygenase 1	Homo sapiens	74-78
23583009-5	2013	Our data showed that chronic ethanol over-activated CYP2E1 but suppressed HO-1 with concurrent hepatic oxidative damage, which was partially normalized by quercetin (100mg/kg.bw.).	Quercetin	155-164	heme oxygenase 1	Homo sapiens	74-78
23583009-6	2013	Quercetin (100 muM) induced HO-1 and depleted heme pool when incubated to human hepatocytes.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	28-32
23583009-7	2013	Ethanol-stimulated (100mM) CYP2E1 upregulation was suppressed by quercetin but further enhanced by HO-1 inhibition with resultant heme accumulation.	Ethanol	0-7	heme oxygenase 1	Homo sapiens	99-103
23665328-6	2013	Treatment of cells with HO-1 inhibitor SnPP IX (tin protoporphyrin IX) attenuated the LPS-mediated responses, HIV-1 replication and secretion of MIP1alpha, MIP1beta, and LD78beta chemokines with little change in surface CCR-5 expression.	tin protoporphyrin IX	48-69	heme oxygenase 1	Homo sapiens	24-28
23535287-7	2013	Our study indicated that treatment of HepG2 cells with CSA induces Nrf2-dependent ARE activity and gene expression of heme oxygenase-1 (HO-1), NAD(P)H quinone oxidoreductase 1 (NQO1), and glutamate-cysteine ligase modifier subunits by activation of PI3K/AKT, ERK and JNK signaling pathways.	3-hydroxy-4-prenyl-5-methoxystilbene-2-carboxylic acid	55-58	heme oxygenase 1	Homo sapiens	118-134
23525690-9	2013	Taken together, our results suggest that PM(2.5)-induced ROS may function as signaling molecules to activate Nrf2-mediated defenses, such as HO-1 expression, against oxidative stress induced by PM(2.5) through the PI3K/AKT signaling pathway.	Reactive Oxygen Species	57-60	heme oxygenase 1	Homo sapiens	141-145
23541843-7	2013	Furthermore, the inhibition of HO-1 activity, by tin mesoporphyrin, caused a complete restoration of MeHg-mediated inhibition of CYP1A1 activity, induced by TCDD.	tin mesoporphyrin	49-66	heme oxygenase 1	Homo sapiens	31-35
23541843-7	2013	Furthermore, the inhibition of HO-1 activity, by tin mesoporphyrin, caused a complete restoration of MeHg-mediated inhibition of CYP1A1 activity, induced by TCDD.	Polychlorinated Dibenzodioxins	157-161	heme oxygenase 1	Homo sapiens	31-35
23541843-8	2013	In addition, transfection of HepG2 cells with siRNA targeting the human HO-1 gene reversed the MeHg-mediated inhibition of TCDD-induced CYP1A1.	Polychlorinated Dibenzodioxins	123-127	heme oxygenase 1	Homo sapiens	72-76
23523860-0	2013	Zinc protoporphyrin suppresses cancer cell viability through a heme oxygenase-1-independent mechanism: the involvement of the Wnt/beta-catenin signaling pathway.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	63-79
23523860-1	2013	Zinc protoporphyrin (ZnPP), a known inhibitor of heme oxygenase-1 (HO-1), has been reported to have anticancer activity in both in vitro and in vivo model systems.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	49-65
23412940-6	2013	HO-1 expression was downregulated in cells treated with SB203580 and RAPA.	SB 203580	56-64	heme oxygenase 1	Homo sapiens	0-4
23412940-7	2013	HO-1 overexpression inhibited apoptosis and induced G2/M arrest in SB203580 and RAPA-treated cells.	SB 203580	67-75	heme oxygenase 1	Homo sapiens	0-4
23412940-8	2013	HO-1 expression was upregulated in the presence of ethanol, and was accompanied by activation of p38MAPK and mTOR.	Ethanol	51-58	heme oxygenase 1	Homo sapiens	0-4
23412940-9	2013	However, ethanol-treated cells exposed to HO-1 inhibitor showed no effect on p38MAPK and mTOR activation.	Ethanol	9-16	heme oxygenase 1	Homo sapiens	42-46
23523860-1	2013	Zinc protoporphyrin (ZnPP), a known inhibitor of heme oxygenase-1 (HO-1), has been reported to have anticancer activity in both in vitro and in vivo model systems.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	67-71
23523860-1	2013	Zinc protoporphyrin (ZnPP), a known inhibitor of heme oxygenase-1 (HO-1), has been reported to have anticancer activity in both in vitro and in vivo model systems.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	49-65
23523860-1	2013	Zinc protoporphyrin (ZnPP), a known inhibitor of heme oxygenase-1 (HO-1), has been reported to have anticancer activity in both in vitro and in vivo model systems.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	67-71
23523860-2	2013	While the mechanisms of ZnPP"s anticancer activity remain to be elucidated, it is generally believed that ZnPP suppresses tumor growth through inhibition of HO-1 activity.	zinc protoporphyrin	106-110	heme oxygenase 1	Homo sapiens	157-161
23523860-3	2013	We examined this hypothesis by altering cellular levels of HO-1 in human ovarian (A2780) and prostate cancer (DU145) cells and found that ZnPP inhibits cancer cell viability through an HO-1-independent mechanism.	zinc protoporphyrin	138-142	heme oxygenase 1	Homo sapiens	59-63
23523860-3	2013	We examined this hypothesis by altering cellular levels of HO-1 in human ovarian (A2780) and prostate cancer (DU145) cells and found that ZnPP inhibits cancer cell viability through an HO-1-independent mechanism.	zinc protoporphyrin	138-142	heme oxygenase 1	Homo sapiens	185-189
23523860-5	2013	Consistent with these observations, tin protoporphyrin (SnPP), a well-established HO-1 inhibitor, was found to be much less cytotoxic than ZnPP, and docosahexaenoic acid (DHA), an HO-1 inducer, enhanced ZnPP"s cytotoxicity.	tin protoporphyrin IX	36-54	heme oxygenase 1	Homo sapiens	82-86
23523860-5	2013	Consistent with these observations, tin protoporphyrin (SnPP), a well-established HO-1 inhibitor, was found to be much less cytotoxic than ZnPP, and docosahexaenoic acid (DHA), an HO-1 inducer, enhanced ZnPP"s cytotoxicity.	S-Nitroso-N-propionyl-D,L-penicillamine	56-60	heme oxygenase 1	Homo sapiens	82-86
23523860-5	2013	Consistent with these observations, tin protoporphyrin (SnPP), a well-established HO-1 inhibitor, was found to be much less cytotoxic than ZnPP, and docosahexaenoic acid (DHA), an HO-1 inducer, enhanced ZnPP"s cytotoxicity.	S-Nitroso-N-propionyl-D,L-penicillamine	56-60	heme oxygenase 1	Homo sapiens	180-184
23412940-10	2013	The data suggest that ethanol-induced upregulation of HO-1 in oesophageal squamous cell carcinoma is accompanied by the activation of the p38MAPK and mTOR pathways.	Ethanol	22-29	heme oxygenase 1	Homo sapiens	54-58
23536693-1	2013	Heme oxygenase-1 (HO-1) is a stress-inducible rate-limiting enzyme in heme degradation that confers cytoprotection against oxidative injury and performs a vital function in the maintenance of cell hemostasis.	Heme	70-74	heme oxygenase 1	Homo sapiens	0-16
23536693-1	2013	Heme oxygenase-1 (HO-1) is a stress-inducible rate-limiting enzyme in heme degradation that confers cytoprotection against oxidative injury and performs a vital function in the maintenance of cell hemostasis.	Heme	70-74	heme oxygenase 1	Homo sapiens	18-22
23536693-4	2013	Specific inhibitors of mitogen-activated protein kinases (MAPKs), SB203580, PD98059, and SP600125, significantly abolished HO-1 expression.	SB 203580	66-74	heme oxygenase 1	Homo sapiens	123-127
23536693-4	2013	Specific inhibitors of mitogen-activated protein kinases (MAPKs), SB203580, PD98059, and SP600125, significantly abolished HO-1 expression.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	76-83	heme oxygenase 1	Homo sapiens	123-127
23536693-4	2013	Specific inhibitors of mitogen-activated protein kinases (MAPKs), SB203580, PD98059, and SP600125, significantly abolished HO-1 expression.	pyrazolanthrone	89-97	heme oxygenase 1	Homo sapiens	123-127
23454680-0	2013	Role of alpha-synuclein aggregation and the nuclear factor E2-related factor 2/heme oxygenase-1 pathway in iron-induced neurotoxicity.	Iron	107-111	heme oxygenase 1	Homo sapiens	44-95
23454680-6	2013	Consistent with these results, knockdown of alpha-syn expression prevents reduction of Nrf2 and HO-1 by ferrous iron, eliminates alpha-syn aggregates, and protects SK-N-SH cells against ferrous iron-induced cell damage.	ferrous iron	104-116	heme oxygenase 1	Homo sapiens	96-100
23649692-0	2013	Reciprocal regulation of cyclooxygenase 2 and heme oxygenase 1 upon arsenic trioxide exposure in normal human lung fibroblast.	Arsenic Trioxide	68-84	heme oxygenase 1	Homo sapiens	46-62
23649692-1	2013	Detoxification enzyme heme oxygenase 1 (HO-1) and proinflammation enzyme cyclooxygenase 2 (Cox-2) are key response proteins that function to promote the survival of cells exposed to arsenic trioxide (ATO).	Arsenic Trioxide	182-198	heme oxygenase 1	Homo sapiens	22-38
23649692-1	2013	Detoxification enzyme heme oxygenase 1 (HO-1) and proinflammation enzyme cyclooxygenase 2 (Cox-2) are key response proteins that function to promote the survival of cells exposed to arsenic trioxide (ATO).	Arsenic Trioxide	182-198	heme oxygenase 1	Homo sapiens	40-44
23649692-1	2013	Detoxification enzyme heme oxygenase 1 (HO-1) and proinflammation enzyme cyclooxygenase 2 (Cox-2) are key response proteins that function to promote the survival of cells exposed to arsenic trioxide (ATO).	Arsenic Trioxide	200-203	heme oxygenase 1	Homo sapiens	22-38
23649692-1	2013	Detoxification enzyme heme oxygenase 1 (HO-1) and proinflammation enzyme cyclooxygenase 2 (Cox-2) are key response proteins that function to promote the survival of cells exposed to arsenic trioxide (ATO).	Arsenic Trioxide	200-203	heme oxygenase 1	Homo sapiens	40-44
23649692-3	2013	In this study, concomitant upregulation of Cox-2 and HO-1 induced by ATO was observed in normal human lung fibroblasts.	Arsenic Trioxide	69-72	heme oxygenase 1	Homo sapiens	53-57
23649692-4	2013	Cox-2 inhibitor NS398 suppressed the upregulation of HO-1, whereas HO-1 inhibitor protoporphyrin IX zinc (II) stimulated the expression of Cox-2.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	16-21	heme oxygenase 1	Homo sapiens	53-57
23649692-4	2013	Cox-2 inhibitor NS398 suppressed the upregulation of HO-1, whereas HO-1 inhibitor protoporphyrin IX zinc (II) stimulated the expression of Cox-2.	protoporphyrin IX	82-99	heme oxygenase 1	Homo sapiens	67-71
23649692-6	2013	Our results confirmed the reciprocal regulations between Cox-2 and HO-1 in ATO-treated normal cells and shed light on the understanding of protecting cells from injury caused by ATO while simultaneously decreasing the inflammation responses, which may be related to the carcinogenicity of ATO.	Arsenic Trioxide	75-78	heme oxygenase 1	Homo sapiens	67-71
23602216-1	2013	BACKGROUND: The glutathione thymidine repeats [(GT)n] of the heme oxygenase (HO)-1 gene promoter have been shown to be correlated with the incidence of coronary artery disease (CAD), patients with shorter repeats being less likely to have CAD.	glutathione thymidine	16-37	heme oxygenase 1	Homo sapiens	61-82
23454680-7	2013	Furthermore, increased HO-1 expression exerts a protective role against ferrous iron.	ferrous iron	72-84	heme oxygenase 1	Homo sapiens	23-27
23454680-8	2013	These results support a new hypothesis of synergistic alpha-syn/iron cytotoxicity, whereby ferrous iron induces alpha-syn aggregation and neurotoxicity by inhibiting Nrf2/HO-1.	Iron	64-68	heme oxygenase 1	Homo sapiens	171-175
23454680-3	2013	Here, we report that down-regulation of nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) may contribute to iron-induced alpha-syn aggregation.	Iron	128-132	heme oxygenase 1	Homo sapiens	86-102
23454680-8	2013	These results support a new hypothesis of synergistic alpha-syn/iron cytotoxicity, whereby ferrous iron induces alpha-syn aggregation and neurotoxicity by inhibiting Nrf2/HO-1.	ferrous iron	91-103	heme oxygenase 1	Homo sapiens	171-175
23454680-9	2013	Inhibition of Nrf2/HO-1 leads to more alpha-syn aggregation and greater toxicity induced by iron, creating a vicious cycle of iron accumulation, alpha-syn aggregation and HO-1 disruption in PD.	Iron	92-96	heme oxygenase 1	Homo sapiens	19-23
23454680-3	2013	Here, we report that down-regulation of nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) may contribute to iron-induced alpha-syn aggregation.	Iron	128-132	heme oxygenase 1	Homo sapiens	104-108
23454680-9	2013	Inhibition of Nrf2/HO-1 leads to more alpha-syn aggregation and greater toxicity induced by iron, creating a vicious cycle of iron accumulation, alpha-syn aggregation and HO-1 disruption in PD.	Iron	126-130	heme oxygenase 1	Homo sapiens	19-23
23454680-4	2013	In this study, we show that ferrous iron down-regulates Nrf2 and HO-1 in a time-dependent manner in SK-N-SH neuroblastoma cells.	ferrous iron	28-40	heme oxygenase 1	Homo sapiens	65-69
23454680-5	2013	Levels of both Nrf2 and HO-1 are decreased even more by ferrous iron in SK-N-SH cells that overexpress alpha-syn and results in greater cell toxicity.	ferrous iron	56-68	heme oxygenase 1	Homo sapiens	24-28
23535360-9	2013	Regression analysis revealed that ho-1 and nqo1 expressions were found to be associated with chemical sensitizer reactivity to cysteine, providing evidence of the importance of chemical reactivity, as a part of danger signals, in DC biology.	Cysteine	127-135	heme oxygenase 1	Homo sapiens	34-38
23307413-4	2013	Here, we found that multiple factors were released from brain astrocytes (RBA-1) exposed to BK in the conditioned culture media (BK-CM), including ROS, MMP-9, and heme oxygenase-1 (HO-1)/carbon monoxide (CO), leading to neuronal cell (SK-N-SH) death.	Carbon Monoxide	187-202	heme oxygenase 1	Homo sapiens	181-185
23307413-4	2013	Here, we found that multiple factors were released from brain astrocytes (RBA-1) exposed to BK in the conditioned culture media (BK-CM), including ROS, MMP-9, and heme oxygenase-1 (HO-1)/carbon monoxide (CO), leading to neuronal cell (SK-N-SH) death.	Carbon Monoxide	204-206	heme oxygenase 1	Homo sapiens	181-185
23691207-0	2013	Resveratrol protects C6 astrocyte cell line against hydrogen peroxide-induced oxidative stress through heme oxygenase 1.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	103-119
23691207-7	2013	Resveratrol per se increased heme oxygenase 1 (HO1) expression and extracellular GSH content.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	29-45
23691207-0	2013	Resveratrol protects C6 astrocyte cell line against hydrogen peroxide-induced oxidative stress through heme oxygenase 1.	Hydrogen Peroxide	52-69	heme oxygenase 1	Homo sapiens	103-119
23691207-7	2013	Resveratrol per se increased heme oxygenase 1 (HO1) expression and extracellular GSH content.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	47-50
27122714-2	2013	In the present study, we investigated if endothelial expression of cell adhesion molecules (CAMs) is inhibited by fenofibrate, a peroxisome proliferator-activated receptor alpha (PPARalpha) agonist with anti-inflammatory and vascular protective effects, through the regulation of heme oxygenase-1 (HO-1).	Fenofibrate	114-125	heme oxygenase 1	Homo sapiens	280-296
23691207-8	2013	In addition, HO1 signaling pathway is involved in the protective effect of resveratrol against H2O2-induced oxidative damage in astroglial cells.	Resveratrol	75-86	heme oxygenase 1	Homo sapiens	13-16
23691207-8	2013	In addition, HO1 signaling pathway is involved in the protective effect of resveratrol against H2O2-induced oxidative damage in astroglial cells.	Hydrogen Peroxide	95-99	heme oxygenase 1	Homo sapiens	13-16
22689053-7	2013	HO-1 downregulation in renal carcinoma cells induces a mitotic delay at G2/M phase by increasing the intracellular reactive oxygen species and the DNA-damage-induced checkpoint activation.	Reactive Oxygen Species	115-138	heme oxygenase 1	Homo sapiens	0-4
23583371-4	2013	Small interfering RNA (siRNA) for HO-1 was transfected into human RPE cell line ARPE-19, and zinc protoporphyrin (ZnPP) was used to inhibit HO-1 activity.	zinc protoporphyrin	93-112	heme oxygenase 1	Homo sapiens	140-144
27122714-0	2013	Fenofibrate Modulates HO-1 and Ameliorates Endothelial Expression of Cell Adhesion Molecules in Systolic Heart Failure.	Fenofibrate	0-11	heme oxygenase 1	Homo sapiens	22-26
27122714-2	2013	In the present study, we investigated if endothelial expression of cell adhesion molecules (CAMs) is inhibited by fenofibrate, a peroxisome proliferator-activated receptor alpha (PPARalpha) agonist with anti-inflammatory and vascular protective effects, through the regulation of heme oxygenase-1 (HO-1).	Fenofibrate	114-125	heme oxygenase 1	Homo sapiens	298-302
27122714-9	2013	Pretreatment with fenofibrate prevented the decrease of HO-1 expression and the activation of NF-kappaB as well as the increase of CAM expression that induced by HF patient serum.	Fenofibrate	18-29	heme oxygenase 1	Homo sapiens	56-60
27122714-10	2013	CONCLUSIONS: Our study demonstrated that fenofibrate may exert beneficial effects in patients with systolic HF through regulation of HO-1 expression and amelioration of endothelial activation.	Fenofibrate	41-52	heme oxygenase 1	Homo sapiens	133-137
23345623-1	2013	BACKGROUND: The objective of this study was to evaluate the interaction between the length polymorphism of the guanosine thymidine repeat [(GT)n] in the heme oxygenase-1 (HO-1) gene and far-infrared (FIR) therapy on access flow (Qa) and arteriovenous fistula (AVF) patency in hemodialysis (HD) patients.	guanosine thymidine	111-130	heme oxygenase 1	Homo sapiens	153-169
23524841-10	2013	CONCLUSIONS: In patients with chronic stable coronary disease, all clinically relevant daily doses of aspirin tested, from 81 to 1300 mg, produce similar and statistically significant increases in HO-1 and decreases in ADMA.	Aspirin	102-109	heme oxygenase 1	Homo sapiens	197-201
23288142-0	2013	Inhibition of matrix metalloproteinase-9 expression by docosahexaenoic acid mediated by heme oxygenase 1 in 12-O-tetradecanoylphorbol-13-acetate-induced MCF-7 human breast cancer cells.	Docosahexaenoic Acids	55-75	heme oxygenase 1	Homo sapiens	88-104
23288142-0	2013	Inhibition of matrix metalloproteinase-9 expression by docosahexaenoic acid mediated by heme oxygenase 1 in 12-O-tetradecanoylphorbol-13-acetate-induced MCF-7 human breast cancer cells.	Tetradecanoylphorbol Acetate	108-144	heme oxygenase 1	Homo sapiens	88-104
23261939-6	2013	The heme oxygenase-1 (HO-1) induction in response to H2O2 and MPP(+) treatment was impaired by the overexpression of the PINK1 P209A mutant.	Hydrogen Peroxide	53-57	heme oxygenase 1	Homo sapiens	4-20
23261939-6	2013	The heme oxygenase-1 (HO-1) induction in response to H2O2 and MPP(+) treatment was impaired by the overexpression of the PINK1 P209A mutant.	Hydrogen Peroxide	53-57	heme oxygenase 1	Homo sapiens	22-26
23345623-1	2013	BACKGROUND: The objective of this study was to evaluate the interaction between the length polymorphism of the guanosine thymidine repeat [(GT)n] in the heme oxygenase-1 (HO-1) gene and far-infrared (FIR) therapy on access flow (Qa) and arteriovenous fistula (AVF) patency in hemodialysis (HD) patients.	guanosine thymidine	111-130	heme oxygenase 1	Homo sapiens	171-175
23419834-10	2013	Treatment with hemin, a HO-1 inducer, and with [Ru(CO)3Cl2]2, a CO donor, decreased LPS-stimulated iNOS induction and NO production.	Hemin	15-20	heme oxygenase 1	Homo sapiens	24-28
23571756-1	2013	Using a luciferase reporter assay, we previously demonstrated that a Z-DNA-forming sequence of alternating thymine-guanine repeats in the human heme oxygenase-1 gene (HO-1) promoter is involved in nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2)-mediated HO-1 promoter activation.	Thymine	107-114	heme oxygenase 1	Homo sapiens	144-160
23571756-1	2013	Using a luciferase reporter assay, we previously demonstrated that a Z-DNA-forming sequence of alternating thymine-guanine repeats in the human heme oxygenase-1 gene (HO-1) promoter is involved in nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2)-mediated HO-1 promoter activation.	Thymine	107-114	heme oxygenase 1	Homo sapiens	167-171
23571756-1	2013	Using a luciferase reporter assay, we previously demonstrated that a Z-DNA-forming sequence of alternating thymine-guanine repeats in the human heme oxygenase-1 gene (HO-1) promoter is involved in nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2)-mediated HO-1 promoter activation.	Thymine	107-114	heme oxygenase 1	Homo sapiens	273-277
23571756-1	2013	Using a luciferase reporter assay, we previously demonstrated that a Z-DNA-forming sequence of alternating thymine-guanine repeats in the human heme oxygenase-1 gene (HO-1) promoter is involved in nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2)-mediated HO-1 promoter activation.	Guanine	115-122	heme oxygenase 1	Homo sapiens	144-160
23571756-1	2013	Using a luciferase reporter assay, we previously demonstrated that a Z-DNA-forming sequence of alternating thymine-guanine repeats in the human heme oxygenase-1 gene (HO-1) promoter is involved in nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2)-mediated HO-1 promoter activation.	Guanine	115-122	heme oxygenase 1	Homo sapiens	167-171
23571756-1	2013	Using a luciferase reporter assay, we previously demonstrated that a Z-DNA-forming sequence of alternating thymine-guanine repeats in the human heme oxygenase-1 gene (HO-1) promoter is involved in nuclear factor erythroid-derived 2 (NF-E2)-related factor 2 (Nrf2)-mediated HO-1 promoter activation.	Guanine	115-122	heme oxygenase 1	Homo sapiens	273-277
23571756-5	2013	Using this detection system, we demonstrated that the glutathione-depleting agent, diethyl maleate, induced Nrf2-dependent Z-DNA formation in the HO-1 promoter, but not in the thioredoxin reductase 1 gene promoter.	Glutathione	54-65	heme oxygenase 1	Homo sapiens	146-150
23571756-5	2013	Using this detection system, we demonstrated that the glutathione-depleting agent, diethyl maleate, induced Nrf2-dependent Z-DNA formation in the HO-1 promoter, but not in the thioredoxin reductase 1 gene promoter.	diethyl maleate	83-98	heme oxygenase 1	Homo sapiens	146-150
23403272-0	2013	Paeoniflorin protects human EA.hy926 endothelial cells against gamma-radiation induced oxidative injury by activating the NF-E2-related factor 2/heme oxygenase-1 pathway.	peoniflorin	0-12	heme oxygenase 1	Homo sapiens	145-161
23602847-8	2013	However, the protective effects of LXA4 were completely blocked by transfection of the cells with HO-1 siRNA, and were partially but significantly blocked by pretreatment of the cells with various blockers of K(+) channels.	lipoxin A4	35-39	heme oxygenase 1	Homo sapiens	98-102
23602847-9	2013	The LXA4-induced expressions of HO-1 in the cells were also inhibited by HO-1 siRNA and various blockers of K(+) channels.	lipoxin A4	4-8	heme oxygenase 1	Homo sapiens	32-36
23602847-9	2013	The LXA4-induced expressions of HO-1 in the cells were also inhibited by HO-1 siRNA and various blockers of K(+) channels.	lipoxin A4	4-8	heme oxygenase 1	Homo sapiens	73-77
23602847-10	2013	The inhibitory effects of LXA4 on enhanced TNF-alpha levels induced by H/R injury were abolished by transfection of the cells with HO-1 siRNA.	lipoxin A4	26-30	heme oxygenase 1	Homo sapiens	131-135
23535229-6	2013	The autophagy inhibitor 3-methyladenine significantly inhibited HO-1 up-regulation and increased the rate of cell death in cells treated with P-VO2, while the HO-1 inhibitor protoporphyrin IX zinc (II) (ZnPP) enhanced the occurrence of cell death in the P-VO2-treated cells while having no effect on the autophagic response induced by P-VO2.	3-methyladenine	24-39	heme oxygenase 1	Homo sapiens	64-68
23328493-8	2013	Finally, DSC inhibited H2O2-induced changes of Bcl-2, Bax, and caspase-3 expression, and all of these effects were reversed by HO-1 silencing.	Hydrogen Peroxide	23-27	heme oxygenase 1	Homo sapiens	127-131
23535229-6	2013	The autophagy inhibitor 3-methyladenine significantly inhibited HO-1 up-regulation and increased the rate of cell death in cells treated with P-VO2, while the HO-1 inhibitor protoporphyrin IX zinc (II) (ZnPP) enhanced the occurrence of cell death in the P-VO2-treated cells while having no effect on the autophagic response induced by P-VO2.	protoporphyrin IX	174-191	heme oxygenase 1	Homo sapiens	159-163
23535229-6	2013	The autophagy inhibitor 3-methyladenine significantly inhibited HO-1 up-regulation and increased the rate of cell death in cells treated with P-VO2, while the HO-1 inhibitor protoporphyrin IX zinc (II) (ZnPP) enhanced the occurrence of cell death in the P-VO2-treated cells while having no effect on the autophagic response induced by P-VO2.	zinc protoporphyrin	203-207	heme oxygenase 1	Homo sapiens	159-163
23570271-5	2013	Genetic studies have provided an opportunity to identify the proteins that link vitamin D to ALS pathology, including major histocompatibility complex (MHC) class II molecules, toll-like receptors, poly(ADP-ribose) polymerase-1, heme oxygenase-1, and calcium-binding proteins, as well as the reduced form of nicotinamide adenine dinucleotide phosphate.	Vitamin D	80-89	heme oxygenase 1	Homo sapiens	229-245
23328493-6	2013	In addition, DSC concentration-dependently induced HO-1 expression associated with nuclear translocation of nuclear factor-erythroid 2 related factor 2 (Nrf-2), while the effect of DSC was inhibited by a phosphoinositide 3-kinase (PI3K) inhibitor LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	247-255	heme oxygenase 1	Homo sapiens	51-55
23290930-0	2013	Hydroquinone regulates hemeoxygenase-1 expression via modulation of Src kinase activity through thiolation of cysteine residues.	hydroquinone	0-12	heme oxygenase 1	Homo sapiens	23-38
23328493-7	2013	Furthermore, the protective effect of DSC on H2O2-induced cell death was abolished by HO-1 inhibitor ZnPP, but was mimicked by carbon monoxide-releasing moiety CORM-3 or HO-1 by-product bilirubin.	Hydrogen Peroxide	45-49	heme oxygenase 1	Homo sapiens	86-90
23090785-1	2013	Heme oxygenase-1 (HO-1) is both beneficial and detrimental to the host in some viral infections by catalyzing the conversion of heme to biliverdin, iron, and carbon monoxide.	Heme	128-132	heme oxygenase 1	Homo sapiens	18-22
23090785-1	2013	Heme oxygenase-1 (HO-1) is both beneficial and detrimental to the host in some viral infections by catalyzing the conversion of heme to biliverdin, iron, and carbon monoxide.	Biliverdine	136-146	heme oxygenase 1	Homo sapiens	18-22
23090785-1	2013	Heme oxygenase-1 (HO-1) is both beneficial and detrimental to the host in some viral infections by catalyzing the conversion of heme to biliverdin, iron, and carbon monoxide.	Iron	148-152	heme oxygenase 1	Homo sapiens	18-22
23291594-10	2013	C18 acid 1 induced the expression of ARE-regulated cytoprotective genes, including NAD(P)H:quinone oxidoreductase 1, heme oxygenase 1, thioredoxin reductase 1, both subunits of the glutamate-cysteine ligase (catalytic subunit and modifier subunit), and the cystine/glutamate exchange transporter, in IMR-32 human neuroblastoma cells.	c18 acid 1	0-10	heme oxygenase 1	Homo sapiens	117-133
23146110-12	2013	Andrographolide up-regulated ARE-regulated gene targets including glutamate-cysteine ligase catalytic (GCLC) subunit, GCL modifier (GCLM) subunit, GPx, GR and heme oxygenase-1 in BEAS-2B cells in response to CSE.	andrographolide	0-15	heme oxygenase 1	Homo sapiens	159-175
23090785-1	2013	Heme oxygenase-1 (HO-1) is both beneficial and detrimental to the host in some viral infections by catalyzing the conversion of heme to biliverdin, iron, and carbon monoxide.	Carbon Monoxide	158-173	heme oxygenase 1	Homo sapiens	18-22
23090785-6	2013	HO-1 overexpression in BGC-823 cells caused the cells containing Blasticidin-resistant gene driven by SV40 promoter to grow slowly under Blasticidin screening, compared with control groups.	blasticidin S	65-76	heme oxygenase 1	Homo sapiens	0-4
23090785-6	2013	HO-1 overexpression in BGC-823 cells caused the cells containing Blasticidin-resistant gene driven by SV40 promoter to grow slowly under Blasticidin screening, compared with control groups.	blasticidin S	137-148	heme oxygenase 1	Homo sapiens	0-4
23290930-0	2013	Hydroquinone regulates hemeoxygenase-1 expression via modulation of Src kinase activity through thiolation of cysteine residues.	Cysteine	110-118	heme oxygenase 1	Homo sapiens	23-38
23350672-4	2013	Heme-hemopexin is relatively resistant to damage by ROS and retains its ability to induce the cytoprotective HO1 after exposure to tert-butylhydroperoxide, although induction is impaired, but not eliminated, by exposure to high concentrations of H(2)O(2) in vitro.	tert-Butylhydroperoxide	131-154	heme oxygenase 1	Homo sapiens	109-112
23274124-3	2013	Thiamine also affects HIV through non-genomic factors, i.e., matrix metalloproteinase, vascular endothelial growth factor, heme oxygenase 1, the prostaglandins, cyclooxygenase 2, reactive oxygen species, and nitric oxide.	Thiamine	0-8	heme oxygenase 1	Homo sapiens	123-139
23567851-0	2013	Homocysteine induces heme oxygenase-1 expression via transcription factor Nrf2 activation in HepG2 cell.	Homocysteine	0-12	heme oxygenase 1	Homo sapiens	21-37
23567851-8	2013	Real time RT-PCR and Western-blotting were performed to evaluate whether homocysteine was able to induce mRNA and protein expression of HO-1.	Homocysteine	73-85	heme oxygenase 1	Homo sapiens	136-140
23567851-11	2013	(iii) Real time RT-PCR and Western-blotting revealed increased mRNA and protein expression of inducible gene HO-1 after treatment with homocysteine.	Homocysteine	135-147	heme oxygenase 1	Homo sapiens	109-113
23567851-13	2013	Therefore, induction of Nrf2-ARE-dependent expression of HO-1 could be a therapeutic option for hepatic cells damage induced by homocysteine.	Homocysteine	128-140	heme oxygenase 1	Homo sapiens	57-61
23350672-4	2013	Heme-hemopexin is relatively resistant to damage by ROS and retains its ability to induce the cytoprotective HO1 after exposure to tert-butylhydroperoxide, although induction is impaired, but not eliminated, by exposure to high concentrations of H(2)O(2) in vitro.	Hydrogen Peroxide	246-254	heme oxygenase 1	Homo sapiens	109-112
22946793-10	2013	Moreover, the protective role of melatonin against damage to endothelial tight junction integrity was addressed by ZO-1 expression, paralleled with the restored heme oxygenase-1 levels during OGD.	Melatonin	33-42	heme oxygenase 1	Homo sapiens	161-177
23350672-8	2013	Hemopexin sequesters heme, thus preventing unregulated heme uptake that leads to toxicity; it safely delivers heme to neuronal cells; and it activates the induction of proteins including HO1 and hAPP that keep heme and iron at safe levels in neurons.	Iron	219-223	heme oxygenase 1	Homo sapiens	187-190
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Heme	59-63	heme oxygenase 1	Homo sapiens	77-81
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Carbon Monoxide	134-149	heme oxygenase 1	Homo sapiens	59-75
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Carbon Monoxide	134-149	heme oxygenase 1	Homo sapiens	77-81
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Carbon Monoxide	151-153	heme oxygenase 1	Homo sapiens	59-75
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Carbon Monoxide	151-153	heme oxygenase 1	Homo sapiens	77-81
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Biliverdine	156-166	heme oxygenase 1	Homo sapiens	59-75
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Biliverdine	156-166	heme oxygenase 1	Homo sapiens	77-81
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Iron	176-180	heme oxygenase 1	Homo sapiens	59-75
23403148-4	2013	One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron.	Iron	176-180	heme oxygenase 1	Homo sapiens	77-81
23403148-5	2013	CO and bilirubin (a downstream product of biliverdin processing) account for the angiogenic, vasodilatory and anti-oxidant properties of HO-1.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	137-141
23403148-5	2013	CO and bilirubin (a downstream product of biliverdin processing) account for the angiogenic, vasodilatory and anti-oxidant properties of HO-1.	Bilirubin	7-16	heme oxygenase 1	Homo sapiens	137-141
23403148-5	2013	CO and bilirubin (a downstream product of biliverdin processing) account for the angiogenic, vasodilatory and anti-oxidant properties of HO-1.	Biliverdine	42-52	heme oxygenase 1	Homo sapiens	137-141
23403148-6	2013	These collective actions of the heme breakdown metabolites generated by HO-1 offer protection against cytotoxicity, inflammation, hypoxia and other forms of cellular stress that are central to the pathogenesis of sPE.	Heme	32-36	heme oxygenase 1	Homo sapiens	72-76
23128353-6	2013	Glucosamine at 50 mM was demonstrated to elevate both the mRNA and protein expression of p53 and heme oxygenase-1 (HO-1), but also caused a reduction in p21 protein expression.	Glucosamine	0-11	heme oxygenase 1	Homo sapiens	97-113
23538684-4	2013	RESULTS: Changes in mRNA levels were most numerous and striking at 6 h after heme treatment but were similar and still numerous at 24 h. After 6 h of heme exposure, the increase in heme oxygenase 1 gene expression was 60-fold by mRNA and 88-fold by quantitative reverse transcription-polymerase chain reaction.	Heme	77-81	heme oxygenase 1	Homo sapiens	181-197
23128353-6	2013	Glucosamine at 50 mM was demonstrated to elevate both the mRNA and protein expression of p53 and heme oxygenase-1 (HO-1), but also caused a reduction in p21 protein expression.	Glucosamine	0-11	heme oxygenase 1	Homo sapiens	115-119
23128353-8	2013	Altogether, our results suggest that a high dose of glucosamine may inhibit cell proliferation through apoptosis and disturb cell cycle progression with a halt at G(0)/G(1) phase, and that this occurs, at least in part, by a reduction in Rb phosphorylation together with modulation of p21, p53 and HO-1 expression, and nuclear p21 accumulation.	Glucosamine	52-63	heme oxygenase 1	Homo sapiens	298-302
23419114-0	2013	Dihydroquercetin (DHQ) induced HO-1 and NQO1 expression against oxidative stress through the Nrf2-dependent antioxidant pathway.	taxifolin	0-16	heme oxygenase 1	Homo sapiens	31-35
23419114-0	2013	Dihydroquercetin (DHQ) induced HO-1 and NQO1 expression against oxidative stress through the Nrf2-dependent antioxidant pathway.	taxifolin	18-21	heme oxygenase 1	Homo sapiens	31-35
23419114-7	2013	DHQ upregulated the Nrf2-related antioxidant genes heme oxygenase-1 (HO-1), NAD(P)H quinone oxidoreductase-1 (NQO1), and glutamate-cysteine ligase modifier subunits.	taxifolin	0-3	heme oxygenase 1	Homo sapiens	51-67
23419114-7	2013	DHQ upregulated the Nrf2-related antioxidant genes heme oxygenase-1 (HO-1), NAD(P)H quinone oxidoreductase-1 (NQO1), and glutamate-cysteine ligase modifier subunits.	taxifolin	0-3	heme oxygenase 1	Homo sapiens	69-73
23324179-9	2013	Metformin (the best known clinical activator of AMPK) suppressed EMT induction through inhibition of ROS via induction of heme oxygenase-1 and endogenous antioxidant thioredoxin.	Metformin	0-9	heme oxygenase 1	Homo sapiens	122-138
23324179-9	2013	Metformin (the best known clinical activator of AMPK) suppressed EMT induction through inhibition of ROS via induction of heme oxygenase-1 and endogenous antioxidant thioredoxin.	Reactive Oxygen Species	101-104	heme oxygenase 1	Homo sapiens	122-138
23538684-4	2013	RESULTS: Changes in mRNA levels were most numerous and striking at 6 h after heme treatment but were similar and still numerous at 24 h. After 6 h of heme exposure, the increase in heme oxygenase 1 gene expression was 60-fold by mRNA and 88-fold by quantitative reverse transcription-polymerase chain reaction.	Heme	150-154	heme oxygenase 1	Homo sapiens	181-197
23090292-1	2013	The aim of this study was to observe the intracellular heat shock protein 72 (HSP72) and heme oxygenase-1 (HSP32) response to prolonged interval cycling following the ingestion of carbohydrates (CHO) and sodium bicarbonate (NaHCO(3)).	cho	195-198	heme oxygenase 1	Homo sapiens	89-105
23322908-4	2013	Vitamin D also exerts its effects on AD by regulating calcium-sensing receptor expression, enhancing amyloid-beta peptides clearance, interleukin 10, downregulating matrix metalloproteinases, upregulating heme oxygenase 1, and suppressing the reduced form of nicotinamide adenine dinucleotide phosphate expression.	Vitamin D	0-9	heme oxygenase 1	Homo sapiens	205-221
23090292-1	2013	The aim of this study was to observe the intracellular heat shock protein 72 (HSP72) and heme oxygenase-1 (HSP32) response to prolonged interval cycling following the ingestion of carbohydrates (CHO) and sodium bicarbonate (NaHCO(3)).	Carbohydrates	180-193	heme oxygenase 1	Homo sapiens	89-105
23090292-1	2013	The aim of this study was to observe the intracellular heat shock protein 72 (HSP72) and heme oxygenase-1 (HSP32) response to prolonged interval cycling following the ingestion of carbohydrates (CHO) and sodium bicarbonate (NaHCO(3)).	Carbohydrates	180-193	heme oxygenase 1	Homo sapiens	107-112
23090292-1	2013	The aim of this study was to observe the intracellular heat shock protein 72 (HSP72) and heme oxygenase-1 (HSP32) response to prolonged interval cycling following the ingestion of carbohydrates (CHO) and sodium bicarbonate (NaHCO(3)).	cho	195-198	heme oxygenase 1	Homo sapiens	107-112
23090292-1	2013	The aim of this study was to observe the intracellular heat shock protein 72 (HSP72) and heme oxygenase-1 (HSP32) response to prolonged interval cycling following the ingestion of carbohydrates (CHO) and sodium bicarbonate (NaHCO(3)).	Sodium Bicarbonate	204-222	heme oxygenase 1	Homo sapiens	89-105
23090292-5	2013	Exogenous CHO had no influence on either HSP72 or HSP32, but the ingestion of NaHCO(3) significantly attenuated HSP32 in monocytes and lymphocytes (p &lt;= 0.042).	Sodium Bicarbonate	78-86	heme oxygenase 1	Homo sapiens	112-117
22717332-7	2013	The HO-1 activator, CoppIX, reversed iNOS/NO up-regulation and HO-1 down-regulation induced by IFN-alpha.	coppix	20-26	heme oxygenase 1	Homo sapiens	4-8
22865541-8	2013	Here, we demonstrate that celastrol, but not classical heat shock treatment, is effective in inducing a set of neuroprotective Hsps in cultures derived from cerebral cortices, including Hsp70, Hsp27 and Hsp32.	celastrol	26-35	heme oxygenase 1	Homo sapiens	203-208
22717332-7	2013	The HO-1 activator, CoppIX, reversed iNOS/NO up-regulation and HO-1 down-regulation induced by IFN-alpha.	coppix	20-26	heme oxygenase 1	Homo sapiens	63-67
23525626-9	2013	These inhibitory effects BL were almost completely abolished by CC and partly by tin protoporphyrin-IX, a competitive inhibitor of HO-1.	tin protoporphyrin IX	81-102	heme oxygenase 1	Homo sapiens	131-135
22849812-0	2013	Anti-inflammatory effect of pachymic acid promotes odontoblastic differentiation via HO-1 in dental pulp cells.	pachymic acid	28-41	heme oxygenase 1	Homo sapiens	85-89
23281030-10	2013	CONCLUSION: We showed that attenuation of Nrf2 and HO-1 expression through induction of miR-132 and miR-200c by OTA elevates ROS levels and profibrotic TGFbeta expression.	Reactive Oxygen Species	125-128	heme oxygenase 1	Homo sapiens	51-55
22264017-9	2013	HMOX1 may thus be a useful biomarker of TOPO-QDOT QD exposure across cell types and species.	topo-qdot	40-49	heme oxygenase 1	Homo sapiens	0-5
23318726-0	2013	Butein protects human dental pulp cells from hydrogen peroxide-induced oxidative toxicity via Nrf2 pathway-dependent heme oxygenase-1 expressions.	butein	0-6	heme oxygenase 1	Homo sapiens	117-133
23318726-0	2013	Butein protects human dental pulp cells from hydrogen peroxide-induced oxidative toxicity via Nrf2 pathway-dependent heme oxygenase-1 expressions.	Hydrogen Peroxide	45-62	heme oxygenase 1	Homo sapiens	117-133
23318726-8	2013	In addition, butein-dependent HO-1 expression was required for the inhibition of H2O2-induced cell death and ROS generation.	Hydrogen Peroxide	81-85	heme oxygenase 1	Homo sapiens	30-34
23318726-8	2013	In addition, butein-dependent HO-1 expression was required for the inhibition of H2O2-induced cell death and ROS generation.	Reactive Oxygen Species	109-112	heme oxygenase 1	Homo sapiens	30-34
23318726-10	2013	Treatment of HDP cells with a c-Jun NH2-terminal kinase (JNK) inhibitor also reduced butein-induced HO-1 expression, and butein treatment led to increased JNK phosphorylation.	butein	85-91	heme oxygenase 1	Homo sapiens	100-104
23525626-0	2013	beta-Lapachone, a substrate of NAD(P)H:quinone oxidoreductase, induces anti-inflammatory heme oxygenase-1 via AMP-activated protein kinase activation in RAW264.7 macrophages.	beta-lapachone	0-14	heme oxygenase 1	Homo sapiens	89-105
23525626-6	2013	5-Aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside, an AMPK activator, also induced HO-1 expression.	acadesine	0-54	heme oxygenase 1	Homo sapiens	88-92
23281030-0	2013	Cross-talk between microRNAs, nuclear factor E2-related factor 2, and heme oxygenase-1 in ochratoxin A-induced toxic effects in renal proximal tubular epithelial cells.	ochratoxin A	90-102	heme oxygenase 1	Homo sapiens	70-86
23281030-2	2013	We investigated the cross-talk between microRNAs, nuclear factor E2-related factor 2 (Nrf2), and heme oxygenase-1 (HO-1) in ochratoxin A-mediated effects.	ochratoxin A	124-136	heme oxygenase 1	Homo sapiens	97-113
23281030-2	2013	We investigated the cross-talk between microRNAs, nuclear factor E2-related factor 2 (Nrf2), and heme oxygenase-1 (HO-1) in ochratoxin A-mediated effects.	ochratoxin A	124-136	heme oxygenase 1	Homo sapiens	115-119
23498787-9	2013	Increased HIF-1alpha activation and HO-1 expression were observed in fenoldopam pretreatment group.	Fenoldopam	69-79	heme oxygenase 1	Homo sapiens	36-40
23498787-11	2013	CONCLUSION: Donor preconditioning by fenoldopam exerts renoprotection in grafts, at least in part, through HIF-1alpha activation and HO-1 expression.	Fenoldopam	37-47	heme oxygenase 1	Homo sapiens	133-137
22849812-2	2013	In this study, pachymic acid from mushroom Formitopsis niagra is examined to determine whether it affects pulpal inflammation and promotes odontogenesis via HO-1 gene expression.	pachymic acid	15-28	heme oxygenase 1	Homo sapiens	157-161
22849812-5	2013	To understand the mechanism of pachymic acid via HO-1 induction, the cells were treated with zinc protoporphyrin IX (ZnPP: HO-1 inhibitor).	pachymic acid	31-44	heme oxygenase 1	Homo sapiens	49-53
22849812-5	2013	To understand the mechanism of pachymic acid via HO-1 induction, the cells were treated with zinc protoporphyrin IX (ZnPP: HO-1 inhibitor).	zinc protoporphyrin	93-115	heme oxygenase 1	Homo sapiens	123-127
22849812-7	2013	However, the HDPCs treated with pachymic acid affected anti-inflammatory effect and induction of odontoblast differentiation through increasing HO-1 expression.	pachymic acid	32-45	heme oxygenase 1	Homo sapiens	144-148
22849812-11	2013	CONCLUSIONS: The pachymic acid showed anti-inflammatory function and odontoblast differentiation via HO-1 pathway.	pachymic acid	17-30	heme oxygenase 1	Homo sapiens	101-105
23333393-3	2013	In addition, berberine also induced heme oxygenase (HO)-1 in a dose-dependent manner, which was mediated through activation of p38 MAPK and NF-E2-related factor 2 (Nrf2) signaling cascade in macrophages.	Berberine	13-22	heme oxygenase 1	Homo sapiens	36-57
23068042-0	2013	Development of a heme sensor using fluorescently labeled heme oxygenase-1.	Heme	17-21	heme oxygenase 1	Homo sapiens	57-73
23025298-7	2013	RECENT ADVANCES: Among the latter, the heme oxygenase-1 (HO-1) pathway is likely to contribute to the established and powerful antioxidant/anti-inflammatory properties of polyphenols.	Polyphenols	171-182	heme oxygenase 1	Homo sapiens	39-55
23025298-7	2013	RECENT ADVANCES: Among the latter, the heme oxygenase-1 (HO-1) pathway is likely to contribute to the established and powerful antioxidant/anti-inflammatory properties of polyphenols.	Polyphenols	171-182	heme oxygenase 1	Homo sapiens	57-61
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	15-19	heme oxygenase 1	Homo sapiens	98-114
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	15-19	heme oxygenase 1	Homo sapiens	116-120
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	98-114
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	116-120
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	98-114
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	116-120
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	98-114
23068042-2	2013	To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	116-120
23068042-4	2013	Each of the three fluorescently labeled HO-1s exhibits a 1:1 binding stoichiometry and an absorption spectrum similar to that of the heme complex of the wild-type HO-1.	Heme	133-137	heme oxygenase 1	Homo sapiens	40-44
23068042-5	2013	Titration of the labeled proteins with hemin resulted in fluorescence quenching in a hemin concentration-dependent manner, presumably due to an energy transfer from the fluorophore to the heme bound to HO-1.	Hemin	39-44	heme oxygenase 1	Homo sapiens	202-206
23068042-5	2013	Titration of the labeled proteins with hemin resulted in fluorescence quenching in a hemin concentration-dependent manner, presumably due to an energy transfer from the fluorophore to the heme bound to HO-1.	Hemin	85-90	heme oxygenase 1	Homo sapiens	202-206
23068042-5	2013	Titration of the labeled proteins with hemin resulted in fluorescence quenching in a hemin concentration-dependent manner, presumably due to an energy transfer from the fluorophore to the heme bound to HO-1.	Heme	188-192	heme oxygenase 1	Homo sapiens	202-206
22704780-9	2013	Western blot analysis revealed that catechin stimulated a time-dependent increase in both the nuclear factor erythroid 2-related factor 2 and total heme oxygenase-1 protein expression in Int-407 cells.	Catechin	36-44	heme oxygenase 1	Homo sapiens	148-164
23392716-6	2013	In vitro treatment with CoPPIX significantly increased the expression of HO-1 in iPECs in a dose-dependent manner.	cobaltiprotoporphyrin	24-30	heme oxygenase 1	Homo sapiens	73-77
23392716-7	2013	Over-expression of HO-1 was successfully achieved by incubation of iPECs with either 50 or 80 mumol/L of CoPPIX.	cobaltiprotoporphyrin	105-111	heme oxygenase 1	Homo sapiens	19-23
23255485-6	2013	In Caco-2 cells, treatment with genistein markedly attenuated H(2)O(2) -induced peroxide formation; this amelioration was reversed by buthionine sulfoximine(GCLC inhibitor) and zinc protoporphyrin(HO-1 inhibitor).	Genistein	32-41	heme oxygenase 1	Homo sapiens	197-201
23255485-6	2013	In Caco-2 cells, treatment with genistein markedly attenuated H(2)O(2) -induced peroxide formation; this amelioration was reversed by buthionine sulfoximine(GCLC inhibitor) and zinc protoporphyrin(HO-1 inhibitor).	Hydrogen Peroxide	62-70	heme oxygenase 1	Homo sapiens	197-201
23255485-6	2013	In Caco-2 cells, treatment with genistein markedly attenuated H(2)O(2) -induced peroxide formation; this amelioration was reversed by buthionine sulfoximine(GCLC inhibitor) and zinc protoporphyrin(HO-1 inhibitor).	zinc protoporphyrin	177-196	heme oxygenase 1	Homo sapiens	197-201
23329300-0	2013	Berberine protects 6-hydroxydopamine-induced human dopaminergic neuronal cell death through the induction of heme oxygenase-1.	Berberine	0-9	heme oxygenase 1	Homo sapiens	109-125
23255485-11	2013	These results suggest the involvement of ERK1/2, PKC, and Nrf2 in inducing HO-1 and GCLC by genistein.	Genistein	92-101	heme oxygenase 1	Homo sapiens	75-79
23329300-0	2013	Berberine protects 6-hydroxydopamine-induced human dopaminergic neuronal cell death through the induction of heme oxygenase-1.	Oxidopamine	19-36	heme oxygenase 1	Homo sapiens	109-125
23329300-4	2013	BBR also upregulated heme oxygenase-1 (HO-1) expression, which conferred protection against 6-OHDA-induced dopaminergic neuron injury and besides, effect of BBR on HO-1 was reversed by siRNA-Nrf2.	Oxidopamine	92-98	heme oxygenase 1	Homo sapiens	21-37
23255485-12	2013	CONCLUSION: Our studies show that genistein up-regulated HO-1 and GCLC expression through the EKR1/2 and PKC /Nrf2 pathways during oxidative stress.	Genistein	34-43	heme oxygenase 1	Homo sapiens	57-61
23026155-2	2013	The intracellular levels of CO can increase under stressful conditions following the induction of HO-1 (heme oxygnase-1), a ubiquitous enzyme responsible for the catabolism of heme.	Heme	104-108	heme oxygenase 1	Homo sapiens	98-102
23085367-6	2013	Xanthohumol, beside the induction of GSTs and HO-1, significantly elevated NQO1 expression in concert with p53 level in normal hepatocytes.	xanthohumol	0-11	heme oxygenase 1	Homo sapiens	46-50
23143154-13	2013	Quercetin also reduced the CSE- and H(2)O(2)-induced upregulation of ROS and HO-1 protein in differentiated OFs and preadipocyte OFs.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	77-81
22716961-9	2013	Moreover, the use of Nrf2 small interfering RNA transfection and HO-1- or PPARgamma-specific antagonists (Znpp and GW9662, respectively) blocked the protective effects of genistein on endothelial cell viability during oxidative stress.	Genistein	171-180	heme oxygenase 1	Homo sapiens	65-70
23143154-13	2013	Quercetin also reduced the CSE- and H(2)O(2)-induced upregulation of ROS and HO-1 protein in differentiated OFs and preadipocyte OFs.	Hydrogen Peroxide	36-44	heme oxygenase 1	Homo sapiens	77-81
23295066-4	2013	Ultimately, physiological studies unveiled the endogenous production of CO, particularly by the heme oxygenase (HO)-1 enzyme, recognizing CO as a beneficial gas when used at therapeutic doses.	Carbon Monoxide	72-74	heme oxygenase 1	Homo sapiens	96-117
23097500-0	2013	Structural insights into human heme oxygenase-1 inhibition by potent and selective azole-based compounds.	Azoles	83-88	heme oxygenase 1	Homo sapiens	31-47
23221079-8	2013	In contrast, HO-1 protein was upregulated by treatment with both hydrogen peroxide and light.	Hydrogen Peroxide	65-82	heme oxygenase 1	Homo sapiens	13-17
23131562-0	2013	Omega-3 polyunsaturated fatty acid has an anti-oxidant effect via the Nrf-2/HO-1 pathway in 3T3-L1 adipocytes.	omega-3 polyunsaturated fatty acid	0-34	heme oxygenase 1	Homo sapiens	76-80
23131562-6	2013	Knockdown of nuclear factor erythroid 2-related factor 2 (Nrf-2) significantly reduced EPA, DHA or 4-HHE-induced HO-1 mRNA and protein expression.	Eicosapentaenoic Acid	87-90	heme oxygenase 1	Homo sapiens	113-117
23131562-6	2013	Knockdown of nuclear factor erythroid 2-related factor 2 (Nrf-2) significantly reduced EPA, DHA or 4-HHE-induced HO-1 mRNA and protein expression.	Docosahexaenoic Acids	92-95	heme oxygenase 1	Homo sapiens	113-117
23131562-7	2013	Also, pretreatment with omega3-PUFA prevented H(2)O(2)-induced cytotoxicity in a HO-1 dependent manner.	Hydrogen Peroxide	46-54	heme oxygenase 1	Homo sapiens	81-85
23131562-8	2013	In conclusion, treatment with EPA and DHA induced HO-1 through the activation of Nrf-2 and prevented oxidative stress in 3T3-L1 adipocytes.	Eicosapentaenoic Acid	30-33	heme oxygenase 1	Homo sapiens	50-54
23131562-8	2013	In conclusion, treatment with EPA and DHA induced HO-1 through the activation of Nrf-2 and prevented oxidative stress in 3T3-L1 adipocytes.	Docosahexaenoic Acids	38-41	heme oxygenase 1	Homo sapiens	50-54
22989377-3	2013	We investigated HO-1-overexpressing A549 cells and find that, as expected, HO-1-overexpressing cells are resistant to killing by hydrogen peroxide.	Hydrogen Peroxide	129-146	heme oxygenase 1	Homo sapiens	75-79
22989377-5	2013	However, HO-1-overexpressing cells contain only ~25% as much "loose" (probably redox active) iron.	Iron	93-97	heme oxygenase 1	Homo sapiens	9-13
22989377-6	2013	Indeed, inhibition of ferritin synthesis [via siRNA (small interfering RNA) directed at the ferritin heavy chain] sensitizes the HO-1-overexpressing cells to peroxide killing.	Peroxides	158-166	heme oxygenase 1	Homo sapiens	129-133
22989377-9	2013	We conclude that, at least in many cases, the cytoprotective effects of HO-1 induction or forced overexpression may derive from elevated expression of ferritin and consequent reduction of redox active "loose" iron.	Iron	209-213	heme oxygenase 1	Homo sapiens	72-76
23046979-0	2013	Diallyl tetrasulfane activates both the eIF2alpha and Nrf2/HO-1 pathways.	diallyl tetrasulfane	0-20	heme oxygenase 1	Homo sapiens	59-63
23046979-8	2013	DATTS treatment of HCT116 cells also caused an up-regulation of phospho-eIF2alpha, nuclear Nrf2 and HO-1 protein levels in a time and concentration-dependent manner.	datts	0-5	heme oxygenase 1	Homo sapiens	100-104
23046979-11	2013	CONCLUSIONS: DATTS activates the ROS-eIF2alpha/Nrf2 HO-1 signaling cascades leading to the up-regulation of HO-1.	datts	13-18	heme oxygenase 1	Homo sapiens	52-56
23046979-11	2013	CONCLUSIONS: DATTS activates the ROS-eIF2alpha/Nrf2 HO-1 signaling cascades leading to the up-regulation of HO-1.	datts	13-18	heme oxygenase 1	Homo sapiens	108-112
23046979-11	2013	CONCLUSIONS: DATTS activates the ROS-eIF2alpha/Nrf2 HO-1 signaling cascades leading to the up-regulation of HO-1.	Reactive Oxygen Species	33-36	heme oxygenase 1	Homo sapiens	52-56
23046979-11	2013	CONCLUSIONS: DATTS activates the ROS-eIF2alpha/Nrf2 HO-1 signaling cascades leading to the up-regulation of HO-1.	Reactive Oxygen Species	33-36	heme oxygenase 1	Homo sapiens	108-112
23811562-6	2013	Other assays revealed that, in keratinocytes, sauchinone decreased reactive oxygen species (ROS) production and increased glutathione levels and heme oxygenase-1.	sauchinone	46-56	heme oxygenase 1	Homo sapiens	145-161
23152113-8	2013	THG213.29 increased mRNA expression of heme-oxygenase 1, Bcl2, and FGF-2 in renal cortex; correspondingly, in EP(4)-transfected HEK293 cells, THG213.29 augmented FGF-2 and abrogated EP(4)-dependent overexpression of inflammatory IL-6 and of apoptotic death domain-associated protein and BCL2-associated agonist of cell death.	thg213	0-6	heme oxygenase 1	Homo sapiens	39-55
23546295-7	2013	The antioxidant potential of EA might be directly correlated with the increased expression of HO-1 and NQO1, whose expression may have surmounted the oxidative stress generated by PQ.	Paraquat	180-182	heme oxygenase 1	Homo sapiens	94-98
23291378-0	2013	Genistein inhibits ox-LDL-induced VCAM-1, ICAM-1 and MCP-1 expression of HUVECs through heme oxygenase-1.	Genistein	0-9	heme oxygenase 1	Homo sapiens	88-104
23291378-7	2013	RESULTS: Pretreatment with genistein markedly reduced ox-LDL-induced MCP-1, VCAM-1 and ICAM-1 secretion and mRNA transcription, which was further decreased by the inducer of HO and reversed by the inhibitor of HO; additionally, the effects were accompanied with upregulating HO-1 mRNA and protein expression and markedly abolished with Nrf2 siRNA.	Genistein	27-36	heme oxygenase 1	Homo sapiens	275-279
24191253-0	2013	Antidiabetic potential of the heme oxygenase-1 inducer curcumin analogues.	Curcumin	55-63	heme oxygenase 1	Homo sapiens	30-46
24009858-7	2013	Interestingly, we found that treatment of finasteride induced the expression of Nrf2 and HO-1 proteins in PC-3 cells.	Finasteride	42-53	heme oxygenase 1	Homo sapiens	89-93
23738323-6	2013	Furthermore, mollugin induced the activation of p38, ERK, and JNK and the expression of heme oxygenase-1 (HO-1) and nuclear factor E2-related factor 2 (Nrf2).	rubimaillin	13-21	heme oxygenase 1	Homo sapiens	88-104
23738323-6	2013	Furthermore, mollugin induced the activation of p38, ERK, and JNK and the expression of heme oxygenase-1 (HO-1) and nuclear factor E2-related factor 2 (Nrf2).	rubimaillin	13-21	heme oxygenase 1	Homo sapiens	106-110
23738323-7	2013	Mollugin-induced growth inhibition and apoptosis of HO-1 were reversed by an HO-1 inhibitor and Nrf2 siRNA.	rubimaillin	0-8	heme oxygenase 1	Homo sapiens	52-56
23738323-7	2013	Mollugin-induced growth inhibition and apoptosis of HO-1 were reversed by an HO-1 inhibitor and Nrf2 siRNA.	rubimaillin	0-8	heme oxygenase 1	Homo sapiens	77-81
23738323-8	2013	Collectively, this is the first report to demonstrate the effectiveness of mollugin as a candidate for a chemotherapeutic agent in OSCCs via the upregulation of the HO-1 and Nrf2 pathways and the downregulation of NF- kappa B.	rubimaillin	75-83	heme oxygenase 1	Homo sapiens	165-169
24009858-0	2013	Finasteride Increases the Expression of Hemoxygenase-1 (HO-1) and NF-E2-Related Factor-2 (Nrf2) Proteins in PC-3 Cells: Implication of Finasteride-Mediated High-Grade Prostate Tumor Occurrence.	Finasteride	0-11	heme oxygenase 1	Homo sapiens	40-54
23868099-6	2013	Additionally, we found that the zinc-induced HO-1 gene transcription can be enhanced by clioquinol, a zinc ionophore, and reversed by pretreatment with TPEN, a known zinc chelator, indicating that an increase in intracellular zinc levels is responsible for this induction.	Clioquinol	88-98	heme oxygenase 1	Homo sapiens	45-49
24009858-0	2013	Finasteride Increases the Expression of Hemoxygenase-1 (HO-1) and NF-E2-Related Factor-2 (Nrf2) Proteins in PC-3 Cells: Implication of Finasteride-Mediated High-Grade Prostate Tumor Occurrence.	Finasteride	0-11	heme oxygenase 1	Homo sapiens	56-60
23087099-6	2013	Such upregulated HO-1 levels were effective in conferring protection against H(2)O(2)-induced cell death and in promoting the proangiogenic phenotype of HMEC-1 cells.	Hydrogen Peroxide	77-85	heme oxygenase 1	Homo sapiens	17-21
23868099-6	2013	Additionally, we found that the zinc-induced HO-1 gene transcription can be enhanced by clioquinol, a zinc ionophore, and reversed by pretreatment with TPEN, a known zinc chelator, indicating that an increase in intracellular zinc levels is responsible for this induction.	N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine	152-156	heme oxygenase 1	Homo sapiens	45-49
23739547-0	2013	Tertiary-butylhydroquinone upregulates expression of ATP-binding cassette transporter A1 via nuclear factor E2-related factor 2/heme oxygenase-1 signaling in THP-1 macrophage-derived foam cells.	2-Butylhydroquinone	9-26	heme oxygenase 1	Homo sapiens	108-144
24247298-0	2013	Clofibrate induces heme oxygenase 1 expression through a PPARalpha-independent mechanism in human cancer cells.	Clofibrate	0-10	heme oxygenase 1	Homo sapiens	19-35
24247298-2	2013	This study examined the effect of clofibrate on heme oxygenase-1 (HO-1) gene expression in A2780 (human ovarian cancer) and DU145 (human prostate cancer) cells.	Clofibrate	34-44	heme oxygenase 1	Homo sapiens	48-64
24247298-2	2013	This study examined the effect of clofibrate on heme oxygenase-1 (HO-1) gene expression in A2780 (human ovarian cancer) and DU145 (human prostate cancer) cells.	Clofibrate	34-44	heme oxygenase 1	Homo sapiens	66-70
24247298-3	2013	METHODS AND RESULTS: We demonstrate that clofibrate induces HO-1 expression in a concentration- and time-dependent manner.	Clofibrate	41-51	heme oxygenase 1	Homo sapiens	60-64
24247298-4	2013	The induction of HO-1 by clofibrate was detected at both mRNA and protein levels and the HO-1 gene promoter activity was also dramatically induced by clofibrate, indicating that clofibrate up-regulates HO-1 gene transcription.	Clofibrate	25-35	heme oxygenase 1	Homo sapiens	17-21
24247298-4	2013	The induction of HO-1 by clofibrate was detected at both mRNA and protein levels and the HO-1 gene promoter activity was also dramatically induced by clofibrate, indicating that clofibrate up-regulates HO-1 gene transcription.	Clofibrate	150-160	heme oxygenase 1	Homo sapiens	89-93
24247298-4	2013	The induction of HO-1 by clofibrate was detected at both mRNA and protein levels and the HO-1 gene promoter activity was also dramatically induced by clofibrate, indicating that clofibrate up-regulates HO-1 gene transcription.	Clofibrate	150-160	heme oxygenase 1	Homo sapiens	89-93
24247298-4	2013	The induction of HO-1 by clofibrate was detected at both mRNA and protein levels and the HO-1 gene promoter activity was also dramatically induced by clofibrate, indicating that clofibrate up-regulates HO-1 gene transcription.	Clofibrate	150-160	heme oxygenase 1	Homo sapiens	89-93
24247298-4	2013	The induction of HO-1 by clofibrate was detected at both mRNA and protein levels and the HO-1 gene promoter activity was also dramatically induced by clofibrate, indicating that clofibrate up-regulates HO-1 gene transcription.	Clofibrate	150-160	heme oxygenase 1	Homo sapiens	89-93
24247298-5	2013	Surprisingly, the induction of HO-1 by clofibrate was mediated by the Nrf2 signaling pathway, not by the PPARalpha pathway.	Clofibrate	39-49	heme oxygenase 1	Homo sapiens	31-35
24247298-6	2013	This was primarily demonstrated by siRNA knockdown of Nrf2 expression that significantly attenuated clofibrate-induced HO-1 gene transcription, and siRNA knockdown of PPARalpha that had no effect on clofibrate-induced HO-1 promoter activity.	Clofibrate	100-110	heme oxygenase 1	Homo sapiens	119-123
24247298-7	2013	Furthermore, deletion of the antioxidant response elements (AREs) in the HO-1 gene promoter diminished clofibrate-induced HO-1 transcription and deletion of the PPAR response elements (PPREs) had no such effect.	Clofibrate	103-113	heme oxygenase 1	Homo sapiens	73-77
24247298-7	2013	Furthermore, deletion of the antioxidant response elements (AREs) in the HO-1 gene promoter diminished clofibrate-induced HO-1 transcription and deletion of the PPAR response elements (PPREs) had no such effect.	Clofibrate	103-113	heme oxygenase 1	Homo sapiens	122-126
24247298-9	2013	CONCLUSION: Clofibrate induces HO-1 gene expression in cancer cells through a PPARalpha-independent mechanism and the Nrf2 signaling pathway is indispensible for this induction.	Clofibrate	12-22	heme oxygenase 1	Homo sapiens	31-35
23739547-5	2013	Furthermore, tBHQ reduced calpain-mediated ABCA1 proteolysis via activation of nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1).	2-tert-butylhydroquinone	13-17	heme oxygenase 1	Homo sapiens	125-141
23739547-5	2013	Furthermore, tBHQ reduced calpain-mediated ABCA1 proteolysis via activation of nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1).	2-tert-butylhydroquinone	13-17	heme oxygenase 1	Homo sapiens	143-147
23739547-6	2013	Inhibition of HO-1 with a pharmacological inhibitor or siRNA and knockdown of Nrf2 suppressed the stimulatory effects of tBHQ on ABCA1 expression and calpain activity.	2-tert-butylhydroquinone	121-125	heme oxygenase 1	Homo sapiens	14-18
23739547-7	2013	CONCLUSIONS: Nrf2/HO-1 signaling is required for the regulation by tBHQ of ABCA1 expression and cholesterol efflux in macrophage-derived foam cells and an antiatherogenic role of tBHQ is suggested.	2-tert-butylhydroquinone	67-71	heme oxygenase 1	Homo sapiens	18-22
23739547-7	2013	CONCLUSIONS: Nrf2/HO-1 signaling is required for the regulation by tBHQ of ABCA1 expression and cholesterol efflux in macrophage-derived foam cells and an antiatherogenic role of tBHQ is suggested.	Cholesterol	96-107	heme oxygenase 1	Homo sapiens	18-22
23739547-7	2013	CONCLUSIONS: Nrf2/HO-1 signaling is required for the regulation by tBHQ of ABCA1 expression and cholesterol efflux in macrophage-derived foam cells and an antiatherogenic role of tBHQ is suggested.	2-tert-butylhydroquinone	179-183	heme oxygenase 1	Homo sapiens	18-22
23720291-6	2013	The rate-controlling step of heme breakdown is catalyzed by heme oxygenase (HMOX), of which there are two isoforms, called HMOX1 and HMOX2.	Heme	29-33	heme oxygenase 1	Homo sapiens	123-128
24327821-4	2013	But the potential role of resveratrol against As2O3 in heart via nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) is unclear.	Resveratrol	26-37	heme oxygenase 1	Homo sapiens	120-136
23092324-5	2013	In the present study we investigated the combined effect of L-Carnosine and EGCG on the activation of two stress-responsive pathways: HO-1 and Hsp72 (the inducible form of Hsp70), which play an important role in cytoprotection against oxidative stress-induced cell damage.	epigallocatechin gallate	76-80	heme oxygenase 1	Homo sapiens	134-138
23092324-6	2013	We demonstrated that the neuroprotective effects of EGCG and L-Carnosine are achieved through the modulation of HO-1/Hsp72 systems.	epigallocatechin gallate	52-56	heme oxygenase 1	Homo sapiens	112-116
23092325-0	2013	Nuclear translocation of heme oxygenase-1 confers resistance to imatinib in chronic myeloid leukemia cells.	Imatinib Mesylate	64-72	heme oxygenase 1	Homo sapiens	25-41
23092325-5	2013	The aim of the present study was to investigate the effect of HO-1 expression on cell proliferation and apoptosis in chronic myeloid leukemia cells, K562 and LAMA-84 cell lines following imatinib treatment.	Imatinib Mesylate	187-195	heme oxygenase 1	Homo sapiens	62-66
23092325-6	2013	Cells were incubated for 24h with Imatinib (1 muM) alone or in combination with Hemin (10muM), an inducer of HO-1.	Imatinib Mesylate	34-42	heme oxygenase 1	Homo sapiens	109-113
23092325-6	2013	Cells were incubated for 24h with Imatinib (1 muM) alone or in combination with Hemin (10muM), an inducer of HO-1.	Hemin	80-85	heme oxygenase 1	Homo sapiens	109-113
23092325-7	2013	In addition, cells were also treated with HO byproducts, bilirubin and carbon monoxide (CO), or with a protease inhibitor (Ed64) to inhibit HO-1 nuclear translocation.	ed64	123-127	heme oxygenase 1	Homo sapiens	140-144
23092325-8	2013	Pharmacological induction of HO-1 was able to overcome the effect of imatinib.	Imatinib Mesylate	69-77	heme oxygenase 1	Homo sapiens	29-33
23092325-12	2013	Finally, imatinib was able to increase the formation of cellular reactive oxygen species (ROS) and this effect was reversed by HO-1 induction or the addition of N-acetylcisteine (NAC).	Imatinib Mesylate	9-17	heme oxygenase 1	Homo sapiens	127-131
23092325-12	2013	Finally, imatinib was able to increase the formation of cellular reactive oxygen species (ROS) and this effect was reversed by HO-1 induction or the addition of N-acetylcisteine (NAC).	Reactive Oxygen Species	65-88	heme oxygenase 1	Homo sapiens	127-131
23092325-12	2013	Finally, imatinib was able to increase the formation of cellular reactive oxygen species (ROS) and this effect was reversed by HO-1 induction or the addition of N-acetylcisteine (NAC).	Reactive Oxygen Species	90-93	heme oxygenase 1	Homo sapiens	127-131
23092325-13	2013	In conclusion, the protective effect of HO-1 on imatinib-induced cytotoxicity does not involve its enzymatic byproducts, but rather the nuclear translocation of HO-1 following proteolytic cleavage.	Imatinib Mesylate	48-56	heme oxygenase 1	Homo sapiens	40-44
23092325-13	2013	In conclusion, the protective effect of HO-1 on imatinib-induced cytotoxicity does not involve its enzymatic byproducts, but rather the nuclear translocation of HO-1 following proteolytic cleavage.	Imatinib Mesylate	48-56	heme oxygenase 1	Homo sapiens	161-165
23092328-0	2013	Heme Oxygenase-1 and breast cancer resistance protein protect against heme-induced toxicity.	Heme	70-74	heme oxygenase 1	Homo sapiens	0-16
23092328-5	2013	We postulated that overexpression of Heme Oxygenase-1 (HO-1) and Breast Cancer Resistance Protein (BCRP) would protect against heme-induced cytotoxicity.	Heme	127-131	heme oxygenase 1	Homo sapiens	37-53
23092328-5	2013	We postulated that overexpression of Heme Oxygenase-1 (HO-1) and Breast Cancer Resistance Protein (BCRP) would protect against heme-induced cytotoxicity.	Heme	127-131	heme oxygenase 1	Homo sapiens	55-59
23092328-6	2013	HO-1 is a heme-degrading enzyme generating carbon monoxide, iron, and biliverdin/bilirubin, while BCRP is a heme efflux transporter.	Carbon Monoxide	43-58	heme oxygenase 1	Homo sapiens	0-4
23092328-6	2013	HO-1 is a heme-degrading enzyme generating carbon monoxide, iron, and biliverdin/bilirubin, while BCRP is a heme efflux transporter.	Iron	60-64	heme oxygenase 1	Homo sapiens	0-4
23746277-9	2013	Historically, the first molecules used as non selective HO-1 inhibitors were metalloporphyrins (Mps).	Metalloporphyrins	77-94	heme oxygenase 1	Homo sapiens	56-60
23746277-9	2013	Historically, the first molecules used as non selective HO-1 inhibitors were metalloporphyrins (Mps).	Metalloporphyrins	96-99	heme oxygenase 1	Homo sapiens	56-60
23746277-10	2013	The subsequent development of the imidazole-dioxolane derivatives afforded the first generation of non-porphyrin based, isozyme selective HO-1 inhibitors.	imidazole-dioxolane	34-53	heme oxygenase 1	Homo sapiens	138-142
23746277-10	2013	The subsequent development of the imidazole-dioxolane derivatives afforded the first generation of non-porphyrin based, isozyme selective HO-1 inhibitors.	Porphyrins	103-112	heme oxygenase 1	Homo sapiens	138-142
23092328-6	2013	HO-1 is a heme-degrading enzyme generating carbon monoxide, iron, and biliverdin/bilirubin, while BCRP is a heme efflux transporter.	Biliverdine	70-80	heme oxygenase 1	Homo sapiens	0-4
23092328-6	2013	HO-1 is a heme-degrading enzyme generating carbon monoxide, iron, and biliverdin/bilirubin, while BCRP is a heme efflux transporter.	Bilirubin	81-90	heme oxygenase 1	Homo sapiens	0-4
23092328-9	2013	Heme-induced cell death was significantly attenuated when cells overexpressed HO-1, BCRP, or both.	Heme	0-4	heme oxygenase 1	Homo sapiens	78-82
23092328-11	2013	Also cells treated with the anti-oxidants N-acetylcysteine or HO-effector molecule bilirubin showed protection against heme insults, which may explain the increased protection by HO-1 compared to BCRP.	Acetylcysteine	42-58	heme oxygenase 1	Homo sapiens	179-183
23092328-11	2013	Also cells treated with the anti-oxidants N-acetylcysteine or HO-effector molecule bilirubin showed protection against heme insults, which may explain the increased protection by HO-1 compared to BCRP.	Bilirubin	83-92	heme oxygenase 1	Homo sapiens	179-183
23092328-11	2013	Also cells treated with the anti-oxidants N-acetylcysteine or HO-effector molecule bilirubin showed protection against heme insults, which may explain the increased protection by HO-1 compared to BCRP.	Heme	119-123	heme oxygenase 1	Homo sapiens	179-183
23092328-12	2013	In conclusion, both HO-1 and BCRP protect against heme-induced toxicity and may thus form novel therapeutic targets for heme-mediated pathologies.	Heme	50-54	heme oxygenase 1	Homo sapiens	20-24
23092328-12	2013	In conclusion, both HO-1 and BCRP protect against heme-induced toxicity and may thus form novel therapeutic targets for heme-mediated pathologies.	Heme	120-124	heme oxygenase 1	Homo sapiens	20-24
24302971-0	2013	Acetylshikonin, a Novel AChE Inhibitor, Inhibits Apoptosis via Upregulation of Heme Oxygenase-1 Expression in SH-SY5Y Cells.	acetylshikonin	0-14	heme oxygenase 1	Homo sapiens	79-95
24302971-7	2013	Furthermore, we identified for the first time that the upregulation of heme oxygenase 1 by acetylshikonin is a key step mediating its antiapoptotic activity from oxidative stress in SH-SY5Y cells.	acetylshikonin	91-105	heme oxygenase 1	Homo sapiens	71-87
24327821-4	2013	But the potential role of resveratrol against As2O3 in heart via nuclear factor erythroid 2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) is unclear.	Resveratrol	26-37	heme oxygenase 1	Homo sapiens	138-142
24327821-8	2013	Furthermore, resveratrol significantly prohibited the downregulation of both Nrf2 and HO-1 gene expressions that were downregulated by As2O3, whereas resveratrol did not alter As2O3-induced nitric oxide formation.	Resveratrol	13-24	heme oxygenase 1	Homo sapiens	86-90
24327821-8	2013	Furthermore, resveratrol significantly prohibited the downregulation of both Nrf2 and HO-1 gene expressions that were downregulated by As2O3, whereas resveratrol did not alter As2O3-induced nitric oxide formation.	Arsenic Trioxide	135-140	heme oxygenase 1	Homo sapiens	86-90
24327821-9	2013	Thus, the protective role of resveratrol against As2O3-induced cardiotoxicity is implemented by the maintenance of redox homeostasis (Nrf2-HO-1 pathway) and facilitating arsenic efflux.	Resveratrol	29-40	heme oxygenase 1	Homo sapiens	139-143
24327821-9	2013	Thus, the protective role of resveratrol against As2O3-induced cardiotoxicity is implemented by the maintenance of redox homeostasis (Nrf2-HO-1 pathway) and facilitating arsenic efflux.	Arsenic Trioxide	49-54	heme oxygenase 1	Homo sapiens	139-143
23573137-0	2013	The protective effect of alpha-lipoic Acid in lipopolysaccharide-induced acute lung injury is mediated by heme oxygenase-1.	Thioctic Acid	25-42	heme oxygenase 1	Homo sapiens	106-122
23573137-6	2013	Interestingly, treatment with ALA significantly increased nuclear factor-erythroid 2-related factor 2 (Nrf2) activation and HO-1 expression in lungs of ALI.	Thioctic Acid	30-33	heme oxygenase 1	Homo sapiens	124-128
23573137-3	2013	The aim of study was to test the hypothesis that the protection of ALA against lipopolysaccharide-(LPS-) induced acute lung injury (ALI) is mediated by HO-1.	Thioctic Acid	67-70	heme oxygenase 1	Homo sapiens	152-156
23573137-7	2013	However, blocking HO-1 activity by tin protoporphyrin IX (SnPP), an HO-1 inhibitor, markedly abolished these beneficial effects of ALA in LPS-induced ALI.	tin protoporphyrin IX	35-56	heme oxygenase 1	Homo sapiens	18-22
23573137-7	2013	However, blocking HO-1 activity by tin protoporphyrin IX (SnPP), an HO-1 inhibitor, markedly abolished these beneficial effects of ALA in LPS-induced ALI.	tin protoporphyrin IX	35-56	heme oxygenase 1	Homo sapiens	68-72
23063670-1	2013	The aim of this study was to evaluate the effect of phloretamide (PA), an apple constituent, on the activation of the Nrf2 transcription factor and the expression of its target genes: glutathione S-transferases (GSTs), NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase-1 (HO-1) in normal human THLE-2 hepatocytes and the hepatoma HepG2 cell line.	phloretamide	52-64	heme oxygenase 1	Homo sapiens	281-285
23573137-7	2013	However, blocking HO-1 activity by tin protoporphyrin IX (SnPP), an HO-1 inhibitor, markedly abolished these beneficial effects of ALA in LPS-induced ALI.	S-Nitroso-N-propionyl-D,L-penicillamine	58-62	heme oxygenase 1	Homo sapiens	18-22
23573137-7	2013	However, blocking HO-1 activity by tin protoporphyrin IX (SnPP), an HO-1 inhibitor, markedly abolished these beneficial effects of ALA in LPS-induced ALI.	S-Nitroso-N-propionyl-D,L-penicillamine	58-62	heme oxygenase 1	Homo sapiens	68-72
23573137-7	2013	However, blocking HO-1 activity by tin protoporphyrin IX (SnPP), an HO-1 inhibitor, markedly abolished these beneficial effects of ALA in LPS-induced ALI.	Thioctic Acid	131-134	heme oxygenase 1	Homo sapiens	18-22
23573137-7	2013	However, blocking HO-1 activity by tin protoporphyrin IX (SnPP), an HO-1 inhibitor, markedly abolished these beneficial effects of ALA in LPS-induced ALI.	Thioctic Acid	131-134	heme oxygenase 1	Homo sapiens	68-72
23573137-8	2013	These results suggest that the protection mechanism of ALA may be through HO-1 induction and in turn suppressing NF- kappa B-mediated inflammatory responses.	Thioctic Acid	55-58	heme oxygenase 1	Homo sapiens	74-78
23063670-1	2013	The aim of this study was to evaluate the effect of phloretamide (PA), an apple constituent, on the activation of the Nrf2 transcription factor and the expression of its target genes: glutathione S-transferases (GSTs), NAD(P)H:quinone oxidoreductase-1 (NQO1) and heme oxygenase-1 (HO-1) in normal human THLE-2 hepatocytes and the hepatoma HepG2 cell line.	phloretamide	66-68	heme oxygenase 1	Homo sapiens	281-285
24094245-3	2013	Electrophoretic mobility-shift assays (EMSAs) showed that ARE was a prominent element for HO-1 induction after low-concentration HBCDs exposure.	hexabromocyclododecane	129-134	heme oxygenase 1	Homo sapiens	90-94
24094245-4	2013	The relationship between PI3K/Akt pathway and Nrf2/HO-1 axis was demonstrated by the finding that pretreatment with PI3K inhibitors (wortmannin, LY294002) attenuated the upregulation of Nrf2 expression induced by HBCDs exposure.	Wortmannin	133-143	heme oxygenase 1	Homo sapiens	51-55
24485305-1	2013	Haem oxygenase 1 (HO-1) plays a pivotal role in metabolic stress protecting cells in dependence on reactive oxygen species.	Reactive Oxygen Species	99-122	heme oxygenase 1	Homo sapiens	0-22
24094245-4	2013	The relationship between PI3K/Akt pathway and Nrf2/HO-1 axis was demonstrated by the finding that pretreatment with PI3K inhibitors (wortmannin, LY294002) attenuated the upregulation of Nrf2 expression induced by HBCDs exposure.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	145-153	heme oxygenase 1	Homo sapiens	51-55
24094245-4	2013	The relationship between PI3K/Akt pathway and Nrf2/HO-1 axis was demonstrated by the finding that pretreatment with PI3K inhibitors (wortmannin, LY294002) attenuated the upregulation of Nrf2 expression induced by HBCDs exposure.	hexabromocyclododecane	213-218	heme oxygenase 1	Homo sapiens	51-55
23103292-1	2013	Heme oxygenase (HO)-1, the inducible isoform of the first and rate-limiting enzyme of heme degradation, affords anti-inflammatory protection via its cell-type-specific effects in endothelial cells (ECs).	Heme	86-90	heme oxygenase 1	Homo sapiens	0-21
23103292-7	2013	Reactive oxygen species, which were generated by NADPH oxidase and in turn activated the phosphatidylinositol 3-kinase (PI3K)/Akt cascade, were involved in this upregulation of HO-1 gene expression.	Reactive Oxygen Species	0-23	heme oxygenase 1	Homo sapiens	177-181
23476651-0	2013	Zinc Protoporphyrin Upregulates Heme Oxygenase-1 in PC-3 Cells via the Stress Response Pathway.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	32-48
23476651-1	2013	Zinc protoporphyrin IX (ZnPP), a naturally occurring molecule formed in iron deficiency or lead poisoning, is a potent competitive inhibitor of heme oxygenase-1 (HO-1).	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	144-160
23476651-1	2013	Zinc protoporphyrin IX (ZnPP), a naturally occurring molecule formed in iron deficiency or lead poisoning, is a potent competitive inhibitor of heme oxygenase-1 (HO-1).	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	162-166
23476651-1	2013	Zinc protoporphyrin IX (ZnPP), a naturally occurring molecule formed in iron deficiency or lead poisoning, is a potent competitive inhibitor of heme oxygenase-1 (HO-1).	zinc protoporphyrin	24-28	heme oxygenase 1	Homo sapiens	144-160
23476651-1	2013	Zinc protoporphyrin IX (ZnPP), a naturally occurring molecule formed in iron deficiency or lead poisoning, is a potent competitive inhibitor of heme oxygenase-1 (HO-1).	zinc protoporphyrin	24-28	heme oxygenase 1	Homo sapiens	162-166
23476651-3	2013	However, the effect of ZnPP on HO-1 expression is controversial.	zinc protoporphyrin	23-27	heme oxygenase 1	Homo sapiens	31-35
23476651-5	2013	The objective of this study is to investigate the effect of ZnPP on HO-1 expression in prostate cancer PC-3 cells.	zinc protoporphyrin	60-64	heme oxygenase 1	Homo sapiens	68-72
23476651-6	2013	Incubation of PC-3 cells with 10  mu M ZnPP for 4 h showed only a slight induction of HO-1 mRNA and protein, but the induction was high after 16 h and was maintained through 48 h of incubation.	zinc protoporphyrin	39-43	heme oxygenase 1	Homo sapiens	86-90
23476651-8	2013	Of the various protein kinase inhibitors and antioxidant tested, only Ro 31-8220 abrogated ZnPP-induced HO-1 expression, suggesting that activation of HO-1 gene by ZnPP may involve protein kinase C (PKC).	zinc protoporphyrin	91-95	heme oxygenase 1	Homo sapiens	104-108
23476651-8	2013	Of the various protein kinase inhibitors and antioxidant tested, only Ro 31-8220 abrogated ZnPP-induced HO-1 expression, suggesting that activation of HO-1 gene by ZnPP may involve protein kinase C (PKC).	zinc protoporphyrin	91-95	heme oxygenase 1	Homo sapiens	151-155
23476651-8	2013	Of the various protein kinase inhibitors and antioxidant tested, only Ro 31-8220 abrogated ZnPP-induced HO-1 expression, suggesting that activation of HO-1 gene by ZnPP may involve protein kinase C (PKC).	zinc protoporphyrin	164-168	heme oxygenase 1	Homo sapiens	104-108
23476651-8	2013	Of the various protein kinase inhibitors and antioxidant tested, only Ro 31-8220 abrogated ZnPP-induced HO-1 expression, suggesting that activation of HO-1 gene by ZnPP may involve protein kinase C (PKC).	zinc protoporphyrin	164-168	heme oxygenase 1	Homo sapiens	151-155
24148794-0	2013	Heme oxygenase-1 mediates the anti-inflammatory effect of molecular hydrogen in LPS-stimulated RAW 264.7 macrophages.	Hydrogen	68-76	heme oxygenase 1	Homo sapiens	0-16
23569422-0	2013	Propofol-induced protection of SH-SY5Y cells against hydrogen peroxide is associated with the HO-1 via the ERK pathway.	Propofol	0-8	heme oxygenase 1	Homo sapiens	94-98
23569422-0	2013	Propofol-induced protection of SH-SY5Y cells against hydrogen peroxide is associated with the HO-1 via the ERK pathway.	Hydrogen Peroxide	53-70	heme oxygenase 1	Homo sapiens	94-98
23569422-5	2013	Additionally, the potential roles of ERK, p 38 MAPK and JNK in the regulation of propofol-induced endogenous HO-1 expression in SH-SY5Y cells were estimated by Western blotting assays.	Propofol	81-89	heme oxygenase 1	Homo sapiens	109-113
24148794-10	2013	Furthermore, H2 treatment could also dose-dependently increase the HO-1 protein expression and activity at 3 h, 6 h, 12 h and 24 h in LPS-activated macrophages.	Hydrogen	13-15	heme oxygenase 1	Homo sapiens	67-71
24148794-11	2013	In addition, blockade of HO-1 activity with ZnPP-IX partly reversed the anti-inflammatory effect of H2 in LPS-stimulated macrophages.	Hydrogen	100-102	heme oxygenase 1	Homo sapiens	25-29
24148794-2	2013	In the present study, we investigated whether heme oxygenase-1 (HO-1) contributes to the anti-inflammatory effect of H2 in lipopolysaccharide (LPS)-stimulated RAW 264.7 macrophages.	Hydrogen	117-119	heme oxygenase 1	Homo sapiens	46-62
24148794-12	2013	CONCLUSIONS: Molecular hydrogen exerts a regulating role in the release of pro- and anti-inflammatory cytokines in LPS-stimulated macrophages, and this effect is at least partly mediated by HO-1 expression and activation.	Hydrogen	23-31	heme oxygenase 1	Homo sapiens	190-194
24148794-2	2013	In the present study, we investigated whether heme oxygenase-1 (HO-1) contributes to the anti-inflammatory effect of H2 in lipopolysaccharide (LPS)-stimulated RAW 264.7 macrophages.	Hydrogen	117-119	heme oxygenase 1	Homo sapiens	64-68
22901690-0	2013	Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-kappaB pathways.	Docosahexaenoic Acids	0-20	heme oxygenase 1	Homo sapiens	89-105
22945906-0	2013	Peroxisome proliferator-activated receptor delta agonist attenuates nicotine suppression effect on human mesenchymal stem cell-derived osteogenesis and involves increased expression of heme oxygenase-1.	Nicotine	68-76	heme oxygenase 1	Homo sapiens	185-201
22819551-3	2013	Here, we report that HO-1 and SOCS-3 were induced in A549 cells and human pulmonary alveolar epithelial cells (HPAEpiCs) treated with (-)-epigallocatechin-3-gallate (EGCG).	epigallocatechin gallate	134-164	heme oxygenase 1	Homo sapiens	21-25
22819551-3	2013	Here, we report that HO-1 and SOCS-3 were induced in A549 cells and human pulmonary alveolar epithelial cells (HPAEpiCs) treated with (-)-epigallocatechin-3-gallate (EGCG).	epigallocatechin gallate	166-170	heme oxygenase 1	Homo sapiens	21-25
25506596-6	2013	Heme also induces a cytoprotective response that includes Nrf2 responsive genes such as heme oxygenase-1, ferritin, haptoglobin, hemopexin, and other antioxidant response genes.	Heme	0-4	heme oxygenase 1	Homo sapiens	88-104
22945906-6	2013	Nicotine caused a dose-dependent decrease in cell proliferation, decreased heme oxygenase-1 (HO-1) expression (p &lt; 0.05) and attenuated osteogenesis (p &lt; 0.05) in hMSCs (45 % reduction at day 14).	Nicotine	0-8	heme oxygenase 1	Homo sapiens	75-91
22945906-6	2013	Nicotine caused a dose-dependent decrease in cell proliferation, decreased heme oxygenase-1 (HO-1) expression (p &lt; 0.05) and attenuated osteogenesis (p &lt; 0.05) in hMSCs (45 % reduction at day 14).	Nicotine	0-8	heme oxygenase 1	Homo sapiens	93-97
22945906-8	2013	Induction of HO-1 by peroxisome proliferator-activated receptor delta agonist (GW0742) prevented the effect of nicotine.	GW0742	79-85	heme oxygenase 1	Homo sapiens	13-17
22945906-8	2013	Induction of HO-1 by peroxisome proliferator-activated receptor delta agonist (GW0742) prevented the effect of nicotine.	Nicotine	111-119	heme oxygenase 1	Homo sapiens	13-17
22945906-10	2013	Therefore, induction of HO-1 prevents the deleterious effects of nicotine on osteogenesis in hMSC.	Nicotine	65-73	heme oxygenase 1	Homo sapiens	24-28
22901690-6	2013	DHA activated Akt, p38 and ERK1/2 phosphorylation, and specific inhibitors of respective pathways attenuated DHA-induced Nrf2 nuclear translocation and HO-1 expression.	Docosahexaenoic Acids	109-112	heme oxygenase 1	Homo sapiens	152-156
22901690-7	2013	Transfection with HO-1 siRNA knocked down HO-1 expression and partially reversed the DHA-mediated inhibition of TNF-alpha-induced p65 nuclear translocation and ICAM-1 expression.	Docosahexaenoic Acids	85-88	heme oxygenase 1	Homo sapiens	18-22
22901690-8	2013	Importantly, we show for the first time that HO-1 plays a down-regulatory role in NF-kappaB nuclear translocation, and inhibition of Nrf2 ubiquitination and proteasome activity are involved in increased cellular Nrf2 level by DHA.	Docosahexaenoic Acids	226-229	heme oxygenase 1	Homo sapiens	45-49
22901690-9	2013	In this study, we show that HO-1 plays a down-regulatory role in NF-kappaB nuclear translocation and that the protective effect of DHA against inflammation is partially via up-regulation of Nrf2-mediated HO-1 expression and inhibition of IKK/NF-kappaB signaling pathway.	Docosahexaenoic Acids	131-134	heme oxygenase 1	Homo sapiens	204-208
22901690-4	2013	DHA triggered early-stage and transient reactive oxygen species (ROS) generation and significantly increased the protein expression of heme oxygenase 1 (HO-1), induced nuclear factor erythroid 2-related factor 2 (Nrf2) translocation to the nucleus and up-regulated antioxidant response element (ARE)-luciferase reporter activity.	Docosahexaenoic Acids	0-3	heme oxygenase 1	Homo sapiens	135-151
22901690-4	2013	DHA triggered early-stage and transient reactive oxygen species (ROS) generation and significantly increased the protein expression of heme oxygenase 1 (HO-1), induced nuclear factor erythroid 2-related factor 2 (Nrf2) translocation to the nucleus and up-regulated antioxidant response element (ARE)-luciferase reporter activity.	Docosahexaenoic Acids	0-3	heme oxygenase 1	Homo sapiens	153-157
22901690-6	2013	DHA activated Akt, p38 and ERK1/2 phosphorylation, and specific inhibitors of respective pathways attenuated DHA-induced Nrf2 nuclear translocation and HO-1 expression.	Docosahexaenoic Acids	0-3	heme oxygenase 1	Homo sapiens	152-156
24101950-0	2013	Therapeutic roles of heme oxygenase-1 in metabolic diseases: curcumin and resveratrol analogues as possible inducers of heme oxygenase-1.	Curcumin	61-69	heme oxygenase 1	Homo sapiens	120-136
23538677-3	2013	In this study, we investigated effects of fisetin, a natural bioactive flavonoid that has been reported to induce HO-1 expression, on the differentiation of macrophages into OCLs.	fisetin	42-49	heme oxygenase 1	Homo sapiens	114-118
23864927-7	2013	SUL exerted antioxidant potential by upregulating expression of antioxidant enzymes including gamma-glutamylcysteine ligase, NAD(P)H:quinone oxidoreductase-1, and heme oxygenase-1 via activation of NF-E2-related factor 2(Nrf2).	sulforaphane	0-3	heme oxygenase 1	Homo sapiens	163-179
24101950-0	2013	Therapeutic roles of heme oxygenase-1 in metabolic diseases: curcumin and resveratrol analogues as possible inducers of heme oxygenase-1.	Resveratrol	74-85	heme oxygenase 1	Homo sapiens	120-136
24288584-10	2013	Thus, our results suggest that quercetin enhances mitochondrial biogenesis mainly via the HO-1/CO system in vitro and in vivo.	Quercetin	31-40	heme oxygenase 1	Homo sapiens	90-97
23536765-2	2013	Since the heme catabolic pathway plays an important role in antioxidant protection, we attempted to assess the gene expression of key enzymes of heme catabolism, heme oxygenase 1 (HMOX1), heme oxygenase 2 (HMOX2), and biliverdin reductase A (BLVRA) in the liver and peripheral blood leukocytes (PBL) of patients chronically infected with HCV.	Heme	10-14	heme oxygenase 1	Homo sapiens	162-178
23134284-10	2013	The expression of HO-1 and nuclear translocation of Nrf2 were increased by Abeta treatment.	UNII-042A8N37WH	75-80	heme oxygenase 1	Homo sapiens	18-22
23536765-2	2013	Since the heme catabolic pathway plays an important role in antioxidant protection, we attempted to assess the gene expression of key enzymes of heme catabolism, heme oxygenase 1 (HMOX1), heme oxygenase 2 (HMOX2), and biliverdin reductase A (BLVRA) in the liver and peripheral blood leukocytes (PBL) of patients chronically infected with HCV.	Heme	10-14	heme oxygenase 1	Homo sapiens	180-185
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	heme - carbon monoxide	105-127	heme oxygenase 1	Homo sapiens	11-27
23874015-4	2013	HO-1, a microsomal enzyme, catalyzes the breakdown of pro-oxidant heme, which is released from heme proteins to equimolar quantities of iron, carbon monoxide, and biliverdin.	Heme	66-70	heme oxygenase 1	Homo sapiens	0-4
23874015-4	2013	HO-1, a microsomal enzyme, catalyzes the breakdown of pro-oxidant heme, which is released from heme proteins to equimolar quantities of iron, carbon monoxide, and biliverdin.	Iron	136-140	heme oxygenase 1	Homo sapiens	0-4
23874015-4	2013	HO-1, a microsomal enzyme, catalyzes the breakdown of pro-oxidant heme, which is released from heme proteins to equimolar quantities of iron, carbon monoxide, and biliverdin.	Carbon Monoxide	142-157	heme oxygenase 1	Homo sapiens	0-4
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	heme - carbon monoxide	105-127	heme oxygenase 1	Homo sapiens	29-33
23874015-4	2013	HO-1, a microsomal enzyme, catalyzes the breakdown of pro-oxidant heme, which is released from heme proteins to equimolar quantities of iron, carbon monoxide, and biliverdin.	Biliverdine	163-173	heme oxygenase 1	Homo sapiens	0-4
23874015-6	2013	The beneficial effects of HO-1 expression are not merely due to heme degradation but are also attributed to the cytoprotective properties of the byproducts of the reaction.	Heme	64-68	heme oxygenase 1	Homo sapiens	26-30
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	Carbon Monoxide	129-131	heme oxygenase 1	Homo sapiens	11-27
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	Carbon Monoxide	129-131	heme oxygenase 1	Homo sapiens	29-33
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	Biliverdine	134-144	heme oxygenase 1	Homo sapiens	11-27
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	Biliverdine	134-144	heme oxygenase 1	Homo sapiens	29-33
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	Iron	150-154	heme oxygenase 1	Homo sapiens	11-27
23140858-2	2013	The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally.	Iron	150-154	heme oxygenase 1	Homo sapiens	29-33
22444871-0	2012	Inhibition of NF-kappaB nuclear translocation via HO-1 activation underlies alpha-tocopheryl succinate toxicity.	alpha-Tocopherol	76-102	heme oxygenase 1	Homo sapiens	50-54
22882835-0	2012	Evaluation of imidazole-based compounds as heme oxygenase-1 inhibitors.	imidazole	14-23	heme oxygenase 1	Homo sapiens	43-59
22882835-4	2012	The binding of the most active compound 11 with heme or heme-conjugated human heme oxygenase-1 was also examined by spectral analyses.	Heme	56-60	heme oxygenase 1	Homo sapiens	78-94
23217388-10	2012	The mRNA expression of HO-1 in the high glucose group was significantly increased in a time-dependent manner compared with that in the control group (P &lt; 0.05).	Glucose	40-47	heme oxygenase 1	Homo sapiens	23-27
23217388-11	2012	Adiponectin further increased the mRNA expression of HO-1 induced by high glucose in a time-dependent manner (P &lt; 0.05).The expression of p66Shc was significantly increased in high glucose group compared with that in the control group (P &lt; 0.05).	Glucose	74-81	heme oxygenase 1	Homo sapiens	53-57
23217388-11	2012	Adiponectin further increased the mRNA expression of HO-1 induced by high glucose in a time-dependent manner (P &lt; 0.05).The expression of p66Shc was significantly increased in high glucose group compared with that in the control group (P &lt; 0.05).	Glucose	184-191	heme oxygenase 1	Homo sapiens	53-57
23000247-6	2012	The CPN-9-mediated upregulation of HO-1, NQO1, and GCLM was abolished by Nrf2 knockdown.	cpn-9	4-9	heme oxygenase 1	Homo sapiens	35-39
23100518-2	2012	This acquired neutrophil dysfunction is a consequence of induction of the cytoprotective, heme-degrading enzyme heme oxygenase-1 (HO-1) in neutrophil progenitors in bone marrow.	Heme	90-94	heme oxygenase 1	Homo sapiens	112-128
23100518-2	2012	This acquired neutrophil dysfunction is a consequence of induction of the cytoprotective, heme-degrading enzyme heme oxygenase-1 (HO-1) in neutrophil progenitors in bone marrow.	Heme	90-94	heme oxygenase 1	Homo sapiens	130-134
23144452-6	2012	Dietary CLA and nitrite supplementation in rodents elevates NO(2)-CLA levels in plasma, urine, and tissues, which in turn induces heme oxygenase-1 (HO-1) expression in the colonic epithelium.	Linoleic Acids, Conjugated	8-11	heme oxygenase 1	Homo sapiens	130-146
23144452-6	2012	Dietary CLA and nitrite supplementation in rodents elevates NO(2)-CLA levels in plasma, urine, and tissues, which in turn induces heme oxygenase-1 (HO-1) expression in the colonic epithelium.	Nitrites	16-23	heme oxygenase 1	Homo sapiens	130-146
23144452-6	2012	Dietary CLA and nitrite supplementation in rodents elevates NO(2)-CLA levels in plasma, urine, and tissues, which in turn induces heme oxygenase-1 (HO-1) expression in the colonic epithelium.	Nitrogen Dioxide	60-65	heme oxygenase 1	Homo sapiens	130-146
22444871-6	2012	This effect is suppressed by the pharmacological inhibition of HO-1 and mimicked by the end-products of HO activity, i.e., bilirubin and carbon monoxide.	Bilirubin	123-132	heme oxygenase 1	Homo sapiens	63-67
22956150-3	2012	Aim of investigation was to study the effects of cholinergic precursors (choline, CDP-choline, Acetylcholine and alpha-Glyceril-Phosphorylcholine) on HO-1 and p21 expression during astroglial cell proliferation and differentiation in primary cultures at 14 and 35 days in vitro (DIV) treated for 24 h with choline metabolites.	Choline	49-56	heme oxygenase 1	Homo sapiens	150-154
22956150-3	2012	Aim of investigation was to study the effects of cholinergic precursors (choline, CDP-choline, Acetylcholine and alpha-Glyceril-Phosphorylcholine) on HO-1 and p21 expression during astroglial cell proliferation and differentiation in primary cultures at 14 and 35 days in vitro (DIV) treated for 24 h with choline metabolites.	Acetylcholine	95-108	heme oxygenase 1	Homo sapiens	150-154
22956150-3	2012	Aim of investigation was to study the effects of cholinergic precursors (choline, CDP-choline, Acetylcholine and alpha-Glyceril-Phosphorylcholine) on HO-1 and p21 expression during astroglial cell proliferation and differentiation in primary cultures at 14 and 35 days in vitro (DIV) treated for 24 h with choline metabolites.	alpha-glyceril-phosphorylcholine	113-145	heme oxygenase 1	Homo sapiens	150-154
22956150-3	2012	Aim of investigation was to study the effects of cholinergic precursors (choline, CDP-choline, Acetylcholine and alpha-Glyceril-Phosphorylcholine) on HO-1 and p21 expression during astroglial cell proliferation and differentiation in primary cultures at 14 and 35 days in vitro (DIV) treated for 24 h with choline metabolites.	Choline	73-80	heme oxygenase 1	Homo sapiens	150-154
22956150-5	2012	On the contrary, ACh and choline induced a significant increase of HO-1 expression in 14 DIV astrocyte cultures.	Acetylcholine	17-20	heme oxygenase 1	Homo sapiens	67-71
22956150-5	2012	On the contrary, ACh and choline induced a significant increase of HO-1 expression in 14 DIV astrocyte cultures.	Choline	25-32	heme oxygenase 1	Homo sapiens	67-71
22956150-6	2012	Surprisingly, choline and ACh dramatically reduced HO-1 expression at 35 DIV.	Choline	14-21	heme oxygenase 1	Homo sapiens	51-55
22956150-6	2012	Surprisingly, choline and ACh dramatically reduced HO-1 expression at 35 DIV.	Acetylcholine	26-29	heme oxygenase 1	Homo sapiens	51-55
23171578-2	2012	CO-RMs containing transition metal carbonyls were initially implemented to mimic the function of heme oxygenase-1 (HMOX1), a stress inducible defensive protein that degrades heme to CO and biliverdin leading to anti-oxidant and anti-inflammatory actions.	Metals	29-34	heme oxygenase 1	Homo sapiens	97-113
23300448-10	2012	Moreover, HMOX-1 mRNA levels are enhanced in lovastatin-treated healthy and infected brains.	Lovastatin	45-55	heme oxygenase 1	Homo sapiens	10-16
23022510-0	2012	L-ascorbate attenuates methamphetamine neurotoxicity through enhancing the induction of endogenous heme oxygenase-1.	Ascorbic Acid	0-11	heme oxygenase 1	Homo sapiens	99-115
23022510-0	2012	L-ascorbate attenuates methamphetamine neurotoxicity through enhancing the induction of endogenous heme oxygenase-1.	Methamphetamine	23-38	heme oxygenase 1	Homo sapiens	99-115
23171578-2	2012	CO-RMs containing transition metal carbonyls were initially implemented to mimic the function of heme oxygenase-1 (HMOX1), a stress inducible defensive protein that degrades heme to CO and biliverdin leading to anti-oxidant and anti-inflammatory actions.	Metals	29-34	heme oxygenase 1	Homo sapiens	115-120
23171578-2	2012	CO-RMs containing transition metal carbonyls were initially implemented to mimic the function of heme oxygenase-1 (HMOX1), a stress inducible defensive protein that degrades heme to CO and biliverdin leading to anti-oxidant and anti-inflammatory actions.	Heme	97-101	heme oxygenase 1	Homo sapiens	115-120
23171578-2	2012	CO-RMs containing transition metal carbonyls were initially implemented to mimic the function of heme oxygenase-1 (HMOX1), a stress inducible defensive protein that degrades heme to CO and biliverdin leading to anti-oxidant and anti-inflammatory actions.	Biliverdine	189-199	heme oxygenase 1	Homo sapiens	97-113
23171578-2	2012	CO-RMs containing transition metal carbonyls were initially implemented to mimic the function of heme oxygenase-1 (HMOX1), a stress inducible defensive protein that degrades heme to CO and biliverdin leading to anti-oxidant and anti-inflammatory actions.	Biliverdine	189-199	heme oxygenase 1	Homo sapiens	115-120
22750196-4	2012	Induction of HO-1 during chronic hypoxia is necessary for the continued breakdown of heme for the enhanced production of hemoglobin and the increased respiratory and sympathetic responses.	Heme	85-89	heme oxygenase 1	Homo sapiens	13-17
24009841-4	2012	Activation of Nrf2 by triterpenoids induces the expression of phase 2 detoxifying and antioxidant enzymes such as NAD(P)H quinone oxidoreductase 1 (NQO1) and heme oxygenase-1 (HO-1) - proteins which can protect cells or tissues against various toxic metabolites.	triterpenoids	22-35	heme oxygenase 1	Homo sapiens	158-174
23026832-8	2012	However, LY294002 markedly quenched ROS and NO generation and diminished the protein expression of heme peroxidase enzyme (HO-1) and inducible nitric oxide synthase (iNOS).	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	9-17	heme oxygenase 1	Homo sapiens	123-127
22965812-2	2012	The expression of heme oxygenase-1 (HO-1), the rate-limiting enzyme involved in heme degradation, correlates well with the severity of psoriasis, and is a heritable trait.	Heme	18-22	heme oxygenase 1	Homo sapiens	36-40
22965812-3	2012	This study aimed to assess the role of (GT)(n) dinucleotide repeat polymorphisms in the promoter region of the HO-1 gene in Chinese-Taiwanese patients with psoriasis.	(n) dinucleotide	43-59	heme oxygenase 1	Homo sapiens	111-115
22966170-2	2012	Heme oxygenase-1 (gene HMOX1; protein HO-1) is the inducible, rate-limiting enzyme in the catabolism of heme and might attenuate the severity of outcomes from vaso-occlusive and hemolytic crises.	Heme	104-108	heme oxygenase 1	Homo sapiens	0-16
22966170-2	2012	Heme oxygenase-1 (gene HMOX1; protein HO-1) is the inducible, rate-limiting enzyme in the catabolism of heme and might attenuate the severity of outcomes from vaso-occlusive and hemolytic crises.	Heme	104-108	heme oxygenase 1	Homo sapiens	23-28
22966170-3	2012	A (GT)(n) dinucleotide repeat located in the promoter region of the HMOX1 gene is highly polymorphic, with long repeat lengths linked to decreased activity and inducibility.	(n) dinucleotide	6-22	heme oxygenase 1	Homo sapiens	68-73
23187004-5	2012	Pretreatment with Ly294002, a PI3K inhibitor, augmented the decrease in HO-1 level by their combination, whereas no obvious changes were observed in Nrf2 levels.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	18-26	heme oxygenase 1	Homo sapiens	72-76
22982394-5	2012	In addition, isochlorogenic acid A declined markedly the content of hepatitis B virus covalently closed circular DNA (HBV cccDNA) and induced significantly the heme oxygenase-1 (HO-1) expression in HepG2.2.15 cells.	Isochlorogenic acid A	13-34	heme oxygenase 1	Homo sapiens	178-182
22922731-0	2012	Curcumin inhibits HCV replication by induction of heme oxygenase-1 and             suppression of AKT.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	50-66
22922731-5	2012	Under the same conditions, curcumin also dose-dependently induced heme oxygenase-1 with the highest induction at 24 h. Hemin, a heme oxygenase-1 inducer, also inhibited HCV protein expression in a dose-dependent manner.	Curcumin	27-35	heme oxygenase 1	Homo sapiens	66-82
22922731-5	2012	Under the same conditions, curcumin also dose-dependently induced heme oxygenase-1 with the highest induction at 24 h. Hemin, a heme oxygenase-1 inducer, also inhibited HCV protein expression in a dose-dependent manner.	Curcumin	27-35	heme oxygenase 1	Homo sapiens	128-144
22922731-6	2012	The knockdown of heme oxygenase-1 partially reversed the curcumin-inhibited HCV protein expression.	Curcumin	57-65	heme oxygenase 1	Homo sapiens	17-33
22922731-7	2012	In addition to the heme oxygenase-1 induction, signaling molecule activities of AKT, extracellular signal-regulated kinases (ERK) and nuclear factor-kappaB (NF-kappaB) were inhibited by curcumin.	Curcumin	186-194	heme oxygenase 1	Homo sapiens	19-35
22922731-10	2012	In summary, curcumin inhibited HCV replication by heme oxygenase-1 induction and AKT pathway inhibition.	Curcumin	12-20	heme oxygenase 1	Homo sapiens	50-66
22940790-1	2012	In response to reactive oxygen species (ROS) or electrophiles, the transcription factor nuclear factor-erythroid 2 (NF-E2)-related factor 2 (Nrf2) rapidly translocates into the nucleus and induces the expression of various antioxidant genes, such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	15-38	heme oxygenase 1	Homo sapiens	250-266
22940790-1	2012	In response to reactive oxygen species (ROS) or electrophiles, the transcription factor nuclear factor-erythroid 2 (NF-E2)-related factor 2 (Nrf2) rapidly translocates into the nucleus and induces the expression of various antioxidant genes, such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	15-38	heme oxygenase 1	Homo sapiens	268-272
22940790-1	2012	In response to reactive oxygen species (ROS) or electrophiles, the transcription factor nuclear factor-erythroid 2 (NF-E2)-related factor 2 (Nrf2) rapidly translocates into the nucleus and induces the expression of various antioxidant genes, such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	40-43	heme oxygenase 1	Homo sapiens	250-266
22940790-1	2012	In response to reactive oxygen species (ROS) or electrophiles, the transcription factor nuclear factor-erythroid 2 (NF-E2)-related factor 2 (Nrf2) rapidly translocates into the nucleus and induces the expression of various antioxidant genes, such as heme oxygenase-1 (HO-1).	Reactive Oxygen Species	40-43	heme oxygenase 1	Homo sapiens	268-272
22982394-8	2012	Overexpression of HO-1 may contribute to the anti-HBV activity of isochlorogenic acid A by reducing the stability of the HBV core protein and thus blocking the refill of nuclear HBV cccDNA.	Isochlorogenic acid A	66-87	heme oxygenase 1	Homo sapiens	18-22
22982394-9	2012	Additionally, the hepatoprotective effect of isochlorogenic acid A could be achieved by its antioxidative property and induction of HO-1.	Isochlorogenic acid A	45-66	heme oxygenase 1	Homo sapiens	132-136
22864061-2	2012	In this study, we investigated whether sildenafil promotes the production of the sGC-stimulatory gases, carbon monoxide and nitric oxide, by stimulating the expression of the inducible isoforms of heme oxygenase (HO-1) and nitric oxide synthase (iNOS) in vascular smooth muscle cells (SMCs).	Sildenafil Citrate	39-49	heme oxygenase 1	Homo sapiens	213-217
22659318-0	2012	Cadmium-induced apoptosis in the BJAB human B cell line: involvement of PKC/ERK1/2/JNK signaling pathways in HO-1 expression.	Cadmium	0-7	heme oxygenase 1	Homo sapiens	109-113
22659318-5	2012	The objective of the present study was to investigate the mechanism of HO-1 induction during cadmium (Cd)-induced oxidative stress and apoptosis in the lymphocyte B cell line BJAB.	Cadmium	93-100	heme oxygenase 1	Homo sapiens	71-75
22659318-5	2012	The objective of the present study was to investigate the mechanism of HO-1 induction during cadmium (Cd)-induced oxidative stress and apoptosis in the lymphocyte B cell line BJAB.	Cadmium	102-104	heme oxygenase 1	Homo sapiens	71-75
22659318-8	2012	Our results indicate that Cd also induces HO-1 expression which is modulated by the thiol redox status, tyrosine kinase and PI3-kinase.	Cadmium	26-28	heme oxygenase 1	Homo sapiens	42-46
22659318-8	2012	Our results indicate that Cd also induces HO-1 expression which is modulated by the thiol redox status, tyrosine kinase and PI3-kinase.	Sulfhydryl Compounds	84-89	heme oxygenase 1	Homo sapiens	42-46
22659318-9	2012	The inhibitory effect of calphostin C suggests that Cd induction of HO-1 expression could be mediated by the PKC pathway in the BJAB cells together with the involvement of ERK 1/2 and JNK in a dose-dependent manner.	Cadmium	52-54	heme oxygenase 1	Homo sapiens	68-72
22864061-3	2012	Sildenafil increased HO-1 expression and potentiated cytokine-mediated expression of iNOS and NO synthesis by SMCs.	Sildenafil Citrate	0-10	heme oxygenase 1	Homo sapiens	21-25
22864061-5	2012	However, the sildenafil-mediated increase in HO-1 promoter activity was abolished by mutating the antioxidant responsive elements in the promoter or by overexpressing a dominant-negative mutant of NF-E2-related factor-2 (Nrf2).	Sildenafil Citrate	13-23	heme oxygenase 1	Homo sapiens	45-49
22842631-0	2012	Globular adiponectin inhibits ethanol-induced apoptosis in HepG2 cells through heme oxygenase-1 induction.	Ethanol	30-37	heme oxygenase 1	Homo sapiens	79-95
22864061-6	2012	Furthermore, the induction of HO-1 by sildenafil was accompanied by an increase in reactive oxygen species (ROS) and blocked by N-acetyl-L-cysteine and rotenone.	Sildenafil Citrate	38-48	heme oxygenase 1	Homo sapiens	30-34
22864061-6	2012	Furthermore, the induction of HO-1 by sildenafil was accompanied by an increase in reactive oxygen species (ROS) and blocked by N-acetyl-L-cysteine and rotenone.	Reactive Oxygen Species	83-106	heme oxygenase 1	Homo sapiens	30-34
22864061-6	2012	Furthermore, the induction of HO-1 by sildenafil was accompanied by an increase in reactive oxygen species (ROS) and blocked by N-acetyl-L-cysteine and rotenone.	Reactive Oxygen Species	108-111	heme oxygenase 1	Homo sapiens	30-34
22864061-6	2012	Furthermore, the induction of HO-1 by sildenafil was accompanied by an increase in reactive oxygen species (ROS) and blocked by N-acetyl-L-cysteine and rotenone.	Acetylcysteine	128-147	heme oxygenase 1	Homo sapiens	30-34
22864061-6	2012	Furthermore, the induction of HO-1 by sildenafil was accompanied by an increase in reactive oxygen species (ROS) and blocked by N-acetyl-L-cysteine and rotenone.	Rotenone	152-160	heme oxygenase 1	Homo sapiens	30-34
22864061-8	2012	In conclusion, these studies demonstrate that sildenafil stimulates the expression of HO-1 and iNOS via the ROS-Nrf2 and sGC-cGMP pathway, respectively.	Sildenafil Citrate	46-56	heme oxygenase 1	Homo sapiens	86-90
22864061-8	2012	In conclusion, these studies demonstrate that sildenafil stimulates the expression of HO-1 and iNOS via the ROS-Nrf2 and sGC-cGMP pathway, respectively.	Reactive Oxygen Species	108-111	heme oxygenase 1	Homo sapiens	86-90
22864061-8	2012	In conclusion, these studies demonstrate that sildenafil stimulates the expression of HO-1 and iNOS via the ROS-Nrf2 and sGC-cGMP pathway, respectively.	Cyclic GMP	125-129	heme oxygenase 1	Homo sapiens	86-90
22864061-9	2012	The ability of sildenafil to block the catabolism of cGMP while stimulating the synthesis of sGC-stimulatory gaseous monoxides through the induction of HO-1 and iNOS provides a potent mechanism by which cGMP-dependent vascular actions of this drug are amplified.	Sildenafil Citrate	15-25	heme oxygenase 1	Homo sapiens	152-156
22864061-9	2012	The ability of sildenafil to block the catabolism of cGMP while stimulating the synthesis of sGC-stimulatory gaseous monoxides through the induction of HO-1 and iNOS provides a potent mechanism by which cGMP-dependent vascular actions of this drug are amplified.	monoxides	117-126	heme oxygenase 1	Homo sapiens	152-156
22864061-9	2012	The ability of sildenafil to block the catabolism of cGMP while stimulating the synthesis of sGC-stimulatory gaseous monoxides through the induction of HO-1 and iNOS provides a potent mechanism by which cGMP-dependent vascular actions of this drug are amplified.	Cyclic GMP	203-207	heme oxygenase 1	Homo sapiens	152-156
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Heme	6-10	heme oxygenase 1	Homo sapiens	31-44
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Oxygen	11-17	heme oxygenase 1	Homo sapiens	31-44
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Iron	140-144	heme oxygenase 1	Homo sapiens	6-29
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Iron	140-144	heme oxygenase 1	Homo sapiens	31-44
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Carbon Monoxide	146-148	heme oxygenase 1	Homo sapiens	6-29
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Carbon Monoxide	146-148	heme oxygenase 1	Homo sapiens	31-44
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Biliverdine	154-164	heme oxygenase 1	Homo sapiens	6-29
22923613-1	2012	Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin.	Biliverdine	154-164	heme oxygenase 1	Homo sapiens	31-44
22875631-0	2012	The heme oxygenase-1 inhibitor ZnPPIX induces non-canonical, Beclin 1-independent, autophagy through p38 MAPK pathway.	zinc protoporphyrin	31-37	heme oxygenase 1	Homo sapiens	4-20
22875631-1	2012	Zinc protoporphyrin IX (ZnPPIX), a heme oxygenase-1 enzyme inhibitor, has been reported to induce apoptosis and to have antitumor properties.	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	35-51
22875631-1	2012	Zinc protoporphyrin IX (ZnPPIX), a heme oxygenase-1 enzyme inhibitor, has been reported to induce apoptosis and to have antitumor properties.	zinc protoporphyrin	24-30	heme oxygenase 1	Homo sapiens	35-51
22954673-4	2012	Additionally, heme activates redox-sensitive proliferation-related signaling routes, such as mitogen activated protein kinase (MAPK) and NF-kappaB, and induces heme oxygenase-1 (HO-1) expression.	Heme	14-18	heme oxygenase 1	Homo sapiens	160-176
22842631-8	2012	Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells.	gacrp	157-162	heme oxygenase 1	Homo sapiens	75-79
22842631-8	2012	Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells.	gacrp	157-162	heme oxygenase 1	Homo sapiens	75-79
22842631-8	2012	Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells.	gacrp	235-240	heme oxygenase 1	Homo sapiens	75-79
22842631-8	2012	Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells.	gacrp	235-240	heme oxygenase 1	Homo sapiens	75-79
22842631-8	2012	Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells.	Ethanol	244-251	heme oxygenase 1	Homo sapiens	75-79
22842631-8	2012	Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells.	Ethanol	244-251	heme oxygenase 1	Homo sapiens	75-79
22842631-10	2012	In conclusion, these data demonstrated that globular adiponectin prevents ethanol-induced apoptosis in HepG2 cells via HO-1 induction and revealed a novel biological response of globular adiponectin in the protection of liver injury from alcohol consumption.	Ethanol	74-81	heme oxygenase 1	Homo sapiens	119-123
22828666-8	2012	At a higher dose, 20 mug/ml, carnosic acid activated the expression of antioxidant (AKR1C2, TNXRD1, HMOX1) and apoptosis (GDF15, PHLDA1, DDIT3) genes and suppressed the expression of inhibitor of transcription (ID3) and cell cycle (CDKN2C) genes.	salvin	29-42	heme oxygenase 1	Homo sapiens	100-105
22801788-3	2012	Vitamin D also exerts protective effects against SLE through non-genomic factors, such as ultraviolet radiation (UV) exposure, matrix metalloproteinase (MMPs), heme oxygenase-1 (HO-1), the prostaglandins (PGs), cyclooxygenase-2 (COX-2), and oxidative stress.	Vitamin D	0-9	heme oxygenase 1	Homo sapiens	160-176
22777293-4	2012	SUMMARY: Treatments based on direct heme-mimetics or other agonists of this pathway have enormous potential for linked antioxidant protection via heme oxygenase 1 and reduced foam cell formation via liver X receptor, a potent combination for treating atherosclerosis.	Heme	36-40	heme oxygenase 1	Homo sapiens	146-162
22212955-4	2012	The (GT)(n)  and (TA)(n)  dinucleotide variations in HMOX1 and UGT1A1 gene promoters, respectively, were determined by fragment analysis.	(n)  dinucleotide	21-38	heme oxygenase 1	Homo sapiens	53-58
22212955-0	2012	Association of serum bilirubin and promoter variations in HMOX1 and UGT1A1 genes with sporadic colorectal cancer.	Bilirubin	21-30	heme oxygenase 1	Homo sapiens	58-63
22419571-1	2012	Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin.	Heme	78-82	heme oxygenase 1	Homo sapiens	0-16
22419571-1	2012	Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin.	Iron	88-92	heme oxygenase 1	Homo sapiens	0-16
22419571-1	2012	Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	0-16
22419571-1	2012	Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin.	Biliverdine	114-124	heme oxygenase 1	Homo sapiens	0-16
22881289-2	2012	The stress protein, HO-1 mediates the degradation of cellular heme to biliverdin/bilirubin, free iron, and CO and is up-regulated in the brains of persons with Alzheimer"s disease and Parkinson"s disease.	Heme	62-66	heme oxygenase 1	Homo sapiens	20-24
22227268-5	2012	Lico-E activates Nrf2-antioxidant response element (ARE) system and up-regulates downstream NAD(P)H:quinone oxidoreductase 1 (NQO1) and heme oxygenase-1 (HO-1).	licochalcone E	0-6	heme oxygenase 1	Homo sapiens	154-158
22227268-6	2012	Anti-inflammatory and cytoprotective effects of Lico-E are attenuated in siRNA-mediated Nrf2-silencing cells as well as in the presence with specific inhibitor of HO-1 or NQO1, respectively.	licochalcone E	48-54	heme oxygenase 1	Homo sapiens	163-167
23248504-1	2012	BACKGROUND: At low concentrations, carbon monoxide (CO) can confer cyto and tissue-protective effects, such as endogenous Heme oxygenase 1 expression, which has antioxidative, anti-inflammatory, antiproliferative, and antiapoptotic effects.	Carbon Monoxide	35-50	heme oxygenase 1	Homo sapiens	122-138
23248504-1	2012	BACKGROUND: At low concentrations, carbon monoxide (CO) can confer cyto and tissue-protective effects, such as endogenous Heme oxygenase 1 expression, which has antioxidative, anti-inflammatory, antiproliferative, and antiapoptotic effects.	Carbon Monoxide	52-54	heme oxygenase 1	Homo sapiens	122-138
22881289-2	2012	The stress protein, HO-1 mediates the degradation of cellular heme to biliverdin/bilirubin, free iron, and CO and is up-regulated in the brains of persons with Alzheimer"s disease and Parkinson"s disease.	Biliverdine	70-80	heme oxygenase 1	Homo sapiens	20-24
22881289-2	2012	The stress protein, HO-1 mediates the degradation of cellular heme to biliverdin/bilirubin, free iron, and CO and is up-regulated in the brains of persons with Alzheimer"s disease and Parkinson"s disease.	Bilirubin	81-90	heme oxygenase 1	Homo sapiens	20-24
22881289-2	2012	The stress protein, HO-1 mediates the degradation of cellular heme to biliverdin/bilirubin, free iron, and CO and is up-regulated in the brains of persons with Alzheimer"s disease and Parkinson"s disease.	Iron	97-101	heme oxygenase 1	Homo sapiens	20-24
23302671-0	2012	[Effects of policosanol on serum lipids and heme oxygenase-1 in patients with hyperlipidemia].	policosanol	12-23	heme oxygenase 1	Homo sapiens	44-60
21756955-8	2012	Pretreatment of the astrocytes with antioxidants or a specific calcium chelator BAPTA-AM, significantly blocked the upregulation of Nrf2, HO-1 and Nqo1.	Calcium	63-70	heme oxygenase 1	Homo sapiens	138-142
21756955-8	2012	Pretreatment of the astrocytes with antioxidants or a specific calcium chelator BAPTA-AM, significantly blocked the upregulation of Nrf2, HO-1 and Nqo1.	1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester	80-88	heme oxygenase 1	Homo sapiens	138-142
23248671-8	2012	Pretreatment with L-serine (0.1-3.2 mM) protected endothelial cells from hydrogen peroxide-mediated cell cytotoxicity (H(2)O(2), 0.5 mM) and lead to significant induction of Nrf2 activity, HO-1 expresssion and NOx production.	Serine	18-26	heme oxygenase 1	Homo sapiens	189-193
23248671-9	2012	These findings demonstrated that L-serine has antioxidant and cytoprotective effects through the elevation of some crucial antioxidant factors such as Nrf2, HO-1 and NO.	Serine	33-41	heme oxygenase 1	Homo sapiens	157-168
22879597-2	2012	Cobalt protoporphyrin (CoPP), a well known heme oxygenase 1 inducer, has been used to promote endogenous CO generation and protect against ischemia/reperfusion injury.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	43-59
22879597-2	2012	Cobalt protoporphyrin (CoPP), a well known heme oxygenase 1 inducer, has been used to promote endogenous CO generation and protect against ischemia/reperfusion injury.	cobaltiprotoporphyrin	23-27	heme oxygenase 1	Homo sapiens	43-59
23302671-1	2012	OBJECTIVE: To evaluate the effects of policosanol on serum lipid and heme oxygenase-1 (HO-1) in patients with hyperlipidemia.	policosanol	38-49	heme oxygenase 1	Homo sapiens	69-85
23302671-1	2012	OBJECTIVE: To evaluate the effects of policosanol on serum lipid and heme oxygenase-1 (HO-1) in patients with hyperlipidemia.	policosanol	38-49	heme oxygenase 1	Homo sapiens	87-91
22918643-10	2012	Simvastatin-dependent HO-1 protein induction was reduced significantly by pharmacological inhibition of the phosphotidylinositol-3-kinase (PI3K)/Akt pathways.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	22-26
22918643-12	2012	CONCLUSIONS: These results demonstrate that HO-1 is a target site and an antioxidant mediator of simvastatin in human RPE cells.	Simvastatin	97-108	heme oxygenase 1	Homo sapiens	44-48
22918643-0	2012	Effects of simvastatin on the expression of heme oxygenase-1 in human RPE cells.	Simvastatin	11-22	heme oxygenase 1	Homo sapiens	44-60
22918643-8	2012	Simvastatin increased the HO-1 mRNA and protein levels in a concentration-dependent manner up to 10 muM.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	26-30
22918643-13	2012	Simvastatin-dependent upregulation of HO-1 is mainly via PI3K/Akt-dependent signaling pathways.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	38-42
22918643-9	2012	HO-1 protein induction by simvastatin was unaffected by mevalonate or N-nitro-L-arginine methyl ester, showing that the isoprenoid- and NO-dependent pathways are not involved.	Simvastatin	26-37	heme oxygenase 1	Homo sapiens	0-4
22917016-5	2012	Therefore, the molecular signaling events affecting resveratrol-mediated heme oxygenase-1 (HO-1) and glyoxalase expression levels were further investigated in this study.	Resveratrol	52-63	heme oxygenase 1	Homo sapiens	73-89
22917016-5	2012	Therefore, the molecular signaling events affecting resveratrol-mediated heme oxygenase-1 (HO-1) and glyoxalase expression levels were further investigated in this study.	Resveratrol	52-63	heme oxygenase 1	Homo sapiens	91-95
22917016-6	2012	Our findings indicated that resveratrol activated the extracellular signal-regulated kinase (ERK) pathway but not the p38 or c-Jun N-terminal kinase (JNK) pathways, subsequently leading to Nrf2 nuclear translocation and elevation of HO-1 and glyoxalase expression levels.	Resveratrol	28-39	heme oxygenase 1	Homo sapiens	233-237
22917016-8	2012	In contrast, depletion of Nrf2 by small interfering RNA (si-RNA) resulted in the abrogation of HO-1 and glyoxalase expression in the MG-treated resveratrol group in Hep G2 cells.	Resveratrol	144-155	heme oxygenase 1	Homo sapiens	95-99
22821808-0	2012	Tunicamycin inhibits PDGF-BB-induced proliferation and migration of vascular smooth muscle cells through induction of HO-1.	Tunicamycin	0-11	heme oxygenase 1	Homo sapiens	118-122
22564156-3	2012	Hence, the ability of exogenously-added copper, iron and zinc to influence HO-1 expression in HCT-116 cells was evaluated.	Copper	40-46	heme oxygenase 1	Homo sapiens	75-79
22843690-5	2012	Rapamycin (RAPA) and sorafenib, two commonly used drugs for renal cancer treatment, were found to induce HO-1 expression in renal cancer cells Caki-1 and 786-O; and the apoptotic effect of these drugs was markedly enhanced upon HO-1 knockdown.	Sirolimus	0-9	heme oxygenase 1	Homo sapiens	105-109
22843690-5	2012	Rapamycin (RAPA) and sorafenib, two commonly used drugs for renal cancer treatment, were found to induce HO-1 expression in renal cancer cells Caki-1 and 786-O; and the apoptotic effect of these drugs was markedly enhanced upon HO-1 knockdown.	Sirolimus	0-9	heme oxygenase 1	Homo sapiens	228-232
22843690-5	2012	Rapamycin (RAPA) and sorafenib, two commonly used drugs for renal cancer treatment, were found to induce HO-1 expression in renal cancer cells Caki-1 and 786-O; and the apoptotic effect of these drugs was markedly enhanced upon HO-1 knockdown.	Sirolimus	11-15	heme oxygenase 1	Homo sapiens	105-109
22843690-5	2012	Rapamycin (RAPA) and sorafenib, two commonly used drugs for renal cancer treatment, were found to induce HO-1 expression in renal cancer cells Caki-1 and 786-O; and the apoptotic effect of these drugs was markedly enhanced upon HO-1 knockdown.	Sirolimus	11-15	heme oxygenase 1	Homo sapiens	228-232
22843690-5	2012	Rapamycin (RAPA) and sorafenib, two commonly used drugs for renal cancer treatment, were found to induce HO-1 expression in renal cancer cells Caki-1 and 786-O; and the apoptotic effect of these drugs was markedly enhanced upon HO-1 knockdown.	Sorafenib	21-30	heme oxygenase 1	Homo sapiens	105-109
22843690-5	2012	Rapamycin (RAPA) and sorafenib, two commonly used drugs for renal cancer treatment, were found to induce HO-1 expression in renal cancer cells Caki-1 and 786-O; and the apoptotic effect of these drugs was markedly enhanced upon HO-1 knockdown.	Sorafenib	21-30	heme oxygenase 1	Homo sapiens	228-232
22843690-6	2012	Overexpression of HO-1 protected the cells from RAPA- and sorafenib-induced apoptosis and also averted drug-mediated inhibition of cell proliferation.	Sirolimus	48-52	heme oxygenase 1	Homo sapiens	18-22
22843690-6	2012	Overexpression of HO-1 protected the cells from RAPA- and sorafenib-induced apoptosis and also averted drug-mediated inhibition of cell proliferation.	Sorafenib	58-67	heme oxygenase 1	Homo sapiens	18-22
22709784-7	2012	Silymarin acted as a potent cytoprotective effector through the effective induction of anti-oxidant related genes, including Nrf2, NQO1 and HO-1, in the presence of PQ.	Silymarin	0-9	heme oxygenase 1	Homo sapiens	140-144
22564156-2	2012	Toxic heavy metals induce HO-1, but it is unclear whether particular metal micronutrients also induce HO-1.	Metals	12-17	heme oxygenase 1	Homo sapiens	26-30
22564156-3	2012	Hence, the ability of exogenously-added copper, iron and zinc to influence HO-1 expression in HCT-116 cells was evaluated.	Iron	48-52	heme oxygenase 1	Homo sapiens	75-79
22564156-7	2012	In contrast, deferoxamine blunted the induction of HO-1 mRNA, protein, and enzymatic activity caused by zinc.	Deferoxamine	13-25	heme oxygenase 1	Homo sapiens	51-55
22564156-8	2012	Additionally, N-acetylcysteine and Tiron inhibited zinc-induced HO-1 upregulation and also nuclear translocation of nuclear factor erythroid 2-related factor 2 (Nrf2).	Acetylcysteine	14-30	heme oxygenase 1	Homo sapiens	64-68
22564156-8	2012	Additionally, N-acetylcysteine and Tiron inhibited zinc-induced HO-1 upregulation and also nuclear translocation of nuclear factor erythroid 2-related factor 2 (Nrf2).	1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt	35-40	heme oxygenase 1	Homo sapiens	64-68
22564156-9	2012	Collectively, these findings suggest that zinc at above normal levels upregulates HO-1 expression in HCT-116 cells in a ROS-independent manner.	Reactive Oxygen Species	120-123	heme oxygenase 1	Homo sapiens	82-86
22583557-4	2012	After undergoing a partial catabolism, alkenals enter into a great number of body"s cells, where they react with Nrf2-Keap1 protein: the transfer of activated Nrf2 into the nucleus and its binding to antioxidant response element (ARE) is the crucial event able to upregulate the synthesis of antioxidant proteins, phase II enzymes and HO-1.	alkenals	39-47	heme oxygenase 1	Homo sapiens	335-339
22137262-0	2012	Epigallocatechin gallate induces expression of heme oxygenase-1 in endothelial cells via p38 MAPK and Nrf-2 that suppresses proinflammatory actions of TNF-alpha.	epigallocatechin gallate	0-24	heme oxygenase 1	Homo sapiens	47-63
22137262-3	2012	When compared with vehicle-treated controls, EGCG treatment (2.5 muM, 8 h) of human aortic endothelial cells (HAEC) caused a ~three-fold increase in heme oxygenase-1 (HO-1) mRNA and protein with comparable increases in HO-1 activity.	epigallocatechin gallate	45-49	heme oxygenase 1	Homo sapiens	149-165
22487967-0	2012	15-deoxy-Delta12,14 -prostaglandin J2 inhibits human immunodeficiency virus-1 tat-induced monocyte chemoattractant protein-1/CCL2 production by blocking the extracellular signal-regulated kinase-1/2 signaling pathway independently of peroxisome proliferator-activated receptor-gamma and heme oxygenase-1 in rat hippocampal slices.	14 -prostaglandin j2	17-37	heme oxygenase 1	Homo sapiens	287-303
22137262-3	2012	When compared with vehicle-treated controls, EGCG treatment (2.5 muM, 8 h) of human aortic endothelial cells (HAEC) caused a ~three-fold increase in heme oxygenase-1 (HO-1) mRNA and protein with comparable increases in HO-1 activity.	epigallocatechin gallate	45-49	heme oxygenase 1	Homo sapiens	167-171
22487967-7	2012	Despite 15d-PGJ2"s increasing the expression of heme oxygenase-1 (HO-1), its action was not abrogated by the HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX), nor was it recapitulated by HO-1 inducers such as cobalt protoporphyrin (CoPP).	15-deoxy-delta(12,14)-prostaglandin J2	8-16	heme oxygenase 1	Homo sapiens	48-64
22137262-3	2012	When compared with vehicle-treated controls, EGCG treatment (2.5 muM, 8 h) of human aortic endothelial cells (HAEC) caused a ~three-fold increase in heme oxygenase-1 (HO-1) mRNA and protein with comparable increases in HO-1 activity.	epigallocatechin gallate	45-49	heme oxygenase 1	Homo sapiens	219-223
22487967-7	2012	Despite 15d-PGJ2"s increasing the expression of heme oxygenase-1 (HO-1), its action was not abrogated by the HO-1 inhibitor zinc protoporphyrin IX (ZnPPIX), nor was it recapitulated by HO-1 inducers such as cobalt protoporphyrin (CoPP).	15-deoxy-delta(12,14)-prostaglandin J2	8-16	heme oxygenase 1	Homo sapiens	66-70
22137262-5	2012	Pretreatment of HAEC with SB203580 (p38 MAPK inhibitor) or siRNA knockdown of p38 MAPK completely blocked EGCG-stimulated induction of HO-1.	SB 203580	26-34	heme oxygenase 1	Homo sapiens	135-139
22487967-11	2012	Collectively, these data demonstrate that the antiinflammatory effects of 15d-PGJ2 on the hippocampus are exerted through inhibition of Tat-mediated ERK1/2 activation, coupled with that of a redox-sensitive pathway, independent of PPARgamma and HO-1.	15-deoxy-delta(12,14)-prostaglandin J2	74-82	heme oxygenase 1	Homo sapiens	245-249
22137262-5	2012	Pretreatment of HAEC with SB203580 (p38 MAPK inhibitor) or siRNA knockdown of p38 MAPK completely blocked EGCG-stimulated induction of HO-1.	epigallocatechin gallate	106-110	heme oxygenase 1	Homo sapiens	135-139
22137262-7	2012	siRNA knockdown of HO-1, p38 MAPK or Nrf-2 blocked these inhibitory actions of EGCG.	epigallocatechin gallate	79-83	heme oxygenase 1	Homo sapiens	19-23
22137262-8	2012	In HAEC transiently transfected with a human HO-1 promoter luciferase reporter (or an isolated Nrf-2 responsive region), luciferase activity increased in response to EGCG.	epigallocatechin gallate	166-170	heme oxygenase 1	Homo sapiens	45-49
22137262-10	2012	EGCG-stimulated expression of HO-1 and Nrf-2 was blocked by siRNA knockdown of Nrf-2 or p38 MAPK.	epigallocatechin gallate	0-4	heme oxygenase 1	Homo sapiens	30-34
22137262-11	2012	Finally, liver from mice chronically treated with EGCG had increased HO-1 and decreased VCAM-1 expression.	epigallocatechin gallate	50-54	heme oxygenase 1	Homo sapiens	69-73
22137262-12	2012	Thus, in vascular endothelium, EGCG requires p38 MAPK to increase expression of Nrf-2 that drives expression of HO-1, resulting in increased HO-1 activity.	epigallocatechin gallate	31-35	heme oxygenase 1	Homo sapiens	112-116
22137262-12	2012	Thus, in vascular endothelium, EGCG requires p38 MAPK to increase expression of Nrf-2 that drives expression of HO-1, resulting in increased HO-1 activity.	epigallocatechin gallate	31-35	heme oxygenase 1	Homo sapiens	141-145
22137262-13	2012	Increased HO-1 expression may underlie anti-inflammatory actions of EGCG in vascular endothelium that may help mediate beneficial cardiovascular actions of green tea.	epigallocatechin gallate	68-72	heme oxygenase 1	Homo sapiens	10-14
22819264-1	2012	INTRODUCTION: Heme oxygenase-1 (HO-1) is the rate limiting enzyme that catalyzes the conversion of heme into biliverdin, free iron, and carbon monoxide (CO).	Heme	99-103	heme oxygenase 1	Homo sapiens	14-30
22819264-1	2012	INTRODUCTION: Heme oxygenase-1 (HO-1) is the rate limiting enzyme that catalyzes the conversion of heme into biliverdin, free iron, and carbon monoxide (CO).	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	14-30
22819264-1	2012	INTRODUCTION: Heme oxygenase-1 (HO-1) is the rate limiting enzyme that catalyzes the conversion of heme into biliverdin, free iron, and carbon monoxide (CO).	Iron	126-130	heme oxygenase 1	Homo sapiens	14-30
22836558-7	2012	Free Hb binds to haptoglobin (Hp) and once Hp-Hb complex is endocytosed by CD163, liberated heme is converted into less toxic compounds by heme oxygenase-1.	Heme	92-96	heme oxygenase 1	Homo sapiens	139-155
22819264-1	2012	INTRODUCTION: Heme oxygenase-1 (HO-1) is the rate limiting enzyme that catalyzes the conversion of heme into biliverdin, free iron, and carbon monoxide (CO).	Carbon Monoxide	136-151	heme oxygenase 1	Homo sapiens	14-30
22819264-1	2012	INTRODUCTION: Heme oxygenase-1 (HO-1) is the rate limiting enzyme that catalyzes the conversion of heme into biliverdin, free iron, and carbon monoxide (CO).	Carbon Monoxide	153-155	heme oxygenase 1	Homo sapiens	14-30
22843070-4	2012	Immunostaining and quantitative  RT-PCR revealed that PQQ treatment promotes nuclear translocation of nuclear  factor erythroid 2-related factor 2 (Nrf2), and up-regulates mRNA expression of  Nrf2 and the antioxidant enzyme genes, heme oxygenase-1 and glutamate cysteine  ligase catalytic in glutamate-injured hippocampal neurons; this is a process  dependent on the PI3K/Akt pathway, as evidenced by blocking experiments with  PI3K inhibitors.	PQQ Cofactor	54-57	heme oxygenase 1	Homo sapiens	231-247
22735309-0	2012	Phenylpropanoid glycosides from plant cell cultures induce heme oxygenase 1 gene expression in a human keratinocyte cell line by affecting the balance of NRF2 and BACH1 transcription factors.	phenylpropanoid glycosides	0-26	heme oxygenase 1	Homo sapiens	59-75
23158494-3	2012	Morphologic observations, flow cytometry Annexin-V and DNA analysis were used to detect apoptosis and determine the content of DNA of MSCs after a 12-hour treatment of Znpp-IX, a Ho-1 special inhibitor.	zinc protoporphyrin	168-175	heme oxygenase 1	Homo sapiens	179-183
22078849-4	2012	However, no study that observed HO-1 in both epithelial and subepithelial tissues of CRS has been reported.	3-cresol	85-88	heme oxygenase 1	Homo sapiens	32-36
22901679-9	2012	Other parameters such as LDH and HO-1 were not influenced by gaseous compounds: Following aerosol exposure, LDH levels appeared elevated at both timepoints and the HO-1 transcript correlated positively with deposited ZnO-dose.	Zinc Oxide	217-220	heme oxygenase 1	Homo sapiens	164-168
22891172-0	2012	Letter by Vitek et al regarding article, "niacin inhibits vascular inflammation via the induction of heme oxygenase-1".	Niacin	42-48	heme oxygenase 1	Homo sapiens	101-118
21695420-6	2012	WI-38 fibroblasts exposed to a subcytotoxic concentration of copper sulfate presented inhibition of cell proliferation, cell enlargement, increased SA beta-gal activity, and mRNA overexpression of several senescence-associated genes such as p21, apolipoprotein J (ApoJ), fibronectin, transforming growth factor beta-1 (TGF beta1), insulin growth factor binding protein 3, and heme oxygenase 1.	Copper Sulfate	61-75	heme oxygenase 1	Homo sapiens	376-392
22078849-6	2012	RESULTS: We found that the expression of HO-1 in the epithelial layers of CRS without eosinophilic infiltration was significantly enhanced as compared with that of CRS with eosinophilic infiltration.	3-cresol	74-77	heme oxygenase 1	Homo sapiens	41-45
22078849-6	2012	RESULTS: We found that the expression of HO-1 in the epithelial layers of CRS without eosinophilic infiltration was significantly enhanced as compared with that of CRS with eosinophilic infiltration.	3-cresol	164-167	heme oxygenase 1	Homo sapiens	41-45
22078849-7	2012	On the other hand, the number of macrophages with HO-1 positive reactions was significantly greater in CRS with eosinophilic infiltration compared with CRS without eosinophilic infiltration.	3-cresol	103-106	heme oxygenase 1	Homo sapiens	50-54
22078849-7	2012	On the other hand, the number of macrophages with HO-1 positive reactions was significantly greater in CRS with eosinophilic infiltration compared with CRS without eosinophilic infiltration.	3-cresol	152-155	heme oxygenase 1	Homo sapiens	50-54
22579918-0	2012	Sustained expression of heme oxygenase-1 alters iron homeostasis in nonerythroid cells.	Iron	48-52	heme oxygenase 1	Homo sapiens	24-40
21547369-5	2012	Expression array analysis revealed DHA-induced upregulation of oxidative and genotoxic stress response genes (GADD45A, GADD153, CDKN1A, PMAIP1, HMOX1, EGR1) in A375 cells.	artenimol	35-38	heme oxygenase 1	Homo sapiens	144-149
22683349-9	2012	Guanosine induced the antioxidant enzyme heme oxygenase-1 (HO-1) expression.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	41-57
22683349-9	2012	Guanosine induced the antioxidant enzyme heme oxygenase-1 (HO-1) expression.	Guanosine	0-9	heme oxygenase 1	Homo sapiens	59-63
22683349-10	2012	The protective effects of guanosine were prevented by heme oxygenase-1 inhibitor, SnPP.	Guanosine	26-35	heme oxygenase 1	Homo sapiens	54-70
22683349-11	2012	Moreover, bilirubin, an antioxidant and physiologic product of HO-1, is protective against mitochondrial oxidative stress.	Bilirubin	10-19	heme oxygenase 1	Homo sapiens	63-67
22683349-12	2012	In conclusion, our results show that guanosine can afford protection against mitochondrial oxidative stress by a signaling pathway that implicates PI3K/Akt/GSK-3beta proteins and induction of the antioxidant enzyme HO-1.	Guanosine	37-46	heme oxygenase 1	Homo sapiens	215-219
22484158-7	2012	Interestingly, the profound up-regulation of HO-1 and Nrf-2 were observed in only ethanol-challenged cells, which evidenced that lucidone-induced induction of HO-/Nrf-2 were specific with oxidative stress.	Ethanol	82-89	heme oxygenase 1	Homo sapiens	45-49
22484158-7	2012	Interestingly, the profound up-regulation of HO-1 and Nrf-2 were observed in only ethanol-challenged cells, which evidenced that lucidone-induced induction of HO-/Nrf-2 were specific with oxidative stress.	lucidone	129-137	heme oxygenase 1	Homo sapiens	45-49
22484158-8	2012	Thus, we concluded that lucidone-mediated up-regulation of phase-II enzymes and HO-1 via Nrf-2 signaling pathway may provide a pivotal mechanism for its hepatoprotective action.	lucidone	24-32	heme oxygenase 1	Homo sapiens	80-84
22931644-1	2012	This study was aimed to investigate the effect of AMN107 (nilotinib) combined with heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin IX (ZnPPIX) on chronic myeloid leukemia (CML) cells and its mechanism.	zinc protoporphyrin	117-139	heme oxygenase 1	Homo sapiens	101-105
22931644-1	2012	This study was aimed to investigate the effect of AMN107 (nilotinib) combined with heme oxygenase-1 (HO-1) inhibitor zinc protoporphyrin IX (ZnPPIX) on chronic myeloid leukemia (CML) cells and its mechanism.	zinc protoporphyrin	141-147	heme oxygenase 1	Homo sapiens	101-105
22580386-1	2012	Antioxidant, anti-inflammatory and anti-atherogenic effects have been associated with elevations of unconjugated bilirubin (UCB) in serum and with the induction of heme oxygenase-1 (HO-1), the rate-limiting enzyme in UCB synthesis.	ucb	217-220	heme oxygenase 1	Homo sapiens	164-180
22580386-1	2012	Antioxidant, anti-inflammatory and anti-atherogenic effects have been associated with elevations of unconjugated bilirubin (UCB) in serum and with the induction of heme oxygenase-1 (HO-1), the rate-limiting enzyme in UCB synthesis.	ucb	217-220	heme oxygenase 1	Homo sapiens	182-186
22580386-4	2012	Moreover, induction of HO-1 with sodium arsenite led to 2.4-fold (p = 0.01) accumulation of intracellular UCB over basal level while sodium azide-derived oxidative stress resulted in a 60% drop (p &lt; 0.001).	sodium arsenite	33-48	heme oxygenase 1	Homo sapiens	23-27
22580386-4	2012	Moreover, induction of HO-1 with sodium arsenite led to 2.4-fold (p = 0.01) accumulation of intracellular UCB over basal level while sodium azide-derived oxidative stress resulted in a 60% drop (p &lt; 0.001).	Sodium Azide	133-145	heme oxygenase 1	Homo sapiens	23-27
22580386-7	2012	In conclusion, hyperbilirubinemia and HO-1 induction associated with inflammation and oxidative stress increase intracellular concentrations of UCB, thus enhancing the protection of cellular lipids against peroxidation.	ucb	144-147	heme oxygenase 1	Homo sapiens	38-42
22580386-8	2012	Therefore, the previously reported protective effects of hyperbilirubinemia and HO-1 induction are at least in part due to intracellular accumulation of UCB.	ucb	153-156	heme oxygenase 1	Homo sapiens	80-84
22753217-8	2012	Inhibition of HO activity by administration of tin mesoporphyrin to HF-fed mice transduced with the aP2-HO-1 reversed the decrease in Peg1/Mesoderm-specific transcript, TNFalpha, and MCP-1 levels.	tin mesoporphyrin	47-64	heme oxygenase 1	Homo sapiens	104-108
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Heme	64-68	heme oxygenase 1	Homo sapiens	82-86
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Biliverdine	144-154	heme oxygenase 1	Homo sapiens	64-80
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Biliverdine	144-154	heme oxygenase 1	Homo sapiens	82-86
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Carbon Monoxide	156-171	heme oxygenase 1	Homo sapiens	64-80
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Carbon Monoxide	156-171	heme oxygenase 1	Homo sapiens	82-86
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Iron	181-185	heme oxygenase 1	Homo sapiens	64-80
22587389-4	2012	One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron.	Iron	181-185	heme oxygenase 1	Homo sapiens	82-86
22484158-0	2012	Hepatoprotective effect of lucidone against alcohol-induced oxidative stress in human hepatic HepG2 cells through the up-regulation of HO-1/Nrf-2 antioxidant genes.	lucidone	27-35	heme oxygenase 1	Homo sapiens	135-139
22484158-6	2012	Furthermore, Western blot and quantitative-PCR analyses showed that ethanol-exposure apparently down-regulated endogenous anti-oxidant hemoxygenase-1 (HO-1) expression, whereas pretreatment with lucidone significantly up-regulates HO-1 expression followed by the transcriptional activation of NF-E2 related factor-2 (Nrf-2).	Ethanol	68-75	heme oxygenase 1	Homo sapiens	135-155
22484158-6	2012	Furthermore, Western blot and quantitative-PCR analyses showed that ethanol-exposure apparently down-regulated endogenous anti-oxidant hemoxygenase-1 (HO-1) expression, whereas pretreatment with lucidone significantly up-regulates HO-1 expression followed by the transcriptional activation of NF-E2 related factor-2 (Nrf-2).	Ethanol	68-75	heme oxygenase 1	Homo sapiens	151-155
22484158-6	2012	Furthermore, Western blot and quantitative-PCR analyses showed that ethanol-exposure apparently down-regulated endogenous anti-oxidant hemoxygenase-1 (HO-1) expression, whereas pretreatment with lucidone significantly up-regulates HO-1 expression followed by the transcriptional activation of NF-E2 related factor-2 (Nrf-2).	lucidone	195-203	heme oxygenase 1	Homo sapiens	151-155
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Heme	36-40	heme oxygenase 1	Homo sapiens	0-16
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Heme	36-40	heme oxygenase 1	Homo sapiens	18-22
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Carbon Monoxide	46-61	heme oxygenase 1	Homo sapiens	0-16
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Carbon Monoxide	46-61	heme oxygenase 1	Homo sapiens	18-22
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Biliverdine	63-73	heme oxygenase 1	Homo sapiens	0-16
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Biliverdine	63-73	heme oxygenase 1	Homo sapiens	18-22
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Iron	84-88	heme oxygenase 1	Homo sapiens	0-16
22302482-1	2012	Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress.	Iron	84-88	heme oxygenase 1	Homo sapiens	18-22
22302482-6	2012	Treatment with the HO-1 inhibitor zinc protoporphyrin decreased the viability of colon cancer cell lines.	zinc protoporphyrin	34-53	heme oxygenase 1	Homo sapiens	19-23
22593583-0	2012	Carbon monoxide mediates the anti-apoptotic effects of heme oxygenase-1 in medulloblastoma DAOY cells via K+ channel inhibition.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	55-71
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Heme	41-45	heme oxygenase 1	Homo sapiens	59-63
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Biliverdine	101-111	heme oxygenase 1	Homo sapiens	41-57
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Biliverdine	101-111	heme oxygenase 1	Homo sapiens	59-63
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	ammonium ferrous sulfate	113-119	heme oxygenase 1	Homo sapiens	41-57
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	ammonium ferrous sulfate	113-119	heme oxygenase 1	Homo sapiens	59-63
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Carbon Monoxide	125-140	heme oxygenase 1	Homo sapiens	41-57
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Carbon Monoxide	125-140	heme oxygenase 1	Homo sapiens	59-63
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Carbon Monoxide	142-144	heme oxygenase 1	Homo sapiens	41-57
22593583-2	2012	Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Carbon Monoxide	142-144	heme oxygenase 1	Homo sapiens	59-63
22579918-2	2012	Sustained induction of heme oxygenase-1 (HO-1) in nonerythroid cells plays a key role in many pathological processes, yet the effect of long-term HO-1 expression on cellular iron metabolism in the absence of exogenous heme is poorly understood.	Heme	23-27	heme oxygenase 1	Homo sapiens	41-45
22579918-3	2012	Here we report that in a model nonerythroid cell, both transient and stable HO-1 expression increased heme oxygenase activity, but total cellular heme content was decreased only with transient enzyme expression.	Heme	102-106	heme oxygenase 1	Homo sapiens	76-80
22579918-4	2012	Sustained HO-1 activity increased the expression of both the mitochondrial iron importer mitoferrin-2 and the rate-limiting enzyme in heme synthesis, aminolevulinate synthase-1, and it augmented the mitochondrial content of heme.	Heme	134-138	heme oxygenase 1	Homo sapiens	10-14
22579918-4	2012	Sustained HO-1 activity increased the expression of both the mitochondrial iron importer mitoferrin-2 and the rate-limiting enzyme in heme synthesis, aminolevulinate synthase-1, and it augmented the mitochondrial content of heme.	Heme	224-228	heme oxygenase 1	Homo sapiens	10-14
22579918-7	2012	Together, our results reveal a novel and coordinated adaptive response of nonerythroid cells to sustained HO-1 induction that has an impact on cellular iron homeostasis.	Iron	152-156	heme oxygenase 1	Homo sapiens	106-110
22526619-7	2012	Furthermore, we found that oroxylin A treatment elevated intracellular reactive oxygen species levels and increased the protein expression level of two of the Nrf2 target genes heme oxygenase-1 and NADP(H):quinone oxidoreductase-1 in HCT-116 cells.	5,7-dihydroxy-6-methoxy-2-phenylchromen-4-one	27-37	heme oxygenase 1	Homo sapiens	177-193
22392462-0	2012	Curcumin ameliorates hydrogen peroxide-induced epithelial barrier disruption by upregulating heme oxygenase-1 expression in human intestinal epithelial cells.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	93-109
22139798-7	2012	HO-1 up-regulation in BCR-ABL1-expressing cells was suppressed by diphenyleneiodonium (DPI), a chemical inhibitor of the NADPH oxidase.	diphenyleneiodonium	66-85	heme oxygenase 1	Homo sapiens	0-4
22139798-7	2012	HO-1 up-regulation in BCR-ABL1-expressing cells was suppressed by diphenyleneiodonium (DPI), a chemical inhibitor of the NADPH oxidase.	diphenyleneiodonium	87-90	heme oxygenase 1	Homo sapiens	0-4
22392462-0	2012	Curcumin ameliorates hydrogen peroxide-induced epithelial barrier disruption by upregulating heme oxygenase-1 expression in human intestinal epithelial cells.	Hydrogen Peroxide	21-38	heme oxygenase 1	Homo sapiens	93-109
22392462-2	2012	Heme oxygenase-1 (HO-1), which can be induced by curcumin (Cur), provides protection against various forms of oxidative stress.	Curcumin	49-57	heme oxygenase 1	Homo sapiens	0-16
22392462-2	2012	Heme oxygenase-1 (HO-1), which can be induced by curcumin (Cur), provides protection against various forms of oxidative stress.	Curcumin	49-57	heme oxygenase 1	Homo sapiens	18-22
22392462-10	2012	CONCLUSION: Cur protects human intestinal epithelial cells against H(2)O(2)-induced disruption of TJ and barrier dysfunction via the HO-1 pathway.	Hydrogen Peroxide	67-75	heme oxygenase 1	Homo sapiens	133-137
22583702-1	2012	Heme oxygenase-1 (HMOX-1) is activated by oxidative stress, and gene responsiveness is reportedly determined by the number of dinucleotide (GT(n)) repeats in its highly polymorphic promoter region.	Dinucleoside Phosphates	126-138	heme oxygenase 1	Homo sapiens	0-16
21129940-5	2012	Heme oxygenase-1, NAD(P)H: quinone oxidoreductase, glutathione-S-transferase, gamma-glutamyl cysteine ligase, and glutathione reductase are among the cytoprotective proteins induced by sulforaphane.	sulforaphane	185-197	heme oxygenase 1	Homo sapiens	0-16
22583702-1	2012	Heme oxygenase-1 (HMOX-1) is activated by oxidative stress, and gene responsiveness is reportedly determined by the number of dinucleotide (GT(n)) repeats in its highly polymorphic promoter region.	Dinucleoside Phosphates	126-138	heme oxygenase 1	Homo sapiens	18-24
22634503-6	2012	Arsenic-mediated ERK1/2 activation negatively regulated DNA polymerase beta expression and up regulated heme-oxygenase-1 at toxic concentrations.	Arsenic	0-7	heme oxygenase 1	Homo sapiens	104-120
26105453-5	2012	HO-1 is also required to maintain nitric oxide synthesis (2).	Nitric Oxide	34-46	heme oxygenase 1	Homo sapiens	0-4
22573121-2	2012	Calcitonin gene-related peptide (CGRP), which prevents circulating EPCs senescence and reverses Ang II-induced EPCs senescence is reduced in hypertensive patients, its level is stimulated by heme oxygenase-1 and is related with stimulation of nitric oxide.	Nitric Oxide	243-255	heme oxygenase 1	Homo sapiens	191-207
22617388-0	2012	Bortezomib induces heme oxygenase-1 expression in multiple myeloma.	Bortezomib	0-10	heme oxygenase 1	Homo sapiens	19-35
22617388-6	2012	Furthermore, we explored the expression of HO-1 in multiple myeloma cells in response to the key anti-myeloma drugs bortezomib and lenalidomide.	Bortezomib	116-126	heme oxygenase 1	Homo sapiens	43-47
22617388-6	2012	Furthermore, we explored the expression of HO-1 in multiple myeloma cells in response to the key anti-myeloma drugs bortezomib and lenalidomide.	Lenalidomide	131-143	heme oxygenase 1	Homo sapiens	43-47
22617388-7	2012	We show here for the first time that bortezomib increases HO-1 expression in a time- and concentration-dependent manner.	Bortezomib	37-47	heme oxygenase 1	Homo sapiens	58-62
22617388-8	2012	Moreover, we also observe that HO-1 is increased in lenalidomide-resistant MM cell lines.	Lenalidomide	52-64	heme oxygenase 1	Homo sapiens	31-35
22549002-3	2012	The induction of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system in the brain represents one of the earliest mechanisms activated by cells to counteract the noxious effects of increased reactive oxygen species and reactive nitrogen species.	reactive	202-210	heme oxygenase 1	Homo sapiens	21-60
22728708-10	2012	Interestingly, HO-1 expression was differently affected following treatment with various melatonin formulations.	Melatonin	89-98	heme oxygenase 1	Homo sapiens	15-19
21352351-0	2012	Puerarin protects human umbilical vein endothelial cells against high glucose-induced apoptosis by upregulating heme oxygenase-1 and inhibiting calpain activation.	puerarin	0-8	heme oxygenase 1	Homo sapiens	112-128
21352351-6	2012	HO-1 mRNA expression and HO activity were decreased in HUVECs treated with HG for 48 h. Compared with the group exposed to HG alone, co-incubation of HUVECs with puerarin and HG induced increases in HO-1 mRNA expression and HO activity.	puerarin	162-170	heme oxygenase 1	Homo sapiens	0-4
21352351-6	2012	HO-1 mRNA expression and HO activity were decreased in HUVECs treated with HG for 48 h. Compared with the group exposed to HG alone, co-incubation of HUVECs with puerarin and HG induced increases in HO-1 mRNA expression and HO activity.	puerarin	162-170	heme oxygenase 1	Homo sapiens	199-203
21352351-7	2012	The HO-1 inhibitor protoporphyrin IX zinc (II) abolished the inhibitory effect of puerarin on HG-induced calpain and caspase-3 activation, as well as apoptosis.	protoporphyrin IX	19-36	heme oxygenase 1	Homo sapiens	4-8
21352351-7	2012	The HO-1 inhibitor protoporphyrin IX zinc (II) abolished the inhibitory effect of puerarin on HG-induced calpain and caspase-3 activation, as well as apoptosis.	puerarin	82-90	heme oxygenase 1	Homo sapiens	4-8
21352351-8	2012	The data show that puerarin protects against HG-induced endothelial cell apoptosis by a mechanism involving upregulation of HO-1 expression and inhibition of calpain activity.	puerarin	19-27	heme oxygenase 1	Homo sapiens	124-128
22549002-3	2012	The induction of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system in the brain represents one of the earliest mechanisms activated by cells to counteract the noxious effects of increased reactive oxygen species and reactive nitrogen species.	reactive	202-210	heme oxygenase 1	Homo sapiens	62-66
22549002-3	2012	The induction of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system in the brain represents one of the earliest mechanisms activated by cells to counteract the noxious effects of increased reactive oxygen species and reactive nitrogen species.	oxygen species	211-225	heme oxygenase 1	Homo sapiens	21-60
22549002-3	2012	The induction of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system in the brain represents one of the earliest mechanisms activated by cells to counteract the noxious effects of increased reactive oxygen species and reactive nitrogen species.	oxygen species	211-225	heme oxygenase 1	Homo sapiens	62-66
22549002-3	2012	The induction of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system in the brain represents one of the earliest mechanisms activated by cells to counteract the noxious effects of increased reactive oxygen species and reactive nitrogen species.	Nitrogen	239-247	heme oxygenase 1	Homo sapiens	21-60
22549002-3	2012	The induction of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system in the brain represents one of the earliest mechanisms activated by cells to counteract the noxious effects of increased reactive oxygen species and reactive nitrogen species.	Nitrogen	239-247	heme oxygenase 1	Homo sapiens	62-66
22549002-10	2012	Interestingly, despite the lack of oxidative stress-induced AD neuropathology in cerebellum, HO-1 demonstrated increased Ser-residue phosphorylation and oxidative posttranslational modifications in this brain area, suggesting HO-1 as a target of oxidative damage even in the cerebellum.	Serine	121-124	heme oxygenase 1	Homo sapiens	93-97
22943759-1	2012	OBJECTIVE: To investigate whether chlorophyllin could protect human umbilical vein endothelial cell (HUVEC) against oxidative damage by inducing the expression of heme oxygenase-1 (HO-1) and to explore the underlying mechanism.	chlorophyllin	34-47	heme oxygenase 1	Homo sapiens	163-179
22447044-0	2012	Protein kinase CK2 mediates peroxynitrite-induced heme oxygenase-1 expression             in articular chondrocytes.	Peroxynitrous Acid	28-41	heme oxygenase 1	Homo sapiens	50-66
22447044-2	2012	In the present study, we examined the role of protein kinase casein             kinase (CK2) on peroxynitrite-induced expression of HO-1 in primary articular             chondrocytes.	Peroxynitrous Acid	96-109	heme oxygenase 1	Homo sapiens	132-136
22271370-2	2012	Heme oxygenase (HO)-1, a rate-limiting enzyme of heme degradation, plays a protective role against oxidative stress.	Heme	49-53	heme oxygenase 1	Homo sapiens	0-21
22447044-11	2012	Taken together, our findings suggest that peroxynitrite activates Nrf2 via CK2             signaling, leading to the upregulation of HO-1 in primary chondrocytes.	Peroxynitrous Acid	42-55	heme oxygenase 1	Homo sapiens	133-137
22440905-8	2012	In iron-challenged, cultured proximal tubule cells, we observed a positive correlation between HO-1 mRNA level and HO-1 release.	Iron	3-7	heme oxygenase 1	Homo sapiens	95-99
22440905-8	2012	In iron-challenged, cultured proximal tubule cells, we observed a positive correlation between HO-1 mRNA level and HO-1 release.	Iron	3-7	heme oxygenase 1	Homo sapiens	115-119
22394342-6	2012	Due to the cumulative effects of HO-1 on heme catabolism and the generation of biologically active downstream products, induction of HO-1 might serve as a protective mechanism against oxidative stress and inflammation-induced injury.	Heme	41-45	heme oxygenase 1	Homo sapiens	33-37
22394342-6	2012	Due to the cumulative effects of HO-1 on heme catabolism and the generation of biologically active downstream products, induction of HO-1 might serve as a protective mechanism against oxidative stress and inflammation-induced injury.	Heme	41-45	heme oxygenase 1	Homo sapiens	133-137
22394342-8	2012	This review highlights the roles of HO-1 in lung disease induced by environmental toxins such as cigarette smoke (CS), silica, and asbestos.	Cesium	114-116	heme oxygenase 1	Homo sapiens	36-40
22394342-8	2012	This review highlights the roles of HO-1 in lung disease induced by environmental toxins such as cigarette smoke (CS), silica, and asbestos.	Silicon Dioxide	119-125	heme oxygenase 1	Homo sapiens	36-40
22943759-1	2012	OBJECTIVE: To investigate whether chlorophyllin could protect human umbilical vein endothelial cell (HUVEC) against oxidative damage by inducing the expression of heme oxygenase-1 (HO-1) and to explore the underlying mechanism.	chlorophyllin	34-47	heme oxygenase 1	Homo sapiens	181-185
22943759-7	2012	Chlorophyllin treatment could induce expression of HO-1 in a dose- and time-dependent manner.	chlorophyllin	0-13	heme oxygenase 1	Homo sapiens	51-55
22943759-9	2012	LY294002, the specific inhibitor of PI3K, could suppress the activation of PI3K/Akt and the induced expression of HO-1 in a dose-dependent manner.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	0-8	heme oxygenase 1	Homo sapiens	114-118
22943759-11	2012	Up-regulation of HO-1 expression plays a pivotal role in the protection of chlorophyllin, while the activation of PI3K/Akt signaling pathway is required in the induction of HO-1.	chlorophyllin	75-88	heme oxygenase 1	Homo sapiens	17-21
22155346-7	2012	ATO activated a silent Nrf2 pathway in cultured OSCC cells as shown by induction of Nrf2 and Nrf2-regulated genes, NAD(P)H:quinone oxidoreductase 1 (NQO1) and heme oxygenase-1 (HO-1), in a dose-dependent manner.	Arsenic Trioxide	0-3	heme oxygenase 1	Homo sapiens	159-175
22586396-7	2012	Heme is degraded by heme oxygenase (HO) that exists as two isoforms: inducible HO-1 and constitutively expressed HO-2.	Heme	0-4	heme oxygenase 1	Homo sapiens	79-83
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Heme	32-36	heme oxygenase 1	Homo sapiens	0-16
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Heme	32-36	heme oxygenase 1	Homo sapiens	18-21
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Biliverdine	40-50	heme oxygenase 1	Homo sapiens	0-16
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Biliverdine	40-50	heme oxygenase 1	Homo sapiens	18-21
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Carbon Monoxide	52-67	heme oxygenase 1	Homo sapiens	0-16
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Carbon Monoxide	52-67	heme oxygenase 1	Homo sapiens	18-21
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Iron	77-81	heme oxygenase 1	Homo sapiens	0-16
22503972-4	2012	Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein.	Iron	77-81	heme oxygenase 1	Homo sapiens	18-21
22503972-10	2012	Taken together, our findings point to three novel functions of STC2, and suggest that STC2 interacts with HO1 to form a eukaryotic "stressosome" involved in the degradation of heme.	Heme	176-180	heme oxygenase 1	Homo sapiens	106-109
22426130-8	2012	siRNA-mediated silencing of VEGFA or VEGFR2 could reverse the inhibitory effect of HO-1 on VSMC migration.	vsmc	91-95	heme oxygenase 1	Homo sapiens	83-87
22386815-0	2012	Ellagic acid protects human keratinocyte (HaCaT) cells against UVA-induced oxidative stress and apoptosis through the upregulation of the HO-1 and Nrf-2 antioxidant genes.	Ellagic Acid	0-12	heme oxygenase 1	Homo sapiens	138-142
22431362-3	2012	The introduction of an oxygen atom in the alkyl linker produced analogues with decreased potency toward HO-1, whereas the presence of a sulfur atom in the linker gave rise to analogues with greater potency toward HO-1 than the carbon-containing analogues.	Sulfur	136-142	heme oxygenase 1	Homo sapiens	213-217
22386815-7	2012	Notably, the antioxidant potential of ellagic acid was directly correlated with the increased expression of HO-1 and SOD, which was followed by the downregulation of Keap1 and the augmented nuclear translocation and transcriptional activation of Nrf2 with or without UVA irradiation.	Ellagic Acid	38-50	heme oxygenase 1	Homo sapiens	108-120
22201606-2	2012	The inducible stress protein heme oxygenase-1 (HO-1) has been implicated in cytoprotection against the toxic action of many xenobiotics, including CS.	Cesium	147-149	heme oxygenase 1	Homo sapiens	29-45
22201606-2	2012	The inducible stress protein heme oxygenase-1 (HO-1) has been implicated in cytoprotection against the toxic action of many xenobiotics, including CS.	Cesium	147-149	heme oxygenase 1	Homo sapiens	47-51
22201606-6	2012	Carbon monoxide (CO), a primary reaction product of HO-1 has been implicated in cytoprotection in many acute lung injury models, though it"s precise role in chronic CS-induced lung injury remains unclear.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	52-56
22201606-6	2012	Carbon monoxide (CO), a primary reaction product of HO-1 has been implicated in cytoprotection in many acute lung injury models, though it"s precise role in chronic CS-induced lung injury remains unclear.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	52-56
22201606-9	2012	The implications of the cytoprotective potential of HO-1/CO system in CS-induced lung injury and COPD are discussed.	Cesium	70-72	heme oxygenase 1	Homo sapiens	52-56
22305882-6	2012	Furthermore, the cytoprotective enzyme heme oxygenase-1 could be upregulated in leonurine-treated HUVEC.	leonurine	80-89	heme oxygenase 1	Homo sapiens	39-55
22326969-6	2012	Instead, the over expression of anti-apoptotic Bcl-2, anti-oxidative heme oxygenase-1 (HO-1) and cell cycle regulator p16INK4 seemed to be more important for the gaining of cisplatin in these human urothelial carcinoma cell.	Cisplatin	173-182	heme oxygenase 1	Homo sapiens	69-85
22781797-0	2012	[The effect of retrovirus-mediated HO-1 gene on chronic myeloid leukemia resistance cell K562/A02 apoptosis induced by nilotinib].	nilotinib	119-128	heme oxygenase 1	Homo sapiens	35-39
22781797-1	2012	OBJECTIVE: To investigate the effect of retrovirus mediated heme oxygenase (HO)-1 gene on chronic myeloid leukemia (CML) resistance cell apoptosis induced by nilotinib (AMN107).	nilotinib	158-167	heme oxygenase 1	Homo sapiens	60-81
22421218-0	2012	Smad7 sensitizes A549 lung cancer cells to cisplatin-induced apoptosis through heme oxygenase-1 inhibition.	Cisplatin	43-52	heme oxygenase 1	Homo sapiens	79-95
22421218-4	2012	The HO-1 protein level was elevated in cisplatin-resistant A549 human lung cancer cells and blockade of HO-1 activation sensitized the cells to apoptosis.	Cisplatin	39-48	heme oxygenase 1	Homo sapiens	4-8
22421218-4	2012	The HO-1 protein level was elevated in cisplatin-resistant A549 human lung cancer cells and blockade of HO-1 activation sensitized the cells to apoptosis.	Cisplatin	39-48	heme oxygenase 1	Homo sapiens	104-108
22421218-7	2012	Consistently, Smad7 sensitized A549 cells to cisplatin-induced apoptosis and these effects were dependent on HO-1 and Akt inhibition.	Cisplatin	45-54	heme oxygenase 1	Homo sapiens	109-113
22492492-0	2012	Concomitant induction of heme oxygenase-1 attenuates the cytotoxicity of arsenic species from lumbricus extract in human liver HepG2 cells.	Arsenic	73-80	heme oxygenase 1	Homo sapiens	25-41
22147556-2	2012	The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested.	Nitric Oxide	18-30	heme oxygenase 1	Homo sapiens	116-132
22147556-2	2012	The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested.	Nitric Oxide	18-30	heme oxygenase 1	Homo sapiens	134-138
22147556-2	2012	The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested.	Nitric Oxide	18-30	heme oxygenase 1	Homo sapiens	230-234
22147556-2	2012	The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested.	Bilirubin	148-157	heme oxygenase 1	Homo sapiens	116-132
22147556-2	2012	The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested.	Bilirubin	148-157	heme oxygenase 1	Homo sapiens	134-138
22147556-5	2012	The results revealed an over-expression of iNOS and HO-1 in the papilla, compared with that in the pulp, mediated by the nuclear factor kappa B transcription factor activated by the reactive oxygen species that acts as scavengers for the superoxide radicals.	Reactive Oxygen Species	182-205	heme oxygenase 1	Homo sapiens	52-56
22147556-5	2012	The results revealed an over-expression of iNOS and HO-1 in the papilla, compared with that in the pulp, mediated by the nuclear factor kappa B transcription factor activated by the reactive oxygen species that acts as scavengers for the superoxide radicals.	Superoxides	238-248	heme oxygenase 1	Homo sapiens	52-56
22492492-8	2012	The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO(2) .	protoporphyrin IX	103-120	heme oxygenase 1	Homo sapiens	84-88
22492492-8	2012	The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO(2) .	S-Nitroso-N-propionyl-D,L-penicillamine	122-126	heme oxygenase 1	Homo sapiens	84-88
22492492-8	2012	The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO(2) .	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	162-170	heme oxygenase 1	Homo sapiens	186-190
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Heme	73-77	heme oxygenase 1	Homo sapiens	0-16
22492492-9	2012	These results suggest that arsenic-containing compounds are responsible for HO-1 induction by Lumbricus extract.	Arsenic	27-34	heme oxygenase 1	Homo sapiens	76-80
22492492-10	2012	Although the exact role of toxic arsenic compounds in the treatment of oxidative injury remains unclear, concomitant HO-1 induction may be a key mechanism to antagonize the cytotoxicity of arsenic compounds in human cells.	Arsenic	189-196	heme oxygenase 1	Homo sapiens	117-121
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Heme	73-77	heme oxygenase 1	Homo sapiens	18-22
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Biliverdine	97-107	heme oxygenase 1	Homo sapiens	0-16
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Biliverdine	97-107	heme oxygenase 1	Homo sapiens	18-22
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	0-16
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	18-22
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Carbon Monoxide	126-128	heme oxygenase 1	Homo sapiens	0-16
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Carbon Monoxide	126-128	heme oxygenase 1	Homo sapiens	18-22
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Iron	135-139	heme oxygenase 1	Homo sapiens	0-16
22492492-1	2012	Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion.	Iron	135-139	heme oxygenase 1	Homo sapiens	18-22
22492492-7	2012	Both p38 MAP kinase and NF-E2-related factor 2 (Nrf2) pathways were found to modulate HO-1 induction by Lumbricus extract and NaAsO(2) .	naaso	126-131	heme oxygenase 1	Homo sapiens	86-90
22492492-8	2012	The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO(2) .	arsenite	20-28	heme oxygenase 1	Homo sapiens	84-88
22492492-8	2012	The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO(2) .	arsenite	20-28	heme oxygenase 1	Homo sapiens	186-190
22492492-8	2012	The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO(2) .	Tin	99-102	heme oxygenase 1	Homo sapiens	84-88
22490514-8	2012	Whether the induction or inhibition of HO-1 by cobalt-protoporphyrin-IX (CoPP) or zinc-protoporphyrin-IX (ZnPP) could affect the sensitivity of MKN-45 cells to cisplatin was also studied.	cobaltiprotoporphyrin	47-71	heme oxygenase 1	Homo sapiens	39-43
22690236-8	2012	HO-1 mRNA expression was positively correlated with levels of carboxyhemoglobin, serum ferritin, and serum MDA and negatively correlated with levels of erythrocyte GSH in CLD patients.	Glutathione	164-167	heme oxygenase 1	Homo sapiens	0-4
22490514-8	2012	Whether the induction or inhibition of HO-1 by cobalt-protoporphyrin-IX (CoPP) or zinc-protoporphyrin-IX (ZnPP) could affect the sensitivity of MKN-45 cells to cisplatin was also studied.	cobaltiprotoporphyrin	73-77	heme oxygenase 1	Homo sapiens	39-43
22490514-8	2012	Whether the induction or inhibition of HO-1 by cobalt-protoporphyrin-IX (CoPP) or zinc-protoporphyrin-IX (ZnPP) could affect the sensitivity of MKN-45 cells to cisplatin was also studied.	zinc protoporphyrin	106-110	heme oxygenase 1	Homo sapiens	39-43
22490514-8	2012	Whether the induction or inhibition of HO-1 by cobalt-protoporphyrin-IX (CoPP) or zinc-protoporphyrin-IX (ZnPP) could affect the sensitivity of MKN-45 cells to cisplatin was also studied.	Cisplatin	160-169	heme oxygenase 1	Homo sapiens	39-43
22490514-10	2012	HO-1 overexpression could lead to an increased resistance to cisplatin, whereas down-regulation of HO-1 expression by siRNA or chemical inhibition of HO-1 could lead to increased chemosensitivity to cisplatin in MKN-45 cells.	Cisplatin	61-70	heme oxygenase 1	Homo sapiens	0-4
22490514-10	2012	HO-1 overexpression could lead to an increased resistance to cisplatin, whereas down-regulation of HO-1 expression by siRNA or chemical inhibition of HO-1 could lead to increased chemosensitivity to cisplatin in MKN-45 cells.	Cisplatin	199-208	heme oxygenase 1	Homo sapiens	99-103
22490514-10	2012	HO-1 overexpression could lead to an increased resistance to cisplatin, whereas down-regulation of HO-1 expression by siRNA or chemical inhibition of HO-1 could lead to increased chemosensitivity to cisplatin in MKN-45 cells.	Cisplatin	199-208	heme oxygenase 1	Homo sapiens	99-103
22197494-8	2012	Resveratrol prevented the up-regulation of early growth response protein-1 (Egr-1), a transcription factor necessary for induction of the vascular endothelial growth factor receptor-1 gene and caused up-regulation of heme oxygenase-1, a cytoprotective enzyme found to be dysfunctional in preeclampsia.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	217-233
22098251-8	2012	RESULTS: Ex vivo, donor liver preconditioning with Nodosin perfusion induced HO-1 expression and enzyme activity significantly, compared with the control group (P &lt; 0.05).	nodosin	51-58	heme oxygenase 1	Homo sapiens	77-81
22240980-8	2012	Reactive oxygen species (ROS) were detected along with the formation of protein carbonyls and the induction of heme oxygenase-1.	Reactive Oxygen Species	0-23	heme oxygenase 1	Homo sapiens	111-127
22240980-8	2012	Reactive oxygen species (ROS) were detected along with the formation of protein carbonyls and the induction of heme oxygenase-1.	Reactive Oxygen Species	25-28	heme oxygenase 1	Homo sapiens	111-127
21971692-6	2012	It was found that EEPV increased HO-1 protein expression in RAW 264.7 cells, which was significantly inhibited by LY294002, but not PD98059, SB203580 or SP600125.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	114-122	heme oxygenase 1	Homo sapiens	33-37
21971692-7	2012	In addition, EEPV activated NF-E2-related factor (Nrf2) to move from the cytosol to the nucleus, and EEPV-induced HO-1 and activation of ARE-luciferase activity were significantly reduced by siNrf2 transfection and LY294002 but not SB203508.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	215-223	heme oxygenase 1	Homo sapiens	114-118
21971692-7	2012	In addition, EEPV activated NF-E2-related factor (Nrf2) to move from the cytosol to the nucleus, and EEPV-induced HO-1 and activation of ARE-luciferase activity were significantly reduced by siNrf2 transfection and LY294002 but not SB203508.	sb203508	232-240	heme oxygenase 1	Homo sapiens	114-118
22197494-9	2012	CONCLUSION: In summary, resveratrol can inhibit sFlt-1 release and up-regulate heme oxygenase-1; thus, may offer therapeutic potential in preeclampsia.	Resveratrol	24-35	heme oxygenase 1	Homo sapiens	79-95
22166397-2	2012	In this study, we examined whether M. cordata extract and/or its major alkaloid constituents, protopine, allocryptopine, sanguinarine and chelerythrine activate the Nrf2 signalling pathway which regulates the expression of cytoprotective enzymes including heme oxygenase-1 (HO-1) and thioredoxin 1.	chelerythrine	138-151	heme oxygenase 1	Homo sapiens	274-278
21954917-4	2012	Treatment with the HO-1 inducer CoPP (cobalt protoporphyrin IX) counteracted the stimulatory effects of IL-1beta on IL-6, nitrite, PGE2 (prostaglandin E2), TGF (transforming growth factor) beta2, TGFbeta3 and osteocalcin.	cobaltiprotoporphyrin	38-62	heme oxygenase 1	Homo sapiens	19-23
21954917-4	2012	Treatment with the HO-1 inducer CoPP (cobalt protoporphyrin IX) counteracted the stimulatory effects of IL-1beta on IL-6, nitrite, PGE2 (prostaglandin E2), TGF (transforming growth factor) beta2, TGFbeta3 and osteocalcin.	Nitrites	122-129	heme oxygenase 1	Homo sapiens	19-23
21954917-4	2012	Treatment with the HO-1 inducer CoPP (cobalt protoporphyrin IX) counteracted the stimulatory effects of IL-1beta on IL-6, nitrite, PGE2 (prostaglandin E2), TGF (transforming growth factor) beta2, TGFbeta3 and osteocalcin.	Dinoprostone	131-135	heme oxygenase 1	Homo sapiens	19-23
21954917-4	2012	Treatment with the HO-1 inducer CoPP (cobalt protoporphyrin IX) counteracted the stimulatory effects of IL-1beta on IL-6, nitrite, PGE2 (prostaglandin E2), TGF (transforming growth factor) beta2, TGFbeta3 and osteocalcin.	Dinoprostone	137-153	heme oxygenase 1	Homo sapiens	19-23
22166397-8	2012	Nonetheless, sanguinarine at micromolar, non-cytotoxic concentrations elevated protein levels of HO-1 and thioredoxin 1 in primary cultures of human hepatocytes.	sanguinarine	13-25	heme oxygenase 1	Homo sapiens	97-101
22203369-1	2012	Probucol inhibits the proliferation of vascular smooth muscle cells in vitro and in vivo, and the drug reduces intimal hyperplasia and atherosclerosis in animals via induction of heme oxygenase-1 (HO-1).	Probucol	0-8	heme oxygenase 1	Homo sapiens	179-195
22203369-1	2012	Probucol inhibits the proliferation of vascular smooth muscle cells in vitro and in vivo, and the drug reduces intimal hyperplasia and atherosclerosis in animals via induction of heme oxygenase-1 (HO-1).	Probucol	0-8	heme oxygenase 1	Homo sapiens	197-201
22203369-4	2012	However, whereas inhibition of HO-1 reversed the antiproliferative effects of probucol, this was not observed with succinobucol.	Probucol	78-86	heme oxygenase 1	Homo sapiens	31-35
21725851-1	2012	Heme oxygenase-1 (HO-1) which is a rate-limiting enzyme in heme degradation processes shows a dinucleotide GT repeat in the promoter that alters the level of gene transcription.	Heme	59-63	heme oxygenase 1	Homo sapiens	0-16
21647550-2	2012	On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences.	Iron	253-257	heme oxygenase 1	Homo sapiens	162-167
21725851-1	2012	Heme oxygenase-1 (HO-1) which is a rate-limiting enzyme in heme degradation processes shows a dinucleotide GT repeat in the promoter that alters the level of gene transcription.	Heme	59-63	heme oxygenase 1	Homo sapiens	18-22
21647550-2	2012	On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences.	Iron	253-257	heme oxygenase 1	Homo sapiens	122-138
21725851-1	2012	Heme oxygenase-1 (HO-1) which is a rate-limiting enzyme in heme degradation processes shows a dinucleotide GT repeat in the promoter that alters the level of gene transcription.	Dinucleoside Phosphates	94-106	heme oxygenase 1	Homo sapiens	0-16
21647550-2	2012	On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences.	Iron	253-257	heme oxygenase 1	Homo sapiens	140-144
21725851-1	2012	Heme oxygenase-1 (HO-1) which is a rate-limiting enzyme in heme degradation processes shows a dinucleotide GT repeat in the promoter that alters the level of gene transcription.	Dinucleoside Phosphates	94-106	heme oxygenase 1	Homo sapiens	18-22
22200816-0	2012	Sulforaphane protects against 6-hydroxydopamine-induced cytotoxicity             by increasing expression of heme oxygenase-1 in a PI3K/Akt-dependent manner.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	109-125
22200816-0	2012	Sulforaphane protects against 6-hydroxydopamine-induced cytotoxicity             by increasing expression of heme oxygenase-1 in a PI3K/Akt-dependent manner.	Oxidopamine	30-47	heme oxygenase 1	Homo sapiens	109-125
22200816-7	2012	SF also             increased heme oxygenase-1 (HO-1) expression, which conferred protection against             6-OHDA-induced cytotoxicity.	Oxidopamine	113-119	heme oxygenase 1	Homo sapiens	30-46
22200816-7	2012	SF also             increased heme oxygenase-1 (HO-1) expression, which conferred protection against             6-OHDA-induced cytotoxicity.	Oxidopamine	113-119	heme oxygenase 1	Homo sapiens	48-52
22200816-9	2012	These results             suggest that SF inhibits 6-OHDA-induced cytotoxicity through increasing HO-1 expression             in a PI3K/Akt-dependent manner.	Oxidopamine	51-57	heme oxygenase 1	Homo sapiens	98-102
22200625-5	2012	Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin.	Heme	102-106	heme oxygenase 1	Homo sapiens	0-16
22200625-5	2012	Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin.	Heme	102-106	heme oxygenase 1	Homo sapiens	18-22
22200625-5	2012	Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin.	Carbon Monoxide	112-127	heme oxygenase 1	Homo sapiens	0-16
22200625-5	2012	Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin.	Carbon Monoxide	112-127	heme oxygenase 1	Homo sapiens	18-22
22200625-5	2012	Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin.	Bilirubin	142-151	heme oxygenase 1	Homo sapiens	0-16
22200625-5	2012	Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin.	Bilirubin	142-151	heme oxygenase 1	Homo sapiens	18-22
25774181-2	2012	Graded concentration and time course experiments demonstrate that curcumin significantly upregulates phosphatidylinositol 3-kinase (PI3K), Akt, nuclear factor E2-related factor-2 (Nrf2), heme oxygenase 1 and ferritin expression, and that it significantly downregulates heme oxygenase 2, reactive oxygen species and amyloid-beta 40/42 expression.	Curcumin	66-74	heme oxygenase 1	Homo sapiens	187-203
22100389-0	2012	Dexamethasone-loaded peptide micelles for delivery of the heme oxygenase-1 gene to ischemic brain.	Dexamethasone	0-13	heme oxygenase 1	Homo sapiens	58-74
25774181-4	2012	The results indicate that the cytoprotection conferred by curcumin on APPswe transfected SH-SY5Y cells is mediated by its ability to regulate the balance between heme oxygenase 1 and 2 via the PI3K/Akt/Nrf2 intracellular signaling pathway.	Curcumin	58-66	heme oxygenase 1	Homo sapiens	162-184
21997482-10	2012	1,2-NQ exposure also causes marked expression of HO-1 that appears to be enhanced by suppression of H2O2.	1,2-naphthoquinone	0-6	heme oxygenase 1	Homo sapiens	49-53
22260728-0	2012	Apo-8"-lycopenal induces expression of HO-1 and NQO-1 via the ERK/p38-Nrf2-ARE pathway in human HepG2 cells.	apo-8'-lycopenal	0-16	heme oxygenase 1	Homo sapiens	39-43
22155307-5	2012	HO-1 was induced with cobalt protoporphyrin IX (CoPP) and by transduction with LV-HO-1.	cobaltiprotoporphyrin	22-46	heme oxygenase 1	Homo sapiens	0-4
22155307-5	2012	HO-1 was induced with cobalt protoporphyrin IX (CoPP) and by transduction with LV-HO-1.	cobaltiprotoporphyrin	48-52	heme oxygenase 1	Homo sapiens	0-4
22155307-8	2012	HO-1 also exerted inhibitory effects on prostaglandin (PG)E(2) production which could be dependent on cyclooxygenase-2 and microsomal PGE synthase-1 down-regulation.	Dinoprostone	40-62	heme oxygenase 1	Homo sapiens	0-4
22095074-0	2012	Guggulsterone induces heme oxygenase-1 expression through activation of Nrf2 in human mammary epithelial cells: PTEN as a putative target.	pregna-4,17-diene-3,16-dione	0-13	heme oxygenase 1	Homo sapiens	22-38
22095074-11	2012	Pretreatment with the thiol-reducing agents attenuated Akt phosphorylation, Nrf2 activation and HO-1 expression, suggesting that cis-GS may cause thiol modification of an upstream signaling modulator.	Sulfhydryl Compounds	22-27	heme oxygenase 1	Homo sapiens	96-100
22095074-11	2012	Pretreatment with the thiol-reducing agents attenuated Akt phosphorylation, Nrf2 activation and HO-1 expression, suggesting that cis-GS may cause thiol modification of an upstream signaling modulator.	pregna-4,17-diene-3,16-dione	129-135	heme oxygenase 1	Homo sapiens	96-100
22095074-13	2012	The mutation in cysteine 124 present in the catalytic domain of PTEN abolished cis-GS-induced HO-1 expression as well as Akt phosphorylation.	Cysteine	16-24	heme oxygenase 1	Homo sapiens	94-98
21992109-1	2012	HO-1 (haem oxygenase-1) is a ubiquitously expressed inducible enzyme degrading haem to CO, biliverdin and Fe(2+).	Carbon Monoxide	87-89	heme oxygenase 1	Homo sapiens	0-22
21992109-1	2012	HO-1 (haem oxygenase-1) is a ubiquitously expressed inducible enzyme degrading haem to CO, biliverdin and Fe(2+).	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	0-22
21992109-1	2012	HO-1 (haem oxygenase-1) is a ubiquitously expressed inducible enzyme degrading haem to CO, biliverdin and Fe(2+).	ammonium ferrous sulfate	106-112	heme oxygenase 1	Homo sapiens	0-22
21997482-10	2012	1,2-NQ exposure also causes marked expression of HO-1 that appears to be enhanced by suppression of H2O2.	Hydrogen Peroxide	100-104	heme oxygenase 1	Homo sapiens	49-53
22019695-0	2012	Reactive oxygen species and PI3K/Akt signaling play key roles in the induction of Nrf2-driven heme oxygenase-1 expression in sulforaphane-treated human mesothelioma MSTO-211H cells.	Reactive Oxygen Species	0-23	heme oxygenase 1	Homo sapiens	94-110
22019695-0	2012	Reactive oxygen species and PI3K/Akt signaling play key roles in the induction of Nrf2-driven heme oxygenase-1 expression in sulforaphane-treated human mesothelioma MSTO-211H cells.	sulforaphane	125-137	heme oxygenase 1	Homo sapiens	94-110
22155056-1	2012	Sulforaphane (SFN) is a dietary isothiocyanate that exerts chemopreventive effects via NF-E2-related factor 2 (Nrf2)-mediated induction of antioxidant/phase II enzymes, such as heme oxygenase-1 (HO-1) and NAD(P)H quinone oxidoreductase 1 (NQO1).	sulforaphane	14-17	heme oxygenase 1	Homo sapiens	177-193
22019695-2	2012	In this study, we investigated Nrf2/HO-1 induction in response to sulforaphane and determined the signaling pathways involved in this process.	sulforaphane	66-78	heme oxygenase 1	Homo sapiens	36-40
22019695-7	2012	Activation of the Nrf2/HO-1 system after sulforaphane treatment was suppressed by pretreatment with NAC or Ly294002, a PI3K inhibitor.	sulforaphane	41-53	heme oxygenase 1	Homo sapiens	23-27
22019695-7	2012	Activation of the Nrf2/HO-1 system after sulforaphane treatment was suppressed by pretreatment with NAC or Ly294002, a PI3K inhibitor.	Acetylcysteine	100-103	heme oxygenase 1	Homo sapiens	23-27
22019695-7	2012	Activation of the Nrf2/HO-1 system after sulforaphane treatment was suppressed by pretreatment with NAC or Ly294002, a PI3K inhibitor.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	107-115	heme oxygenase 1	Homo sapiens	23-27
22019695-8	2012	Knockdown of Nrf2 with siRNA decreased cell viability and attenuated sulforaphane-induced HO-1 up-regulation.	sulforaphane	69-81	heme oxygenase 1	Homo sapiens	90-94
22019695-9	2012	Overall, our results indicate that ROS generation and/or activation of PI3K/Akt signaling regulate cell survival and Nrf2-driven HO-1 expression in sulforaphane-treated MSTO-211H cells.	Reactive Oxygen Species	35-38	heme oxygenase 1	Homo sapiens	129-133
22019695-9	2012	Overall, our results indicate that ROS generation and/or activation of PI3K/Akt signaling regulate cell survival and Nrf2-driven HO-1 expression in sulforaphane-treated MSTO-211H cells.	sulforaphane	148-160	heme oxygenase 1	Homo sapiens	129-133
22155056-1	2012	Sulforaphane (SFN) is a dietary isothiocyanate that exerts chemopreventive effects via NF-E2-related factor 2 (Nrf2)-mediated induction of antioxidant/phase II enzymes, such as heme oxygenase-1 (HO-1) and NAD(P)H quinone oxidoreductase 1 (NQO1).	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	177-193
22155056-1	2012	Sulforaphane (SFN) is a dietary isothiocyanate that exerts chemopreventive effects via NF-E2-related factor 2 (Nrf2)-mediated induction of antioxidant/phase II enzymes, such as heme oxygenase-1 (HO-1) and NAD(P)H quinone oxidoreductase 1 (NQO1).	isothiocyanic acid	32-46	heme oxygenase 1	Homo sapiens	177-193
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Iron	114-118	heme oxygenase 1	Homo sapiens	0-16
22309084-4	2012	Interestingly, the switch from stimulatory to inhibitory actions occurred within a narrow concentration range and correlated with the ability of 15d-PGJ(2) to induce heme oxygenase 1 and gamma-GCSm expression.	15d-pgj	145-152	heme oxygenase 1	Homo sapiens	166-182
22037960-12	2012	Furthermore,             we found a significant positive correlation between exhaled CO levels and HO-1             gene expression levels.	Carbon Monoxide	85-87	heme oxygenase 1	Homo sapiens	99-103
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Iron	114-118	heme oxygenase 1	Homo sapiens	18-22
22037960-15	2012	These results suggest that HO-1-mediated heme breakdown is caused             by I/R during LDLT, since it is associated with increased exhaled CO levels and             liver damage.	Heme	41-45	heme oxygenase 1	Homo sapiens	27-31
22037960-15	2012	These results suggest that HO-1-mediated heme breakdown is caused             by I/R during LDLT, since it is associated with increased exhaled CO levels and             liver damage.	Carbon Monoxide	144-146	heme oxygenase 1	Homo sapiens	27-31
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	0-16
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	18-22
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Carbon Monoxide	137-139	heme oxygenase 1	Homo sapiens	0-16
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Carbon Monoxide	137-139	heme oxygenase 1	Homo sapiens	18-22
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Biliverdine	158-176	heme oxygenase 1	Homo sapiens	0-16
22037960-3	2012	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme             in heme catabolism and results in the production of iron, carbon monoxide (CO),             and biliverdin IXalpha.	Biliverdine	158-176	heme oxygenase 1	Homo sapiens	18-22
22236404-1	2012	INTRODUCTION: Critical illness leads to increased endogenous production of carbon monoxide (CO) due to the induction of the stress-response enzyme, heme oxygenase-1 (HO-1).	Carbon Monoxide	75-90	heme oxygenase 1	Homo sapiens	148-164
22120038-6	2012	On the other hand, the inhibitory effect of Pb(2+) on the induction of CYP1A1 coincided with an increase in heme oxygenase-1 (HO-1) mRNA level and reactive oxygen species production at the posttranslational level.	Lead	44-46	heme oxygenase 1	Homo sapiens	108-124
22120038-6	2012	On the other hand, the inhibitory effect of Pb(2+) on the induction of CYP1A1 coincided with an increase in heme oxygenase-1 (HO-1) mRNA level and reactive oxygen species production at the posttranslational level.	Lead	44-46	heme oxygenase 1	Homo sapiens	126-130
21447045-0	2012	Atorvastatin activates heme oxygenase-1 at the stress response elements.	Atorvastatin	0-12	heme oxygenase 1	Homo sapiens	23-39
21447045-5	2012	Among the antioxidant response genes, heme oxygenase-1 (HO-1) was significantly up-regulated by atorvastatin.	Atorvastatin	96-108	heme oxygenase 1	Homo sapiens	38-54
21447045-5	2012	Among the antioxidant response genes, heme oxygenase-1 (HO-1) was significantly up-regulated by atorvastatin.	Atorvastatin	96-108	heme oxygenase 1	Homo sapiens	56-60
21447045-6	2012	Pre-incubation of the cells with geranylgeranyl pyrophosphate blocked atorvastatin-induced apoptosis, but not up-regulation of HO-1, suggesting that atorvastatin-induced apoptosis is dependent on GTPase activity and up-regulation of HO-1 gene is not.	geranylgeranyl pyrophosphate	33-61	heme oxygenase 1	Homo sapiens	233-237
21447045-6	2012	Pre-incubation of the cells with geranylgeranyl pyrophosphate blocked atorvastatin-induced apoptosis, but not up-regulation of HO-1, suggesting that atorvastatin-induced apoptosis is dependent on GTPase activity and up-regulation of HO-1 gene is not.	Atorvastatin	149-161	heme oxygenase 1	Homo sapiens	233-237
21447045-9	2012	Because these StRE sites are present in clusters in HO-1 promoter, up-regulation of HO-1 by atorvastatin may involve multiple StRE sites.	Atorvastatin	92-104	heme oxygenase 1	Homo sapiens	52-56
21447045-9	2012	Because these StRE sites are present in clusters in HO-1 promoter, up-regulation of HO-1 by atorvastatin may involve multiple StRE sites.	Atorvastatin	92-104	heme oxygenase 1	Homo sapiens	84-88
21447045-10	2012	The role of HO-1 in atorvastatin-induced apoptosis in PC-3 and MCF-7 remains to be studied.	Atorvastatin	20-32	heme oxygenase 1	Homo sapiens	12-16
21447442-0	2012	Epigallocatechin-gallate stimulates NF-E2-related factor and heme oxygenase-1 via caveolin-1 displacement.	epigallocatechin gallate	0-24	heme oxygenase 1	Homo sapiens	61-77
21447442-6	2012	To test this hypothesis, we explored the effect of EGCG on the induction of NF-E2-related factor (Nrf2) and HO-1 in endothelial cells with or without functional caveolae.	epigallocatechin gallate	51-55	heme oxygenase 1	Homo sapiens	108-112
21447442-7	2012	Treatment with EGCG activated Nrf2 and increased HO-1 expression and cellular production of bilirubin.	epigallocatechin gallate	15-19	heme oxygenase 1	Homo sapiens	49-53
22120038-7	2012	Furthermore, the inhibition of HO-1 activity, by tin mesoporphyrin, or supplementing heme, using hemin, caused a partial restoration of Pb(2+)-mediated inhibition of CYP1A1 induction by TCDD.	tin mesoporphyrin	49-66	heme oxygenase 1	Homo sapiens	31-35
22120038-7	2012	Furthermore, the inhibition of HO-1 activity, by tin mesoporphyrin, or supplementing heme, using hemin, caused a partial restoration of Pb(2+)-mediated inhibition of CYP1A1 induction by TCDD.	Hemin	97-102	heme oxygenase 1	Homo sapiens	31-35
22120038-7	2012	Furthermore, the inhibition of HO-1 activity, by tin mesoporphyrin, or supplementing heme, using hemin, caused a partial restoration of Pb(2+)-mediated inhibition of CYP1A1 induction by TCDD.	Polychlorinated Dibenzodioxins	186-190	heme oxygenase 1	Homo sapiens	31-35
22120038-8	2012	In addition, transfection of HepG2 cells with siRNA targeting the human HO-1 gene restored the Pb(2+)-mediated inhibition of TCDD-induced CYP1A1.	Polychlorinated Dibenzodioxins	125-129	heme oxygenase 1	Homo sapiens	72-76
22158875-9	2012	The IL-19-induced reduction in ROS concentration is attenuated when HO-1 is reduced by siRNA, indicating that the IL-19-driven decrease in ROS is mediated by HO-1 expression.	Reactive Oxygen Species	31-34	heme oxygenase 1	Homo sapiens	68-72
22158875-9	2012	The IL-19-induced reduction in ROS concentration is attenuated when HO-1 is reduced by siRNA, indicating that the IL-19-driven decrease in ROS is mediated by HO-1 expression.	Reactive Oxygen Species	31-34	heme oxygenase 1	Homo sapiens	158-162
22158875-9	2012	The IL-19-induced reduction in ROS concentration is attenuated when HO-1 is reduced by siRNA, indicating that the IL-19-driven decrease in ROS is mediated by HO-1 expression.	Reactive Oxygen Species	139-142	heme oxygenase 1	Homo sapiens	68-72
22158875-9	2012	The IL-19-induced reduction in ROS concentration is attenuated when HO-1 is reduced by siRNA, indicating that the IL-19-driven decrease in ROS is mediated by HO-1 expression.	Reactive Oxygen Species	139-142	heme oxygenase 1	Homo sapiens	158-162
22142471-4	2012	In this study, the cancer-chemopreventive agent nordihydroguaiaretic acid (NDGA) increased the level of Nrf2 protein and expression of heme oxygenase-1 (HO-1) in kidney-derived LLC-PK1 and HEK293T cells and in wild-type mouse embryo fibroblasts (MEFs).	Masoprocol	48-73	heme oxygenase 1	Homo sapiens	153-157
22142471-4	2012	In this study, the cancer-chemopreventive agent nordihydroguaiaretic acid (NDGA) increased the level of Nrf2 protein and expression of heme oxygenase-1 (HO-1) in kidney-derived LLC-PK1 and HEK293T cells and in wild-type mouse embryo fibroblasts (MEFs).	Masoprocol	75-79	heme oxygenase 1	Homo sapiens	153-157
22142471-6	2012	The relevance of the Nrf2/HO-1 axis to antioxidant protection was further demonstrated by the finding that the HO-1 inhibitor stannous-mesoporphyrin abolished protection against hydrogen peroxide conferred by NDGA.	stannous mesoporphyrin	126-148	heme oxygenase 1	Homo sapiens	26-30
22142471-6	2012	The relevance of the Nrf2/HO-1 axis to antioxidant protection was further demonstrated by the finding that the HO-1 inhibitor stannous-mesoporphyrin abolished protection against hydrogen peroxide conferred by NDGA.	stannous mesoporphyrin	126-148	heme oxygenase 1	Homo sapiens	111-115
22142471-6	2012	The relevance of the Nrf2/HO-1 axis to antioxidant protection was further demonstrated by the finding that the HO-1 inhibitor stannous-mesoporphyrin abolished protection against hydrogen peroxide conferred by NDGA.	Hydrogen Peroxide	178-195	heme oxygenase 1	Homo sapiens	26-30
22142471-6	2012	The relevance of the Nrf2/HO-1 axis to antioxidant protection was further demonstrated by the finding that the HO-1 inhibitor stannous-mesoporphyrin abolished protection against hydrogen peroxide conferred by NDGA.	Hydrogen Peroxide	178-195	heme oxygenase 1	Homo sapiens	111-115
22142473-0	2012	Resistance of neuroblastoma GI-ME-N cell line to glutathione depletion involves Nrf2 and heme oxygenase-1.	Glutathione	49-60	heme oxygenase 1	Homo sapiens	89-105
22142473-3	2012	Here, we show that in GI-ME-N cells, BSO activates Nrf2 and up-regulates heme oxygenase-1 (HO-1).	Nitrogen	28-29	heme oxygenase 1	Homo sapiens	73-89
22142473-3	2012	Here, we show that in GI-ME-N cells, BSO activates Nrf2 and up-regulates heme oxygenase-1 (HO-1).	Nitrogen	28-29	heme oxygenase 1	Homo sapiens	91-95
22142473-5	2012	Inhibition of HO-1 and silencing of Nrf2 or HO-1 sensitized GI-ME-N cells to BSO, leading to reactive oxygen/nitrogen species overproduction and decreasing viability.	reactive oxygen/nitrogen species	93-125	heme oxygenase 1	Homo sapiens	44-48
22142473-6	2012	Moreover, targeting the Nrf2/HO-1 axis sensitized GI-ME-N cells to etoposide more than GSH depletion.	gi-me-n	50-57	heme oxygenase 1	Homo sapiens	29-33
22142473-6	2012	Moreover, targeting the Nrf2/HO-1 axis sensitized GI-ME-N cells to etoposide more than GSH depletion.	Etoposide	67-76	heme oxygenase 1	Homo sapiens	29-33
22138245-10	2012	Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia.	Heme	68-72	heme oxygenase 1	Homo sapiens	48-52
22138245-10	2012	Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia.	Heme	68-72	heme oxygenase 1	Homo sapiens	96-100
22138245-10	2012	Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia.	Carbon Monoxide	78-80	heme oxygenase 1	Homo sapiens	48-52
22138245-10	2012	Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia.	Carbon Monoxide	78-80	heme oxygenase 1	Homo sapiens	96-100
22138245-10	2012	Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia.	Bilirubin	85-94	heme oxygenase 1	Homo sapiens	48-52
22138245-10	2012	Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia.	Bilirubin	85-94	heme oxygenase 1	Homo sapiens	96-100
22052915-4	2012	OBJECTIVE: This study aimed to define the key transcription factor(s) involved in HO-1 induction by heme.	Heme	100-104	heme oxygenase 1	Homo sapiens	82-86
22052915-9	2012	Heme-induced HO-1 and LXR-beta were suppressed by knockdown of ATF-1, and HO-1 and LXR-beta were induced by ATF-1 transfection.	Heme	0-4	heme oxygenase 1	Homo sapiens	13-17
22052915-9	2012	Heme-induced HO-1 and LXR-beta were suppressed by knockdown of ATF-1, and HO-1 and LXR-beta were induced by ATF-1 transfection.	Heme	0-4	heme oxygenase 1	Homo sapiens	74-78
22052915-13	2012	CONCLUSIONS: These results show that ATF-1 mediates HO-1 induction by heme and drives macrophage adaptation to intraplaque hemorrhage.	Heme	70-74	heme oxygenase 1	Homo sapiens	52-56
22236404-1	2012	INTRODUCTION: Critical illness leads to increased endogenous production of carbon monoxide (CO) due to the induction of the stress-response enzyme, heme oxygenase-1 (HO-1).	Carbon Monoxide	75-90	heme oxygenase 1	Homo sapiens	166-170
22236404-1	2012	INTRODUCTION: Critical illness leads to increased endogenous production of carbon monoxide (CO) due to the induction of the stress-response enzyme, heme oxygenase-1 (HO-1).	Carbon Monoxide	92-94	heme oxygenase 1	Homo sapiens	148-164
22236404-1	2012	INTRODUCTION: Critical illness leads to increased endogenous production of carbon monoxide (CO) due to the induction of the stress-response enzyme, heme oxygenase-1 (HO-1).	Carbon Monoxide	92-94	heme oxygenase 1	Homo sapiens	166-170
22195275-0	2012	Heme Oxygenase-1 Attenuates Hypoxia-Induced sFlt-1 and Oxidative Stress in Placental Villi through Its Metabolic Products CO and Bilirubin.	Bilirubin	129-138	heme oxygenase 1	Homo sapiens	0-16
22095827-0	2012	Niacin inhibits vascular inflammation via the induction of heme oxygenase-1.	Niacin	0-6	heme oxygenase 1	Homo sapiens	59-75
22095827-2	2012	Niacin is a pleiotropic drug that slows the progression of coronary artery disease and increases serum levels of the HO-1 enzymatic product bilirubin.	Niacin	0-6	heme oxygenase 1	Homo sapiens	117-121
22095827-2	2012	Niacin is a pleiotropic drug that slows the progression of coronary artery disease and increases serum levels of the HO-1 enzymatic product bilirubin.	Bilirubin	140-149	heme oxygenase 1	Homo sapiens	117-121
22095827-3	2012	This study asks if the cardioprotective properties of niacin involve the induction of HO-1.	Niacin	54-60	heme oxygenase 1	Homo sapiens	86-90
22095827-8	2012	Treatment of the animals with tin protoporphyrin-IX, a global HO inhibitor, or HO-1 small interfering RNA to knock down carotid artery HO-1 attenuated the ability of niacin to inhibit vascular inflammation.	tin protoporphyrin IX	30-51	heme oxygenase 1	Homo sapiens	135-139
22095827-8	2012	Treatment of the animals with tin protoporphyrin-IX, a global HO inhibitor, or HO-1 small interfering RNA to knock down carotid artery HO-1 attenuated the ability of niacin to inhibit vascular inflammation.	Niacin	166-172	heme oxygenase 1	Homo sapiens	79-83
22095827-8	2012	Treatment of the animals with tin protoporphyrin-IX, a global HO inhibitor, or HO-1 small interfering RNA to knock down carotid artery HO-1 attenuated the ability of niacin to inhibit vascular inflammation.	Niacin	166-172	heme oxygenase 1	Homo sapiens	135-139
22095827-11	2012	CONCLUSIONS: Niacin activates HO-1 in vivo and in vitro.	Niacin	13-19	heme oxygenase 1	Homo sapiens	30-34
22701506-5	2012	In addition, 3,4-O-dicaffeoylquinic acid significantly increased the expression of heme oxygenase-1 (HO-1) in HepG2.2.15 cells.	caffeoylquinic acid	13-40	heme oxygenase 1	Homo sapiens	83-99
22701506-5	2012	In addition, 3,4-O-dicaffeoylquinic acid significantly increased the expression of heme oxygenase-1 (HO-1) in HepG2.2.15 cells.	caffeoylquinic acid	13-40	heme oxygenase 1	Homo sapiens	101-105
22165967-0	2012	The Hsp32 inhibitors SMA-ZnPP and PEG-ZnPP exert major growth-inhibitory effects on D34+/CD38+ and CD34+/CD38- AML progenitor cells.	pegylated zinc protoporphyrin	34-42	heme oxygenase 1	Homo sapiens	4-9
22506100-0	2012	Heme oxygenase-1 induction and organic nitrate therapy: beneficial effects on endothelial dysfunction, nitrate tolerance, and vascular oxidative stress.	Nitrates	103-110	heme oxygenase 1	Homo sapiens	0-16
22506100-4	2012	We therefore speculated that induction of heme oxygenase-1 (HO-1) could be an efficient strategy to overcome nitrate tolerance and the associated side effects.	Nitrates	109-116	heme oxygenase 1	Homo sapiens	42-58
22518279-4	2012	In the present paper, we will discuss the role of heme oxygenase (HO)-1 which is an enzyme of the heme catabolism and cleaves heme to form biliverdin and carbon monoxide (CO).	Biliverdine	139-149	heme oxygenase 1	Homo sapiens	50-71
22195275-3	2012	Recently, HO-1 has been shown to downregulate two of these factors, reactive oxygen species and sFlt-1, and we have reported that HO-1 induction attenuates many of the pathological factors of placental ischemia experimentally.	Reactive Oxygen Species	68-91	heme oxygenase 1	Homo sapiens	10-14
22518279-4	2012	In the present paper, we will discuss the role of heme oxygenase (HO)-1 which is an enzyme of the heme catabolism and cleaves heme to form biliverdin and carbon monoxide (CO).	Carbon Monoxide	154-169	heme oxygenase 1	Homo sapiens	50-71
22506100-4	2012	We therefore speculated that induction of heme oxygenase-1 (HO-1) could be an efficient strategy to overcome nitrate tolerance and the associated side effects.	Nitrates	109-116	heme oxygenase 1	Homo sapiens	60-64
22506100-8	2012	With the present paper, we present and discuss our recent and previous findings on the role of HO-1 for the prevention of nitroglycerin-induced nitrate tolerance and for the beneficial effects of PETN therapy.	Nitroglycerin	122-135	heme oxygenase 1	Homo sapiens	95-99
22518279-4	2012	In the present paper, we will discuss the role of heme oxygenase (HO)-1 which is an enzyme of the heme catabolism and cleaves heme to form biliverdin and carbon monoxide (CO).	Carbon Monoxide	171-173	heme oxygenase 1	Homo sapiens	50-71
22195275-4	2012	Here, we have examined the direct effect of HO-1 and its bioactive metabolites on hypoxia-induced changes in superoxide and sFlt-1 in placental vascular explants and showed that HO-1 and its metabolites attenuate the production of both factors in this system.	Superoxides	109-119	heme oxygenase 1	Homo sapiens	44-48
22518279-6	2012	Recent evidence supports the involvement of HO-1 in the antioxidant and antiinflammatory effect of cyclooxygenase(COX)-2-dependent prostacyclin in the vasculature.	Epoprostenol	131-143	heme oxygenase 1	Homo sapiens	44-48
22506100-8	2012	With the present paper, we present and discuss our recent and previous findings on the role of HO-1 for the prevention of nitroglycerin-induced nitrate tolerance and for the beneficial effects of PETN therapy.	Nitrates	144-151	heme oxygenase 1	Homo sapiens	95-99
22195275-4	2012	Here, we have examined the direct effect of HO-1 and its bioactive metabolites on hypoxia-induced changes in superoxide and sFlt-1 in placental vascular explants and showed that HO-1 and its metabolites attenuate the production of both factors in this system.	Superoxides	109-119	heme oxygenase 1	Homo sapiens	178-182
23095372-5	2012	RESULTS: CD163-expressing macrophages, HO-1 and NADPH-p22 expression were located in areas surrounding tubules with iron deposits and filled with erythrocyte casts.	Iron	116-120	heme oxygenase 1	Homo sapiens	39-43
22619734-4	2012	Genetic studies have helped identify a number of proteins linking vitamin D to PD pathology, including the major histocompatibility complex (MHC) class II, the vitamin D receptor (VDR), cytochrome P450 2D6 (CYP2D6), chromosome 22, the renin-angiotensin system (RAS), heme oxygenase-1 (HO-1), poly(ADP-ribose) polymerase-1 gene (PARP-1), neurotrophic factor (NTF), and Sp1 transcription factor.	Vitamin D	66-75	heme oxygenase 1	Homo sapiens	267-283
22247601-0	2012	Okanin, a chalcone found in the genus Bidens, and 3-penten-2-one inhibit inducible nitric oxide synthase expression via heme oxygenase-1 induction in RAW264.7 macrophages activated with lipopolysaccharide.	okanin	0-6	heme oxygenase 1	Homo sapiens	120-136
22247601-0	2012	Okanin, a chalcone found in the genus Bidens, and 3-penten-2-one inhibit inducible nitric oxide synthase expression via heme oxygenase-1 induction in RAW264.7 macrophages activated with lipopolysaccharide.	3-PENTEN-2-ONE	50-64	heme oxygenase 1	Homo sapiens	120-136
22247601-2	2012	Heme oxygenase-1 expression via activation of nuclear factor-erythroid 2-related factor 2 inhibits nitric oxide production and inducible nitric oxide synthase expression in activated macrophages.	Nitric Oxide	99-111	heme oxygenase 1	Homo sapiens	0-16
22247601-4	2012	Here, we found that okanin (possessing the alpha-beta unsaturated carbonyl group) induced heme oxygenase-1 expression via nuclear factor-erythroid 2-related factor 2 activation in RAW264.7 macrophages.	okanin	20-26	heme oxygenase 1	Homo sapiens	90-106
22247601-5	2012	3-Penten-2-one, of which structure, as in okanin, possesses the alpha-beta unsaturated carbonyl group, also induced nuclear factor-erythroid 2-related factor 2-dependent heme oxygenase-1 expression, while both 2-pentanone (lacking a double bond) and 2-pentene (lacking a carbonyl group) were virtually inactive.	3-PENTEN-2-ONE	0-14	heme oxygenase 1	Homo sapiens	170-186
22247601-5	2012	3-Penten-2-one, of which structure, as in okanin, possesses the alpha-beta unsaturated carbonyl group, also induced nuclear factor-erythroid 2-related factor 2-dependent heme oxygenase-1 expression, while both 2-pentanone (lacking a double bond) and 2-pentene (lacking a carbonyl group) were virtually inactive.	okanin	42-48	heme oxygenase 1	Homo sapiens	170-186
22247601-6	2012	In lipopolysaccharide-activated RAW264.7 macrophages, both okanin and 3-penten-2-one inhibited nitric oxide production and inducible nitric oxide synthase expression via heme oxygenase-1 expression.	okanin	59-65	heme oxygenase 1	Homo sapiens	170-186
22247601-6	2012	In lipopolysaccharide-activated RAW264.7 macrophages, both okanin and 3-penten-2-one inhibited nitric oxide production and inducible nitric oxide synthase expression via heme oxygenase-1 expression.	3-PENTEN-2-ONE	70-84	heme oxygenase 1	Homo sapiens	170-186
22247601-7	2012	Collectively, our findings suggest that by virtue of its alpha-beta unsaturated carbonyl functional group, okanin can inhibit nitric oxide production and inducible nitric oxide synthase expression via nuclear factor-erythroid 2-related factor 2-dependent heme oxygenase-1 expression in lipopolysaccharide-activated macrophages.	okanin	107-113	heme oxygenase 1	Homo sapiens	255-271
22539869-0	2012	Curcumin protects retinal pigment epithelial cells against oxidative stress via induction of heme oxygenase-1 expression and reduction of reactive oxygen.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	93-109
22539869-1	2012	PURPOSE: To determine whether curcumin induces expression of the defensive enzyme heme oxygenase-1 (HO-1) and protects cells against oxidative stress in cultured human retinal pigment epithelial cells.	Curcumin	30-38	heme oxygenase 1	Homo sapiens	82-98
22539869-1	2012	PURPOSE: To determine whether curcumin induces expression of the defensive enzyme heme oxygenase-1 (HO-1) and protects cells against oxidative stress in cultured human retinal pigment epithelial cells.	Curcumin	30-38	heme oxygenase 1	Homo sapiens	100-104
22539869-5	2012	To confirm the protective role of HO-1 in oxidative stress, small interfering RNA (siRNA) against HO-1 or inhibitor of HO-1 was treated with curcumin in retinal pigment epithelium cells.	Curcumin	141-149	heme oxygenase 1	Homo sapiens	98-123
22539869-10	2012	Curcumin"s effect on the reduction of ROS was mediated by the increase in HO-1 expression.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	74-78
22539869-10	2012	Curcumin"s effect on the reduction of ROS was mediated by the increase in HO-1 expression.	Reactive Oxygen Species	38-41	heme oxygenase 1	Homo sapiens	74-78
22539869-11	2012	CONCLUSIONS: Curcumin upregulated the oxidative stress defense enzyme HO-1 and may protect human retinal pigment epithelial cells against oxidative stress by reducing ROS levels.	Curcumin	13-21	heme oxygenase 1	Homo sapiens	70-74
23071605-3	2012	In the present study we assessed effect of transgenic expression of human heme oxygenase-1 (hHO-1), an inducible protein capable of cytoprotection by scavenging reactive oxygen species and preventing apoptosis caused by cellular stress during inflammatory processes, in neonatal porcine islet-like cluster cells (NPCCs).	Reactive Oxygen Species	161-184	heme oxygenase 1	Homo sapiens	74-90
22246987-10	2012	Expression of Nrf2-dependent anti-oxidant genes including gamma-glutamylcysteine ligase, heme oxygenase-1, and quinone oxidoreductase were down-regulated in MCF-7/ADR cells, and Nrf2 overexpression partially decreased the susceptibility of ALA-hx PDT in MCF-7/ADR cells.	Aminolevulinic Acid	240-243	heme oxygenase 1	Homo sapiens	89-105
23209658-0	2012	Desipramine protects neuronal cell death and induces heme oxygenase-1 expression in Mes23.5 dopaminergic neurons.	Desipramine	0-11	heme oxygenase 1	Homo sapiens	53-69
23209658-6	2012	Desipramine induces endogenous anti-oxidative enzyme, heme oxygenase-1 (HO-1) protein and mRNA expression in concentration- and time-dependent manners.	Desipramine	0-11	heme oxygenase 1	Homo sapiens	54-70
23209658-6	2012	Desipramine induces endogenous anti-oxidative enzyme, heme oxygenase-1 (HO-1) protein and mRNA expression in concentration- and time-dependent manners.	Desipramine	0-11	heme oxygenase 1	Homo sapiens	72-76
23209658-7	2012	A different type of antidepressant SSRI (selective serotonin reuptake inhibitor), fluoxetine also shows similar effects of desipramine on HO-1 expression.	Fluoxetine	82-92	heme oxygenase 1	Homo sapiens	138-142
23209658-7	2012	A different type of antidepressant SSRI (selective serotonin reuptake inhibitor), fluoxetine also shows similar effects of desipramine on HO-1 expression.	Desipramine	123-134	heme oxygenase 1	Homo sapiens	138-142
23209658-8	2012	Moreover, desipramine induces HO-1 expression through activation of ERK and JNK signaling pathways.	Desipramine	10-21	heme oxygenase 1	Homo sapiens	30-34
23209658-10	2012	Moreover, desipramine-mediated increase of HO-1 expression is reduced by transfection with siRNA against Nrf2.	Desipramine	10-21	heme oxygenase 1	Homo sapiens	43-47
23209658-12	2012	Furthermore, inhibition of HO-1 activity by a HO-1 pharmacological inhibitor, ZnPP IX, attenuates the neuroprotective effect of desipramine.	zinc protoporphyrin	78-85	heme oxygenase 1	Homo sapiens	27-31
23209658-12	2012	Furthermore, inhibition of HO-1 activity by a HO-1 pharmacological inhibitor, ZnPP IX, attenuates the neuroprotective effect of desipramine.	zinc protoporphyrin	78-85	heme oxygenase 1	Homo sapiens	46-50
23209658-12	2012	Furthermore, inhibition of HO-1 activity by a HO-1 pharmacological inhibitor, ZnPP IX, attenuates the neuroprotective effect of desipramine.	Desipramine	128-139	heme oxygenase 1	Homo sapiens	27-31
23209658-12	2012	Furthermore, inhibition of HO-1 activity by a HO-1 pharmacological inhibitor, ZnPP IX, attenuates the neuroprotective effect of desipramine.	Desipramine	128-139	heme oxygenase 1	Homo sapiens	46-50
23209658-13	2012	Otherwise, activation of HO-1 activity by HO-1 activator and inducer protect 6-OHDA-induced neuronal death.	Oxidopamine	77-83	heme oxygenase 1	Homo sapiens	25-29
23209658-13	2012	Otherwise, activation of HO-1 activity by HO-1 activator and inducer protect 6-OHDA-induced neuronal death.	Oxidopamine	77-83	heme oxygenase 1	Homo sapiens	42-46
23209658-14	2012	CONCLUSIONS/SIGNIFICANCE: These findings suggest that desipramine-increased HO-1 expression is mediated by Nrf2 activation through the ERK and JNK signaling pathways.	Desipramine	54-65	heme oxygenase 1	Homo sapiens	76-80
23071605-3	2012	In the present study we assessed effect of transgenic expression of human heme oxygenase-1 (hHO-1), an inducible protein capable of cytoprotection by scavenging reactive oxygen species and preventing apoptosis caused by cellular stress during inflammatory processes, in neonatal porcine islet-like cluster cells (NPCCs).	Reactive Oxygen Species	161-184	heme oxygenase 1	Homo sapiens	92-97
23071605-4	2012	Transduction of NPCCs with adenovirus containing hHO-1 gene significantly reduced apoptosis compared with the GFP-expressing adenovirus control after treatment with either hydrogen peroxide or hTNF-alpha and cycloheximide.	Hydrogen Peroxide	172-189	heme oxygenase 1	Homo sapiens	49-54
23071605-4	2012	Transduction of NPCCs with adenovirus containing hHO-1 gene significantly reduced apoptosis compared with the GFP-expressing adenovirus control after treatment with either hydrogen peroxide or hTNF-alpha and cycloheximide.	Cycloheximide	208-221	heme oxygenase 1	Homo sapiens	49-54
23071605-5	2012	These protective effects were diminished by co-treatment of hHO-1 antagonist, Zinc protoporphyrin IX.	zinc protoporphyrin	78-100	heme oxygenase 1	Homo sapiens	60-65
23071605-9	2012	As expected, fibroblasts derived from the hHO-1 transgenic pigs were significantly resistant to both hydrogen peroxide damage and hTNF-alpha and cycloheximide-mediated apoptosis when compared with wild-type fibroblasts.	Hydrogen Peroxide	101-118	heme oxygenase 1	Homo sapiens	42-47
23071605-9	2012	As expected, fibroblasts derived from the hHO-1 transgenic pigs were significantly resistant to both hydrogen peroxide damage and hTNF-alpha and cycloheximide-mediated apoptosis when compared with wild-type fibroblasts.	Cycloheximide	145-158	heme oxygenase 1	Homo sapiens	42-47
22514698-5	2012	Inhibition of HO-1 by zinc protoporphyrin IX (ZnPP) sensitized both cell types to the cytotoxicity of chemotherapeutic agents.	zinc protoporphyrin	22-44	heme oxygenase 1	Homo sapiens	14-18
22848562-0	2012	Induction of heme oxygenase-1 inhibits cell death in crotonaldehyde-stimulated HepG2 cells via the PKC-delta-p38-Nrf2 pathway.	2-butenal	53-67	heme oxygenase 1	Homo sapiens	13-29
22848562-5	2012	The aim of this study was to examine the effects of HO-1 induction on cell survival in crotonaldehyde-stimulated human hepatocellular carcinoma (HepG2) cells.	2-butenal	87-101	heme oxygenase 1	Homo sapiens	52-56
22848562-6	2012	METHODS: To investigate the signaling pathway involved in crotonaldehyde-induced HO-1 expression, we compared levels of inhibition efficiency of specific inhibitors and specific small interfering RNAs (siRNAs) of several kinases.	2-butenal	58-72	heme oxygenase 1	Homo sapiens	81-85
22848562-9	2012	Treatment with inhibitors of the protein kinase C-delta (PKC-delta) and p38 pathways resulted in obvious blockage of crotonaldehyde-induced HO-1 expression.	2-butenal	117-131	heme oxygenase 1	Homo sapiens	140-144
22848562-10	2012	Furthermore, treatment with HO-1 siRNA and the specific HO-1 inhibitor zinc-protoporphyrin produced an increase in the G(0)/G(1) phase of the cell cycle in crotonaldehyde-stimulated HepG2 cells.	protoporphyrin IX	76-90	heme oxygenase 1	Homo sapiens	28-32
22848562-10	2012	Furthermore, treatment with HO-1 siRNA and the specific HO-1 inhibitor zinc-protoporphyrin produced an increase in the G(0)/G(1) phase of the cell cycle in crotonaldehyde-stimulated HepG2 cells.	protoporphyrin IX	76-90	heme oxygenase 1	Homo sapiens	56-60
22848562-10	2012	Furthermore, treatment with HO-1 siRNA and the specific HO-1 inhibitor zinc-protoporphyrin produced an increase in the G(0)/G(1) phase of the cell cycle in crotonaldehyde-stimulated HepG2 cells.	2-butenal	156-170	heme oxygenase 1	Homo sapiens	28-32
22848562-10	2012	Furthermore, treatment with HO-1 siRNA and the specific HO-1 inhibitor zinc-protoporphyrin produced an increase in the G(0)/G(1) phase of the cell cycle in crotonaldehyde-stimulated HepG2 cells.	2-butenal	156-170	heme oxygenase 1	Homo sapiens	56-60
22848562-11	2012	CONCLUSIONS: Taken together, the results support an anti-apoptotic role for HO-1 in crotonaldehyde-stimulated human hepatocellular carcinoma cells and provide a mechanism by which induction of HO-1 expression via PKC-delta-p38 MAPK-Nrf2 pathway may promote tumor resistance to oxidative stress.	2-butenal	84-98	heme oxygenase 1	Homo sapiens	76-80
22848562-11	2012	CONCLUSIONS: Taken together, the results support an anti-apoptotic role for HO-1 in crotonaldehyde-stimulated human hepatocellular carcinoma cells and provide a mechanism by which induction of HO-1 expression via PKC-delta-p38 MAPK-Nrf2 pathway may promote tumor resistance to oxidative stress.	2-butenal	84-98	heme oxygenase 1	Homo sapiens	193-197
22514698-5	2012	Inhibition of HO-1 by zinc protoporphyrin IX (ZnPP) sensitized both cell types to the cytotoxicity of chemotherapeutic agents.	zinc protoporphyrin	46-50	heme oxygenase 1	Homo sapiens	14-18
22514698-7	2012	Induction of HO-1 protein expression by stannous chloride enhanced the cytoprotection and suppression of apoptosis caused by anticancer agents.	stannous chloride	40-57	heme oxygenase 1	Homo sapiens	13-17
22272327-6	2012	In HUVECs exposed to smokers" serum but not to non-smokers" serum we found that oxidative stress increased, whereas nitric oxide and GSH concentrations decreased; interestingly the expression of Nrf2, of heme oxygenase-1 (HO-1) and of glutamate-cysteine ligase catalytic (GCLC) subunit, the rate-limiting step of synthesis of GSH, was decreased.	Nitric Oxide	116-128	heme oxygenase 1	Homo sapiens	204-220
22457802-2	2012	The inducible form of the enzyme heme oxygenase, HO-1, which conducts heme degradation, is absent in erythroblasts where hemoglobin (Hb) is synthesized.	Heme	33-37	heme oxygenase 1	Homo sapiens	49-53
22457802-3	2012	Yet, the central macrophage, which retains high HO-1 activity, might be suitable to take over degradation of extra, harmful, Hb heme.	Heme	128-132	heme oxygenase 1	Homo sapiens	48-52
22879979-0	2012	Heme oxygenase-1 protects retinal endothelial cells against high glucose- and oxidative/nitrosative stress-induced toxicity.	Glucose	65-72	heme oxygenase 1	Homo sapiens	0-16
22879979-10	2012	However, a short-time exposure (24 h) to elevated glucose did not alter cell viability, but increased both the levels of intracellular ROS and HO-1 content.	Glucose	50-57	heme oxygenase 1	Homo sapiens	143-147
22879979-11	2012	Moreover, the inhibition of HO with SnPPIX unmasked the toxic effect of high glucose and revealed the protection conferred by HO-1.	tin protoporphyrin IX	36-42	heme oxygenase 1	Homo sapiens	126-130
22272327-6	2012	In HUVECs exposed to smokers" serum but not to non-smokers" serum we found that oxidative stress increased, whereas nitric oxide and GSH concentrations decreased; interestingly the expression of Nrf2, of heme oxygenase-1 (HO-1) and of glutamate-cysteine ligase catalytic (GCLC) subunit, the rate-limiting step of synthesis of GSH, was decreased.	Glutathione	326-329	heme oxygenase 1	Homo sapiens	204-220
22879979-16	2012	Overexpression of HO-1 prevented the toxic effect induced by H(2)O(2) and NOC-18.	Water	61-66	heme oxygenase 1	Homo sapiens	18-22
22272327-6	2012	In HUVECs exposed to smokers" serum but not to non-smokers" serum we found that oxidative stress increased, whereas nitric oxide and GSH concentrations decreased; interestingly the expression of Nrf2, of heme oxygenase-1 (HO-1) and of glutamate-cysteine ligase catalytic (GCLC) subunit, the rate-limiting step of synthesis of GSH, was decreased.	Glutathione	326-329	heme oxygenase 1	Homo sapiens	222-226
22438807-1	2012	Heme oxygenase 1 (HO-1) is an essential enzyme induced by heme and multiple stimuli associated with critical illness.	Heme	58-62	heme oxygenase 1	Homo sapiens	0-16
22438807-1	2012	Heme oxygenase 1 (HO-1) is an essential enzyme induced by heme and multiple stimuli associated with critical illness.	Heme	58-62	heme oxygenase 1	Homo sapiens	18-22
22438807-6	2012	Neutrophils were the main HO-1-expressing cells in peripheral blood, and HMOX1 mRNA expression was upregulated by heme-moieties of lysed erythrocytes.	Heme	114-118	heme oxygenase 1	Homo sapiens	73-78
22036727-6	2012	The role of HO-1 in cytoprotection against nano-Ag was reinforced by results using pharmacological inducer of HO-1: cobalt protoporphyrin-mediated HO-1 activation in the NRF2i cells prevented nano-Ag-mediated cell death.	cobaltiprotoporphyrin	116-137	heme oxygenase 1	Homo sapiens	12-16
22036727-6	2012	The role of HO-1 in cytoprotection against nano-Ag was reinforced by results using pharmacological inducer of HO-1: cobalt protoporphyrin-mediated HO-1 activation in the NRF2i cells prevented nano-Ag-mediated cell death.	cobaltiprotoporphyrin	116-137	heme oxygenase 1	Homo sapiens	110-114
22036727-6	2012	The role of HO-1 in cytoprotection against nano-Ag was reinforced by results using pharmacological inducer of HO-1: cobalt protoporphyrin-mediated HO-1 activation in the NRF2i cells prevented nano-Ag-mediated cell death.	cobaltiprotoporphyrin	116-137	heme oxygenase 1	Homo sapiens	110-114
21833623-7	2011	Our results indicated that HO-1 counteracts oxidative imbalance reducing ROS levels.	ros	73-76	heme oxygenase 1	Homo sapiens	27-31
22001321-11	2011	Inhibitor of HO-1 activity, tin protoporphyrin IX, further increased HA-mediated reactivation of HIV-1 "mini-virus" in Jurkat clones, and this effect was also inhibited by N-acetyl cysteine.	tin protoporphyrin IX	28-49	heme oxygenase 1	Homo sapiens	13-17
21910007-1	2011	Treatment of melanoma cells by sodium arsenite or statins (simvastatin and lovastatin) dramatically modified activities of the main cell signaling pathways resulting in the induction of heme oxygenase-1 (HO-1) and in a downregulation of cyclooxygenase-2 (COX-2) protein levels.	sodium arsenite	31-46	heme oxygenase 1	Homo sapiens	186-202
21910007-1	2011	Treatment of melanoma cells by sodium arsenite or statins (simvastatin and lovastatin) dramatically modified activities of the main cell signaling pathways resulting in the induction of heme oxygenase-1 (HO-1) and in a downregulation of cyclooxygenase-2 (COX-2) protein levels.	sodium arsenite	31-46	heme oxygenase 1	Homo sapiens	204-208
21910007-1	2011	Treatment of melanoma cells by sodium arsenite or statins (simvastatin and lovastatin) dramatically modified activities of the main cell signaling pathways resulting in the induction of heme oxygenase-1 (HO-1) and in a downregulation of cyclooxygenase-2 (COX-2) protein levels.	Simvastatin	59-70	heme oxygenase 1	Homo sapiens	186-202
21910007-1	2011	Treatment of melanoma cells by sodium arsenite or statins (simvastatin and lovastatin) dramatically modified activities of the main cell signaling pathways resulting in the induction of heme oxygenase-1 (HO-1) and in a downregulation of cyclooxygenase-2 (COX-2) protein levels.	Simvastatin	59-70	heme oxygenase 1	Homo sapiens	204-208
21910007-1	2011	Treatment of melanoma cells by sodium arsenite or statins (simvastatin and lovastatin) dramatically modified activities of the main cell signaling pathways resulting in the induction of heme oxygenase-1 (HO-1) and in a downregulation of cyclooxygenase-2 (COX-2) protein levels.	Lovastatin	75-85	heme oxygenase 1	Homo sapiens	186-202
21910007-1	2011	Treatment of melanoma cells by sodium arsenite or statins (simvastatin and lovastatin) dramatically modified activities of the main cell signaling pathways resulting in the induction of heme oxygenase-1 (HO-1) and in a downregulation of cyclooxygenase-2 (COX-2) protein levels.	Lovastatin	75-85	heme oxygenase 1	Homo sapiens	204-208
21910007-4	2011	We demonstrated in the present study that treatment by sodium arsenite or statins with an additional inhibition of HO-1 expression (or activation) caused a substantial upregulation of apoptosis in melanoma cells.	sodium arsenite	55-70	heme oxygenase 1	Homo sapiens	115-119
21910007-2	2011	Through heme degradation and the production of carbon monoxide and biliverdin, HO-1 plays a protective role in different scenario of oxidative stress followed by mitochondrial apoptosis.	Carbon Monoxide	47-62	heme oxygenase 1	Homo sapiens	79-83
22001321-11	2011	Inhibitor of HO-1 activity, tin protoporphyrin IX, further increased HA-mediated reactivation of HIV-1 "mini-virus" in Jurkat clones, and this effect was also inhibited by N-acetyl cysteine.	Acetylcysteine	172-189	heme oxygenase 1	Homo sapiens	13-17
21910007-2	2011	Through heme degradation and the production of carbon monoxide and biliverdin, HO-1 plays a protective role in different scenario of oxidative stress followed by mitochondrial apoptosis.	Biliverdine	67-77	heme oxygenase 1	Homo sapiens	79-83
21945498-0	2011	Association of heme oxygenase-1 GT-repeat polymorphism with blood pressure phenotypes and its relevance to future cardiovascular mortality risk: an observation based on arsenic-exposed individuals.	Arsenic	169-176	heme oxygenase 1	Homo sapiens	15-31
21840000-2	2011	As statins can stimulate heme oxygenase-1 (HO-1), which increases bilirubin production, we investigated whether statins in routine use increase total bilirubin levels in subjects at high cardiovascular risk.	Bilirubin	66-75	heme oxygenase 1	Homo sapiens	25-41
21917385-2	2011	Induction of heme oxygenase-1 (HO-1) in lymphocytes has a similar effect, and it is not likely to be accidental that a key product of HO-1 activity, biliverdin, is homologous to the structure of phycocyanin"s chromophore phycocyanobilin (PhyCB).	Biliverdine	149-159	heme oxygenase 1	Homo sapiens	134-138
22466441-0	2011	Ferulic acid induces heme oxygenase-1 via activation of ERK and Nrf2.	ferulic acid	0-12	heme oxygenase 1	Homo sapiens	21-37
22466441-1	2011	This study investigated the effect of ferulic acid (FA) on the up-regulation of heme oxygenase-1 (HO-1) in lymphocytes and the molecular mechanisms involved.	ferulic acid	38-50	heme oxygenase 1	Homo sapiens	80-96
22466441-1	2011	This study investigated the effect of ferulic acid (FA) on the up-regulation of heme oxygenase-1 (HO-1) in lymphocytes and the molecular mechanisms involved.	ferulic acid	38-50	heme oxygenase 1	Homo sapiens	98-102
22466441-6	2011	In addition, lymphocytes treated with FA exhibited activation of extracellular regulated kinase (ERK) and treatments with U0126 (an ERK kinase inhibitor) attenuated the FA induced activation of Nrf2, resulting in a decrease in HO-1 expression.	U 0126	122-127	heme oxygenase 1	Homo sapiens	227-231
22466441-7	2011	Zinc protoporphyrin (ZnPP, a HO-1 inhibitor) markedly suppressed cytoprotection from radiation-induced cell damage by FA.	zinc protoporphyrin	0-19	heme oxygenase 1	Homo sapiens	29-33
22466441-7	2011	Zinc protoporphyrin (ZnPP, a HO-1 inhibitor) markedly suppressed cytoprotection from radiation-induced cell damage by FA.	zinc protoporphyrin	21-25	heme oxygenase 1	Homo sapiens	29-33
21982894-1	2011	Heme oxygenase 1 (HO-1) is a stress-inducible enzyme that degrades redox-active heme-producing biliverdin, carbon monoxide, and Fe(2+).	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	0-22
21982894-1	2011	Heme oxygenase 1 (HO-1) is a stress-inducible enzyme that degrades redox-active heme-producing biliverdin, carbon monoxide, and Fe(2+).	Carbon Monoxide	107-122	heme oxygenase 1	Homo sapiens	0-22
21982894-1	2011	Heme oxygenase 1 (HO-1) is a stress-inducible enzyme that degrades redox-active heme-producing biliverdin, carbon monoxide, and Fe(2+).	ammonium ferrous sulfate	128-134	heme oxygenase 1	Homo sapiens	0-22
21982894-7	2011	Oligonucleotides mimicking miR-155 efficiently inhibited BACH1 protein translation, resulting in a concentration-dependent increase in HMOX1 mRNA and protein expression in human umbilical vein endothelial cells.	Oligonucleotides	0-16	heme oxygenase 1	Homo sapiens	135-140
21321939-7	2011	Consistently, overexpression of HO-1 attenuated EV71-induced NADPH oxidase/ROS generation and EV71 replication which were abrogated by pretreatment with an HO-1 inhibitor, zinc protoporphyrin IX (ZnPP IX).	Reactive Oxygen Species	75-78	heme oxygenase 1	Homo sapiens	32-36
21321939-7	2011	Consistently, overexpression of HO-1 attenuated EV71-induced NADPH oxidase/ROS generation and EV71 replication which were abrogated by pretreatment with an HO-1 inhibitor, zinc protoporphyrin IX (ZnPP IX).	Reactive Oxygen Species	75-78	heme oxygenase 1	Homo sapiens	156-160
21321939-7	2011	Consistently, overexpression of HO-1 attenuated EV71-induced NADPH oxidase/ROS generation and EV71 replication which were abrogated by pretreatment with an HO-1 inhibitor, zinc protoporphyrin IX (ZnPP IX).	zinc protoporphyrin	172-194	heme oxygenase 1	Homo sapiens	32-36
21321939-7	2011	Consistently, overexpression of HO-1 attenuated EV71-induced NADPH oxidase/ROS generation and EV71 replication which were abrogated by pretreatment with an HO-1 inhibitor, zinc protoporphyrin IX (ZnPP IX).	zinc protoporphyrin	196-203	heme oxygenase 1	Homo sapiens	32-36
21321939-8	2011	Moreover, metabolite of HO-1, carbon monoxide (CO), also diminished ROS formation and EV71 replication which were reversed by pretreatment with a CO scavenger (hemoglobin) and a cyclic GMP-dependent protein kinase (PKG) inhibitor (KT5823).	Carbon Monoxide	30-45	heme oxygenase 1	Homo sapiens	24-28
21321939-8	2011	Moreover, metabolite of HO-1, carbon monoxide (CO), also diminished ROS formation and EV71 replication which were reversed by pretreatment with a CO scavenger (hemoglobin) and a cyclic GMP-dependent protein kinase (PKG) inhibitor (KT5823).	Carbon Monoxide	47-49	heme oxygenase 1	Homo sapiens	24-28
21321939-8	2011	Moreover, metabolite of HO-1, carbon monoxide (CO), also diminished ROS formation and EV71 replication which were reversed by pretreatment with a CO scavenger (hemoglobin) and a cyclic GMP-dependent protein kinase (PKG) inhibitor (KT5823).	Reactive Oxygen Species	68-71	heme oxygenase 1	Homo sapiens	24-28
21917385-4	2011	These considerations suggest that bilirubin, generated within lymphocytes by HO-1 activation, may play a physiological role in the promotion of Treg immunomodulation.	Bilirubin	34-43	heme oxygenase 1	Homo sapiens	77-81
21917385-5	2011	This effect of bilirubin is likely to be independent of NADPH oxidase inhibition, since the NAPDH oxidase activity of macrophages is necessary for Treg induction, possibly because it contributes to HO-1 induction in lymphocytes.	Bilirubin	15-24	heme oxygenase 1	Homo sapiens	198-202
21963524-0	2011	Manganese potentiates LPS-induced heme-oxygenase 1 in microglia but not dopaminergic cells: role in controlling microglial hydrogen peroxide and inflammatory cytokine output.	Manganese	0-9	heme oxygenase 1	Homo sapiens	34-50
21910986-5	2011	Pretreatment with the HO-1 inhibitor, tin protoporphyrin (SnPP), attenuated the inhibitory activities of LA on LPS-induced inflammatory NO, PGE(2), IL-1beta, TNF-alpha, IL-6 and IL-12 production.	tin protoporphyrin IX	38-56	heme oxygenase 1	Homo sapiens	22-26
21910986-5	2011	Pretreatment with the HO-1 inhibitor, tin protoporphyrin (SnPP), attenuated the inhibitory activities of LA on LPS-induced inflammatory NO, PGE(2), IL-1beta, TNF-alpha, IL-6 and IL-12 production.	S-Nitroso-N-propionyl-D,L-penicillamine	58-62	heme oxygenase 1	Homo sapiens	22-26
21910986-5	2011	Pretreatment with the HO-1 inhibitor, tin protoporphyrin (SnPP), attenuated the inhibitory activities of LA on LPS-induced inflammatory NO, PGE(2), IL-1beta, TNF-alpha, IL-6 and IL-12 production.	Prostaglandins E	140-143	heme oxygenase 1	Homo sapiens	22-26
21925249-0	2011	Simvastatin inhibits pro-inflammatory mediators through induction of heme oxygenase-1 expression in lipopolysaccharide-stimulated RAW264.7 macrophages.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	69-85
21925249-3	2011	Here, the possibility that HO-1 is involved in the anti-inflammatory action of simvastatin, using lipopolysaccharide (LPS)-stimulated RAW264.7 macrophages as a model system has been specifically addressed.	Simvastatin	79-90	heme oxygenase 1	Homo sapiens	27-31
21925249-4	2011	Our results demonstrated that in the presence of LPS, simvastatin significantly increased HO-1 expression and activity in a dose-dependent manner compared to that of LPS-stimulated alone macrophages.	Simvastatin	54-65	heme oxygenase 1	Homo sapiens	90-94
21925249-7	2011	However, these anti-inflammatory activities of simvastatin were markedly reversed by addition of a HO-1 inhibitor zinc protoporphyrin (ZnPP).	Simvastatin	47-58	heme oxygenase 1	Homo sapiens	99-103
21925249-7	2011	However, these anti-inflammatory activities of simvastatin were markedly reversed by addition of a HO-1 inhibitor zinc protoporphyrin (ZnPP).	zinc protoporphyrin	114-133	heme oxygenase 1	Homo sapiens	99-103
21925249-7	2011	However, these anti-inflammatory activities of simvastatin were markedly reversed by addition of a HO-1 inhibitor zinc protoporphyrin (ZnPP).	zinc protoporphyrin	135-139	heme oxygenase 1	Homo sapiens	99-103
21925249-8	2011	Accordingly, the present results indicate that the anti-inflammatory activity of simvastatin could, at least in part, be regulated by induction of HO-1-mediated processes.	Simvastatin	81-92	heme oxygenase 1	Homo sapiens	147-151
21910986-0	2011	Anti-inflammatory effects of lindenenyl acetate via heme oxygenase-1 and AMPK in human periodontal ligament cells.	lindenenyl acetate	29-47	heme oxygenase 1	Homo sapiens	52-68
21552291-8	2011	Although p53 and its classical targets such as p21 and Mdm2 are activated by both H(2)O(2) and CDDP, we found that the expression of haeme-oxygenase-1 (HO-1)-an antioxidant and antiapoptotic protein-was directly induced only upon H(2)O(2) treatment in a p53-dependent manner.	Hydrogen Peroxide	82-90	heme oxygenase 1	Homo sapiens	152-156
21552291-11	2011	Finally, H(2)O(2)-mediated cell death was rescued significantly in p53-deficient cells by antioxidant treatment, as well as by bilirubin, a by-product of HO-1 metabolism.	Bilirubin	127-136	heme oxygenase 1	Homo sapiens	154-158
21600248-3	2011	We found SMA-ZnPP showed higher and more efficient (about 2.5 times) intracellular uptake rate than PEG-ZnPP, although both SMA-ZnPP and PEG-ZnPP micelles were localized at endoplasmic reticulum (ER) and inhibited the target enzyme heme oxygenase 1 (HO-1) similarly.	peg-znpp	100-108	heme oxygenase 1	Homo sapiens	232-248
21552291-8	2011	Although p53 and its classical targets such as p21 and Mdm2 are activated by both H(2)O(2) and CDDP, we found that the expression of haeme-oxygenase-1 (HO-1)-an antioxidant and antiapoptotic protein-was directly induced only upon H(2)O(2) treatment in a p53-dependent manner.	Cisplatin	95-99	heme oxygenase 1	Homo sapiens	152-156
21552291-8	2011	Although p53 and its classical targets such as p21 and Mdm2 are activated by both H(2)O(2) and CDDP, we found that the expression of haeme-oxygenase-1 (HO-1)-an antioxidant and antiapoptotic protein-was directly induced only upon H(2)O(2) treatment in a p53-dependent manner.	Hydrogen Peroxide	230-238	heme oxygenase 1	Homo sapiens	133-150
21552291-8	2011	Although p53 and its classical targets such as p21 and Mdm2 are activated by both H(2)O(2) and CDDP, we found that the expression of haeme-oxygenase-1 (HO-1)-an antioxidant and antiapoptotic protein-was directly induced only upon H(2)O(2) treatment in a p53-dependent manner.	Hydrogen Peroxide	230-238	heme oxygenase 1	Homo sapiens	152-156
21552291-11	2011	Finally, H(2)O(2)-mediated cell death was rescued significantly in p53-deficient cells by antioxidant treatment, as well as by bilirubin, a by-product of HO-1 metabolism.	Hydrogen Peroxide	9-17	heme oxygenase 1	Homo sapiens	154-158
22118543-0	2011	Dimethylsulfoxide (DMSO) induces downregulation of heme oxygenase-1 (HO-1) in HL-60 cells: involvement of HO-1 in HL-60 cell differentiation.	Dimethyl Sulfoxide	0-17	heme oxygenase 1	Homo sapiens	51-67
21868703-0	2011	Heme induces heme oxygenase 1 via Nrf2: role in the homeostatic macrophage response to intraplaque hemorrhage.	Heme	0-4	heme oxygenase 1	Homo sapiens	13-29
21868703-7	2011	Challenge of macrophages with purified heme provoked nuclear translocation of Nrf2, and Nrf2 small interfering RNA resulted in significant inhibition of the ability of heme to induce HO-1 protein.	Heme	39-43	heme oxygenase 1	Homo sapiens	183-187
21868703-7	2011	Challenge of macrophages with purified heme provoked nuclear translocation of Nrf2, and Nrf2 small interfering RNA resulted in significant inhibition of the ability of heme to induce HO-1 protein.	Heme	168-172	heme oxygenase 1	Homo sapiens	183-187
21868703-9	2011	However, an inducible protein transactivator is also probably necessary, as heme-induced HO-1 mRNA expression was fully inhibited by the protein synthesis inhibitor cycloheximide.	Cycloheximide	165-178	heme oxygenase 1	Homo sapiens	89-93
22118543-3	2011	Dimethyl sulfoxide (DMSO) completely decreased HO-1 expression in a time-dependent manner, but clearly induced HL-60 cell differentiation, as evidenced by a marked increase in CD11b expression.	Dimethyl Sulfoxide	20-24	heme oxygenase 1	Homo sapiens	47-51
22118543-0	2011	Dimethylsulfoxide (DMSO) induces downregulation of heme oxygenase-1 (HO-1) in HL-60 cells: involvement of HO-1 in HL-60 cell differentiation.	Dimethyl Sulfoxide	0-17	heme oxygenase 1	Homo sapiens	69-73
22118543-4	2011	Interestingly, zinc protoporphyrin (ZnPP), a strong inhibitor of HO-1, induced HL-60 cell differentiation.	zinc protoporphyrin	15-34	heme oxygenase 1	Homo sapiens	65-69
22118543-4	2011	Interestingly, zinc protoporphyrin (ZnPP), a strong inhibitor of HO-1, induced HL-60 cell differentiation.	zinc protoporphyrin	36-40	heme oxygenase 1	Homo sapiens	65-69
22118543-0	2011	Dimethylsulfoxide (DMSO) induces downregulation of heme oxygenase-1 (HO-1) in HL-60 cells: involvement of HO-1 in HL-60 cell differentiation.	Dimethyl Sulfoxide	0-17	heme oxygenase 1	Homo sapiens	106-110
22118543-5	2011	In contrast, treatment with cobalt protoporphyrin (CoPP), an activator of HO-1, decreased CD11b expression.	cobaltiprotoporphyrin	28-49	heme oxygenase 1	Homo sapiens	74-78
22118543-5	2011	In contrast, treatment with cobalt protoporphyrin (CoPP), an activator of HO-1, decreased CD11b expression.	cobaltiprotoporphyrin	51-55	heme oxygenase 1	Homo sapiens	74-78
22118543-6	2011	Additionally, ZnPP downregulated HO-1 protein expression in HL-60 cells, whereas CoPP induced upregulation.	zinc protoporphyrin	14-18	heme oxygenase 1	Homo sapiens	33-37
22118543-7	2011	These results suggest that HO-1 might have a negative function in DMSO-induced HL-60 cell differentiation.	Dimethyl Sulfoxide	66-70	heme oxygenase 1	Homo sapiens	27-31
22118543-8	2011	This study provides the first evidence that HO-1 plays an important role in DMSO-induced HL-60 cell differentiation.	Dimethyl Sulfoxide	76-80	heme oxygenase 1	Homo sapiens	44-48
22118543-0	2011	Dimethylsulfoxide (DMSO) induces downregulation of heme oxygenase-1 (HO-1) in HL-60 cells: involvement of HO-1 in HL-60 cell differentiation.	Dimethyl Sulfoxide	19-23	heme oxygenase 1	Homo sapiens	51-67
22118543-0	2011	Dimethylsulfoxide (DMSO) induces downregulation of heme oxygenase-1 (HO-1) in HL-60 cells: involvement of HO-1 in HL-60 cell differentiation.	Dimethyl Sulfoxide	19-23	heme oxygenase 1	Homo sapiens	69-73
22118543-0	2011	Dimethylsulfoxide (DMSO) induces downregulation of heme oxygenase-1 (HO-1) in HL-60 cells: involvement of HO-1 in HL-60 cell differentiation.	Dimethyl Sulfoxide	19-23	heme oxygenase 1	Homo sapiens	106-110
22118543-3	2011	Dimethyl sulfoxide (DMSO) completely decreased HO-1 expression in a time-dependent manner, but clearly induced HL-60 cell differentiation, as evidenced by a marked increase in CD11b expression.	Dimethyl Sulfoxide	0-18	heme oxygenase 1	Homo sapiens	47-51
21840424-4	2011	We first observed that alpha-iso-cubebenol induced HO-1 mRNA and protein expression in a dose- and time-dependent manner via activation of erythroid-specific nuclear factor-regulated factor 2 (Nrf2).	alpha-iso-cubebenol	23-42	heme oxygenase 1	Homo sapiens	51-55
21750082-5	2011	RESULTS: In beta-thalassemia the increased production of reactive oxygen species was associated with down-regulation of heme oxygenase-1 and biliverdin reductase and up-regulation of peroxiredoxin-2.	Reactive Oxygen Species	57-80	heme oxygenase 1	Homo sapiens	120-136
21840424-7	2011	These results suggested that alpha-iso-cubebenol induced HO-1 expression through the activation of PI3K/Akt, ERK, and Nrf2 signaling.	alpha-iso-cubebenol	29-48	heme oxygenase 1	Homo sapiens	57-61
21840424-10	2011	Additionally, treatment with tin-protoporphyrin (SnPP), a selective inhibitor of HO-1, reversed the alpha-iso-cubebenol-mediated inhibition of P. gingivalis LPS-induced pro-inflammatory cytokines.	tin protoporphyrin IX	29-47	heme oxygenase 1	Homo sapiens	81-85
21840424-10	2011	Additionally, treatment with tin-protoporphyrin (SnPP), a selective inhibitor of HO-1, reversed the alpha-iso-cubebenol-mediated inhibition of P. gingivalis LPS-induced pro-inflammatory cytokines.	S-Nitroso-N-propionyl-D,L-penicillamine	49-53	heme oxygenase 1	Homo sapiens	81-85
21725585-1	2011	Cobalt protoporphyrin (CoPP) is a potent and effective metalloporphyrin inducer of heme oxygenase-1 (HO-1) activity in many tissues.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	83-99
21840424-10	2011	Additionally, treatment with tin-protoporphyrin (SnPP), a selective inhibitor of HO-1, reversed the alpha-iso-cubebenol-mediated inhibition of P. gingivalis LPS-induced pro-inflammatory cytokines.	alpha-iso-cubebenol	100-119	heme oxygenase 1	Homo sapiens	81-85
21725585-1	2011	Cobalt protoporphyrin (CoPP) is a potent and effective metalloporphyrin inducer of heme oxygenase-1 (HO-1) activity in many tissues.	cobaltiprotoporphyrin	23-27	heme oxygenase 1	Homo sapiens	83-99
21840424-11	2011	Hence, alpha-iso-cubebenol might induce anti-inflammatory effects on P. gingivalis LPS-stimulated human THP-1 macrophages by mediating the activation of PI3k/Akt and ERK that leads to over-expression of HO-1 and Nrf-2.	alpha-iso-cubebenol	7-26	heme oxygenase 1	Homo sapiens	203-207
21725585-1	2011	Cobalt protoporphyrin (CoPP) is a potent and effective metalloporphyrin inducer of heme oxygenase-1 (HO-1) activity in many tissues.	Metalloporphyrins	55-71	heme oxygenase 1	Homo sapiens	83-99
22065904-9	2011	Knockdown of Nrf2 with siRNA attenuated SFN-induced heme oxygenase-1 (HO-1) up-regulation.	sulforaphane	40-43	heme oxygenase 1	Homo sapiens	52-68
22168142-2	2011	Heme oxygenase-1 (HO-1) and its derivatives have anti-apoptotic, anti-inflammatory effects and protect against reactive oxygen species, rendering HO-1 a promising molecule to control AVR.	Reactive Oxygen Species	111-134	heme oxygenase 1	Homo sapiens	0-16
21735318-6	2011	In addition, we show that combined dopamine and paraquat treatment increases the expression of heme oxygenase-1, an antioxidant response protein.	Dopamine	35-43	heme oxygenase 1	Homo sapiens	95-111
21735318-6	2011	In addition, we show that combined dopamine and paraquat treatment increases the expression of heme oxygenase-1, an antioxidant response protein.	Paraquat	48-56	heme oxygenase 1	Homo sapiens	95-111
22168142-2	2011	Heme oxygenase-1 (HO-1) and its derivatives have anti-apoptotic, anti-inflammatory effects and protect against reactive oxygen species, rendering HO-1 a promising molecule to control AVR.	Reactive Oxygen Species	111-134	heme oxygenase 1	Homo sapiens	18-22
21911884-3	2011	The (GT)n and (TA)n dinucleotide variations in HMOX1 and UGT1A1 gene promoters, respectively, were determined by fragment analysis in all subjects.	Dinucleoside Phosphates	20-32	heme oxygenase 1	Homo sapiens	47-52
22168142-11	2011	These effects could be abrogated by the incubation of transgenic PAECs with the specific HO-1 inhibitor zinc protoporphorine IX (Zn(II)PPIX, 20 mum).	zinc protoporphorine ix	104-127	heme oxygenase 1	Homo sapiens	89-93
22168142-11	2011	These effects could be abrogated by the incubation of transgenic PAECs with the specific HO-1 inhibitor zinc protoporphorine IX (Zn(II)PPIX, 20 mum).	zn(ii)ppix	129-139	heme oxygenase 1	Homo sapiens	89-93
22090784-1	2011	Heme oxygenase-1 (HO-1) system catalyzes heme to biologically active products: carbon monoxide, biliverdin/bilirubin and free iron.	Carbon Monoxide	79-94	heme oxygenase 1	Homo sapiens	0-16
22090784-1	2011	Heme oxygenase-1 (HO-1) system catalyzes heme to biologically active products: carbon monoxide, biliverdin/bilirubin and free iron.	Biliverdine	96-106	heme oxygenase 1	Homo sapiens	0-16
22090784-1	2011	Heme oxygenase-1 (HO-1) system catalyzes heme to biologically active products: carbon monoxide, biliverdin/bilirubin and free iron.	Bilirubin	107-116	heme oxygenase 1	Homo sapiens	0-16
22090784-1	2011	Heme oxygenase-1 (HO-1) system catalyzes heme to biologically active products: carbon monoxide, biliverdin/bilirubin and free iron.	Iron	126-130	heme oxygenase 1	Homo sapiens	0-16
21380847-6	2011	Furthermore, our results show that the hormetic effects of low levels of curcumin are achieved by virtue of it being a hormetin in terms of the induction of stress response pathways, including Nrf2 and HO-1 in human cells.	Curcumin	73-81	heme oxygenase 1	Homo sapiens	202-206
21091076-3	2011	By degrading the oxidant heme and generating the antioxidant bilirubin and anti-inflammatory molecule carbon monoxide, HO-1 may protect cell from injury due to oxidative and pathological stress.	Heme	25-29	heme oxygenase 1	Homo sapiens	119-123
21091076-3	2011	By degrading the oxidant heme and generating the antioxidant bilirubin and anti-inflammatory molecule carbon monoxide, HO-1 may protect cell from injury due to oxidative and pathological stress.	Bilirubin	61-70	heme oxygenase 1	Homo sapiens	119-123
21091076-3	2011	By degrading the oxidant heme and generating the antioxidant bilirubin and anti-inflammatory molecule carbon monoxide, HO-1 may protect cell from injury due to oxidative and pathological stress.	Carbon Monoxide	102-117	heme oxygenase 1	Homo sapiens	119-123
21950555-8	2011	Inhibitor of HO-1, Znpp, can increase the radiosensitivity of human NSCLC A549 cells.	zinc protoporphyrin	19-23	heme oxygenase 1	Homo sapiens	13-17
21844097-2	2011	Pentaerithrityl tetranitrate (PETN) is an organic nitrate with potent antioxidant properties via induction of heme oxygenase-1 (HO-1).	Pentaerythritol Tetranitrate	0-28	heme oxygenase 1	Homo sapiens	110-126
21950555-2	2011	The aim of this study was to evaluate whether Inhibitor of HO-1, zinc protoporphyrin IX (Znpp), enhances the radiosensitivity in human nonsmall cell lung cancer (NSCLC) A549 Cells.	zinc protoporphyrin	89-93	heme oxygenase 1	Homo sapiens	59-87
21950555-6	2011	First, overexpression of the HO-1 mRNA was found in treatment with irradiation alone in A549 cells, and expression of the HO-1 mRNA was reduced after combined treatments with 12 mumol/L of Znpp and irradiation.	zinc protoporphyrin	189-193	heme oxygenase 1	Homo sapiens	29-33
21950555-6	2011	First, overexpression of the HO-1 mRNA was found in treatment with irradiation alone in A549 cells, and expression of the HO-1 mRNA was reduced after combined treatments with 12 mumol/L of Znpp and irradiation.	zinc protoporphyrin	189-193	heme oxygenase 1	Homo sapiens	122-126
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Heme	68-72	heme oxygenase 1	Homo sapiens	12-28
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Heme	68-72	heme oxygenase 1	Homo sapiens	30-34
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Carbon Monoxide	78-93	heme oxygenase 1	Homo sapiens	12-28
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Carbon Monoxide	78-93	heme oxygenase 1	Homo sapiens	30-34
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	12-28
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	30-34
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Iron	115-119	heme oxygenase 1	Homo sapiens	12-28
22088544-1	2011	BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron.	Iron	115-119	heme oxygenase 1	Homo sapiens	30-34
21844097-2	2011	Pentaerithrityl tetranitrate (PETN) is an organic nitrate with potent antioxidant properties via induction of heme oxygenase-1 (HO-1).	Pentaerythritol Tetranitrate	0-28	heme oxygenase 1	Homo sapiens	128-132
21844097-2	2011	Pentaerithrityl tetranitrate (PETN) is an organic nitrate with potent antioxidant properties via induction of heme oxygenase-1 (HO-1).	Pentaerythritol Tetranitrate	30-34	heme oxygenase 1	Homo sapiens	110-126
21844097-2	2011	Pentaerithrityl tetranitrate (PETN) is an organic nitrate with potent antioxidant properties via induction of heme oxygenase-1 (HO-1).	Pentaerythritol Tetranitrate	30-34	heme oxygenase 1	Homo sapiens	128-132
21844097-2	2011	Pentaerithrityl tetranitrate (PETN) is an organic nitrate with potent antioxidant properties via induction of heme oxygenase-1 (HO-1).	Nitrates	21-28	heme oxygenase 1	Homo sapiens	110-126
21844097-2	2011	Pentaerithrityl tetranitrate (PETN) is an organic nitrate with potent antioxidant properties via induction of heme oxygenase-1 (HO-1).	Nitrates	21-28	heme oxygenase 1	Homo sapiens	128-132
21844097-13	2011	The expression of the antioxidant enzyme, HO-1, was increased by STZ treatment and further upregulated by PETN, but not ISMN, via activation of the transcription factor NRF2.	Streptozocin	65-68	heme oxygenase 1	Homo sapiens	42-46
21902835-2	2011	Heme oxygenase-1 (HMOX1) is an essential enzyme in heme catabolism that is induced by oxidative stress and may play a protective role as an antioxidant in the lung.	Heme	51-55	heme oxygenase 1	Homo sapiens	0-16
21499987-3	2011	Data from our and other laboratories have previously demonstrated that curcumin, the yellow pigment of curry, strongly induces heme-oxygenase-1 (HO-1) expression and activity in different brain cells via the activation of heterodimers of NF-E2-related factors 2 (Nrf2)/antioxidant responsive element (ARE) pathway.	Curcumin	71-79	heme oxygenase 1	Homo sapiens	127-143
21499987-3	2011	Data from our and other laboratories have previously demonstrated that curcumin, the yellow pigment of curry, strongly induces heme-oxygenase-1 (HO-1) expression and activity in different brain cells via the activation of heterodimers of NF-E2-related factors 2 (Nrf2)/antioxidant responsive element (ARE) pathway.	Curcumin	71-79	heme oxygenase 1	Homo sapiens	145-149
21499987-6	2011	Recent and unpublished data from our group revealed that low concentrations of epigallocatechin-3-gallate, the major green tea catechin, induces HO-1 by ARE/Nrf2 pathway in hippocampal neurons, and by this induction, it is able to protect neurons against different models of oxidative damages.	epigallocatechin gallate	79-105	heme oxygenase 1	Homo sapiens	145-149
21499987-6	2011	Recent and unpublished data from our group revealed that low concentrations of epigallocatechin-3-gallate, the major green tea catechin, induces HO-1 by ARE/Nrf2 pathway in hippocampal neurons, and by this induction, it is able to protect neurons against different models of oxidative damages.	Catechin	87-95	heme oxygenase 1	Homo sapiens	145-149
21499987-7	2011	Furthermore, we have demonstrated that other phenolics, such as caffeic acid phenethyl ester and ethyl ferulate, are also able to protect neurons via HO-1 induction.	caffeic acid phenethyl ester	64-92	heme oxygenase 1	Homo sapiens	150-154
21499987-7	2011	Furthermore, we have demonstrated that other phenolics, such as caffeic acid phenethyl ester and ethyl ferulate, are also able to protect neurons via HO-1 induction.	ethyl ferulate	97-111	heme oxygenase 1	Homo sapiens	150-154
21681819-3	2011	Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact.	Hemin	79-84	heme oxygenase 1	Homo sapiens	0-16
21681819-3	2011	Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact.	Hemin	79-84	heme oxygenase 1	Homo sapiens	18-22
21681819-3	2011	Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact.	Hemin	201-206	heme oxygenase 1	Homo sapiens	0-16
21681819-3	2011	Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact.	Hemin	201-206	heme oxygenase 1	Homo sapiens	18-22
21681819-3	2011	Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact.	Hemin	201-206	heme oxygenase 1	Homo sapiens	0-16
21681819-3	2011	Heme oxygenase-1 (HO-1) expression was first evident after 2 h incubation with hemin, with maximal expression being observed by 24 h. Despite the induction of HO-1, it was found that the proportion of hemin metabolized by astrocytes remained fairly constant throughout the 24 h period, with 70-80% of intracellular hemin remaining intact.	Hemin	201-206	heme oxygenase 1	Homo sapiens	18-22
22008538-9	2011	Auranofin-inducted HO-1 gene expression was observed in human primary hepatocytes as well as mouse primary hepatocytes.	Auranofin	0-9	heme oxygenase 1	Homo sapiens	19-23
21902835-2	2011	Heme oxygenase-1 (HMOX1) is an essential enzyme in heme catabolism that is induced by oxidative stress and may play a protective role as an antioxidant in the lung.	Heme	51-55	heme oxygenase 1	Homo sapiens	18-23
21741353-1	2011	Genetic variations in POR, encoding NADPH-cytochrome P450 oxidoreductase (CYPOR), can diminish the function of numerous cytochromes P450, and also have the potential to block degradation of heme by heme oxygenase-1 (HO-1).	Heme	190-194	heme oxygenase 1	Homo sapiens	198-214
21741353-1	2011	Genetic variations in POR, encoding NADPH-cytochrome P450 oxidoreductase (CYPOR), can diminish the function of numerous cytochromes P450, and also have the potential to block degradation of heme by heme oxygenase-1 (HO-1).	Heme	190-194	heme oxygenase 1	Homo sapiens	216-220
21741353-6	2011	When mixed with WT CYPOR, only the Y181D CYPOR variant inhibited heme degradation by sequestering HO-1, whereas Y459H and V492E were unable to inhibit HO-1 activity suggesting that CYPOR variants might have differential binding affinities with redox partners.	Heme	65-69	heme oxygenase 1	Homo sapiens	98-102
21669191-5	2011	It was found that the electron-withdrawing (NO(2), CN, halogen) groups in BMN molecules and double meta-MeO substituents increased the HO-1 gene induction, while the electron-donating groups in ortho/para position (OH, MeO and N-morpholino) significantly decreased it.	Halogens	55-62	heme oxygenase 1	Homo sapiens	135-139
21975817-1	2011	In the present study, we investigated an anti-inflammatory effect of ethyl gallate (EG) isolated from Galla Rhois as evaluated by inhibition of nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) expression, and a potential role of heme oxygenase-1 (HO-1) in the inhibition of NO production elicited by EG.	ethyl gallate	69-82	heme oxygenase 1	Homo sapiens	252-268
21975817-1	2011	In the present study, we investigated an anti-inflammatory effect of ethyl gallate (EG) isolated from Galla Rhois as evaluated by inhibition of nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) expression, and a potential role of heme oxygenase-1 (HO-1) in the inhibition of NO production elicited by EG.	ethyl gallate	69-82	heme oxygenase 1	Homo sapiens	270-274
21975817-1	2011	In the present study, we investigated an anti-inflammatory effect of ethyl gallate (EG) isolated from Galla Rhois as evaluated by inhibition of nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) expression, and a potential role of heme oxygenase-1 (HO-1) in the inhibition of NO production elicited by EG.	ethyl gallate	84-86	heme oxygenase 1	Homo sapiens	252-268
21975817-1	2011	In the present study, we investigated an anti-inflammatory effect of ethyl gallate (EG) isolated from Galla Rhois as evaluated by inhibition of nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) expression, and a potential role of heme oxygenase-1 (HO-1) in the inhibition of NO production elicited by EG.	ethyl gallate	84-86	heme oxygenase 1	Homo sapiens	270-274
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	S-Nitroso-N-propionyl-D,L-penicillamine	28-32	heme oxygenase 1	Homo sapiens	70-74
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	S-Nitroso-N-propionyl-D,L-penicillamine	28-32	heme oxygenase 1	Homo sapiens	166-170
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	tin protoporphyrin IX	34-55	heme oxygenase 1	Homo sapiens	70-74
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	tin protoporphyrin IX	34-55	heme oxygenase 1	Homo sapiens	166-170
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	ethyl gallate	124-126	heme oxygenase 1	Homo sapiens	70-74
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	ethyl gallate	124-126	heme oxygenase 1	Homo sapiens	166-170
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	Nitrites	130-137	heme oxygenase 1	Homo sapiens	166-170
21975817-5	2011	In addition, treatment with SnPP (tin protoporphyrin IX), a selective HO-1 inhibitor, counteracted the inhibitory effect of EG on nitrite production, suggesting that HO-1 is, at least in part, implicated in the inhibition of NO production induced by EG treatment.	ethyl gallate	250-252	heme oxygenase 1	Homo sapiens	166-170
21975817-0	2011	Involvement of heme oxygenase-1 induction in inhibitory effect of ethyl gallate isolated from Galla Rhois on nitric oxide production in RAW 264.7 macrophages.	ethyl gallate	66-79	heme oxygenase 1	Homo sapiens	15-31
21975817-0	2011	Involvement of heme oxygenase-1 induction in inhibitory effect of ethyl gallate isolated from Galla Rhois on nitric oxide production in RAW 264.7 macrophages.	Nitric Oxide	109-121	heme oxygenase 1	Homo sapiens	15-31
21669191-5	2011	It was found that the electron-withdrawing (NO(2), CN, halogen) groups in BMN molecules and double meta-MeO substituents increased the HO-1 gene induction, while the electron-donating groups in ortho/para position (OH, MeO and N-morpholino) significantly decreased it.	bmn	74-77	heme oxygenase 1	Homo sapiens	135-139
21669191-5	2011	It was found that the electron-withdrawing (NO(2), CN, halogen) groups in BMN molecules and double meta-MeO substituents increased the HO-1 gene induction, while the electron-donating groups in ortho/para position (OH, MeO and N-morpholino) significantly decreased it.	meta-	99-104	heme oxygenase 1	Homo sapiens	135-139
21669191-5	2011	It was found that the electron-withdrawing (NO(2), CN, halogen) groups in BMN molecules and double meta-MeO substituents increased the HO-1 gene induction, while the electron-donating groups in ortho/para position (OH, MeO and N-morpholino) significantly decreased it.	n-morpholino	227-239	heme oxygenase 1	Homo sapiens	135-139
21620964-0	2011	An IkappaBalpha phosphorylation inhibitor induces heme oxygenase-1(HO-1) expression through the activation of reactive oxygen species (ROS)-Nrf2-ARE signaling and ROS-PI3K/Akt signaling in an NF-kappaB-independent mechanism.	Reactive Oxygen Species	110-133	heme oxygenase 1	Homo sapiens	50-71
21843792-4	2011	Additionally, PGEA inhibited the TNF-alpha/IFN-gamma-co-induced activation of NF-kappaB and STAT1 and increased the expression of heme oxygenase-1 (HO-1) protein and mRNA.	pgea	14-18	heme oxygenase 1	Homo sapiens	130-146
21843792-4	2011	Additionally, PGEA inhibited the TNF-alpha/IFN-gamma-co-induced activation of NF-kappaB and STAT1 and increased the expression of heme oxygenase-1 (HO-1) protein and mRNA.	pgea	14-18	heme oxygenase 1	Homo sapiens	148-152
21843792-5	2011	HO-1 inhibitor enhanced the suppressive effects of PGEA on TNF-alpha/IFN-gamma-co-induced TARC production and gene expression.	pgea	51-55	heme oxygenase 1	Homo sapiens	0-4
21843792-6	2011	Collectively, these data demonstrate that PGEA inhibits chemokine expression in keratinocytes by inducing HO-1 expression and it suggests a possible therapeutic application in atopic dermatitis and other inflammatory skin diseases.	pgea	42-46	heme oxygenase 1	Homo sapiens	106-110
21520244-0	2011	Fisetin induces Nrf2-mediated HO-1 expression through PKC-delta and p38 in human umbilical vein endothelial cells.	fisetin	0-7	heme oxygenase 1	Homo sapiens	30-34
21520244-3	2011	In the present study, we investigated the effect of fisetin on the up-regulation of HO-1 in human umbilical vein endothelial cells (HUVECs).	fisetin	52-59	heme oxygenase 1	Homo sapiens	84-88
21520244-5	2011	Fisetin treatment resulted in significantly increased NF-E2-related factor 2 (Nrf2) nuclear translocation, and antioxidant response element (ARE)-luciferase activity, leading to up-regulation of HO-1 expression.	fisetin	0-7	heme oxygenase 1	Homo sapiens	195-199
21520244-6	2011	In addition, fisetin pretreatment reduced hydrogen peroxide (H(2)O(2))-induced cell death, and this effect was reversed by ZnPP, an inhibitor of HO-1.	fisetin	13-20	heme oxygenase 1	Homo sapiens	145-149
21520244-6	2011	In addition, fisetin pretreatment reduced hydrogen peroxide (H(2)O(2))-induced cell death, and this effect was reversed by ZnPP, an inhibitor of HO-1.	Hydrogen Peroxide	42-59	heme oxygenase 1	Homo sapiens	145-149
21520244-6	2011	In addition, fisetin pretreatment reduced hydrogen peroxide (H(2)O(2))-induced cell death, and this effect was reversed by ZnPP, an inhibitor of HO-1.	Hydrogen Peroxide	61-69	heme oxygenase 1	Homo sapiens	145-149
21520244-6	2011	In addition, fisetin pretreatment reduced hydrogen peroxide (H(2)O(2))-induced cell death, and this effect was reversed by ZnPP, an inhibitor of HO-1.	zinc protoporphyrin	123-127	heme oxygenase 1	Homo sapiens	145-149
21520244-7	2011	In summary, these findings suggest that induction of HO-1 expression via Nrf2 activation may contribute to the cytoprotection exerted by fisetin against H(2)O(2) -induced oxidative stress in HUVECs.	Hydrogen Peroxide	153-161	heme oxygenase 1	Homo sapiens	53-57
21620964-0	2011	An IkappaBalpha phosphorylation inhibitor induces heme oxygenase-1(HO-1) expression through the activation of reactive oxygen species (ROS)-Nrf2-ARE signaling and ROS-PI3K/Akt signaling in an NF-kappaB-independent mechanism.	Reactive Oxygen Species	135-138	heme oxygenase 1	Homo sapiens	50-71
21620964-0	2011	An IkappaBalpha phosphorylation inhibitor induces heme oxygenase-1(HO-1) expression through the activation of reactive oxygen species (ROS)-Nrf2-ARE signaling and ROS-PI3K/Akt signaling in an NF-kappaB-independent mechanism.	Reactive Oxygen Species	163-166	heme oxygenase 1	Homo sapiens	50-71
21620964-3	2011	Antioxidant enzymes, such as, heme oxygenase-1 (HO-1), tightly regulate ROS levels within cells.	Reactive Oxygen Species	72-75	heme oxygenase 1	Homo sapiens	30-46
21620964-3	2011	Antioxidant enzymes, such as, heme oxygenase-1 (HO-1), tightly regulate ROS levels within cells.	Reactive Oxygen Species	72-75	heme oxygenase 1	Homo sapiens	48-52
21620964-6	2011	In addition, PI3K/Akt inhibitor (LY294002) blocked Bay-induced HO-1 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	33-41	heme oxygenase 1	Homo sapiens	63-67
21620964-7	2011	Pretreatment with anti-oxidants (N-acetylcysteine (NAC) or glutathione) significantly reduced Bay-induced HO-1 mRNA/protein expression, nuclear translocation of Nrf2 and phosphorylation of Akt.	Acetylcysteine	33-49	heme oxygenase 1	Homo sapiens	106-110
21620964-7	2011	Pretreatment with anti-oxidants (N-acetylcysteine (NAC) or glutathione) significantly reduced Bay-induced HO-1 mRNA/protein expression, nuclear translocation of Nrf2 and phosphorylation of Akt.	Acetylcysteine	51-54	heme oxygenase 1	Homo sapiens	106-110
21620964-7	2011	Pretreatment with anti-oxidants (N-acetylcysteine (NAC) or glutathione) significantly reduced Bay-induced HO-1 mRNA/protein expression, nuclear translocation of Nrf2 and phosphorylation of Akt.	Glutathione	59-70	heme oxygenase 1	Homo sapiens	106-110
21620964-9	2011	Furthermore, other NF-kappaB inhibitors, such as pyrrolidine dithiocarbamate (PDTC) and MG132, also increased HO-1 mRNA and protein expression.	pyrrolidine dithiocarbamic acid	49-76	heme oxygenase 1	Homo sapiens	110-114
21620964-9	2011	Furthermore, other NF-kappaB inhibitors, such as pyrrolidine dithiocarbamate (PDTC) and MG132, also increased HO-1 mRNA and protein expression.	pyrrolidine dithiocarbamic acid	78-82	heme oxygenase 1	Homo sapiens	110-114
21620964-9	2011	Furthermore, other NF-kappaB inhibitors, such as pyrrolidine dithiocarbamate (PDTC) and MG132, also increased HO-1 mRNA and protein expression.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	88-93	heme oxygenase 1	Homo sapiens	110-114
21620964-11	2011	Taken together, our results suggest that in human colon cancer HT29 cells, Bay induces HO-1 expression by increasing ROS production in an Nrf2-ARE and PI3K dependent manner, but Bay acts independently of NF-kappaB.	Reactive Oxygen Species	117-120	heme oxygenase 1	Homo sapiens	87-91
21327864-0	2011	Inhibition of heme oxygenase-1 enhances anti-cancer effects of arsenic trioxide on glioma cells.	Arsenic Trioxide	63-79	heme oxygenase 1	Homo sapiens	14-30
21327864-2	2011	In this study we showed that ATO induced cell damage and heme oxygenase-1 (HO-1) expression in glioma cells via ROS generation.	Arsenic Trioxide	29-32	heme oxygenase 1	Homo sapiens	57-73
21327864-2	2011	In this study we showed that ATO induced cell damage and heme oxygenase-1 (HO-1) expression in glioma cells via ROS generation.	Arsenic Trioxide	29-32	heme oxygenase 1	Homo sapiens	75-79
21327864-2	2011	In this study we showed that ATO induced cell damage and heme oxygenase-1 (HO-1) expression in glioma cells via ROS generation.	ros	112-115	heme oxygenase 1	Homo sapiens	75-79
21327864-3	2011	HO-1 inducer clearly protected from ATO-induced cell death and ROS generation, and HO-1 inhibitor led to a significant increase in cell death and ROS generation induced by ATO.	Arsenic Trioxide	36-39	heme oxygenase 1	Homo sapiens	0-4
21327864-3	2011	HO-1 inducer clearly protected from ATO-induced cell death and ROS generation, and HO-1 inhibitor led to a significant increase in cell death and ROS generation induced by ATO.	ros	63-66	heme oxygenase 1	Homo sapiens	0-4
21327864-3	2011	HO-1 inducer clearly protected from ATO-induced cell death and ROS generation, and HO-1 inhibitor led to a significant increase in cell death and ROS generation induced by ATO.	ros	146-149	heme oxygenase 1	Homo sapiens	83-87
21327864-3	2011	HO-1 inducer clearly protected from ATO-induced cell death and ROS generation, and HO-1 inhibitor led to a significant increase in cell death and ROS generation induced by ATO.	Arsenic Trioxide	172-175	heme oxygenase 1	Homo sapiens	0-4
21327864-3	2011	HO-1 inducer clearly protected from ATO-induced cell death and ROS generation, and HO-1 inhibitor led to a significant increase in cell death and ROS generation induced by ATO.	Arsenic Trioxide	172-175	heme oxygenase 1	Homo sapiens	83-87
21327864-4	2011	In addition, knockdown of nuclear factor (erythroid-derived 2)-like 2 (Nrf2) strongly inhibited HO-1 expression induced by ATO, and significantly enhanced ATO-induced oxidative damage.	Arsenic Trioxide	123-126	heme oxygenase 1	Homo sapiens	96-100
21327864-6	2011	Considering that HO-1 is highly expressed in glioma tissues, administration of ATO in combination with either HO-1 inhibitor or Nrf2 knockdown may act as a new approach to the treatment of glioma.	Arsenic Trioxide	79-82	heme oxygenase 1	Homo sapiens	17-21
21533649-0	2011	Dimethyl sulfoxide induces heme oxygenase-1 expression via JNKs and Nrf2 pathways in human umbilical vein endothelial cells.	Dimethyl Sulfoxide	0-18	heme oxygenase 1	Homo sapiens	27-43
21533649-3	2011	In this paper, we investigated the capability of DMSO to up-regulate heme oxygenase-1(HO-1) expression, as well as the possible underlying mechanisms in human umbilical vein endothelial cells (HUVECs).	Dimethyl Sulfoxide	49-53	heme oxygenase 1	Homo sapiens	69-85
21911919-4	2011	This study aims to analyse the role of HO-1 in regulating apoptosis in AML cells in response to two front-line chemotherapeutic agents used for AML, cytarabine and daunorubicin.	Cytarabine	149-159	heme oxygenase 1	Homo sapiens	39-43
21640381-0	2011	Carbon monoxide, a reaction product of heme oxygenase-1, suppresses the expression of C-reactive protein by endoplasmic reticulum stress through modulation of the unfolded protein response.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	39-55
21668870-6	2011	The ALA-dependent accumulation of protoporphyrin was decreased in HeLa cells by transfection with HO-1 and HO-2 cDNA.	Aminolevulinic Acid	4-7	heme oxygenase 1	Homo sapiens	98-111
21668870-6	2011	The ALA-dependent accumulation of protoporphyrin was decreased in HeLa cells by transfection with HO-1 and HO-2 cDNA.	protoporphyrin IX	34-48	heme oxygenase 1	Homo sapiens	98-111
21911919-4	2011	This study aims to analyse the role of HO-1 in regulating apoptosis in AML cells in response to two front-line chemotherapeutic agents used for AML, cytarabine and daunorubicin.	Daunorubicin	164-176	heme oxygenase 1	Homo sapiens	39-43
21911919-5	2011	Here we show that HO-1 expression in AML samples was increased in response to both cytarabine and daunorubicin treatment, and micro RNA (miRNA) silenced HO-1 expression in combination with either daunorubicin or cytarabine induced a greater apoptotic responses in AML cells.	Cytarabine	83-93	heme oxygenase 1	Homo sapiens	18-22
21911919-5	2011	Here we show that HO-1 expression in AML samples was increased in response to both cytarabine and daunorubicin treatment, and micro RNA (miRNA) silenced HO-1 expression in combination with either daunorubicin or cytarabine induced a greater apoptotic responses in AML cells.	Daunorubicin	98-110	heme oxygenase 1	Homo sapiens	18-22
21911919-5	2011	Here we show that HO-1 expression in AML samples was increased in response to both cytarabine and daunorubicin treatment, and micro RNA (miRNA) silenced HO-1 expression in combination with either daunorubicin or cytarabine induced a greater apoptotic responses in AML cells.	Cytarabine	212-222	heme oxygenase 1	Homo sapiens	153-157
21911919-7	2011	However, ROS-dependent induction of HO-1 was limiting the apoptotic response that is seen in AML towards cytarabine and daunorubicin treatment.	Reactive Oxygen Species	9-12	heme oxygenase 1	Homo sapiens	36-40
21911919-7	2011	However, ROS-dependent induction of HO-1 was limiting the apoptotic response that is seen in AML towards cytarabine and daunorubicin treatment.	Cytarabine	105-115	heme oxygenase 1	Homo sapiens	36-40
21911919-7	2011	However, ROS-dependent induction of HO-1 was limiting the apoptotic response that is seen in AML towards cytarabine and daunorubicin treatment.	Daunorubicin	120-132	heme oxygenase 1	Homo sapiens	36-40
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Glutathione	19-30	heme oxygenase 1	Homo sapiens	122-126
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Glutathione	19-30	heme oxygenase 1	Homo sapiens	220-224
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Acetylcysteine	37-56	heme oxygenase 1	Homo sapiens	122-126
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Acetylcysteine	37-56	heme oxygenase 1	Homo sapiens	220-224
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Carbon Monoxide	274-276	heme oxygenase 1	Homo sapiens	122-126
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Biliverdine	278-288	heme oxygenase 1	Homo sapiens	122-126
21635873-5	2011	Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin.	Bilirubin	293-302	heme oxygenase 1	Homo sapiens	122-126
20094823-12	2011	The analysis reveals that eCO levels were significantly raised in asthma and it may attribute to high expression of HO-1, but there were no significantly high eCO levels between AR and control groups.	ECO	26-29	heme oxygenase 1	Homo sapiens	116-120
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Heme	17-21	heme oxygenase 1	Homo sapiens	35-38
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Carbon Monoxide	108-110	heme oxygenase 1	Homo sapiens	17-33
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Carbon Monoxide	108-110	heme oxygenase 1	Homo sapiens	35-38
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Biliverdine	96-106	heme oxygenase 1	Homo sapiens	17-33
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Iron	123-127	heme oxygenase 1	Homo sapiens	17-33
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Biliverdine	96-106	heme oxygenase 1	Homo sapiens	35-38
21079975-3	2011	Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron.	Iron	123-127	heme oxygenase 1	Homo sapiens	35-38
22053693-6	2011	The ROS promotes lipid oxidation and are known to induce stress proteins, such as hemeoxygenase 1 (HO-1) and heat-shock protein 70 (HSP70).	Reactive Oxygen Species	4-7	heme oxygenase 1	Homo sapiens	82-97
21079975-6	2011	OBJECTIVE: This study focused on the uptake and transport of heme iron and on the role of heme oxygenase-1 on heme iron metabolism.	Iron	115-119	heme oxygenase 1	Homo sapiens	90-106
21079975-8	2011	A full-length heme oxygenase-1 cDNA was expressed in Caco-2 cells and intracellular iron and heme-Fe content, heme uptake, heme and iron transport and heme oxygenase-1 immunolocalization were assessed in these cells.	Iron	84-88	heme oxygenase 1	Homo sapiens	14-30
21079975-9	2011	RESULTS: Heme-Fe was bioavailable and induced an intracellular increase in iron, ferritin and HO1 levels and a decrease in DMT1 expression.	heme-fe	9-16	heme oxygenase 1	Homo sapiens	94-97
21079975-10	2011	In cells overexpressing HO1, heme-Fe uptake and transepithelial Fe transport was higher than in controls.	Heme	29-33	heme oxygenase 1	Homo sapiens	24-27
21079975-10	2011	In cells overexpressing HO1, heme-Fe uptake and transepithelial Fe transport was higher than in controls.	Iron	34-36	heme oxygenase 1	Homo sapiens	24-27
21079975-10	2011	In cells overexpressing HO1, heme-Fe uptake and transepithelial Fe transport was higher than in controls.	Iron	64-66	heme oxygenase 1	Homo sapiens	24-27
21079975-13	2011	In a high heme-Fe condition, HO1 is found near the plasma membrane.	Heme	10-14	heme oxygenase 1	Homo sapiens	29-32
21079975-14	2011	CONCLUSIONS: These results suggest that heme oxygenase-1 catabolizes most of the heme-Fe and favors iron influx and efflux in intestinal cells.	heme-fe	81-88	heme oxygenase 1	Homo sapiens	40-56
21079975-14	2011	CONCLUSIONS: These results suggest that heme oxygenase-1 catabolizes most of the heme-Fe and favors iron influx and efflux in intestinal cells.	Iron	100-104	heme oxygenase 1	Homo sapiens	40-56
21622902-0	2011	Nrf-2 regulates cyclosporine-stimulated HO-1 expression in gingiva.	Cyclosporine	16-28	heme oxygenase 1	Homo sapiens	40-44
21622902-6	2011	ERK inhibition significantly decreased CsA-stimulated Nrf-2 nuclear translocation and HO-1 mRNA expression.	Cyclosporine	39-42	heme oxygenase 1	Homo sapiens	86-90
21622902-1	2011	Cyclosporine-A (CsA) stimulates heme oxygenase-1 (HO-1) expression in the gingiva, but the regulation and the role of HO-1 in gingival overgrowth are not well-understood.	Cyclosporine	0-14	heme oxygenase 1	Homo sapiens	32-48
21622902-8	2011	These findings suggest that CsA-stimulated HO-1 expression is mediated through the activation of ERK, and that Nrf-2 plays a protective role against CsA-induced gingival fibrosis by modulating collagen turnover-related genes.	Cyclosporine	28-31	heme oxygenase 1	Homo sapiens	43-47
21622902-1	2011	Cyclosporine-A (CsA) stimulates heme oxygenase-1 (HO-1) expression in the gingiva, but the regulation and the role of HO-1 in gingival overgrowth are not well-understood.	Cyclosporine	0-14	heme oxygenase 1	Homo sapiens	50-54
21622902-1	2011	Cyclosporine-A (CsA) stimulates heme oxygenase-1 (HO-1) expression in the gingiva, but the regulation and the role of HO-1 in gingival overgrowth are not well-understood.	Cyclosporine	16-19	heme oxygenase 1	Homo sapiens	32-48
21622902-1	2011	Cyclosporine-A (CsA) stimulates heme oxygenase-1 (HO-1) expression in the gingiva, but the regulation and the role of HO-1 in gingival overgrowth are not well-understood.	Cyclosporine	16-19	heme oxygenase 1	Homo sapiens	50-54
21622902-3	2011	The aim of this study was to examine the role of Nrf-2 in the regulation of CsA-stimulated HO-1 expression in human gingival fibroblasts.	Cyclosporine	76-79	heme oxygenase 1	Homo sapiens	91-95
21622902-5	2011	Treatment with siNrf-2, but not with an NF-kappaB inhibitor, reduced CsA-stimulated HO-1 mRNA expression.	Cyclosporine	69-72	heme oxygenase 1	Homo sapiens	84-88
21994478-4	2011	Treatment with cilostazol increased HO-1 expression and phosphorylation of AMPK in a dose- and time-dependent manner.	Cilostazol	15-25	heme oxygenase 1	Homo sapiens	36-40
21994478-0	2011	Cilostazol Inhibits Vascular Smooth Muscle Cell Proliferation and Reactive Oxygen Species Production through Activation of AMP-activated Protein Kinase Induced by Heme Oxygenase-1.	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	163-179
21372182-9	2011	TcdA increased HO-1 expression as seen by immunohistochemistry.	tcda	0-4	heme oxygenase 1	Homo sapiens	15-19
21372182-10	2011	These results suggest that the HO-1/CO pathway exerts a protective role in TcdA-induced enteritis and that its pharmacological modulation might be important for the management of C. difficile-associated disease.	tcda	75-79	heme oxygenase 1	Homo sapiens	31-35
21994478-5	2011	Cilostazol also significantly decreased platelet-derived growth factor (PDGF)-induced VSMC proliferation and ROS production by activating AMPK induced by HO-1.	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	154-158
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Cilostazol	68-78	heme oxygenase 1	Homo sapiens	42-46
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Cilostazol	68-78	heme oxygenase 1	Homo sapiens	182-186
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Reactive Oxygen Species	124-127	heme oxygenase 1	Homo sapiens	42-46
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Cilostazol	163-173	heme oxygenase 1	Homo sapiens	42-46
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Cilostazol	163-173	heme oxygenase 1	Homo sapiens	182-186
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Reactive Oxygen Species	270-273	heme oxygenase 1	Homo sapiens	42-46
21994478-6	2011	Pharmacological and genetic inhibition of HO-1 and AMPK blocked the cilostazol-induced inhibition of cell proliferation and ROS production.These data suggest that cilostazol-induced HO-1 expression and AMPK activation might attenuate PDGF-induced VSMC proliferation and ROS production.	Reactive Oxygen Species	270-273	heme oxygenase 1	Homo sapiens	182-186
21765607-6	2011	Taurine chloramine increased heme oxygenase-1 expression and heme oxygenase activity.	N-chlorotaurine	0-18	heme oxygenase 1	Homo sapiens	29-45
21549697-6	2011	In contrast to the level of HO-1 expression in high tidal volume group, pretreatment with hemin, an inducer of HO-1, further up-regulated HO-1 expression.	Hemin	90-95	heme oxygenase 1	Homo sapiens	28-32
21549697-6	2011	In contrast to the level of HO-1 expression in high tidal volume group, pretreatment with hemin, an inducer of HO-1, further up-regulated HO-1 expression.	Hemin	90-95	heme oxygenase 1	Homo sapiens	111-115
21549697-6	2011	In contrast to the level of HO-1 expression in high tidal volume group, pretreatment with hemin, an inducer of HO-1, further up-regulated HO-1 expression.	Hemin	90-95	heme oxygenase 1	Homo sapiens	111-115
21722625-6	2011	High dose of glucose enhanced the expression of HO-1 mRNA and HO-1 protein in a time-dependent manner.	Glucose	13-20	heme oxygenase 1	Homo sapiens	48-52
21722625-6	2011	High dose of glucose enhanced the expression of HO-1 mRNA and HO-1 protein in a time-dependent manner.	Glucose	13-20	heme oxygenase 1	Homo sapiens	62-66
21722625-7	2011	LAB enhanced the expression of HO-1 mRNA and HO-1 protein in a dose-dependent manner treated with high dose of glucose.	Glucose	111-118	heme oxygenase 1	Homo sapiens	31-35
21722625-7	2011	LAB enhanced the expression of HO-1 mRNA and HO-1 protein in a dose-dependent manner treated with high dose of glucose.	Glucose	111-118	heme oxygenase 1	Homo sapiens	45-49
21689633-4	2011	Hyperoside further enhanced the cellular antioxidant defense system through increasing the activity of heme oxygenase-1 (HO-1), and by up-regulating HO-1 expression.	hyperoside	0-10	heme oxygenase 1	Homo sapiens	103-119
21689633-4	2011	Hyperoside further enhanced the cellular antioxidant defense system through increasing the activity of heme oxygenase-1 (HO-1), and by up-regulating HO-1 expression.	hyperoside	0-10	heme oxygenase 1	Homo sapiens	121-125
21689633-4	2011	Hyperoside further enhanced the cellular antioxidant defense system through increasing the activity of heme oxygenase-1 (HO-1), and by up-regulating HO-1 expression.	hyperoside	0-10	heme oxygenase 1	Homo sapiens	149-153
21689633-6	2011	Collectively, our data provide the first description of the mechanism underlying hyperoside"s ability to attenuate H(2)O(2)-induced cell damage, namely this compound interacts with the MAPK-dependent Keap(1)-Nrf(2)-ARE signaling pathway to up-regulate HO-1 expression and enhance intracellular antioxidant activity.	hyperoside	81-91	heme oxygenase 1	Homo sapiens	252-256
21752292-8	2011	Although most oil components may reduce oxidant stress by undergoing reduction, orange oil was demonstrated to have the ability to induce long-lasting gene expression of several antioxidant enzymes linked to Nrf2, including HO-1, NQO1, GCLm and GCLc, and to mitigate the pro-inflammatory signaling of endotoxin in cell culture systems.	orange oil	80-90	heme oxygenase 1	Homo sapiens	224-228
21752292-10	2011	Treatment with the aerosolized oil preparation increased baseline levels of nasal mucosal HO-1 expression in 9 of 12 subjects.	Oils	31-34	heme oxygenase 1	Homo sapiens	90-94
21793851-6	2011	Carbon monoxide (CO), a reaction product of heme oxygenase-1 (HO-1), reduces oxidative stress and inflammatory response and protects cells from ER stress.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	44-60
21793851-6	2011	Carbon monoxide (CO), a reaction product of heme oxygenase-1 (HO-1), reduces oxidative stress and inflammatory response and protects cells from ER stress.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	62-66
21793851-6	2011	Carbon monoxide (CO), a reaction product of heme oxygenase-1 (HO-1), reduces oxidative stress and inflammatory response and protects cells from ER stress.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	44-60
21793851-6	2011	Carbon monoxide (CO), a reaction product of heme oxygenase-1 (HO-1), reduces oxidative stress and inflammatory response and protects cells from ER stress.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	62-66
21793851-8	2011	In addition to its anti-inflammatory effects and antiapoptotic effects, HO-1 plays an important role in insulin release and glucose metabolism.	Glucose	124-131	heme oxygenase 1	Homo sapiens	72-76
21787730-6	2011	Levels of NQO1 and HO1 mRNA are also increased by -fold and -fold following 24h exposure to 5 and 10 muM cadmium.	Cadmium	105-112	heme oxygenase 1	Homo sapiens	19-22
21765607-9	2011	Combined, these results indicate that the taurine chloramine, produced and released endogenously by the activated neutrophils, can protect the macrophages in inflamed tissues from the H(2)O(2)-derived apoptosis not only by increasing the expression of cytoprotective enzymes like heme oxygenase-1 and catalase, but also by increasing the intracellular antioxidant GSH level.	Taurine	42-49	heme oxygenase 1	Homo sapiens	280-309
21765607-9	2011	Combined, these results indicate that the taurine chloramine, produced and released endogenously by the activated neutrophils, can protect the macrophages in inflamed tissues from the H(2)O(2)-derived apoptosis not only by increasing the expression of cytoprotective enzymes like heme oxygenase-1 and catalase, but also by increasing the intracellular antioxidant GSH level.	chloramine	50-60	heme oxygenase 1	Homo sapiens	280-309
21765607-7	2011	The taurine chloramine-derived upregulation of heme oxygenase-1 expression was blocked by inhibition of ERK phosphorylation.	Taurine	4-11	heme oxygenase 1	Homo sapiens	47-63
21412259-0	2011	Heme oxygenase-1 protects human melanocytes from H2O2-induced oxidative stress via the Nrf2-ARE pathway.	Hydrogen Peroxide	49-53	heme oxygenase 1	Homo sapiens	0-16
21412259-6	2011	Our study demonstrated that heme oxygenase-1 (HO-1) was the most induced antioxidant gene in PIG1 cells after treatment with H(2)O(2).	Water	125-130	heme oxygenase 1	Homo sapiens	28-44
21765607-7	2011	The taurine chloramine-derived upregulation of heme oxygenase-1 expression was blocked by inhibition of ERK phosphorylation.	chloramine	12-22	heme oxygenase 1	Homo sapiens	47-63
21412259-6	2011	Our study demonstrated that heme oxygenase-1 (HO-1) was the most induced antioxidant gene in PIG1 cells after treatment with H(2)O(2).	Water	125-130	heme oxygenase 1	Homo sapiens	46-50
21412259-8	2011	In addition, the H(2)O(2)-induced Nrf2-ARE/HO-1 pathway was confirmed in primary cultured human melanocytes by examining the expression and translocation of Nrf2 and HO-1.	Hydrogen Peroxide	17-25	heme oxygenase 1	Homo sapiens	43-47
21327520-0	2011	Ferrearin C induces apoptosis via heme oxygenase-1 (HO-1) induction in neuroblastoma.	ferrearin c	0-11	heme oxygenase 1	Homo sapiens	34-50
21412259-8	2011	In addition, the H(2)O(2)-induced Nrf2-ARE/HO-1 pathway was confirmed in primary cultured human melanocytes by examining the expression and translocation of Nrf2 and HO-1.	Hydrogen Peroxide	17-25	heme oxygenase 1	Homo sapiens	166-170
21412259-9	2011	These data suggested that regulation of the Nrf2/HO-1 pathway can reduce H(2)O(2)-induced oxidative damage in human melanocytes.	Hydrogen Peroxide	73-81	heme oxygenase 1	Homo sapiens	49-53
21327520-0	2011	Ferrearin C induces apoptosis via heme oxygenase-1 (HO-1) induction in neuroblastoma.	ferrearin c	0-11	heme oxygenase 1	Homo sapiens	52-56
21861350-5	2011	Moreover, HO-1 mRNA expression were also significantly induced by sodium arsenite exposure, and a definite dose-effect relationship was confirmed (P &lt; 0.01).	sodium arsenite	66-81	heme oxygenase 1	Homo sapiens	10-14
21593686-0	2011	Propofol upregulates heme oxygenase-1 through activation of ERKs in human umbilical vein endothelial cells under oxidative stress conditions.	Propofol	0-8	heme oxygenase 1	Homo sapiens	21-37
21593686-2	2011	We examined the effect of propofol on the regulation of HO-1 expression and its activity in human umbilical vein endothelial cells (HUVECs) under oxidative stress conditions.	Propofol	26-34	heme oxygenase 1	Homo sapiens	56-60
21593686-3	2011	We further assessed whether extracellular signal-regulated kinases (ERKs), cJun-N-terminal kinases (JNKs), and p38-mitogen-activated protein kinase mediate propofol-induced HO-1 expression.	Propofol	156-164	heme oxygenase 1	Homo sapiens	173-177
21593686-8	2011	HO-1 activity was determined in microsomal fractions from HUVECs by monitoring the conversion of heme into bilirubin.	Heme	97-101	heme oxygenase 1	Homo sapiens	0-4
21593686-8	2011	HO-1 activity was determined in microsomal fractions from HUVECs by monitoring the conversion of heme into bilirubin.	Bilirubin	107-116	heme oxygenase 1	Homo sapiens	0-4
21593686-11	2011	RESULTS: Under oxidative stress conditions, HO-1 expression and activity were increased by propofol in a dose-dependent and time-dependent manner.	Propofol	91-99	heme oxygenase 1	Homo sapiens	44-48
21593686-12	2011	PD98059, but not SB203580 or SP600125, effectively reduced propofol-induced HO-1 protein levels.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	0-7	heme oxygenase 1	Homo sapiens	76-80
21593686-12	2011	PD98059, but not SB203580 or SP600125, effectively reduced propofol-induced HO-1 protein levels.	Propofol	59-67	heme oxygenase 1	Homo sapiens	76-80
21593686-15	2011	CONCLUSIONS: These findings show that, under oxidative stress conditions, propofol induces HO-1 expression in HUVECs and this effect is mediated, at least in part, via ERKs pathways.	Propofol	74-82	heme oxygenase 1	Homo sapiens	91-95
21481475-6	2011	HMOX1, an indicator of stress due to reactive oxygen intermediates (ROIs) and/or metals, was upregulated at the later time point as well.	reactive oxygen	37-52	heme oxygenase 1	Homo sapiens	0-5
21861350-6	2011	CONCLUSION: No elevation of Nrf2 transcription was found, while inorganic arsenic could increase the Nrf2-regulated NQO1 and HO-1 mRNA expression in human hepatocytes.	Arsenic	74-81	heme oxygenase 1	Homo sapiens	125-129
21367956-4	2011	Treatment of mouse epidermal JB6 cells with zerumbone caused a marked increase of Nrf2 nuclear translocation followed by the promoter activity of HO-1, and also enhanced direct binding of Nrf2 to the antioxidant response element.	zerumbone	44-53	heme oxygenase 1	Homo sapiens	146-150
21620381-0	2011	MG132 enhances neurite outgrowth in neurons overexpressing mutant TAR DNA-binding protein-43 via increase of HO-1.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	heme oxygenase 1	Homo sapiens	109-113
21620381-5	2011	Heme oxygenase-1 (HO-1) known as antioxidase was restored by MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	61-66	heme oxygenase 1	Homo sapiens	0-16
21620381-5	2011	Heme oxygenase-1 (HO-1) known as antioxidase was restored by MG132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	61-66	heme oxygenase 1	Homo sapiens	18-22
21620381-8	2011	However, MG132 increased the expression of HO-1 independent of the Nrf2 pathway.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	9-14	heme oxygenase 1	Homo sapiens	43-47
21367956-5	2011	Moreover, knockdown of Nrf2 in JB6 cells diminished the zerumbone-induced upregulation of HO-1.	zerumbone	56-65	heme oxygenase 1	Homo sapiens	90-94
21367956-8	2011	Interestingly, when JB6 cells were treated with carbon monoxide-releasing molecule that mimics the HO-1 activity, the TPA-induced ROS production was markedly reduced.	Carbon Monoxide	48-63	heme oxygenase 1	Homo sapiens	99-103
21367956-8	2011	Interestingly, when JB6 cells were treated with carbon monoxide-releasing molecule that mimics the HO-1 activity, the TPA-induced ROS production was markedly reduced.	Tetradecanoylphorbol Acetate	118-121	heme oxygenase 1	Homo sapiens	99-103
21367956-8	2011	Interestingly, when JB6 cells were treated with carbon monoxide-releasing molecule that mimics the HO-1 activity, the TPA-induced ROS production was markedly reduced.	Reactive Oxygen Species	130-133	heme oxygenase 1	Homo sapiens	99-103
21396424-6	2011	Furthermore, [6]-gingerol treatment up-regulated the mRNA and protein expression of antioxidant enzymes such as gamma-glutamylcysteine ligase (GCL) and heme oxygenase-1 (HO-1), the rate limiting enzymes in the glutathione biosynthesis and the degradation of heme, respectively.	gingerol	17-25	heme oxygenase 1	Homo sapiens	152-168
21426408-6	2011	Heme oxygenase encoding genes were subsequently cloned to study consequences of either gene product on cell viability, demonstrating that HO-1 but not HO-2 overexpression offers protection from stress-induced cell death in MTT assays.	monooxyethylene trimethylolpropane tristearate	223-226	heme oxygenase 1	Homo sapiens	138-142
21671166-4	2011	The results showed that CdCl(2) and nano-TiO(2) at a low concentration of 0.75 total toxic unit (TU) exerted an additive effects on HO-1 gene expression, CAT activities and MDA concentrations.	cdcl	24-28	heme oxygenase 1	Homo sapiens	132-136
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Heme	93-97	heme oxygenase 1	Homo sapiens	0-16
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Heme	93-97	heme oxygenase 1	Homo sapiens	18-22
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Iron	124-136	heme oxygenase 1	Homo sapiens	0-16
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Iron	124-136	heme oxygenase 1	Homo sapiens	18-22
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	138-153	heme oxygenase 1	Homo sapiens	0-16
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	138-153	heme oxygenase 1	Homo sapiens	18-22
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	155-157	heme oxygenase 1	Homo sapiens	0-16
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	155-157	heme oxygenase 1	Homo sapiens	18-22
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Biliverdine	164-174	heme oxygenase 1	Homo sapiens	0-16
21622183-1	2011	Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin.	Biliverdine	164-174	heme oxygenase 1	Homo sapiens	18-22
21622183-4	2011	HO-1 represses inflammation by removing the pro-inflammatory molecule heme and by generating CO and the bile pigments, biliverdin and bilirubin.	Heme	70-74	heme oxygenase 1	Homo sapiens	0-4
21622183-4	2011	HO-1 represses inflammation by removing the pro-inflammatory molecule heme and by generating CO and the bile pigments, biliverdin and bilirubin.	Biliverdine	119-129	heme oxygenase 1	Homo sapiens	0-4
21622183-4	2011	HO-1 represses inflammation by removing the pro-inflammatory molecule heme and by generating CO and the bile pigments, biliverdin and bilirubin.	Bilirubin	134-143	heme oxygenase 1	Homo sapiens	0-4
21136273-10	2011	However, blockade of HO-1 using ZnPPIX totally abolished BMP-6-regulated MMP-9 activation in MCF-7 cells.	zinc protoporphyrin	32-38	heme oxygenase 1	Homo sapiens	21-25
21333731-8	2011	On the other hand, RSG notably increased the expression of key antioxidant transcription factor Nrf2 and antioxidant enzyme HO-1 in a PPARgamma-dependent manner, leading to the elimination of excessive ROS.	Reactive Oxygen Species	202-205	heme oxygenase 1	Homo sapiens	124-128
21333731-10	2011	Furthermore, the activation of Akt and MAPKs was involved in the effect of RSG on Nrf2, HO-1 and COX-2.	Rosiglitazone	75-78	heme oxygenase 1	Homo sapiens	88-92
21693314-2	2011	MATERIALS AND METHODS: To increase the expression of HO-1, both donors and recipients were injected with heme through the abdomen before the operation.	Heme	105-109	heme oxygenase 1	Homo sapiens	53-57
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	54-60	heme oxygenase 1	Homo sapiens	100-116
21781496-0	2011	[Effects of HO-1 gene expression on proliferation of imatinib resistant CML cells].	Imatinib Mesylate	53-61	heme oxygenase 1	Homo sapiens	12-16
21781496-1	2011	OBJECTIVE: To investigate the effect of heme oxygenase-1 (HO-1) expression on cell growth and apoptosis in imatinib resistant chronic myeloid leukemia (CML) cells (K562/A02-IM), and explore the relationship between HO-1 gene and CML.	Imatinib Mesylate	107-115	heme oxygenase 1	Homo sapiens	40-56
21781496-1	2011	OBJECTIVE: To investigate the effect of heme oxygenase-1 (HO-1) expression on cell growth and apoptosis in imatinib resistant chronic myeloid leukemia (CML) cells (K562/A02-IM), and explore the relationship between HO-1 gene and CML.	Imatinib Mesylate	107-115	heme oxygenase 1	Homo sapiens	58-62
21781496-3	2011	Different concentrations of hemin were used to induce HO-1 expression of K562/A02-IM, HO-1 expression at different time was detected by RT-PCR and Western blot analysis.	Hemin	28-33	heme oxygenase 1	Homo sapiens	54-58
21781496-3	2011	Different concentrations of hemin were used to induce HO-1 expression of K562/A02-IM, HO-1 expression at different time was detected by RT-PCR and Western blot analysis.	Hemin	28-33	heme oxygenase 1	Homo sapiens	86-90
21781496-9	2011	When HO-1 was inhibited by ZPP, the cells survival was sharply decreased compared to that of the control group (P &lt; 0.05).	zinc protoporphyrin	27-30	heme oxygenase 1	Homo sapiens	5-9
21443188-0	2011	tBHQ-induced HO-1 expression is mediated by calcium through regulation of Nrf2 binding to enhancer and polymerase II to promoter region of HO-1.	2-tert-butylhydroquinone	0-4	heme oxygenase 1	Homo sapiens	13-17
21443188-0	2011	tBHQ-induced HO-1 expression is mediated by calcium through regulation of Nrf2 binding to enhancer and polymerase II to promoter region of HO-1.	2-tert-butylhydroquinone	0-4	heme oxygenase 1	Homo sapiens	139-143
21443188-0	2011	tBHQ-induced HO-1 expression is mediated by calcium through regulation of Nrf2 binding to enhancer and polymerase II to promoter region of HO-1.	Calcium	44-51	heme oxygenase 1	Homo sapiens	13-17
21443188-0	2011	tBHQ-induced HO-1 expression is mediated by calcium through regulation of Nrf2 binding to enhancer and polymerase II to promoter region of HO-1.	Calcium	44-51	heme oxygenase 1	Homo sapiens	139-143
21443188-2	2011	The goal of this study was to examine the role of calcium [Ca(2+)] in regulating a well-known phenolic chemopreventive compound tertiary-butylhydroquinone (tBHQ) activation of Nrf2 and induction of Nrf2 downstream target gene heme-oxygenase (HO-1).	Calcium	50-57	heme oxygenase 1	Homo sapiens	242-246
21443188-2	2011	The goal of this study was to examine the role of calcium [Ca(2+)] in regulating a well-known phenolic chemopreventive compound tertiary-butylhydroquinone (tBHQ) activation of Nrf2 and induction of Nrf2 downstream target gene heme-oxygenase (HO-1).	2-Butylhydroquinone	137-154	heme oxygenase 1	Homo sapiens	242-246
21443188-2	2011	The goal of this study was to examine the role of calcium [Ca(2+)] in regulating a well-known phenolic chemopreventive compound tertiary-butylhydroquinone (tBHQ) activation of Nrf2 and induction of Nrf2 downstream target gene heme-oxygenase (HO-1).	2-tert-butylhydroquinone	156-160	heme oxygenase 1	Homo sapiens	242-246
21443188-3	2011	tBHQ alone caused Nrf2 nuclear localization and induced HO-1 mRNA and protein expression in a dose-dependent manner.	2-tert-butylhydroquinone	0-4	heme oxygenase 1	Homo sapiens	56-60
21443188-4	2011	Using RT-PCR and Western blotting, we showed that tBHQ-induced transcription of HO-1 is Ca(2+)-dependent.	2-tert-butylhydroquinone	50-54	heme oxygenase 1	Homo sapiens	80-84
21443188-5	2011	Chelation of [Ca(2+)](ext) or [Ca(2+)](intra) by EGTA or BAPTA attenuated tBHQ-induced HO-1.	Egtazic Acid	49-53	heme oxygenase 1	Homo sapiens	87-91
21443188-5	2011	Chelation of [Ca(2+)](ext) or [Ca(2+)](intra) by EGTA or BAPTA attenuated tBHQ-induced HO-1.	1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid	57-62	heme oxygenase 1	Homo sapiens	87-91
21443188-5	2011	Chelation of [Ca(2+)](ext) or [Ca(2+)](intra) by EGTA or BAPTA attenuated tBHQ-induced HO-1.	2-tert-butylhydroquinone	74-78	heme oxygenase 1	Homo sapiens	87-91
21443188-8	2011	Additionally, EGTA and BAPTA treatments decreased basal nuclear phosphorylation of CREB and decreased tBHQ-induced Nrf2-CBP binding and Nrf2 binding to enhancer as well as polymerase II binding to the promoter of HO-1 gene.	Egtazic Acid	14-18	heme oxygenase 1	Homo sapiens	213-217
21443188-8	2011	Additionally, EGTA and BAPTA treatments decreased basal nuclear phosphorylation of CREB and decreased tBHQ-induced Nrf2-CBP binding and Nrf2 binding to enhancer as well as polymerase II binding to the promoter of HO-1 gene.	1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid	23-28	heme oxygenase 1	Homo sapiens	213-217
21443188-8	2011	Additionally, EGTA and BAPTA treatments decreased basal nuclear phosphorylation of CREB and decreased tBHQ-induced Nrf2-CBP binding and Nrf2 binding to enhancer as well as polymerase II binding to the promoter of HO-1 gene.	2-tert-butylhydroquinone	102-106	heme oxygenase 1	Homo sapiens	213-217
21443188-9	2011	Furthermore, tBHQ in combination with higher [Ca(2+)](ext) augmented HO-1 induction both in vitro and in vivo, indicating that the modulation of [Ca(2+)](int) could be used as an adjuvant to increase the efficacy of chemopreventive agents.	2-tert-butylhydroquinone	13-17	heme oxygenase 1	Homo sapiens	69-73
21443188-10	2011	Taken together, our results indicated that in addition to tBHQ-induced oxidative stress-mediated Nrf2 translocation, HO-1 induction by tBHQ also appears to be dependent on a series of Ca(2+)-regulated mechanisms.	2-tert-butylhydroquinone	135-139	heme oxygenase 1	Homo sapiens	117-121
21518986-4	2011	METHODS AND RESULTS: We generated bitransgenic mice that overexpress human heme oxygenase-1 under doxycycline control in an inducible, lung-specific manner.	Doxycycline	98-109	heme oxygenase 1	Homo sapiens	75-91
21572963-4	2011	Western blot analysis revealed that the expression of the cytoprotective enzyme, heme oxygenase-1 (HO-1), was induced and coincident with the anti-inflammatory action of NaHS.	sodium bisulfide	170-174	heme oxygenase 1	Homo sapiens	81-97
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	54-60	heme oxygenase 1	Homo sapiens	118-122
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	54-60	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	54-60	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	54-60	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	128-134	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	128-134	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	Oxidopamine	128-134	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	244-263	heme oxygenase 1	Homo sapiens	100-116
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	244-263	heme oxygenase 1	Homo sapiens	118-122
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	244-263	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	244-263	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	244-263	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	265-269	heme oxygenase 1	Homo sapiens	100-116
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	265-269	heme oxygenase 1	Homo sapiens	118-122
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	265-269	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	265-269	heme oxygenase 1	Homo sapiens	190-194
21397656-7	2011	In another experiment, exposure of C6 glioma cells to 6-OHDA resulted in an increased expression of heme oxygenase-1 (HO-1) and 6-OHDA-induced cytotoxicity was effectively suppressed by the HO-1 inducer SnCl(2) and aggravated by HO-1 inhibitor zinc protoporphyrin (ZnPP), supporting the cytoprotective role of HO-1.	zinc protoporphyrin	265-269	heme oxygenase 1	Homo sapiens	190-194
21397656-8	2011	To elucidate the molecular mechanism underlying 6-OHDA-mediated HO-1 induction, we have examined the possible involvement of NF-E2-related factor 2 (Nrf2), which plays an important role in the transcriptional regulation of phase II detoxifying and antioxidant enzymes.	Oxidopamine	48-54	heme oxygenase 1	Homo sapiens	64-68
21397656-10	2011	Taken together these findings suggest that HO-1 up-regulation via Nrf2 activation may mediate the cellular adaptive survival response to 6-OHDA-induced nitrosative cell death in C6 glioma cells.	Oxidopamine	137-143	heme oxygenase 1	Homo sapiens	43-47
21248240-3	2011	An additional feature of neuronal oxidative stress is the up-regulation of the inducible enzyme heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Biliverdine	156-166	heme oxygenase 1	Homo sapiens	96-112
21354100-3	2011	The present study aimed at clarifying whether exposure of endothelial cells to pro-inflammatory HOCl-HDL impacts on expression of heme oxygenase-1, a potential rescue pathway against endothelial dysfunction.	Hypochlorous Acid	96-100	heme oxygenase 1	Homo sapiens	130-146
21354100-4	2011	Our findings revealed that HDL modified by HOCl, added as reagent or generated enzymatically, induced phosphorylation of p42/44 mitogen-activated protein kinase, expression of transcription factor early growth response-1 (Egr-1) and enhanced expression of heme oxygenase-1 in human endothelial cells.	Hypochlorous Acid	43-47	heme oxygenase 1	Homo sapiens	256-272
21248240-3	2011	An additional feature of neuronal oxidative stress is the up-regulation of the inducible enzyme heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	ammonium ferrous sulfate	168-174	heme oxygenase 1	Homo sapiens	96-112
21248240-3	2011	An additional feature of neuronal oxidative stress is the up-regulation of the inducible enzyme heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Carbon Monoxide	180-195	heme oxygenase 1	Homo sapiens	96-112
21248240-3	2011	An additional feature of neuronal oxidative stress is the up-regulation of the inducible enzyme heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO).	Carbon Monoxide	197-199	heme oxygenase 1	Homo sapiens	96-112
21414301-0	2011	Celastrol induces expression of heme oxygenase-1 through ROS/Nrf2/ARE signaling in the HaCaT cells.	celastrol	0-9	heme oxygenase 1	Homo sapiens	32-48
21399873-8	2011	Microarray data from cells treated with nifurtimox and TM validated the induction of oxidative stress, as many Nrf2 target genes (HMOX1, GCLM, SLC7A11 and SRXN1) (p&lt;10(-5)) were upregulated.	Nifurtimox	40-50	heme oxygenase 1	Homo sapiens	130-135
21529713-5	2011	Carbon monoxide (CO), a byproduct of heme catabolism by HO-1, prevents further accumulation of circulating free heme after Plasmodium infection, suppressing the pathogenesis of ECM.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	56-60
21529713-5	2011	Carbon monoxide (CO), a byproduct of heme catabolism by HO-1, prevents further accumulation of circulating free heme after Plasmodium infection, suppressing the pathogenesis of ECM.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	56-60
21529713-5	2011	Carbon monoxide (CO), a byproduct of heme catabolism by HO-1, prevents further accumulation of circulating free heme after Plasmodium infection, suppressing the pathogenesis of ECM.	Heme	37-41	heme oxygenase 1	Homo sapiens	56-60
21529713-5	2011	Carbon monoxide (CO), a byproduct of heme catabolism by HO-1, prevents further accumulation of circulating free heme after Plasmodium infection, suppressing the pathogenesis of ECM.	Heme	112-116	heme oxygenase 1	Homo sapiens	56-60
21787712-11	2011	Furthermore, the indirect effect of Cd through HO-1 (genetic polymorphism and prevalence of long GT(n) repeats) and 20-HETE was inconclusive.	Cadmium	36-38	heme oxygenase 1	Homo sapiens	47-51
21315065-0	2011	Lipoic acid ameliorates arsenic trioxide-induced HO-1 expression and oxidative stress in THP-1 monocytes and macrophages.	Thioctic Acid	0-11	heme oxygenase 1	Homo sapiens	49-53
21315065-0	2011	Lipoic acid ameliorates arsenic trioxide-induced HO-1 expression and oxidative stress in THP-1 monocytes and macrophages.	Arsenic Trioxide	24-40	heme oxygenase 1	Homo sapiens	49-53
21315065-3	2011	We found that a non-lethal concentration of arsenic trioxide (1 muM) significantly induced the expression of heme oxygenase-1 (HO-1), a response biomarker to arsenic, without stimulating measurable superoxide production.	Arsenic Trioxide	44-60	heme oxygenase 1	Homo sapiens	109-125
21315065-3	2011	We found that a non-lethal concentration of arsenic trioxide (1 muM) significantly induced the expression of heme oxygenase-1 (HO-1), a response biomarker to arsenic, without stimulating measurable superoxide production.	Arsenic Trioxide	44-60	heme oxygenase 1	Homo sapiens	127-131
21315065-3	2011	We found that a non-lethal concentration of arsenic trioxide (1 muM) significantly induced the expression of heme oxygenase-1 (HO-1), a response biomarker to arsenic, without stimulating measurable superoxide production.	Arsenic	44-51	heme oxygenase 1	Homo sapiens	109-125
21315065-3	2011	We found that a non-lethal concentration of arsenic trioxide (1 muM) significantly induced the expression of heme oxygenase-1 (HO-1), a response biomarker to arsenic, without stimulating measurable superoxide production.	Arsenic	44-51	heme oxygenase 1	Homo sapiens	127-131
21315065-4	2011	Co-treatment of cells with the HO-1 competitive inhibitor zinc protoporphyrin (Znpp) potentiated arsenic-induced cytotoxicity, indicating that HO-1 confers a cytoprotective effect against arsenic toxicity.	zinc protoporphyrin	58-77	heme oxygenase 1	Homo sapiens	31-35
21315065-4	2011	Co-treatment of cells with the HO-1 competitive inhibitor zinc protoporphyrin (Znpp) potentiated arsenic-induced cytotoxicity, indicating that HO-1 confers a cytoprotective effect against arsenic toxicity.	zinc protoporphyrin	58-77	heme oxygenase 1	Homo sapiens	143-147
21315065-4	2011	Co-treatment of cells with the HO-1 competitive inhibitor zinc protoporphyrin (Znpp) potentiated arsenic-induced cytotoxicity, indicating that HO-1 confers a cytoprotective effect against arsenic toxicity.	zinc protoporphyrin	79-83	heme oxygenase 1	Homo sapiens	31-35
21315065-4	2011	Co-treatment of cells with the HO-1 competitive inhibitor zinc protoporphyrin (Znpp) potentiated arsenic-induced cytotoxicity, indicating that HO-1 confers a cytoprotective effect against arsenic toxicity.	zinc protoporphyrin	79-83	heme oxygenase 1	Homo sapiens	143-147
21315065-4	2011	Co-treatment of cells with the HO-1 competitive inhibitor zinc protoporphyrin (Znpp) potentiated arsenic-induced cytotoxicity, indicating that HO-1 confers a cytoprotective effect against arsenic toxicity.	Arsenic	97-104	heme oxygenase 1	Homo sapiens	31-35
21315065-4	2011	Co-treatment of cells with the HO-1 competitive inhibitor zinc protoporphyrin (Znpp) potentiated arsenic-induced cytotoxicity, indicating that HO-1 confers a cytoprotective effect against arsenic toxicity.	Arsenic	97-104	heme oxygenase 1	Homo sapiens	143-147
21414301-0	2011	Celastrol induces expression of heme oxygenase-1 through ROS/Nrf2/ARE signaling in the HaCaT cells.	ros	57-60	heme oxygenase 1	Homo sapiens	32-48
21414301-1	2011	We previously demonstrated that celastrol, a quinone methide triterpenoid derived from the medicinal plant Tripterygium wilfordii, exerts its anti-inflammatory activity through up-regulation of heme oxygenase-1 (HO-1) expression in the keratinocytes.	celastrol	32-41	heme oxygenase 1	Homo sapiens	194-210
21414301-1	2011	We previously demonstrated that celastrol, a quinone methide triterpenoid derived from the medicinal plant Tripterygium wilfordii, exerts its anti-inflammatory activity through up-regulation of heme oxygenase-1 (HO-1) expression in the keratinocytes.	celastrol	32-41	heme oxygenase 1	Homo sapiens	212-216
21414301-2	2011	In this study, we examined the signaling pathways that lead to the up-regulation of HO-1 expression by celastrol.	celastrol	103-112	heme oxygenase 1	Homo sapiens	84-88
21414301-3	2011	In HaCaT cells, celastrol-induced HO-1 expression was dependent on ROS generation.	celastrol	16-25	heme oxygenase 1	Homo sapiens	34-38
21414301-3	2011	In HaCaT cells, celastrol-induced HO-1 expression was dependent on ROS generation.	ros	67-70	heme oxygenase 1	Homo sapiens	34-38
21414301-4	2011	ERK and p38 MAPK were major MAPK pathways responsible for celastrol-induced HO-1 expression.	celastrol	58-67	heme oxygenase 1	Homo sapiens	76-80
21414301-6	2011	Nrf2 knockdown using small interfering RNA (siRNA) inhibited celastrol-induced HO-1 expression.	celastrol	61-70	heme oxygenase 1	Homo sapiens	79-83
21414301-9	2011	Taken together, our results indicate that celastrol can activate the ROS-ERK/p38-Nrf2-ARE signaling cascades leading to the up-regulation of HO-1 which is partly responsible for its anti-inflammatory activity in the keratinocytes.	celastrol	42-51	heme oxygenase 1	Homo sapiens	141-145
21414301-9	2011	Taken together, our results indicate that celastrol can activate the ROS-ERK/p38-Nrf2-ARE signaling cascades leading to the up-regulation of HO-1 which is partly responsible for its anti-inflammatory activity in the keratinocytes.	ros	69-72	heme oxygenase 1	Homo sapiens	141-145
21382015-0	2011	The anti-inflammatory effects of dimethyl fumarate in astrocytes involve glutathione and haem oxygenase-1.	Dimethyl Fumarate	33-50	heme oxygenase 1	Homo sapiens	89-105
21382015-2	2011	DMF modifies glutathione (GSH) levels that can induce expression of the anti-inflammatory protein HO-1 (haem oxygenase-1).	Dimethyl Fumarate	0-3	heme oxygenase 1	Homo sapiens	98-120
21382015-2	2011	DMF modifies glutathione (GSH) levels that can induce expression of the anti-inflammatory protein HO-1 (haem oxygenase-1).	Glutathione	13-24	heme oxygenase 1	Homo sapiens	98-120
21382015-2	2011	DMF modifies glutathione (GSH) levels that can induce expression of the anti-inflammatory protein HO-1 (haem oxygenase-1).	Glutathione	26-29	heme oxygenase 1	Homo sapiens	98-120
21382015-10	2011	In astrocytes, BG-12 increased HO-1 mRNA levels and effects on nitrite levels were blocked by an HO-1 inhibitor.	Nitrites	63-70	heme oxygenase 1	Homo sapiens	97-101
21483629-7	2011	Bach1 and HMOX-1 RNA were also downregulated by LS treatment (P &lt; 0.01), while Nrf2 protein was increased (P &lt; 0.05).	leucylserine	48-50	heme oxygenase 1	Homo sapiens	10-16
21325398-5	2011	Insulin induced HOX-1 expression in a time- and dose-dependent manner, an effect attenuated by selective inhibitors of ERK1/2 (PD98059), Src (4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d] pyrimidine), and c-Jun terminal kinases 1 and 2 (SP600125) pathways.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	127-134	heme oxygenase 1	Homo sapiens	16-21
21544718-7	2011	Heme oxygenase-1 is considered to be an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron and biliverdin, while SIRT1 is the mammalian homologue of the yeast silent information regulator (Sir)-2, which are involved in the suppression of inflammatory mediators or factors that may be used to improve atopy-related symptoms.	Heme	76-80	heme oxygenase 1	Homo sapiens	0-16
21544718-7	2011	Heme oxygenase-1 is considered to be an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron and biliverdin, while SIRT1 is the mammalian homologue of the yeast silent information regulator (Sir)-2, which are involved in the suppression of inflammatory mediators or factors that may be used to improve atopy-related symptoms.	Carbon Monoxide	84-99	heme oxygenase 1	Homo sapiens	0-16
21544718-7	2011	Heme oxygenase-1 is considered to be an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron and biliverdin, while SIRT1 is the mammalian homologue of the yeast silent information regulator (Sir)-2, which are involved in the suppression of inflammatory mediators or factors that may be used to improve atopy-related symptoms.	Iron	106-110	heme oxygenase 1	Homo sapiens	0-16
21544718-7	2011	Heme oxygenase-1 is considered to be an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron and biliverdin, while SIRT1 is the mammalian homologue of the yeast silent information regulator (Sir)-2, which are involved in the suppression of inflammatory mediators or factors that may be used to improve atopy-related symptoms.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	0-16
21168266-6	2011	Celastrol"s ability to modulate the expression of pro-inflammatory cytokines, MHC II, HO-1, iNOS, NF-kappaB, Notch-1, AKT/mTOR, CXCR4, TRAIL receptors DR4 and DR5, CHOP, JNK, VEGF, adhesion molecules, proteasome activity, topoisomerase II, potassium channels, and heat shock response has been reported.	celastrol	0-9	heme oxygenase 1	Homo sapiens	86-90
21325398-5	2011	Insulin induced HOX-1 expression in a time- and dose-dependent manner, an effect attenuated by selective inhibitors of ERK1/2 (PD98059), Src (4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d] pyrimidine), and c-Jun terminal kinases 1 and 2 (SP600125) pathways.	AG 1879	142-206	heme oxygenase 1	Homo sapiens	16-21
21325398-5	2011	Insulin induced HOX-1 expression in a time- and dose-dependent manner, an effect attenuated by selective inhibitors of ERK1/2 (PD98059), Src (4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d] pyrimidine), and c-Jun terminal kinases 1 and 2 (SP600125) pathways.	pyrazolanthrone	245-253	heme oxygenase 1	Homo sapiens	16-21
21198350-0	2011	Association of (GT)n repeats promoter polymorphism of heme oxygenase-1 gene with serum bilirubin levels in healthy Indian adults.	Bilirubin	87-96	heme oxygenase 1	Homo sapiens	54-70
21198350-1	2011	AIM: The present study was undertaken to investigate a length polymorphism of (GT)n repeats of the heme oxygenase-1 (HMOX-1) gene and its association with serum bilirubin levels in apparently healthy adults.	Bilirubin	161-170	heme oxygenase 1	Homo sapiens	99-115
21198350-1	2011	AIM: The present study was undertaken to investigate a length polymorphism of (GT)n repeats of the heme oxygenase-1 (HMOX-1) gene and its association with serum bilirubin levels in apparently healthy adults.	Bilirubin	161-170	heme oxygenase 1	Homo sapiens	117-123
21238556-0	2011	Upregulation of heme oxygenase-1 as an adaptive mechanism for protection against crotonaldehyde in human umbilical vein endothelial cells.	2-butenal	81-95	heme oxygenase 1	Homo sapiens	16-32
21462044-5	2011	HO-1 is an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron, and biliverdin, all of which are involved in the suppression of inflammatory mediators.	Heme	47-51	heme oxygenase 1	Homo sapiens	0-4
21462044-5	2011	HO-1 is an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron, and biliverdin, all of which are involved in the suppression of inflammatory mediators.	Carbon Monoxide	55-70	heme oxygenase 1	Homo sapiens	0-4
21462044-5	2011	HO-1 is an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron, and biliverdin, all of which are involved in the suppression of inflammatory mediators.	Iron	77-81	heme oxygenase 1	Homo sapiens	0-4
21462044-5	2011	HO-1 is an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron, and biliverdin, all of which are involved in the suppression of inflammatory mediators.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	0-4
21660147-6	2011	Moreover, cilostazol increased HO-1 protein and mRNA expression.	Cilostazol	10-20	heme oxygenase 1	Homo sapiens	31-35
21660147-7	2011	Cilostazol-induced HO-1 induction was markedly attenuated not only by ZnPP but also by copper-protoporphyrin IX (CuPP).	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	19-23
21660147-7	2011	Cilostazol-induced HO-1 induction was markedly attenuated not only by ZnPP but also by copper-protoporphyrin IX (CuPP).	Zinc protoporphyrin	70-74	heme oxygenase 1	Homo sapiens	19-23
21660147-7	2011	Cilostazol-induced HO-1 induction was markedly attenuated not only by ZnPP but also by copper-protoporphyrin IX (CuPP).	copper protoporphyrin IX	87-111	heme oxygenase 1	Homo sapiens	19-23
21660147-7	2011	Cilostazol-induced HO-1 induction was markedly attenuated not only by ZnPP but also by copper-protoporphyrin IX (CuPP).	cupp	113-117	heme oxygenase 1	Homo sapiens	19-23
21660147-8	2011	In an assay measuring peroxisome proliferator-activated receptor-gamma (PPAR-gamma) transcription activity, cilostazol directly increased PPAR-gamma transcriptional activity which was completely abolished by HO-1 inhibitor.	Cilostazol	108-118	heme oxygenase 1	Homo sapiens	208-212
21660147-9	2011	Furthermore, increased PPAR-gamma activity by cilostazol and rosiglitazone was completely abolished in cells transfected with HO-1 siRNA.	Cilostazol	46-56	heme oxygenase 1	Homo sapiens	126-130
21660147-9	2011	Furthermore, increased PPAR-gamma activity by cilostazol and rosiglitazone was completely abolished in cells transfected with HO-1 siRNA.	Rosiglitazone	61-74	heme oxygenase 1	Homo sapiens	126-130
21660147-10	2011	Taken together, these results indicate that cilostazol up-regulates HO-1 and protects cells against TNF-alpha-induced endothelial cytotoxicity via a PPAR-gamma-dependent pathway.	Cilostazol	44-54	heme oxygenase 1	Homo sapiens	68-72
21146245-7	2011	Indeed, in CYP2E1-expressing HepG2 cells exposed to ethanol, the expression of ISR target genes (HMOX-1, GCLC, AsnS, IGFBP-1, GADD34,CHOP, ATF3, CHAC1) was induced.	Ethanol	52-59	heme oxygenase 1	Homo sapiens	97-103
21660147-0	2011	HO-1 Induced by Cilostazol Protects Against TNF-alpha-associated Cytotoxicity via a PPAR-gamma-dependent Pathway in Human Endothelial Cells.	Cilostazol	16-26	heme oxygenase 1	Homo sapiens	0-4
21660147-2	2011	In our previous study, cilostazol was found to increase the expression of the antioxidant enzyme heme oxygenase-1 (HO-1) in synovial cells.	Cilostazol	23-33	heme oxygenase 1	Homo sapiens	97-113
21660147-2	2011	In our previous study, cilostazol was found to increase the expression of the antioxidant enzyme heme oxygenase-1 (HO-1) in synovial cells.	Cilostazol	23-33	heme oxygenase 1	Homo sapiens	115-119
21660147-3	2011	Thus, the present study was undertaken to examine whether cilostazol is able to counteract tumor necrosis factor-alpha (TNF-alpha)-induced cell death in endothelial cells via the induction of HO-1 expression.	Cilostazol	58-68	heme oxygenase 1	Homo sapiens	192-196
21660147-5	2011	Pretreatment with cilostazol markedly reduced TNF-alpha-induced viability loss in the HUVECs, which was reversed by zinc protoporphyrine IX (ZnPP), an inhibitor of HO-1.	Cilostazol	18-28	heme oxygenase 1	Homo sapiens	164-168
21660147-5	2011	Pretreatment with cilostazol markedly reduced TNF-alpha-induced viability loss in the HUVECs, which was reversed by zinc protoporphyrine IX (ZnPP), an inhibitor of HO-1.	zinc protoporphyrine ix	116-139	heme oxygenase 1	Homo sapiens	164-168
21660147-5	2011	Pretreatment with cilostazol markedly reduced TNF-alpha-induced viability loss in the HUVECs, which was reversed by zinc protoporphyrine IX (ZnPP), an inhibitor of HO-1.	Zinc protoporphyrin	141-145	heme oxygenase 1	Homo sapiens	164-168
21172416-7	2011	Transcriptomics, western blot and immunofluorescence showed an induction of both HO-1 and NQO1 with Cd and Diq exposure, but not with CsA treatment.	Cadmium	100-102	heme oxygenase 1	Homo sapiens	81-85
21172416-7	2011	Transcriptomics, western blot and immunofluorescence showed an induction of both HO-1 and NQO1 with Cd and Diq exposure, but not with CsA treatment.	Diquat	107-110	heme oxygenase 1	Homo sapiens	81-85
21172416-9	2011	siRNA knock down of HO-1, but not NQO1, enhanced Cd induced H(2)O(2) production and Cd induced toxicity.	Cadmium	49-51	heme oxygenase 1	Homo sapiens	20-24
21172416-9	2011	siRNA knock down of HO-1, but not NQO1, enhanced Cd induced H(2)O(2) production and Cd induced toxicity.	Hydrogen Peroxide	60-68	heme oxygenase 1	Homo sapiens	20-24
21172416-9	2011	siRNA knock down of HO-1, but not NQO1, enhanced Cd induced H(2)O(2) production and Cd induced toxicity.	Cadmium	84-86	heme oxygenase 1	Homo sapiens	20-24
21481317-3	2011	The effect of low dose propofol on expression of heme oxygenase-1 (HO-1) was confirmed by Real-time quantitative PCR.	Propofol	23-31	heme oxygenase 1	Homo sapiens	49-65
21481317-3	2011	The effect of low dose propofol on expression of heme oxygenase-1 (HO-1) was confirmed by Real-time quantitative PCR.	Propofol	23-31	heme oxygenase 1	Homo sapiens	67-71
21481317-5	2011	And low dose propofol increased the expression of HO-1 mRNA in a dose-dependment manner.	Propofol	13-21	heme oxygenase 1	Homo sapiens	50-54
21481317-6	2011	CONCLUSION: Low dose propofol affects the biological behavior of esophageal squamous cell carcinoma cell line Eca109, which has a relationship with increasing the expression of HO-1.	Propofol	21-29	heme oxygenase 1	Homo sapiens	177-181
21352808-4	2011	Notably, GW501516 up-regulated the expression of antioxidant genes, such as glutathione peroxidase 1, thioredoxin 1, manganese superoxide dismutase and heme oxygenase 1.	GW 501516	9-17	heme oxygenase 1	Homo sapiens	152-168
21361338-3	2011	Most of the TCEs having two different kinds of nonenolizable cyano enones in rings A and C are highly potent suppressors of induction of inducible nitric oxide synthase stimulated with interferon-gamma and are highly potent inducers of the cytoprotective enzymes heme oxygenase-1 and NAD(P)H:quinone oxidoreductase-1.	tces	12-16	heme oxygenase 1	Homo sapiens	263-316
21361338-3	2011	Most of the TCEs having two different kinds of nonenolizable cyano enones in rings A and C are highly potent suppressors of induction of inducible nitric oxide synthase stimulated with interferon-gamma and are highly potent inducers of the cytoprotective enzymes heme oxygenase-1 and NAD(P)H:quinone oxidoreductase-1.	cyano enones	61-73	heme oxygenase 1	Homo sapiens	263-316
21238556-5	2011	In this study, we examined the effects of crotonaldehyde on HO-1 induction and determined the signaling pathways in human umbilical vein endothelial cells (HUVECs).	2-butenal	42-56	heme oxygenase 1	Homo sapiens	60-64
21238556-6	2011	Inhibition of the protein kinase C-delta (PKC-delta) and p38 pathways resulted in significant blockage of crotonaldehyde-mediated HO-1 induction.	2-butenal	106-120	heme oxygenase 1	Homo sapiens	130-134
21238556-7	2011	Crotonaldehyde treatment caused a dramatic increase in translocation of NF-E2 related factor (Nrf2), leading to induction of HO-1.	2-butenal	0-14	heme oxygenase 1	Homo sapiens	125-129
21238556-8	2011	In addition, small interfering RNA knockdown of Nrf2 and treatment with the specific HO-1 inhibitor ZnPP exhibited an obvious increase of apoptosis of crotonaldehyde-treated HUVECs.	zinc protoporphyrin	100-104	heme oxygenase 1	Homo sapiens	85-89
21238556-8	2011	In addition, small interfering RNA knockdown of Nrf2 and treatment with the specific HO-1 inhibitor ZnPP exhibited an obvious increase of apoptosis of crotonaldehyde-treated HUVECs.	2-butenal	151-165	heme oxygenase 1	Homo sapiens	85-89
21238556-9	2011	Taken together, our results demonstrated that crotonaldehyde-induced HO-1 expression is mediated by the PKC-delta-p38 MAPK-Nrf2-HO-1 pathway in HUVECs, which is an adaptive response to oxidative stress.	2-butenal	46-60	heme oxygenase 1	Homo sapiens	69-73
21238556-9	2011	Taken together, our results demonstrated that crotonaldehyde-induced HO-1 expression is mediated by the PKC-delta-p38 MAPK-Nrf2-HO-1 pathway in HUVECs, which is an adaptive response to oxidative stress.	2-butenal	46-60	heme oxygenase 1	Homo sapiens	128-132
21185934-3	2011	Under hypoxia, the expression of major iron homeostasis genes including transferrin, transferrin receptor, ceruloplasmin, and heme oxygenase-1 is activated by hypoxia-inducible factors to provide increased iron availability for erythropoiesis in an attempt to enhance oxygen uptake and delivery to hypoxic cells.	Iron	39-43	heme oxygenase 1	Homo sapiens	126-142
21185934-3	2011	Under hypoxia, the expression of major iron homeostasis genes including transferrin, transferrin receptor, ceruloplasmin, and heme oxygenase-1 is activated by hypoxia-inducible factors to provide increased iron availability for erythropoiesis in an attempt to enhance oxygen uptake and delivery to hypoxic cells.	Iron	206-210	heme oxygenase 1	Homo sapiens	126-142
21374664-7	2011	IL-10 and heme oxygenase-1 (HO-1) were up-regulated in patients receiving norfloxacin and correlated with norfloxacin in a concentration-dependent manner, whereas proinflammatory inducible nitric oxide synthase, cyclooxygenase-2, and nuclear factor-kappaB behaved inversely.	Norfloxacin	74-85	heme oxygenase 1	Homo sapiens	10-26
21307647-0	2011	Lipopolysaccaride induces autophagic signaling in macrophages via a TLR4, heme oxygenase-1 dependent pathway.	lipopolysaccaride	0-17	heme oxygenase 1	Homo sapiens	74-90
21374664-7	2011	IL-10 and heme oxygenase-1 (HO-1) were up-regulated in patients receiving norfloxacin and correlated with norfloxacin in a concentration-dependent manner, whereas proinflammatory inducible nitric oxide synthase, cyclooxygenase-2, and nuclear factor-kappaB behaved inversely.	Norfloxacin	74-85	heme oxygenase 1	Homo sapiens	28-32
21374664-7	2011	IL-10 and heme oxygenase-1 (HO-1) were up-regulated in patients receiving norfloxacin and correlated with norfloxacin in a concentration-dependent manner, whereas proinflammatory inducible nitric oxide synthase, cyclooxygenase-2, and nuclear factor-kappaB behaved inversely.	Norfloxacin	106-117	heme oxygenase 1	Homo sapiens	10-26
21374664-7	2011	IL-10 and heme oxygenase-1 (HO-1) were up-regulated in patients receiving norfloxacin and correlated with norfloxacin in a concentration-dependent manner, whereas proinflammatory inducible nitric oxide synthase, cyclooxygenase-2, and nuclear factor-kappaB behaved inversely.	Norfloxacin	106-117	heme oxygenase 1	Homo sapiens	28-32
20836698-8	2011	Lentiviral transduction with the VECAD-HO-1 construct attenuated the increase in blood pressure (p &lt; 0.05), improved vascular relaxation, increased plasma adiponectin, and prevented the elevation in urinary protein and plasma creatinine in Ang II-treated rats.	Creatinine	229-239	heme oxygenase 1	Homo sapiens	39-43
21374664-10	2011	Neutrophilic in vitro assays showed that the effect of LPS on proinflammatory mediator levels in the presence of norfloxacin was abrogated by significantly increasing IL-10 and HO-1 expression.	Norfloxacin	113-124	heme oxygenase 1	Homo sapiens	177-181
21374664-13	2011	CONCLUSION: Although the described association does not necessarily mean causality, an IL-10-mediated HO-1-induced anti-inflammatory mechanism is present in patients with cirrhosis receiving norfloxacin, that is directly associated with cell-modulating events in these patients.	Norfloxacin	191-202	heme oxygenase 1	Homo sapiens	102-106
21259326-4	2011	In this study, we demonstrate that MGF24-induced heme oxygenase-1 up-regulation is dependent on activation of protein kinase Cepsilon and NF-E2-related factor-2 (Nrf2).	mgf24	35-40	heme oxygenase 1	Homo sapiens	49-65
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Heme	73-77	heme oxygenase 1	Homo sapiens	0-16
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Heme	73-77	heme oxygenase 1	Homo sapiens	18-22
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Biliverdine	105-115	heme oxygenase 1	Homo sapiens	0-16
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Biliverdine	105-115	heme oxygenase 1	Homo sapiens	18-22
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Iron	122-126	heme oxygenase 1	Homo sapiens	0-16
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Iron	122-126	heme oxygenase 1	Homo sapiens	18-22
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	0-16
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	18-22
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Carbon Monoxide	148-150	heme oxygenase 1	Homo sapiens	0-16
21373265-1	2011	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO).	Carbon Monoxide	148-150	heme oxygenase 1	Homo sapiens	18-22
21373265-6	2011	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by ischemia-reperfusion, indomethacin, lipopolysaccharide-associated sepsis, trinitrobenzene sulfonic acid, and dextran sulfate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the gastrointestinal tract.	Indomethacin	155-167	heme oxygenase 1	Homo sapiens	45-49
21373265-6	2011	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by ischemia-reperfusion, indomethacin, lipopolysaccharide-associated sepsis, trinitrobenzene sulfonic acid, and dextran sulfate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the gastrointestinal tract.	Trinitrobenzenesulfonic Acid	207-236	heme oxygenase 1	Homo sapiens	45-49
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Biliverdine	120-130	heme oxygenase 1	Homo sapiens	18-22
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Bilirubin	131-140	heme oxygenase 1	Homo sapiens	0-16
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Bilirubin	131-140	heme oxygenase 1	Homo sapiens	18-22
20563825-3	2011	Astroglial induction of the Hmox1 gene by beta-amyloid, pro-inflammatory cytokines and hydrogen peroxide promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergy failure amply documented in AD-affected neural tissues.	Hydrogen Peroxide	87-104	heme oxygenase 1	Homo sapiens	28-33
20563825-3	2011	Astroglial induction of the Hmox1 gene by beta-amyloid, pro-inflammatory cytokines and hydrogen peroxide promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergy failure amply documented in AD-affected neural tissues.	Iron	161-165	heme oxygenase 1	Homo sapiens	28-33
20563825-3	2011	Astroglial induction of the Hmox1 gene by beta-amyloid, pro-inflammatory cytokines and hydrogen peroxide promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergy failure amply documented in AD-affected neural tissues.	Iron	232-236	heme oxygenase 1	Homo sapiens	28-33
20563825-4	2011	Glial HO-1 expression may also impact cell survival and neuroplasticity in AD by modulating brain sterol/oxysterol metabolism and the degradation of tau by the proteasome.	Sterols	98-104	heme oxygenase 1	Homo sapiens	6-10
20563825-4	2011	Glial HO-1 expression may also impact cell survival and neuroplasticity in AD by modulating brain sterol/oxysterol metabolism and the degradation of tau by the proteasome.	Oxysterols	105-114	heme oxygenase 1	Homo sapiens	6-10
20563825-5	2011	Suppression of glial HO-1 activity by pharmacological or other means may confer neuroprotection in AD by curtailing iron-mediated neurotoxicity.	Iron	116-120	heme oxygenase 1	Homo sapiens	21-25
21062351-9	2011	The capacity of melatonin to modulate Nrf2 pathway was associated with increased heme oxygenase-1 (HO-1) expression, which strengthens antioxidant defense.	Melatonin	16-25	heme oxygenase 1	Homo sapiens	81-97
21373265-6	2011	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by ischemia-reperfusion, indomethacin, lipopolysaccharide-associated sepsis, trinitrobenzene sulfonic acid, and dextran sulfate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the gastrointestinal tract.	Dextran Sulfate	242-264	heme oxygenase 1	Homo sapiens	45-49
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Heme	78-82	heme oxygenase 1	Homo sapiens	0-16
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Heme	78-82	heme oxygenase 1	Homo sapiens	18-22
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	ferrous iron	86-98	heme oxygenase 1	Homo sapiens	0-16
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	ferrous iron	86-98	heme oxygenase 1	Homo sapiens	18-22
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Carbon Monoxide	100-115	heme oxygenase 1	Homo sapiens	0-16
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Carbon Monoxide	100-115	heme oxygenase 1	Homo sapiens	18-22
20563825-1	2011	Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders.	Biliverdine	120-130	heme oxygenase 1	Homo sapiens	0-16
21073519-0	2011	Melatonin synergistically increases resveratrol-induced heme oxygenase-1 expression through the inhibition of ubiquitin-dependent proteasome pathway: a possible role in neuroprotection.	Melatonin	0-9	heme oxygenase 1	Homo sapiens	56-72
21073519-0	2011	Melatonin synergistically increases resveratrol-induced heme oxygenase-1 expression through the inhibition of ubiquitin-dependent proteasome pathway: a possible role in neuroprotection.	Resveratrol	36-47	heme oxygenase 1	Homo sapiens	56-72
21073519-4	2011	We assessed whether the co-administration of melatonin and RSV shows synergistic effects in terms of their neuroprotective properties through HO-1.	Melatonin	45-54	heme oxygenase 1	Homo sapiens	142-146
21073519-4	2011	We assessed whether the co-administration of melatonin and RSV shows synergistic effects in terms of their neuroprotective properties through HO-1.	Resveratrol	59-62	heme oxygenase 1	Homo sapiens	142-146
21073519-5	2011	RSV significantly increased the expression levels of HO-1 protein in a concentration-dependent manner both in primary cortical neurons and in astrocytes, while melatonin per se did not.	Resveratrol	0-3	heme oxygenase 1	Homo sapiens	53-57
21073519-6	2011	Melatonin + RSV showed a synergistic increase in the expression levels of HO-1 protein but not in the HO-1 mRNA level compared to either melatonin or RSV alone, which is mediated by the activation of PI3K-Akt pathway.	Melatonin	0-9	heme oxygenase 1	Homo sapiens	74-78
21073519-6	2011	Melatonin + RSV showed a synergistic increase in the expression levels of HO-1 protein but not in the HO-1 mRNA level compared to either melatonin or RSV alone, which is mediated by the activation of PI3K-Akt pathway.	Resveratrol	12-15	heme oxygenase 1	Homo sapiens	74-78
21073519-6	2011	Melatonin + RSV showed a synergistic increase in the expression levels of HO-1 protein but not in the HO-1 mRNA level compared to either melatonin or RSV alone, which is mediated by the activation of PI3K-Akt pathway.	Resveratrol	12-15	heme oxygenase 1	Homo sapiens	102-106
21259326-5	2011	MGF24 induces nuclear translocation of Nrf2, and siRNA knockdown of Nrf2 or of heme oxygenase-1 prevents MGF24-induced heme oxygenase-1 up-regulation and neuroprotection of SH-SY5Y cells against 6-hydroxydopamine-induced cell death.	Oxidopamine	195-212	heme oxygenase 1	Homo sapiens	79-95
21073519-8	2011	The blockade of HO-1 induction by shRNA attenuated HO-1 induction by melatonin + RSV and hindered the neuroprotective effects against oxidative stress induced by H(2) O(2) .	Melatonin	69-78	heme oxygenase 1	Homo sapiens	16-20
21073519-8	2011	The blockade of HO-1 induction by shRNA attenuated HO-1 induction by melatonin + RSV and hindered the neuroprotective effects against oxidative stress induced by H(2) O(2) .	Melatonin	69-78	heme oxygenase 1	Homo sapiens	51-55
21073519-8	2011	The blockade of HO-1 induction by shRNA attenuated HO-1 induction by melatonin + RSV and hindered the neuroprotective effects against oxidative stress induced by H(2) O(2) .	Resveratrol	81-84	heme oxygenase 1	Homo sapiens	16-20
21073519-8	2011	The blockade of HO-1 induction by shRNA attenuated HO-1 induction by melatonin + RSV and hindered the neuroprotective effects against oxidative stress induced by H(2) O(2) .	Resveratrol	81-84	heme oxygenase 1	Homo sapiens	51-55
21073519-9	2011	The treatment of MG132 + RSV mimicked the effects of melatonin + RSV, and melatonin + RSV inhibited ubiquitination of HO-1.	Melatonin	74-83	heme oxygenase 1	Homo sapiens	118-122
21073519-10	2011	These data suggest that melatonin potentiates the neuroprotective effect of RSV against oxidative injury, by enhancing HO-1 induction through inhibiting ubiquitination-dependent proteasome pathway, which may provide an effective means to treat neurodegenerative disorders.	Melatonin	24-33	heme oxygenase 1	Homo sapiens	119-123
21073519-10	2011	These data suggest that melatonin potentiates the neuroprotective effect of RSV against oxidative injury, by enhancing HO-1 induction through inhibiting ubiquitination-dependent proteasome pathway, which may provide an effective means to treat neurodegenerative disorders.	Resveratrol	76-79	heme oxygenase 1	Homo sapiens	119-123
21259326-5	2011	MGF24 induces nuclear translocation of Nrf2, and siRNA knockdown of Nrf2 or of heme oxygenase-1 prevents MGF24-induced heme oxygenase-1 up-regulation and neuroprotection of SH-SY5Y cells against 6-hydroxydopamine-induced cell death.	Oxidopamine	195-212	heme oxygenase 1	Homo sapiens	119-135
21259326-9	2011	Taken together, these results demonstrate that PKC activity is needed for MGF24"s activation of Nrf2, which in turn increases heme oxygenase-1 expression, a critical event in mediating MGF24"s neuroprotection against 6-hydroxydopamine-induced apoptosis.	Oxidopamine	217-234	heme oxygenase 1	Homo sapiens	126-142
21206978-6	2011	In addition, we administered an HO-1 inhibitor, zinc protoporphyrin IX, to mice with subcutaneous T24 tumors to assess the modulation of angiogenesis in solid tumors in vivo.	zinc protoporphyrin	48-70	heme oxygenase 1	Homo sapiens	32-36
20938987-0	2011	Curcumin induces heme oxygenase-1 in normal human skin fibroblasts through redox signaling: relevance for anti-aging intervention.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	17-33
20938987-2	2011	METHODS AND RESULTS: Early passage young human skin fibroblasts treated with low doses of curcumin (below 20 muM) showed a time- and concentration-dependent induction of heme oxygenase-1 (HO-1), followed by compensatory increase in glutathione-S-transferase activity, GSH levels and GSH/GSSG ratio.	Curcumin	90-98	heme oxygenase 1	Homo sapiens	170-186
20938987-2	2011	METHODS AND RESULTS: Early passage young human skin fibroblasts treated with low doses of curcumin (below 20 muM) showed a time- and concentration-dependent induction of heme oxygenase-1 (HO-1), followed by compensatory increase in glutathione-S-transferase activity, GSH levels and GSH/GSSG ratio.	Curcumin	90-98	heme oxygenase 1	Homo sapiens	188-192
20938987-5	2011	The use of the antioxidant N-acetyl cysteine prevented the induction of HO-1 by curcumin.	Acetylcysteine	27-44	heme oxygenase 1	Homo sapiens	72-76
20938987-5	2011	The use of the antioxidant N-acetyl cysteine prevented the induction of HO-1 by curcumin.	Curcumin	80-88	heme oxygenase 1	Homo sapiens	72-76
20938987-6	2011	Pharmacological inhibition of phosphatidylinositol 3-kinase, but not other kinases, significantly prevented curcumin-induced HO-1 levels, which was corroborated by the induction of phospho-Akt levels by curcumin.	Curcumin	108-116	heme oxygenase 1	Homo sapiens	125-129
20938987-7	2011	Late passage senescent cells already had higher HO-1 levels, and further induction of HO-1 by curcumin was considerably impaired.	Curcumin	94-102	heme oxygenase 1	Homo sapiens	86-90
21281968-8	2011	NaAs systematically and significantly up-regulated a set of 35 genes, including several immune and stress genes, such as IL13, granulocyte-macrophage colony stimulating factor, lymphotoxin alpha and heme oxygenase-1 (HO-1).	naas	0-4	heme oxygenase 1	Homo sapiens	199-215
21281968-8	2011	NaAs systematically and significantly up-regulated a set of 35 genes, including several immune and stress genes, such as IL13, granulocyte-macrophage colony stimulating factor, lymphotoxin alpha and heme oxygenase-1 (HO-1).	naas	0-4	heme oxygenase 1	Homo sapiens	217-221
21281968-9	2011	Up-regulation of HO-1, a stress and immunosuppressive protein, was rapidly detectable, both in T cells and in PBMC treated with NaAs.	naas	128-132	heme oxygenase 1	Homo sapiens	17-21
21281968-11	2011	Our findings demonstrate that, at least in vitro, inorganic arsenic acts directly on human T cells and impairs their activity, probably independently of HO-1 expression and monocyte-related accessory signals.	Arsenic	60-67	heme oxygenase 1	Homo sapiens	153-157
21206978-9	2011	Hypoxic conditions induced upregulation of HO-1, VEGF, HIF-1alpha, HIF-2alpha, and COX-2 in T24 cells and increased VEGF secretion, which could be suppressed by zinc protoporphyrin IX.	zinc protoporphyrin	161-183	heme oxygenase 1	Homo sapiens	43-47
21319354-8	2011	The HO-1 expression in the PF group was significantly higher than that in MF group at the corresponding time points (p &lt; 0.05, respectively).	pyrazofurin	27-29	heme oxygenase 1	Homo sapiens	4-8
21362092-3	2011	Cobalt protoporphyrin induced expression of HO-1 protein with maximal levels attaining a plateau at 48 hours.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	44-48
21148661-2	2011	The aim of this study was to evaluate the role of HO-1 in the regulation of insulin resistance and glucose tolerance in women with polycystic ovary syndrome (PCOS).	Glucose	99-106	heme oxygenase 1	Homo sapiens	50-54
21362092-5	2011	Similarly, expression of HO-1 by introduction of a recombinant plasmid also showed a resistance to deoxycholate-induced apoptosis.	Deoxycholic Acid	99-111	heme oxygenase 1	Homo sapiens	25-29
21144877-0	2011	Induction of apoptosis in human leukemia cells through the production of reactive oxygen species and activation of HMOX1 and Noxa by benzene, toluene, and o-xylene.	Benzene	133-140	heme oxygenase 1	Homo sapiens	115-120
21144877-0	2011	Induction of apoptosis in human leukemia cells through the production of reactive oxygen species and activation of HMOX1 and Noxa by benzene, toluene, and o-xylene.	Toluene	142-149	heme oxygenase 1	Homo sapiens	115-120
21144877-0	2011	Induction of apoptosis in human leukemia cells through the production of reactive oxygen species and activation of HMOX1 and Noxa by benzene, toluene, and o-xylene.	2-xylene	155-163	heme oxygenase 1	Homo sapiens	115-120
21106538-1	2011	Heme oxygenase-1 (HO-1) enzyme plays a critical role in metabolizing the excess heme generated during hemolysis.	Heme	80-84	heme oxygenase 1	Homo sapiens	0-16
21106538-1	2011	Heme oxygenase-1 (HO-1) enzyme plays a critical role in metabolizing the excess heme generated during hemolysis.	Heme	80-84	heme oxygenase 1	Homo sapiens	18-22
21144877-7	2011	Real-time RT-PCR revealed increased HMOX1 and Noxa expression in BZ-, TOL-, and o-XY-treated HL-60 cells, confirming the results of previous microarray analyses.	Benzene	65-67	heme oxygenase 1	Homo sapiens	36-41
21144877-7	2011	Real-time RT-PCR revealed increased HMOX1 and Noxa expression in BZ-, TOL-, and o-XY-treated HL-60 cells, confirming the results of previous microarray analyses.	2-xylene	80-84	heme oxygenase 1	Homo sapiens	36-41
21148661-9	2011	Serum insulin and glucose levels and BMI showed a significant negative correlation with the level of HO-1 (P&lt; 0.05).	Glucose	18-25	heme oxygenase 1	Homo sapiens	101-105
20888844-8	2011	Sulforaphane stimulation for 4 h induced an Nrf2-dependent increase of Nqo1 and Hmox1 mRNA that remained elevated for 24 h, and the corresponding proteins remained elevated for over 48 h. In addition, peroxide-clearing activity and the levels of glutathione were elevated for more than 20 h after stimulation for 4 h with sulforaphane, resulting in an increased resistance to superoxide-induced cell damage.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	80-85
21148661-10	2011	CONCLUSIONS: Our results suggest that the HO-1-adiponectin axis may be associated with the regulation of insulin resistance and glucose intolerance in women with PCOS.	Glucose	128-135	heme oxygenase 1	Homo sapiens	42-46
21099244-5	2011	Additionally, depletion of BLVRA reduced the H2O2-dependent induction of heme oxygenase-1 (HO-1) in young HDFs, but not in senescent cells, suggesting an aging-dependent differential modulation of responses to oxidative stress.	Hydrogen Peroxide	45-49	heme oxygenase 1	Homo sapiens	73-89
21262447-5	2011	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	72-87	heme oxygenase 1	Homo sapiens	29-45
21262447-5	2011	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	72-87	heme oxygenase 1	Homo sapiens	47-51
21262447-5	2011	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	29-45
21262447-5	2011	An anti-inflammatory enzyme, heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO), inhibit sFlt-1 and sEng release.	Carbon Monoxide	89-91	heme oxygenase 1	Homo sapiens	47-51
21199573-0	2011	Ascorbic acid partly antagonizes resveratrol mediated heme oxygenase-1 but not paraoxonase-1 induction in cultured hepatocytes - role of the redox-regulated transcription factor Nrf2.	Ascorbic Acid	0-13	heme oxygenase 1	Homo sapiens	54-70
21076374-4	2011	OBJECTIVE: To test whether preconditioning with fenoldopam (FD) induce HO-1 and protect kidneys against cold storage injury and whether HO-1 plays a role in protection.	Fenoldopam	48-58	heme oxygenase 1	Homo sapiens	71-75
21081499-1	2011	Heme oxygenase-1 (HO-1) degrades heme and protects cells from oxidative challenge.	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
21081499-2	2011	This antioxidant activity is thought to result from the HO-1 enzymatic activity, manifested by a decrease in the concentration of the pro-oxidant substrate heme, and an increase in the antioxidant product bilirubin.	Heme	156-160	heme oxygenase 1	Homo sapiens	56-60
21081499-2	2011	This antioxidant activity is thought to result from the HO-1 enzymatic activity, manifested by a decrease in the concentration of the pro-oxidant substrate heme, and an increase in the antioxidant product bilirubin.	Bilirubin	205-214	heme oxygenase 1	Homo sapiens	56-60
21171611-12	2011	The induction of oxidative stress and inflammatory responses (evaluated by HO-1 mRNA expression and TNF-alpha mRNA and protein expression) revealed a reduction in inflammogenicity upon iron loading and a more inflammogenic potency of DQ12 ascribed to undissociated SiOH interacting via H-bonding with cell membrane components.	Iron	185-189	heme oxygenase 1	Homo sapiens	75-79
21199573-6	2011	Heme oxygenase-1 induction by resveratrol was accompanied by an increase in Nrf2 transactivation.	Resveratrol	30-41	heme oxygenase 1	Homo sapiens	0-16
21199573-7	2011	Resveratrol mediated Nrf2 transactivation as well as heme oxygenase-1 induction were partly antagonized by 1000 mumol/l ascorbic acid.	Ascorbic Acid	120-133	heme oxygenase 1	Homo sapiens	53-69
21199573-0	2011	Ascorbic acid partly antagonizes resveratrol mediated heme oxygenase-1 but not paraoxonase-1 induction in cultured hepatocytes - role of the redox-regulated transcription factor Nrf2.	Resveratrol	33-44	heme oxygenase 1	Homo sapiens	54-70
21199573-9	2011	Addition of resveratrol to the cell culture medium produced relatively low levels of hydrogen peroxide which may be a positive hormetic redox-signal for Nrf2 dependent gene expression thereby driving heme oxygenase-1 induction.	Resveratrol	12-23	heme oxygenase 1	Homo sapiens	200-216
21199573-3	2011	METHODS: The antioxidant enzymes heme oxygenase-1 and paraoxonase-1 were analysed for their mRNA and protein levels in HUH7 liver cells treated with 10 and 25 mumol/l resveratrol in the absence and presence of 100 and 1000 mumol/l ascorbic acid.	Resveratrol	167-178	heme oxygenase 1	Homo sapiens	33-49
21199573-9	2011	Addition of resveratrol to the cell culture medium produced relatively low levels of hydrogen peroxide which may be a positive hormetic redox-signal for Nrf2 dependent gene expression thereby driving heme oxygenase-1 induction.	Hydrogen Peroxide	85-102	heme oxygenase 1	Homo sapiens	200-216
21199573-5	2011	RESULTS: Here, we demonstrate that resveratrol induces the antioxidant enzymes heme oxygenase-1 and paraoxonase-1 in cultured hepatocytes.	Resveratrol	35-46	heme oxygenase 1	Homo sapiens	79-95
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Heme	51-55	heme oxygenase 1	Homo sapiens	0-16
22162689-0	2011	Heme Oxygenase-1: A Critical Link between Iron Metabolism, Erythropoiesis, and Development.	Iron	42-46	heme oxygenase 1	Homo sapiens	0-16
22162689-4	2011	Null mutation of Hmox1 results in significant embryonic mortality as well as anemia and defective iron recycling.	Iron	98-102	heme oxygenase 1	Homo sapiens	17-22
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Heme	51-55	heme oxygenase 1	Homo sapiens	18-22
21905282-10	2011	SHXW essential oil suppressed Abeta-induced apoptosis and ROS production via an up-regulation of HO-1 and Nrf2 expression in SH-SY5Y cells.	Oils, Volatile	5-18	heme oxygenase 1	Homo sapiens	97-101
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	0-16
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	18-22
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Biliverdine	85-95	heme oxygenase 1	Homo sapiens	0-16
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Biliverdine	85-95	heme oxygenase 1	Homo sapiens	18-22
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Iron	101-105	heme oxygenase 1	Homo sapiens	0-16
22254194-3	2011	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron.	Iron	101-105	heme oxygenase 1	Homo sapiens	18-22
21037234-4	2011	Induction of HO-1 by AICAR was blocked by the AMPK inhibitor compound C, the adenosine kinase inhibitor 5"-iodotubercidin, and by silencing AMPK-alpha(1/2) and was mimicked by the AMPK activator A-769662 and by infecting ECs with an adenovirus expressing constitutively active AMPK-alpha(1).	5-iodotubercidin	104-121	heme oxygenase 1	Homo sapiens	13-17
21037234-2	2011	Treatment of human ECs with the AMPK activator 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside (AICAR) stimulated a concentration- and time-dependent increase in HO-1 protein and mRNA expression that was associated with a prominent increase in nuclear factor-erythroid 2-related factor 2 (Nrf2) protein.	acadesine	47-101	heme oxygenase 1	Homo sapiens	169-173
21037234-2	2011	Treatment of human ECs with the AMPK activator 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside (AICAR) stimulated a concentration- and time-dependent increase in HO-1 protein and mRNA expression that was associated with a prominent increase in nuclear factor-erythroid 2-related factor 2 (Nrf2) protein.	acadesine	103-108	heme oxygenase 1	Homo sapiens	169-173
21037234-4	2011	Induction of HO-1 by AICAR was blocked by the AMPK inhibitor compound C, the adenosine kinase inhibitor 5"-iodotubercidin, and by silencing AMPK-alpha(1/2) and was mimicked by the AMPK activator A-769662 and by infecting ECs with an adenovirus expressing constitutively active AMPK-alpha(1).	acadesine	21-26	heme oxygenase 1	Homo sapiens	13-17
20934533-0	2011	Cellular iron depletion weakens induction of heme oxygenase-1 by cadmium.	Iron	9-13	heme oxygenase 1	Homo sapiens	45-61
21328623-0	2011	The outcome of 5-ALA-mediated photodynamic treatment in melanoma cells is influenced by vitamin C and heme oxygenase-1.	Aminolevulinic Acid	15-20	heme oxygenase 1	Homo sapiens	102-118
22125774-2	2011	METHODS: SiO(2)-induced oxidative stress was assessed by examining formation of reactive oxygen species (ROS), the induction of superoxide dismutase (SOD) and heme oxygenase-1 (HO-1), as well as cytotoxicity effect was evaluation by cell viability.	Silicon Dioxide	9-15	heme oxygenase 1	Homo sapiens	159-175
22125774-2	2011	METHODS: SiO(2)-induced oxidative stress was assessed by examining formation of reactive oxygen species (ROS), the induction of superoxide dismutase (SOD) and heme oxygenase-1 (HO-1), as well as cytotoxicity effect was evaluation by cell viability.	Silicon Dioxide	9-15	heme oxygenase 1	Homo sapiens	177-181
22125774-6	2011	The expression of SOD protein was not changed, whereas that of HO-1 was increased by SiO(2) nanoparticle exposure.	silicon monoxide	85-88	heme oxygenase 1	Homo sapiens	63-67
22125774-8	2011	SiO(2) nanoparticles induce induction of HO-1 via Nrf-2-ERK MAP kinase pathway.	Silicon Dioxide	0-6	heme oxygenase 1	Homo sapiens	41-45
20966033-1	2011	Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis.	Hemin	37-42	heme oxygenase 1	Homo sapiens	0-16
20966033-1	2011	Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis.	Hemin	37-42	heme oxygenase 1	Homo sapiens	18-22
20966033-1	2011	Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis.	Hemin	46-56	heme oxygenase 1	Homo sapiens	0-16
20966033-1	2011	Heme oxygenase-1 (HO-1) induction by hemin or Panhematin protects against experimental pancreatitis.	Hemin	46-56	heme oxygenase 1	Homo sapiens	18-22
20966033-2	2011	As a preclinical first step toward determining whether HO-1 upregulation is a viable target in acute pancreatitis (AP) patients, we tested the hypothesis that HO-1 expression in peripheral blood mononuclear cell (PBMC) subsets of hospitalized patients with mild AP is upregulated then normalizes upon recovery and that cells from AP patients have the potential to upregulate their HO-1 ex vivo if exposed to Panhematin.	Hemin	408-418	heme oxygenase 1	Homo sapiens	159-163
20966033-2	2011	As a preclinical first step toward determining whether HO-1 upregulation is a viable target in acute pancreatitis (AP) patients, we tested the hypothesis that HO-1 expression in peripheral blood mononuclear cell (PBMC) subsets of hospitalized patients with mild AP is upregulated then normalizes upon recovery and that cells from AP patients have the potential to upregulate their HO-1 ex vivo if exposed to Panhematin.	Hemin	408-418	heme oxygenase 1	Homo sapiens	159-163
20966033-6	2011	Panhematin induced HO-1 in ex vivo cultured AP PBMCs more readily than in HC or VC PBMCs.	Hemin	0-10	heme oxygenase 1	Homo sapiens	19-23
21660298-4	2011	A PCR-based method was used to search for oxidized purine base products in selected 200 bp sequences in promoters and coding regions of the VEGF, TGF-beta1, HO-1, Egr1, and beta-actin genes while quantitative Southern blot analysis was used to detect oxidative damage to the mitochondrial genome in lung tissue from control subjects and COPD patients.	purine	51-57	heme oxygenase 1	Homo sapiens	157-161
20934533-0	2011	Cellular iron depletion weakens induction of heme oxygenase-1 by cadmium.	Cadmium	65-72	heme oxygenase 1	Homo sapiens	45-61
20934533-3	2011	In HCT-116 cells, cadmium increased heme oxygenase-1 enzymatic activity.	Cadmium	18-25	heme oxygenase 1	Homo sapiens	36-52
20934533-4	2011	This effect of cadmium was weaker in cells made iron-deficient with the iron chelator, desferrioxamine, which was associated with repression of heme oxygenase-1 protein and mRNA expression.	Cadmium	15-22	heme oxygenase 1	Homo sapiens	144-160
20934533-4	2011	This effect of cadmium was weaker in cells made iron-deficient with the iron chelator, desferrioxamine, which was associated with repression of heme oxygenase-1 protein and mRNA expression.	Iron	48-52	heme oxygenase 1	Homo sapiens	144-160
20934533-4	2011	This effect of cadmium was weaker in cells made iron-deficient with the iron chelator, desferrioxamine, which was associated with repression of heme oxygenase-1 protein and mRNA expression.	Iron	72-76	heme oxygenase 1	Homo sapiens	144-160
20934533-4	2011	This effect of cadmium was weaker in cells made iron-deficient with the iron chelator, desferrioxamine, which was associated with repression of heme oxygenase-1 protein and mRNA expression.	Deferoxamine	87-102	heme oxygenase 1	Homo sapiens	144-160
20934533-5	2011	The repression by desferrioxamine of cadmium-induced heme oxygenase-1 upregulation was reversed upon iron replenishment of the cells.	Deferoxamine	18-33	heme oxygenase 1	Homo sapiens	53-69
20934533-5	2011	The repression by desferrioxamine of cadmium-induced heme oxygenase-1 upregulation was reversed upon iron replenishment of the cells.	Cadmium	37-44	heme oxygenase 1	Homo sapiens	53-69
20934533-5	2011	The repression by desferrioxamine of cadmium-induced heme oxygenase-1 upregulation was reversed upon iron replenishment of the cells.	Iron	101-105	heme oxygenase 1	Homo sapiens	53-69
20934533-6	2011	Additionally, it was found that thiol antioxidants inhibited the heme oxygenase-1 upregulation caused by cadmium and also by ethacrynic acid, which each decreased intracellular glutathione as did buthionine sulfoxamine.	Sulfhydryl Compounds	32-37	heme oxygenase 1	Homo sapiens	65-81
20934533-6	2011	Additionally, it was found that thiol antioxidants inhibited the heme oxygenase-1 upregulation caused by cadmium and also by ethacrynic acid, which each decreased intracellular glutathione as did buthionine sulfoxamine.	Cadmium	105-112	heme oxygenase 1	Homo sapiens	65-81
20934533-6	2011	Additionally, it was found that thiol antioxidants inhibited the heme oxygenase-1 upregulation caused by cadmium and also by ethacrynic acid, which each decreased intracellular glutathione as did buthionine sulfoxamine.	Ethacrynic Acid	125-140	heme oxygenase 1	Homo sapiens	65-81
20934533-6	2011	Additionally, it was found that thiol antioxidants inhibited the heme oxygenase-1 upregulation caused by cadmium and also by ethacrynic acid, which each decreased intracellular glutathione as did buthionine sulfoxamine.	Glutathione	177-188	heme oxygenase 1	Homo sapiens	65-81
20934533-6	2011	Additionally, it was found that thiol antioxidants inhibited the heme oxygenase-1 upregulation caused by cadmium and also by ethacrynic acid, which each decreased intracellular glutathione as did buthionine sulfoxamine.	Buthionine Sulfoximine	196-218	heme oxygenase 1	Homo sapiens	65-81
20934533-7	2011	Interestingly, cadmium and ethacrynic acid increased nuclear translocation of Nrf2 and subsequent heme oxygenase-1 expression, but buthionine sulfoxamine did not.	Cadmium	15-22	heme oxygenase 1	Homo sapiens	98-114
20934533-7	2011	Interestingly, cadmium and ethacrynic acid increased nuclear translocation of Nrf2 and subsequent heme oxygenase-1 expression, but buthionine sulfoxamine did not.	Ethacrynic Acid	27-42	heme oxygenase 1	Homo sapiens	98-114
20934533-8	2011	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin, and a superoxide scavenger (Tiron) inhibited cadmium-induced upregulation of heme oxygenase-1.	diphenyleneiodonium	39-58	heme oxygenase 1	Homo sapiens	150-166
20934533-8	2011	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin, and a superoxide scavenger (Tiron) inhibited cadmium-induced upregulation of heme oxygenase-1.	acetovanillone	63-71	heme oxygenase 1	Homo sapiens	150-166
20934533-8	2011	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin, and a superoxide scavenger (Tiron) inhibited cadmium-induced upregulation of heme oxygenase-1.	Superoxides	79-89	heme oxygenase 1	Homo sapiens	150-166
20934533-8	2011	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin, and a superoxide scavenger (Tiron) inhibited cadmium-induced upregulation of heme oxygenase-1.	1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt	101-106	heme oxygenase 1	Homo sapiens	150-166
20934533-8	2011	Furthermore, NADPH oxidase inhibitors (diphenyleneiodonium and apocynin, and a superoxide scavenger (Tiron) inhibited cadmium-induced upregulation of heme oxygenase-1.	Cadmium	118-125	heme oxygenase 1	Homo sapiens	150-166
20934533-10	2011	It is concluded that adequate amounts of iron, which at the atomic level can serve as the pivotal element of heme in NADPH oxidase, must be present in cells to permit what appears to be thiol redox-sensitive, NADPH oxidase-dependent upregulation of heme oxygenase-1.	Iron	41-45	heme oxygenase 1	Homo sapiens	249-265
20934533-10	2011	It is concluded that adequate amounts of iron, which at the atomic level can serve as the pivotal element of heme in NADPH oxidase, must be present in cells to permit what appears to be thiol redox-sensitive, NADPH oxidase-dependent upregulation of heme oxygenase-1.	Sulfhydryl Compounds	186-191	heme oxygenase 1	Homo sapiens	249-265
20934533-11	2011	Thus, these findings are significant because they suggest that cells without adequate iron would be unable to fully express the stress gene, heme oxygenase-1, when confronted with the toxic metal, cadmium.	Metals	190-195	heme oxygenase 1	Homo sapiens	141-157
20934533-11	2011	Thus, these findings are significant because they suggest that cells without adequate iron would be unable to fully express the stress gene, heme oxygenase-1, when confronted with the toxic metal, cadmium.	Cadmium	197-204	heme oxygenase 1	Homo sapiens	141-157
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Heme	60-64	heme oxygenase 1	Homo sapiens	0-16
21297920-4	2011	Under these circumstances, the cells exhibited global protein arginine methylation: this event was also reproduced by the cell treatment with hemin, a heme oxygenase-1 inducer.	Arginine	62-70	heme oxygenase 1	Homo sapiens	151-167
21297920-4	2011	Under these circumstances, the cells exhibited global protein arginine methylation: this event was also reproduced by the cell treatment with hemin, a heme oxygenase-1 inducer.	Hemin	142-147	heme oxygenase 1	Homo sapiens	151-167
21088618-1	2011	Heme oxygenase-1 (HO-1) is a stress-induced enzyme that catalyses the oxidation of heme to biliverdin.	Heme	83-87	heme oxygenase 1	Homo sapiens	0-16
21088618-1	2011	Heme oxygenase-1 (HO-1) is a stress-induced enzyme that catalyses the oxidation of heme to biliverdin.	Heme	83-87	heme oxygenase 1	Homo sapiens	18-22
21088618-1	2011	Heme oxygenase-1 (HO-1) is a stress-induced enzyme that catalyses the oxidation of heme to biliverdin.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	0-16
21088618-1	2011	Heme oxygenase-1 (HO-1) is a stress-induced enzyme that catalyses the oxidation of heme to biliverdin.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	18-22
20561893-3	2011	METHODS: A PowerWave XS plate reader was used to monitor the absorbance (as a function of time) of heme bound to purified truncated human heme oxygenase-1 (hHO-1) in the individual wells of a standard 96-well plate (with or without the addition of a test compound).	Heme	99-103	heme oxygenase 1	Homo sapiens	138-154
20561893-3	2011	METHODS: A PowerWave XS plate reader was used to monitor the absorbance (as a function of time) of heme bound to purified truncated human heme oxygenase-1 (hHO-1) in the individual wells of a standard 96-well plate (with or without the addition of a test compound).	Heme	99-103	heme oxygenase 1	Homo sapiens	156-161
20561893-4	2011	The degradation of heme by heme oxygenase-1 was initiated using l-ascorbic acid, and the collected relevant absorbance data were analyzed by three different methods to calculate the percent control activity occurring in wells containing test compounds relative to that occurring in control wells with no test compound present.	Heme	19-23	heme oxygenase 1	Homo sapiens	27-43
20561893-4	2011	The degradation of heme by heme oxygenase-1 was initiated using l-ascorbic acid, and the collected relevant absorbance data were analyzed by three different methods to calculate the percent control activity occurring in wells containing test compounds relative to that occurring in control wells with no test compound present.	Ascorbic Acid	64-79	heme oxygenase 1	Homo sapiens	27-43
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Heme	60-64	heme oxygenase 1	Homo sapiens	18-22
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Heme	60-64	heme oxygenase 1	Homo sapiens	180-184
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Biliverdine	128-138	heme oxygenase 1	Homo sapiens	0-16
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Biliverdine	128-138	heme oxygenase 1	Homo sapiens	18-22
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Biliverdine	128-138	heme oxygenase 1	Homo sapiens	180-184
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Iron	167-171	heme oxygenase 1	Homo sapiens	0-16
20941616-1	2011	Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli.	Iron	167-171	heme oxygenase 1	Homo sapiens	18-22
21311138-6	2011	The mRNA and protein levels of ET-1 were decreased, and the mRNA and protein levels of HO-1 increased in the Danshensu groups in a dose-dependent manner compared with the high glucose group.	Glucose	176-183	heme oxygenase 1	Homo sapiens	87-91
21850179-10	2011	HO-1, catalase, GST-pi, and Nrf-2 were elevated in ARPE-19 cells after treatment with different concentrations of canolol for 24 h. Finally, canolol was found to activate extracellular signal regulated kinase (ERK) phosphorylation in ARPE-19 cells under the condition, with or without t-BH.	4-vinyl-2,6-dimethoxyphenol	114-121	heme oxygenase 1	Homo sapiens	0-14
21850179-10	2011	HO-1, catalase, GST-pi, and Nrf-2 were elevated in ARPE-19 cells after treatment with different concentrations of canolol for 24 h. Finally, canolol was found to activate extracellular signal regulated kinase (ERK) phosphorylation in ARPE-19 cells under the condition, with or without t-BH.	4-vinyl-2,6-dimethoxyphenol	141-148	heme oxygenase 1	Homo sapiens	0-14
20974203-7	2011	We also found that Tg induced the expression of the antioxidant gene heme oxygenase-1 (HO-1) in a dose-dependent manner, whereas Tm had a weak effect on HO-1 induction.	Thapsigargin	19-21	heme oxygenase 1	Homo sapiens	69-85
20974203-7	2011	We also found that Tg induced the expression of the antioxidant gene heme oxygenase-1 (HO-1) in a dose-dependent manner, whereas Tm had a weak effect on HO-1 induction.	Thapsigargin	19-21	heme oxygenase 1	Homo sapiens	87-91
20974203-10	2011	Because actinomycin D inhibited HO-1 induction by Tg, the induction of HO-1 may be regulated at the transcriptional level.	Dactinomycin	8-21	heme oxygenase 1	Homo sapiens	32-36
20974203-10	2011	Because actinomycin D inhibited HO-1 induction by Tg, the induction of HO-1 may be regulated at the transcriptional level.	Dactinomycin	8-21	heme oxygenase 1	Homo sapiens	71-75
20974203-10	2011	Because actinomycin D inhibited HO-1 induction by Tg, the induction of HO-1 may be regulated at the transcriptional level.	Thapsigargin	50-52	heme oxygenase 1	Homo sapiens	32-36
20974203-10	2011	Because actinomycin D inhibited HO-1 induction by Tg, the induction of HO-1 may be regulated at the transcriptional level.	Thapsigargin	50-52	heme oxygenase 1	Homo sapiens	71-75
20974203-11	2011	Moreover, the specific eIF2alpha phosphatase inhibitor salubrinal augmented Tg-induced HO-1 expression.	salubrinal	55-65	heme oxygenase 1	Homo sapiens	87-91
20974203-11	2011	Moreover, the specific eIF2alpha phosphatase inhibitor salubrinal augmented Tg-induced HO-1 expression.	Thapsigargin	76-78	heme oxygenase 1	Homo sapiens	87-91
20974203-13	2011	On the other hand, the reporter assay revealed that Tg stimulated the antioxidant response element (ARE) that is located in regulatory regions of antioxidant genes such as HO-1.	Thapsigargin	52-54	heme oxygenase 1	Homo sapiens	172-176
21765894-2	2011	Heme-oxygenase 1 (HO-1) is known to be the heme inducible isoform, whereas heme-oxygenase 2 (HO-2) is the constitutive enzyme.	Heme	43-47	heme oxygenase 1	Homo sapiens	0-16
21765894-2	2011	Heme-oxygenase 1 (HO-1) is known to be the heme inducible isoform, whereas heme-oxygenase 2 (HO-2) is the constitutive enzyme.	Heme	43-47	heme oxygenase 1	Homo sapiens	18-22
22203790-0	2011	Quercetin protects primary human osteoblasts exposed to cigarette smoke through activation of the antioxidative enzymes HO-1 and SOD-1.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	120-124
22203790-6	2011	Quercetin increased the expression of the anti-oxidative enzymes heme-oxygenase- (HO-) 1 and superoxide-dismutase- (SOD-) 1.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	65-88
22203790-7	2011	Inhibiting HO-1 activity abolished the protective effect of Quercetin.	Quercetin	60-69	heme oxygenase 1	Homo sapiens	11-15
22203790-9	2011	Quercetin can diminish this damage by scavenging the radicals and by upregulating the expression of HO-1 and SOD-1.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	100-104
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Arsenic Trioxide	0-3	heme oxygenase 1	Homo sapiens	32-48
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Arsenic Trioxide	0-3	heme oxygenase 1	Homo sapiens	50-54
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Iron	111-115	heme oxygenase 1	Homo sapiens	32-48
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Iron	111-115	heme oxygenase 1	Homo sapiens	50-54
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	epigallocatechin gallate	120-124	heme oxygenase 1	Homo sapiens	32-48
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	epigallocatechin gallate	120-124	heme oxygenase 1	Homo sapiens	50-54
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Hydrogen Peroxide	133-150	heme oxygenase 1	Homo sapiens	32-48
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Hydrogen Peroxide	133-150	heme oxygenase 1	Homo sapiens	50-54
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Reactive Oxygen Species	215-238	heme oxygenase 1	Homo sapiens	32-48
20950636-7	2011	ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell.	Reactive Oxygen Species	215-238	heme oxygenase 1	Homo sapiens	50-54
20950636-9	2011	This investigation also provided evidence that ATO, since mainly acted to induce HO-1 in simultaneous treatment with EGCG, could be replaced by other HO-1 inducer with much less human toxicity.	Arsenic Trioxide	47-50	heme oxygenase 1	Homo sapiens	81-85
20950636-9	2011	This investigation also provided evidence that ATO, since mainly acted to induce HO-1 in simultaneous treatment with EGCG, could be replaced by other HO-1 inducer with much less human toxicity.	Arsenic Trioxide	47-50	heme oxygenase 1	Homo sapiens	150-154
21857081-4	2011	We found that phloretin induced the expression of heme oxygenase-1 (HO-1) protein in a concentration- and time-dependent manner.	Phloretin	14-23	heme oxygenase 1	Homo sapiens	50-66
21857081-4	2011	We found that phloretin induced the expression of heme oxygenase-1 (HO-1) protein in a concentration- and time-dependent manner.	Phloretin	14-23	heme oxygenase 1	Homo sapiens	68-72
21857081-5	2011	Phloretin induced nuclear factor-E2-related factor 2 (Nrf2) nuclear translocation, and dominant-negative Nrf2 attenuated phloretin-induced expression of HO-1.	Phloretin	121-130	heme oxygenase 1	Homo sapiens	153-157
21857081-6	2011	Phloretin activated the JNK, ERK and p38 mitogen-activated protein kinase (MAPK) pathways, and the JNK pathway played an important role in phloretin-induced HO-1 expression.	Phloretin	139-148	heme oxygenase 1	Homo sapiens	157-161
21857081-10	2011	These results demonstrate that the expression of HO-1 induced by phloretin is mediated by both the JNK pathway and Nrf2; the expression inhibits cisplatin-induced apoptosis in HEI-OC1 cells.	Phloretin	65-74	heme oxygenase 1	Homo sapiens	49-53
21857081-10	2011	These results demonstrate that the expression of HO-1 induced by phloretin is mediated by both the JNK pathway and Nrf2; the expression inhibits cisplatin-induced apoptosis in HEI-OC1 cells.	Cisplatin	145-154	heme oxygenase 1	Homo sapiens	49-53
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Heme	77-81	heme oxygenase 1	Homo sapiens	0-16
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Heme	77-81	heme oxygenase 1	Homo sapiens	18-22
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	0-16
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	18-22
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Iron	104-108	heme oxygenase 1	Homo sapiens	0-16
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Iron	104-108	heme oxygenase 1	Homo sapiens	18-22
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	0-16
21182221-2	2010	Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide.	Carbon Monoxide	113-128	heme oxygenase 1	Homo sapiens	18-22
20643109-1	2010	Heme oxygenase (HO)-1 is the inducible isoform of the first and rate-limiting enzyme of heme degradation.	Heme	88-92	heme oxygenase 1	Homo sapiens	0-21
20643109-4	2010	Beneficial protective effects of HO-1 in inflammation are not only mediated via enzymatic degradation of proinflammatory free heme, but also via production of the anti-inflammatory compounds bilirubin and carbon monoxide.	Heme	126-130	heme oxygenase 1	Homo sapiens	33-37
20643109-4	2010	Beneficial protective effects of HO-1 in inflammation are not only mediated via enzymatic degradation of proinflammatory free heme, but also via production of the anti-inflammatory compounds bilirubin and carbon monoxide.	Bilirubin	191-200	heme oxygenase 1	Homo sapiens	33-37
20643109-4	2010	Beneficial protective effects of HO-1 in inflammation are not only mediated via enzymatic degradation of proinflammatory free heme, but also via production of the anti-inflammatory compounds bilirubin and carbon monoxide.	Carbon Monoxide	205-220	heme oxygenase 1	Homo sapiens	33-37
20837117-6	2010	Importantly, Hg(2+) increased the expression of heme oxygenase-1 (HO-1), a rate limiting enzyme in heme degradation, which coincided with further decrease in the CYP1A1 catalytic activity levels.	Heme	48-52	heme oxygenase 1	Homo sapiens	66-70
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Heme	85-89	heme oxygenase 1	Homo sapiens	0-16
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Heme	85-89	heme oxygenase 1	Homo sapiens	18-22
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Iron	98-102	heme oxygenase 1	Homo sapiens	0-16
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Iron	98-102	heme oxygenase 1	Homo sapiens	18-22
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Carbon Monoxide	104-119	heme oxygenase 1	Homo sapiens	0-16
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Carbon Monoxide	104-119	heme oxygenase 1	Homo sapiens	18-22
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Biliverdine	125-135	heme oxygenase 1	Homo sapiens	0-16
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Biliverdine	125-135	heme oxygenase 1	Homo sapiens	18-22
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Bilirubin	182-191	heme oxygenase 1	Homo sapiens	0-16
20713168-4	2010	Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Bilirubin	182-191	heme oxygenase 1	Homo sapiens	18-22
20837117-7	2010	Upon using a competitive HO-1 inhibitor, tin mesoporphyrin, heme precursor, hemin, or transfecting the HepG2 cells with siRNA for HO-1 there was a partial restoration of the inhibition of TCDD-mediated induction of CYP1A1 catalytic activity.	Polychlorinated Dibenzodioxins	188-192	heme oxygenase 1	Homo sapiens	25-29
20837117-7	2010	Upon using a competitive HO-1 inhibitor, tin mesoporphyrin, heme precursor, hemin, or transfecting the HepG2 cells with siRNA for HO-1 there was a partial restoration of the inhibition of TCDD-mediated induction of CYP1A1 catalytic activity.	Polychlorinated Dibenzodioxins	188-192	heme oxygenase 1	Homo sapiens	130-134
20724175-6	2010	DHP-lysine photosensitization induced intracellular oxidative stress, p38 MAPkinase activation, and upregulation of heme oxygenase-1 expression.	dhp-lysine	0-10	heme oxygenase 1	Homo sapiens	116-132
20833156-0	2010	Heme oxygenase-1 signals are involved in preferential inhibition of pro-inflammatory cytokine release by surfactin in cells activated with Porphyromonas gingivalis lipopolysaccharide.	surfactin peptide	105-114	heme oxygenase 1	Homo sapiens	0-16
20833156-7	2010	We also examined whether the regulatory effect of surfactin on P. gingivalis LPS-stimulated human THP-1 macrophages was mediated by the induction of heme oxygenase-1 (HO-1) signals, and determined that surfactin also induced HO-1 mRNA and protein expression via activation of Nrf-2.	surfactin peptide	50-59	heme oxygenase 1	Homo sapiens	149-165
20833156-7	2010	We also examined whether the regulatory effect of surfactin on P. gingivalis LPS-stimulated human THP-1 macrophages was mediated by the induction of heme oxygenase-1 (HO-1) signals, and determined that surfactin also induced HO-1 mRNA and protein expression via activation of Nrf-2.	surfactin peptide	50-59	heme oxygenase 1	Homo sapiens	167-171
20833156-8	2010	Additionally, we found that small interfering RNA-mediated knock-down of Nrf-2 significantly inhibited surfactin-induced HO-1 expression.	surfactin peptide	103-112	heme oxygenase 1	Homo sapiens	121-125
20833156-9	2010	Furthermore, inhibition of phosphoinositide 3-kinase (PI3K)/Akt and extracellular signal-regulated kinase (ERK) significantly decreased surfactin-induced HO-1 expression, which is consistent with the suggestion that surfactin-induced HO-1 expression occurs via PI3K/Akt, ERK, and Nrf-2.	surfactin peptide	136-145	heme oxygenase 1	Homo sapiens	154-158
20833156-9	2010	Furthermore, inhibition of phosphoinositide 3-kinase (PI3K)/Akt and extracellular signal-regulated kinase (ERK) significantly decreased surfactin-induced HO-1 expression, which is consistent with the suggestion that surfactin-induced HO-1 expression occurs via PI3K/Akt, ERK, and Nrf-2.	surfactin peptide	136-145	heme oxygenase 1	Homo sapiens	234-238
20833156-9	2010	Furthermore, inhibition of phosphoinositide 3-kinase (PI3K)/Akt and extracellular signal-regulated kinase (ERK) significantly decreased surfactin-induced HO-1 expression, which is consistent with the suggestion that surfactin-induced HO-1 expression occurs via PI3K/Akt, ERK, and Nrf-2.	surfactin peptide	216-225	heme oxygenase 1	Homo sapiens	154-158
20833156-9	2010	Furthermore, inhibition of phosphoinositide 3-kinase (PI3K)/Akt and extracellular signal-regulated kinase (ERK) significantly decreased surfactin-induced HO-1 expression, which is consistent with the suggestion that surfactin-induced HO-1 expression occurs via PI3K/Akt, ERK, and Nrf-2.	surfactin peptide	216-225	heme oxygenase 1	Homo sapiens	234-238
20833156-10	2010	Treatment with a selective inhibitor of HO-1 reversed the surfactin-mediated inhibition of pro-inflammatory cytokines, suggesting that surfactin induces anti-inflammatory effects by activating Nrf-2-mediated HO-1 induction via PI3K/Akt and ERK signaling.	surfactin peptide	58-67	heme oxygenase 1	Homo sapiens	40-44
20833156-10	2010	Treatment with a selective inhibitor of HO-1 reversed the surfactin-mediated inhibition of pro-inflammatory cytokines, suggesting that surfactin induces anti-inflammatory effects by activating Nrf-2-mediated HO-1 induction via PI3K/Akt and ERK signaling.	surfactin peptide	58-67	heme oxygenase 1	Homo sapiens	208-212
20833156-10	2010	Treatment with a selective inhibitor of HO-1 reversed the surfactin-mediated inhibition of pro-inflammatory cytokines, suggesting that surfactin induces anti-inflammatory effects by activating Nrf-2-mediated HO-1 induction via PI3K/Akt and ERK signaling.	surfactin peptide	135-144	heme oxygenase 1	Homo sapiens	40-44
20833156-10	2010	Treatment with a selective inhibitor of HO-1 reversed the surfactin-mediated inhibition of pro-inflammatory cytokines, suggesting that surfactin induces anti-inflammatory effects by activating Nrf-2-mediated HO-1 induction via PI3K/Akt and ERK signaling.	surfactin peptide	135-144	heme oxygenase 1	Homo sapiens	208-212
21151599-14	2010	FDP-lysine accumulation was associated with the induction of HO-1, no change in GFAP, a decrease in protein levels of the potassium channel subunit Kir4.1, and upregulation of transcripts for VEGF, IL-6, and TNF-alpha.	Lysine	4-10	heme oxygenase 1	Homo sapiens	61-65
20446774-0	2010	Nrf2-Mediated heme oxygenase-1 upregulation as adaptive survival response to glucose deprivation-induced apoptosis in HepG2 cells.	Glucose	77-84	heme oxygenase 1	Homo sapiens	14-30
20446774-5	2010	To confirm the involvement of Nrf2 in the induction of HO-1 caused by glucose deprivation, we used embryonic fibroblasts prepared from nrf2-(/)-, nrf2(+/)-, and nrf2(+/+) embryos.	Glucose	70-77	heme oxygenase 1	Homo sapiens	55-59
20446774-3	2010	Treatment of HepG2 cells with SnCl2, a HO-1 inducer, rescued these cells from glucose deprivation-induced apoptosis, while inhibition of the HO activity with zinc protoporphyrin IX exacerbated apoptosis under the same condition.	Glucose	78-85	heme oxygenase 1	Homo sapiens	39-43
20446774-6	2010	Compared to the wild-type and the nrf2(+/)- embryonic fibroblasts, nrf2-(/)- cells were less prone to induce HO-1 expression upon glucose deprivation.	Glucose	130-137	heme oxygenase 1	Homo sapiens	109-113
20446774-8	2010	Pretreatment with N-acetylcysteine prevented the glucose deprivation-induced ROS accumulation and also the HO-1 expression.	Acetylcysteine	18-34	heme oxygenase 1	Homo sapiens	107-111
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Iron	105-107	heme oxygenase 1	Homo sapiens	459-463
20446774-9	2010	In conclusion, the Nrf2-mediated HO-1 upregulation upon glucose deprivation is mediated by ROS in HepG2 cells, and responsible for the adaptive survival response.	Glucose	56-63	heme oxygenase 1	Homo sapiens	33-37
20446774-9	2010	In conclusion, the Nrf2-mediated HO-1 upregulation upon glucose deprivation is mediated by ROS in HepG2 cells, and responsible for the adaptive survival response.	Reactive Oxygen Species	91-94	heme oxygenase 1	Homo sapiens	33-37
20868356-4	2010	HO-1 is the enzyme responsible for the conversion of the heme group to billiverdin, carbon monoxide and iron; a highly regulated cytoprotective enzyme able to respond to numerous chemical or physical stressors, many of which decrease oxygen availability and generate oxidative stress.	Heme	57-61	heme oxygenase 1	Homo sapiens	0-4
20868356-4	2010	HO-1 is the enzyme responsible for the conversion of the heme group to billiverdin, carbon monoxide and iron; a highly regulated cytoprotective enzyme able to respond to numerous chemical or physical stressors, many of which decrease oxygen availability and generate oxidative stress.	billiverdin	71-82	heme oxygenase 1	Homo sapiens	0-4
20868356-4	2010	HO-1 is the enzyme responsible for the conversion of the heme group to billiverdin, carbon monoxide and iron; a highly regulated cytoprotective enzyme able to respond to numerous chemical or physical stressors, many of which decrease oxygen availability and generate oxidative stress.	Carbon Monoxide	84-99	heme oxygenase 1	Homo sapiens	0-4
20868356-4	2010	HO-1 is the enzyme responsible for the conversion of the heme group to billiverdin, carbon monoxide and iron; a highly regulated cytoprotective enzyme able to respond to numerous chemical or physical stressors, many of which decrease oxygen availability and generate oxidative stress.	Iron	104-108	heme oxygenase 1	Homo sapiens	0-4
20868356-4	2010	HO-1 is the enzyme responsible for the conversion of the heme group to billiverdin, carbon monoxide and iron; a highly regulated cytoprotective enzyme able to respond to numerous chemical or physical stressors, many of which decrease oxygen availability and generate oxidative stress.	Oxygen	234-240	heme oxygenase 1	Homo sapiens	0-4
20704544-2	2010	BVR is the sole catalyst for the conversion of biliverdin-IXalpha the activity product of the stress-inducible HO-1 and the constitutive HO-2, to bilirubin-IXalpha.	Biliverdine	47-57	heme oxygenase 1	Homo sapiens	111-115
20704544-2	2010	BVR is the sole catalyst for the conversion of biliverdin-IXalpha the activity product of the stress-inducible HO-1 and the constitutive HO-2, to bilirubin-IXalpha.	ixalpha	58-65	heme oxygenase 1	Homo sapiens	111-115
20704544-2	2010	BVR is the sole catalyst for the conversion of biliverdin-IXalpha the activity product of the stress-inducible HO-1 and the constitutive HO-2, to bilirubin-IXalpha.	Bilirubin	146-155	heme oxygenase 1	Homo sapiens	111-115
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-16
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	41-56	heme oxygenase 1	Homo sapiens	0-16
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	41-56	heme oxygenase 1	Homo sapiens	18-22
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	58-60	heme oxygenase 1	Homo sapiens	0-16
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	58-60	heme oxygenase 1	Homo sapiens	18-22
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Biliverdine	63-73	heme oxygenase 1	Homo sapiens	0-16
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Biliverdine	63-73	heme oxygenase 1	Homo sapiens	18-22
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Iron	79-91	heme oxygenase 1	Homo sapiens	0-16
20704546-1	2010	Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron.	Iron	79-91	heme oxygenase 1	Homo sapiens	18-22
20704548-3	2010	HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase.	Heme	48-52	heme oxygenase 1	Homo sapiens	0-4
20704548-3	2010	HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase.	Iron	56-60	heme oxygenase 1	Homo sapiens	0-4
20704548-3	2010	HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase.	Carbon Monoxide	62-77	heme oxygenase 1	Homo sapiens	0-4
20704548-3	2010	HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase.	Carbon Monoxide	79-81	heme oxygenase 1	Homo sapiens	0-4
20704548-3	2010	HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	0-4
20704548-3	2010	HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase.	Bilirubin	131-140	heme oxygenase 1	Homo sapiens	0-4
20704548-4	2010	In addition to the degradation of free heme, a pro-oxidant, HO-1 exerts anti-oxidant, anti-inflammatory and anti-apoptotic properties via its reaction products.	Heme	39-43	heme oxygenase 1	Homo sapiens	60-64
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Heme	45-49	heme oxygenase 1	Homo sapiens	0-16
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Heme	45-49	heme oxygenase 1	Homo sapiens	18-22
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	0-16
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	18-22
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Iron	75-79	heme oxygenase 1	Homo sapiens	0-16
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Iron	75-79	heme oxygenase 1	Homo sapiens	18-22
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Biliverdine	85-95	heme oxygenase 1	Homo sapiens	0-16
20704549-1	2010	Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection.	Biliverdine	85-95	heme oxygenase 1	Homo sapiens	18-22
20704549-6	2010	From the therapeutic side, the blood brain barrier represents an obstacle to directly modulate heme oxygenase activity, but drugs activating the transcription actor Nrf2, which have a very diverse molecular structure, may be good candidates to induce HO-1 in concert with other antioxidant and detoxification enzymes.	Heme	95-99	heme oxygenase 1	Homo sapiens	251-255
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Heme	36-40	heme oxygenase 1	Homo sapiens	0-16
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Heme	36-40	heme oxygenase 1	Homo sapiens	18-22
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	0-16
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	18-22
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Carbon Monoxide	70-72	heme oxygenase 1	Homo sapiens	0-16
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Carbon Monoxide	70-72	heme oxygenase 1	Homo sapiens	18-22
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Biliverdine	75-85	heme oxygenase 1	Homo sapiens	0-16
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Biliverdine	75-85	heme oxygenase 1	Homo sapiens	18-22
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Iron	91-95	heme oxygenase 1	Homo sapiens	0-16
20875851-8	2010	Furthermore, PNU282987 increased the expression of heme oxygenase-1 (HO-1), a critical cell defense enzyme against oxidative stress; this increase was prevented by AG490 or LY294002.	PNU-282987	13-22	heme oxygenase 1	Homo sapiens	51-67
20875851-8	2010	Furthermore, PNU282987 increased the expression of heme oxygenase-1 (HO-1), a critical cell defense enzyme against oxidative stress; this increase was prevented by AG490 or LY294002.	PNU-282987	13-22	heme oxygenase 1	Homo sapiens	69-73
20875851-8	2010	Furthermore, PNU282987 increased the expression of heme oxygenase-1 (HO-1), a critical cell defense enzyme against oxidative stress; this increase was prevented by AG490 or LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	173-181	heme oxygenase 1	Homo sapiens	51-67
20875851-8	2010	Furthermore, PNU282987 increased the expression of heme oxygenase-1 (HO-1), a critical cell defense enzyme against oxidative stress; this increase was prevented by AG490 or LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	173-181	heme oxygenase 1	Homo sapiens	69-73
20875851-9	2010	The HO-1 inhibitor Sn(IV) protoporphyrin-IX also inhibited the PST/PNU protecting effects.	protoporphyrin IX	26-43	heme oxygenase 1	Homo sapiens	4-8
21383490-3	2010	Heme-oxygenase-1 (HO-1) is a rate-limiting enzyme for heme breakdown.	Heme	54-58	heme oxygenase 1	Homo sapiens	0-16
21383490-3	2010	Heme-oxygenase-1 (HO-1) is a rate-limiting enzyme for heme breakdown.	Heme	54-58	heme oxygenase 1	Homo sapiens	18-22
21383490-4	2010	HO-1 breaks down heme to yield CO, iron and biliverdin.	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4
21383490-4	2010	HO-1 breaks down heme to yield CO, iron and biliverdin.	Carbon Monoxide	31-33	heme oxygenase 1	Homo sapiens	0-4
21383490-4	2010	HO-1 breaks down heme to yield CO, iron and biliverdin.	Iron	35-39	heme oxygenase 1	Homo sapiens	0-4
21383490-4	2010	HO-1 breaks down heme to yield CO, iron and biliverdin.	Biliverdine	44-54	heme oxygenase 1	Homo sapiens	0-4
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Iron	99-103	heme oxygenase 1	Homo sapiens	441-457
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Iron	99-103	heme oxygenase 1	Homo sapiens	459-463
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Iron	105-107	heme oxygenase 1	Homo sapiens	441-457
20718734-2	2010	In this study, we have investigated the role of haem arginate (HA) in human male subjects in the modulation of HO-1 expression and its correlation with the GT length polymorphism (GT(n)) in the promoter of the HO-1 gene.	heme arginate	48-61	heme oxygenase 1	Homo sapiens	111-115
20718734-2	2010	In this study, we have investigated the role of haem arginate (HA) in human male subjects in the modulation of HO-1 expression and its correlation with the GT length polymorphism (GT(n)) in the promoter of the HO-1 gene.	heme arginate	48-61	heme oxygenase 1	Homo sapiens	210-214
20704550-1	2010	Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron.	Iron	91-95	heme oxygenase 1	Homo sapiens	18-22
20704550-5	2010	The vasoprotection afforded by HO-1 is largely attributable to its end products: CO and the bile pigments, biliverdin and bilirubin.	Carbon Monoxide	81-83	heme oxygenase 1	Homo sapiens	31-35
20704550-5	2010	The vasoprotection afforded by HO-1 is largely attributable to its end products: CO and the bile pigments, biliverdin and bilirubin.	Biliverdine	107-117	heme oxygenase 1	Homo sapiens	31-35
20704550-5	2010	The vasoprotection afforded by HO-1 is largely attributable to its end products: CO and the bile pigments, biliverdin and bilirubin.	Bilirubin	122-131	heme oxygenase 1	Homo sapiens	31-35
20704550-9	2010	Pharmacological induction of HO-1 by heme derivatives, dietary antioxidants, or currently available drugs, is a promising near-term approach, while HO-1 gene delivery is a long-term therapeutic goal.	Heme	37-41	heme oxygenase 1	Homo sapiens	29-33
20704552-4	2010	HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron.	Heme	14-18	heme oxygenase 1	Homo sapiens	0-4
20704552-4	2010	HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron.	Biliverdine	22-40	heme oxygenase 1	Homo sapiens	0-4
20704552-4	2010	HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron.	Carbon Monoxide	42-57	heme oxygenase 1	Homo sapiens	0-4
20704552-4	2010	HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron.	Carbon Monoxide	59-61	heme oxygenase 1	Homo sapiens	0-4
20704552-4	2010	HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron.	Iron	68-72	heme oxygenase 1	Homo sapiens	0-4
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Copper	113-119	heme oxygenase 1	Homo sapiens	441-457
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Copper	113-119	heme oxygenase 1	Homo sapiens	459-463
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Copper	121-123	heme oxygenase 1	Homo sapiens	441-457
20730621-8	2010	The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1).	Copper	121-123	heme oxygenase 1	Homo sapiens	459-463
20851746-12	2010	These findings suggest that CPDT can protect CMNs from THA-induced motor neuron death by activating the Nrf2 pathway and increasing HO-1 protein expression.	tha	55-58	heme oxygenase 1	Homo sapiens	132-136
20938215-5	2010	Low PTL concentrations (5 to 10 microM) led to Nrf2-dependent HO-1 induction, which attenuated the apoptogenic effect of PTL in Choi-CK and SCK cells.	parthenolide	4-7	heme oxygenase 1	Homo sapiens	62-66
20938215-5	2010	Low PTL concentrations (5 to 10 microM) led to Nrf2-dependent HO-1 induction, which attenuated the apoptogenic effect of PTL in Choi-CK and SCK cells.	parthenolide	121-124	heme oxygenase 1	Homo sapiens	62-66
20938215-6	2010	PTL-mediated apoptosis was enhanced by the protein kinase C-alpha inhibitor Ro317549 (Ro) through inhibition of expression and nuclear translocation of Nrf2, resulting in blockage of HO-1 expression.	ro317549	76-84	heme oxygenase 1	Homo sapiens	183-187
20938215-6	2010	PTL-mediated apoptosis was enhanced by the protein kinase C-alpha inhibitor Ro317549 (Ro) through inhibition of expression and nuclear translocation of Nrf2, resulting in blockage of HO-1 expression.	ro	76-78	heme oxygenase 1	Homo sapiens	183-187
20828541-10	2010	We also demonstrated that the specific ERK inhibitor, PD98059, concentration-dependently blocked on ATX-induced HO-1 expression, and meanwhile PD98059 reversed the protective effect of ATX against Abeta25-35-induced cell death.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	54-61	heme oxygenase 1	Homo sapiens	112-116
20833713-3	2010	We showed that Kupffer cells from ethanol-fed rats and ethanol-treated rat Kupffer cells and THP-1 cells displayed increased mRNA expression of HO-1, NQO1, and hypoxia-inducible factor-1alpha (HIF-1alpha).	Ethanol	55-62	heme oxygenase 1	Homo sapiens	144-148
20828541-0	2010	Astaxanthin upregulates heme oxygenase-1 expression through ERK1/2 pathway and its protective effect against beta-amyloid-induced cytotoxicity in SH-SY5Y cells.	astaxanthine	0-11	heme oxygenase 1	Homo sapiens	24-40
20828541-8	2010	Moreover, we for the first time have revealed the ATX increased antioxidant enzyme heme oxygenase-1 (HO-1) expression in concentration-dependent and time-dependent manners, which were correlated with its protective effect against Abeta(25-35)-induced injury.	astaxanthine	50-53	heme oxygenase 1	Homo sapiens	83-99
20828541-8	2010	Moreover, we for the first time have revealed the ATX increased antioxidant enzyme heme oxygenase-1 (HO-1) expression in concentration-dependent and time-dependent manners, which were correlated with its protective effect against Abeta(25-35)-induced injury.	astaxanthine	50-53	heme oxygenase 1	Homo sapiens	101-105
20828541-9	2010	Because the inhibitor of HO-1 activity, ZnPP reversed the protective effect of ATX against Abeta(25-35)-induced cell death.	astaxanthine	79-82	heme oxygenase 1	Homo sapiens	25-29
20833713-3	2010	We showed that Kupffer cells from ethanol-fed rats and ethanol-treated rat Kupffer cells and THP-1 cells displayed increased mRNA expression of HO-1, NQO1, and hypoxia-inducible factor-1alpha (HIF-1alpha).	Ethanol	34-41	heme oxygenase 1	Homo sapiens	144-148
20828541-10	2010	We also demonstrated that the specific ERK inhibitor, PD98059, concentration-dependently blocked on ATX-induced HO-1 expression, and meanwhile PD98059 reversed the protective effect of ATX against Abeta25-35-induced cell death.	astaxanthine	100-103	heme oxygenase 1	Homo sapiens	112-116
20828541-11	2010	Taken together, these findings suggest that astaxanthin can induce HO-1 expression through activation of ERK signal pathways, thereby protecting the SH-SY5Y cells from Abeta(25-35)-induced oxidative cell death.	astaxanthine	44-55	heme oxygenase 1	Homo sapiens	67-71
20920477-0	2010	Low concentration of 4-hydroxy hexenal increases heme oxygenase-1 expression through activation of Nrf2 and antioxidative activity in vascular endothelial cells.	4-hydroxyhexenal	21-38	heme oxygenase 1	Homo sapiens	49-65
20679134-4	2010	The goal of this study was to determine whether HO-1 activity could be monitored directly by following BV generation or iron release (using the ferrous iron chelator, ferrozine) in the absence of BVR.	ferrous iron chelator	144-165	heme oxygenase 1	Homo sapiens	48-52
21116791-0	2010	Sulforaphane suppresses TARC/CCL17 and MDC/CCL22 expression through heme oxygenase-1 and NF-kappaB in human keratinocytes.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	68-84
21116791-1	2010	Sulforaphane (4-methylsulfinylbutyl isothiocyanate, SFN) from broccoli has been used a chemopreventive photochemical as detoxification of xenobiotics and anti-inflammatory, however, there is no studies for Th2 chemokine expression through heme oxygenase-1 and NF-kappaB in keratinocytes.	sulforaphane	0-12	heme oxygenase 1	Homo sapiens	239-255
21116791-1	2010	Sulforaphane (4-methylsulfinylbutyl isothiocyanate, SFN) from broccoli has been used a chemopreventive photochemical as detoxification of xenobiotics and anti-inflammatory, however, there is no studies for Th2 chemokine expression through heme oxygenase-1 and NF-kappaB in keratinocytes.	sulforaphane	14-50	heme oxygenase 1	Homo sapiens	239-255
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Oxygen	5-11	heme oxygenase 1	Homo sapiens	18-22
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Heme	108-112	heme oxygenase 1	Homo sapiens	0-16
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Heme	108-112	heme oxygenase 1	Homo sapiens	18-22
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Carbon Monoxide	116-118	heme oxygenase 1	Homo sapiens	0-16
20679134-4	2010	The goal of this study was to determine whether HO-1 activity could be monitored directly by following BV generation or iron release (using the ferrous iron chelator, ferrozine) in the absence of BVR.	Ferrozine	167-176	heme oxygenase 1	Homo sapiens	48-52
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Carbon Monoxide	116-118	heme oxygenase 1	Homo sapiens	18-22
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Iron	128-132	heme oxygenase 1	Homo sapiens	0-16
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Iron	128-132	heme oxygenase 1	Homo sapiens	18-22
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Biliverdine	138-148	heme oxygenase 1	Homo sapiens	0-16
20615444-5	2010	The mechanisms of salidroside protected neurons from oxidative stress included the induction of antioxidant enzymes, thioredoxin (Trx), heme oxygenase-1 (HO-1), and peroxiredoxin-I (PrxI); the downregulation of pro-apoptotic protein Bax and the upregulation of anti-apoptotic protein Bcl-X(L).	rhodioloside	18-29	heme oxygenase 1	Homo sapiens	136-152
20679134-1	2010	Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV).	Biliverdine	138-148	heme oxygenase 1	Homo sapiens	18-22
20679134-2	2010	Enzymatic studies with the purified 30-kDa form of HO-1 routinely use a coupled assay containing biliverdin reductase (BVR), which converts BV to bilirubin (BR).	Biliverdine	119-121	heme oxygenase 1	Homo sapiens	51-55
20679134-2	2010	Enzymatic studies with the purified 30-kDa form of HO-1 routinely use a coupled assay containing biliverdin reductase (BVR), which converts BV to bilirubin (BR).	Bilirubin	146-155	heme oxygenase 1	Homo sapiens	51-55
20679134-4	2010	The goal of this study was to determine whether HO-1 activity could be monitored directly by following BV generation or iron release (using the ferrous iron chelator, ferrozine) in the absence of BVR.	Iron	120-124	heme oxygenase 1	Homo sapiens	48-52
20815781-5	2010	Notably, DMSO inhibited methionine sulfoxide reductase activity, induced heme oxygenase-1 (ho-1) mRNA and enhanced oxidant-induced cell death, which indicated that DMSO intensified oxidative stress.	Dimethyl Sulfoxide	9-13	heme oxygenase 1	Homo sapiens	73-89
20815781-5	2010	Notably, DMSO inhibited methionine sulfoxide reductase activity, induced heme oxygenase-1 (ho-1) mRNA and enhanced oxidant-induced cell death, which indicated that DMSO intensified oxidative stress.	Dimethyl Sulfoxide	9-13	heme oxygenase 1	Homo sapiens	91-95
20815781-5	2010	Notably, DMSO inhibited methionine sulfoxide reductase activity, induced heme oxygenase-1 (ho-1) mRNA and enhanced oxidant-induced cell death, which indicated that DMSO intensified oxidative stress.	Dimethyl Sulfoxide	164-168	heme oxygenase 1	Homo sapiens	73-89
20815781-5	2010	Notably, DMSO inhibited methionine sulfoxide reductase activity, induced heme oxygenase-1 (ho-1) mRNA and enhanced oxidant-induced cell death, which indicated that DMSO intensified oxidative stress.	Dimethyl Sulfoxide	164-168	heme oxygenase 1	Homo sapiens	91-95
20921523-0	2010	Naive human T cells are activated and proliferate in response to the heme oxygenase-1 inhibitor tin mesoporphyrin.	tin mesoporphyrin	96-113	heme oxygenase 1	Homo sapiens	69-85
20921523-3	2010	We demonstrate here that the HO-1 inhibitor tin mesoporphyrin (SnMP) induces activation, proliferation, and maturation of naive CD4(+) and CD8(+) T cells via interactions with CD14(+) monocytes in vitro.	tin mesoporphyrin	44-61	heme oxygenase 1	Homo sapiens	29-33
20921523-3	2010	We demonstrate here that the HO-1 inhibitor tin mesoporphyrin (SnMP) induces activation, proliferation, and maturation of naive CD4(+) and CD8(+) T cells via interactions with CD14(+) monocytes in vitro.	tin mesoporphyrin	63-67	heme oxygenase 1	Homo sapiens	29-33
21211285-15	2010	The mRNA expressions of Nrf2, HO-1 and NQO1 were increased in LPS + LXA(4) group compared with LPS group (P &lt; 0.05).	N-(1H-benzimidazol-2-ylmethyl)-2-methoxyacetamide	68-71	heme oxygenase 1	Homo sapiens	30-34
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Heme	55-59	heme oxygenase 1	Homo sapiens	0-16
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Heme	55-59	heme oxygenase 1	Homo sapiens	18-22
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Iron	93-97	heme oxygenase 1	Homo sapiens	0-16
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Iron	93-97	heme oxygenase 1	Homo sapiens	18-22
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Carbon Monoxide	99-114	heme oxygenase 1	Homo sapiens	0-16
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Carbon Monoxide	99-114	heme oxygenase 1	Homo sapiens	18-22
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Biliverdine	119-129	heme oxygenase 1	Homo sapiens	0-16
20819190-1	2010	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin.	Biliverdine	119-129	heme oxygenase 1	Homo sapiens	18-22
20708634-0	2010	GT-repeat polymorphism in the heme oxygenase-1 gene promoter is associated with cardiovascular mortality risk in an arsenic-exposed population in northeastern Taiwan.	Arsenic	116-123	heme oxygenase 1	Homo sapiens	30-46
20708634-3	2010	The relationship of HO-1 genotype with arsenic-associated cardiovascular disease has not been studied.	Arsenic	39-46	heme oxygenase 1	Homo sapiens	20-24
20708634-4	2010	In this study, we evaluated the relationship between the HO-1 GT-repeat polymorphism and cardiovascular mortality in an arsenic-exposed population.	Arsenic	120-127	heme oxygenase 1	Homo sapiens	57-61
20708634-12	2010	Shorter (GT)n repeats in the HO-1 gene promoter may confer protective effects against cardiovascular mortality related to arsenic exposure.	Arsenic	122-129	heme oxygenase 1	Homo sapiens	29-33
21223723-8	2010	The HO-1 mRNA expression and the generation of intracellular ROS were downregulated at a specific concentration of H2O2 in the ALDH2 gene transfected group.	Hydrogen Peroxide	115-119	heme oxygenase 1	Homo sapiens	4-8
20805033-5	2010	Among 42 organoselenium compounds tested, two compounds, 3-selena-1-dethiacephem 13 and 3-selena-1-dethiacephem 14 strongly activated the Nrf2/ARE (antioxidant response element) signaling and thus markedly increased expression of heme oxygenase-1 (HO-1), a phase II antioxidant enzyme.	organoselenium	9-23	heme oxygenase 1	Homo sapiens	230-246
20961405-0	2010	DMF inhibits PDGF-BB induced airway smooth muscle cell proliferation through induction of heme-oxygenase-1.	Dimethyl Fumarate	0-3	heme oxygenase 1	Homo sapiens	90-106
20621084-8	2010	SnPP, a specific inhibitor of HO-1, partly blocked sappanchalcone mediated suppression of inflammatory mediator production, in LPS-stimulated HPDL cells.	S-Nitroso-N-propionyl-D,L-penicillamine	0-4	heme oxygenase 1	Homo sapiens	30-34
20621084-8	2010	SnPP, a specific inhibitor of HO-1, partly blocked sappanchalcone mediated suppression of inflammatory mediator production, in LPS-stimulated HPDL cells.	sappanchalcone	51-65	heme oxygenase 1	Homo sapiens	30-34
20621084-10	2010	The expression of HO-1 protein by sappanchalcone was significantly reduced by pretreatment with JNK inhibitor.	sappanchalcone	34-48	heme oxygenase 1	Homo sapiens	18-22
20621084-11	2010	In conclusion, induction of HO-1 is an important cytoprotective mechanism by which sappanchalcone protects HDP cells from H(2)O(2) and in addition it also exhibits anti-inflammatory effects in LPS-stimulated HPDL cells.	sappanchalcone	83-97	heme oxygenase 1	Homo sapiens	28-32
20621084-0	2010	Effects of sappanchalcone on the cytoprotection and anti-inflammation via heme oxygenase-1 in human pulp and periodontal ligament cells.	sappanchalcone	11-25	heme oxygenase 1	Homo sapiens	74-90
20621084-4	2010	Sappanchalone concentration proportionately increased heme oxygenase (HO)-1 protein expression and enzyme activity in both HDP and HPDL cells.	sappanchalone	0-13	heme oxygenase 1	Homo sapiens	54-75
20621084-6	2010	The cytoprotective effect of sappanchalcone was nullified by HO-1 inhibitor, Tin protoporphyrin (SnPP).	sappanchalcone	29-43	heme oxygenase 1	Homo sapiens	61-65
20621084-6	2010	The cytoprotective effect of sappanchalcone was nullified by HO-1 inhibitor, Tin protoporphyrin (SnPP).	tin protoporphyrin IX	77-95	heme oxygenase 1	Homo sapiens	61-65
20621084-6	2010	The cytoprotective effect of sappanchalcone was nullified by HO-1 inhibitor, Tin protoporphyrin (SnPP).	S-Nitroso-N-propionyl-D,L-penicillamine	97-101	heme oxygenase 1	Homo sapiens	61-65
21112485-11	2010	24-hour treatment with 500 mumol/L H2O2 induced remarkable up-regulation of HO-1 and PARP-1 in ARPE-19 cells.	Hydrogen Peroxide	35-39	heme oxygenase 1	Homo sapiens	76-80
20805033-5	2010	Among 42 organoselenium compounds tested, two compounds, 3-selena-1-dethiacephem 13 and 3-selena-1-dethiacephem 14 strongly activated the Nrf2/ARE (antioxidant response element) signaling and thus markedly increased expression of heme oxygenase-1 (HO-1), a phase II antioxidant enzyme.	organoselenium	9-23	heme oxygenase 1	Homo sapiens	248-252
20805033-5	2010	Among 42 organoselenium compounds tested, two compounds, 3-selena-1-dethiacephem 13 and 3-selena-1-dethiacephem 14 strongly activated the Nrf2/ARE (antioxidant response element) signaling and thus markedly increased expression of heme oxygenase-1 (HO-1), a phase II antioxidant enzyme.	3-selena-1-dethiacephem	57-80	heme oxygenase 1	Homo sapiens	230-246
20805033-5	2010	Among 42 organoselenium compounds tested, two compounds, 3-selena-1-dethiacephem 13 and 3-selena-1-dethiacephem 14 strongly activated the Nrf2/ARE (antioxidant response element) signaling and thus markedly increased expression of heme oxygenase-1 (HO-1), a phase II antioxidant enzyme.	3-selena-1-dethiacephem	57-80	heme oxygenase 1	Homo sapiens	248-252
20805033-5	2010	Among 42 organoselenium compounds tested, two compounds, 3-selena-1-dethiacephem 13 and 3-selena-1-dethiacephem 14 strongly activated the Nrf2/ARE (antioxidant response element) signaling and thus markedly increased expression of heme oxygenase-1 (HO-1), a phase II antioxidant enzyme.	3-selena-1-dethiacephem	88-111	heme oxygenase 1	Homo sapiens	230-246
20805033-5	2010	Among 42 organoselenium compounds tested, two compounds, 3-selena-1-dethiacephem 13 and 3-selena-1-dethiacephem 14 strongly activated the Nrf2/ARE (antioxidant response element) signaling and thus markedly increased expression of heme oxygenase-1 (HO-1), a phase II antioxidant enzyme.	3-selena-1-dethiacephem	88-111	heme oxygenase 1	Homo sapiens	248-252
20678535-7	2010	Western blot showed that hesperidin facilitated ERK/MAPK phosphorylation which appeared to be responsible for nuclear translocation of Nrf2, thereby inducing cytoprotective heme oxygenase-1 (HO-1) expression.	Hesperidin	25-35	heme oxygenase 1	Homo sapiens	173-189
20603117-0	2010	Heme oxygenase 1: another possible target to explain the neuroprotective action of resveratrol, a multifaceted nutrient-based molecule.	Resveratrol	83-94	heme oxygenase 1	Homo sapiens	0-16
20603117-5	2010	Resveratrol protects against experimental stroke: putative neuroprotective role of heme oxygenase 1.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	83-99
20603117-9	2010	), the authors raise a hypothesis that the induction of heme oxygenase 1, an endogenous enzyme that provides resistance against oxidative stress-related neuronal damage, contributes, at least in part, to the neuroprotective action of resveratrol.	Resveratrol	234-245	heme oxygenase 1	Homo sapiens	56-72
20709802-0	2010	Adiponectin-mediated heme oxygenase-1 induction protects against iron-induced liver injury via a PPARalpha dependent mechanism.	Iron	65-69	heme oxygenase 1	Homo sapiens	21-37
20709802-2	2010	Herein, we show that the deleterious effects of iron dextran on liver function and iron deposition were significantly reversed by adiponectin gene therapy, which was accompanied by AMP-activated protein kinase (AMPK) phosphorylation and heme oxygenase (HO)-1 induction.	Iron-Dextran Complex	48-60	heme oxygenase 1	Homo sapiens	237-258
20709802-2	2010	Herein, we show that the deleterious effects of iron dextran on liver function and iron deposition were significantly reversed by adiponectin gene therapy, which was accompanied by AMP-activated protein kinase (AMPK) phosphorylation and heme oxygenase (HO)-1 induction.	Iron	48-52	heme oxygenase 1	Homo sapiens	237-258
20605906-5	2010	Sodium nitroprusside (SNP, an NO donor) and 3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole [YC-1; acts directly on soluble guanylate cyclase (sGC)] led to further relaxation, yet the residual contraction remained 2 to 3 times higher in H(mox)1(-/-) than H(mox)1(+/+) mice (p &lt; 0.001).	3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole	44-91	heme oxygenase 1	Homo sapiens	237-244
20605906-5	2010	Sodium nitroprusside (SNP, an NO donor) and 3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole [YC-1; acts directly on soluble guanylate cyclase (sGC)] led to further relaxation, yet the residual contraction remained 2 to 3 times higher in H(mox)1(-/-) than H(mox)1(+/+) mice (p &lt; 0.001).	Nitroprusside	0-20	heme oxygenase 1	Homo sapiens	237-244
20605906-5	2010	Sodium nitroprusside (SNP, an NO donor) and 3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole [YC-1; acts directly on soluble guanylate cyclase (sGC)] led to further relaxation, yet the residual contraction remained 2 to 3 times higher in H(mox)1(-/-) than H(mox)1(+/+) mice (p &lt; 0.001).	3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole	44-91	heme oxygenase 1	Homo sapiens	255-262
20605906-5	2010	Sodium nitroprusside (SNP, an NO donor) and 3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole [YC-1; acts directly on soluble guanylate cyclase (sGC)] led to further relaxation, yet the residual contraction remained 2 to 3 times higher in H(mox)1(-/-) than H(mox)1(+/+) mice (p &lt; 0.001).	Nitroprusside	0-20	heme oxygenase 1	Homo sapiens	255-262
20668435-0	2010	Docosahexaenoic acid suppresses neuroinflammatory responses and induces heme oxygenase-1 expression in BV-2 microglia: implications of antidepressant effects for omega-3 fatty acids.	Docosahexaenoic Acids	0-20	heme oxygenase 1	Homo sapiens	72-88
20580034-0	2010	Epigallocatechin gallate-mediated protection against tumor necrosis factor-alpha-induced monocyte chemoattractant protein-1 expression is heme oxygenase-1 dependent.	epigallocatechin gallate	0-24	heme oxygenase 1	Homo sapiens	138-154
20580034-3	2010	We hypothesize that flavonoids can down-regulate endothelial inflammatory parameters by modulating HO-1-regulated cell signaling.	Flavonoids	20-30	heme oxygenase 1	Homo sapiens	99-103
20580034-4	2010	We focused on the role of HO-1 and its major metabolic product, bilirubin, on mechanisms of tumor necrosis factor-alpha-induced endothelial cell activation and protection by the catechin epigallocatechin gallate (EGCG).	catechin epigallocatechin gallate	178-211	heme oxygenase 1	Homo sapiens	26-30
20580034-4	2010	We focused on the role of HO-1 and its major metabolic product, bilirubin, on mechanisms of tumor necrosis factor-alpha-induced endothelial cell activation and protection by the catechin epigallocatechin gallate (EGCG).	epigallocatechin gallate	213-217	heme oxygenase 1	Homo sapiens	26-30
20580034-6	2010	Moreover, EGCG up-regulated the expression of HO-1 and further induced the secretion of bilirubin.	epigallocatechin gallate	10-14	heme oxygenase 1	Homo sapiens	46-50
20580034-7	2010	The observed anti-inflammatory effects of EGCG were mimicked by the HO-1 inducer cobalt protoporphyrin and abolished by HO-1 gene silencing.	epigallocatechin gallate	42-46	heme oxygenase 1	Homo sapiens	68-72
20580034-7	2010	The observed anti-inflammatory effects of EGCG were mimicked by the HO-1 inducer cobalt protoporphyrin and abolished by HO-1 gene silencing.	epigallocatechin gallate	42-46	heme oxygenase 1	Homo sapiens	120-124
20580034-7	2010	The observed anti-inflammatory effects of EGCG were mimicked by the HO-1 inducer cobalt protoporphyrin and abolished by HO-1 gene silencing.	cobaltiprotoporphyrin	81-102	heme oxygenase 1	Homo sapiens	68-72
20580034-8	2010	These data suggest that the protective properties of flavonoids, such as EGCG, against endothelial inflammation may be regulated in part though induction of HO-1 and subsequent activator protein-1 signaling.	Flavonoids	53-63	heme oxygenase 1	Homo sapiens	157-196
20580034-8	2010	These data suggest that the protective properties of flavonoids, such as EGCG, against endothelial inflammation may be regulated in part though induction of HO-1 and subsequent activator protein-1 signaling.	epigallocatechin gallate	73-77	heme oxygenase 1	Homo sapiens	157-196
20668435-4	2010	The results of this study showed that DHA reduced expressions of tumor necrosis factor-alpha, interleukin-6, nitric oxide synthase, and cyclo-oxygenase-2, induced by interferon-gamma, and induced upregulation of heme oxygenase-1 (HO-1) in BV-2 microglia.	Docosahexaenoic Acids	38-41	heme oxygenase 1	Homo sapiens	212-228
20668435-4	2010	The results of this study showed that DHA reduced expressions of tumor necrosis factor-alpha, interleukin-6, nitric oxide synthase, and cyclo-oxygenase-2, induced by interferon-gamma, and induced upregulation of heme oxygenase-1 (HO-1) in BV-2 microglia.	Docosahexaenoic Acids	38-41	heme oxygenase 1	Homo sapiens	230-234
20668435-5	2010	The inhibitory effect of DHA on nitric oxide production was abolished by HO-1 inhibitor zinc protoporphyrin IX.	Docosahexaenoic Acids	25-28	heme oxygenase 1	Homo sapiens	73-77
20668435-5	2010	The inhibitory effect of DHA on nitric oxide production was abolished by HO-1 inhibitor zinc protoporphyrin IX.	Nitric Oxide	32-44	heme oxygenase 1	Homo sapiens	73-77
20668435-5	2010	The inhibitory effect of DHA on nitric oxide production was abolished by HO-1 inhibitor zinc protoporphyrin IX.	protoporphyrin IX	93-110	heme oxygenase 1	Homo sapiens	73-77
20668435-6	2010	In addition, DHA caused AKT and ERK activation in a time-dependent manner, and the DHA-induced HO-1 upregulation could be attenuated by PI-3 kinase/AKT and MEK/ERK inhibitors.	Docosahexaenoic Acids	83-86	heme oxygenase 1	Homo sapiens	95-99
20668435-7	2010	DHA also increased IKKalpha/beta phosphorylation, IkappaBalpha phosphorylation, and IkappaBalpha degradation, whereas both nuclear factor-kappaB and IkappaB protease inhibitors could inhibit DHA-induced HO-1 expressions.	Docosahexaenoic Acids	0-3	heme oxygenase 1	Homo sapiens	203-207
20668435-8	2010	The other major n-3 PUFA, eicosapentaenoic acid, showed similar effects of DHA on inflammation and HO-1 in repeated key experiments.	Eicosapentaenoic Acid	26-47	heme oxygenase 1	Homo sapiens	99-103
20615462-7	2010	Inhibition of gamma-GCS or HO-1 prevented the inhibitory effect of FGF9 on MPP(+)-induced H(2)O(2) production and death in mesencephalic dopaminergic and cortical neurons.	mangion-purified polysaccharide (Candida albicans)	75-81	heme oxygenase 1	Homo sapiens	27-31
20732302-0	2010	Altered heme catabolism by heme oxygenase-1 caused by mutations in human NADPH cytochrome P450 reductase.	Heme	8-12	heme oxygenase 1	Homo sapiens	27-43
20732302-1	2010	Human heme oxygenase-1 (HO-1) carries out heme catabolism supported by electrons supplied from the NADPH through NADPH P450 reductase (POR, CPR).	Heme	6-10	heme oxygenase 1	Homo sapiens	24-28
20732302-1	2010	Human heme oxygenase-1 (HO-1) carries out heme catabolism supported by electrons supplied from the NADPH through NADPH P450 reductase (POR, CPR).	NADP	99-104	heme oxygenase 1	Homo sapiens	6-22
20732302-1	2010	Human heme oxygenase-1 (HO-1) carries out heme catabolism supported by electrons supplied from the NADPH through NADPH P450 reductase (POR, CPR).	NADP	99-104	heme oxygenase 1	Homo sapiens	24-28
20732302-4	2010	We used purified preparations of wild type and mutant human POR and in vitro reconstitution with purified HO-1 to measure heme degradation in a coupled assay using biliverdin reductase.	Heme	122-126	heme oxygenase 1	Homo sapiens	106-110
20732302-5	2010	Here we show that mutations in POR found in patients may reduce HO-1 activity, potentially influencing heme catabolism in individuals carrying mutant POR alleles.	Heme	103-107	heme oxygenase 1	Homo sapiens	64-68
20732302-8	2010	Loss of HO-1 activity may result in increased oxidative neurotoxicity, anemia, growth retardation and iron deposition.	Iron	102-106	heme oxygenase 1	Homo sapiens	8-12
20599928-5	2010	CAPE increased the expression of Nrf2-dependent luciferase and heme oxygenase-1, a target gene of Nrf2, and elevated the nuclear level of Nrf2 protein, indicating that CAPE activated the Nrf2 pathway.	caffeic acid phenethyl ester	168-172	heme oxygenase 1	Homo sapiens	63-79
20846452-4	2010	In this study, the association between malaria disease pathogenicity/severity and (GT)n repeat polymorphism in the promoter region of the inducible HO-1 including the effect of cadmium exposure (potent inducer of HO-1 transcription) as well as polymorphism of TNF were investigated.	Cadmium	177-184	heme oxygenase 1	Homo sapiens	148-152
20846452-4	2010	In this study, the association between malaria disease pathogenicity/severity and (GT)n repeat polymorphism in the promoter region of the inducible HO-1 including the effect of cadmium exposure (potent inducer of HO-1 transcription) as well as polymorphism of TNF were investigated.	Cadmium	177-184	heme oxygenase 1	Homo sapiens	213-217
20599928-5	2010	CAPE increased the expression of Nrf2-dependent luciferase and heme oxygenase-1, a target gene of Nrf2, and elevated the nuclear level of Nrf2 protein, indicating that CAPE activated the Nrf2 pathway.	caffeic acid phenethyl ester	0-4	heme oxygenase 1	Homo sapiens	63-79
20615462-7	2010	Inhibition of gamma-GCS or HO-1 prevented the inhibitory effect of FGF9 on MPP(+)-induced H(2)O(2) production and death in mesencephalic dopaminergic and cortical neurons.	Hydrogen Peroxide	90-98	heme oxygenase 1	Homo sapiens	27-31
20822529-4	2010	In this study, we tested the hypothesis that upregulation of HO-1 would inhibit production of the free radical (NO) by interleukin (IL)-1beta-activated human astrocytes.	Free Radicals	98-110	heme oxygenase 1	Homo sapiens	61-65
20600671-7	2010	However, sulforaphane could upregulate the expression of HO-1 and NAD(P)H/quinone oxidoreductase-1 (NQO-1) in cells transfected with the empty vector and the wild-type TDP-43.	sulforaphane	9-21	heme oxygenase 1	Homo sapiens	57-61
20594940-0	2010	Simvastatin-dependent up-regulation of heme oxygenase-1 via mRNA stabilization in human endothelial cells.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	39-55
20594940-1	2010	Heme oxygenase (HO)-1, which is the inducible isoform of the rate-limiting enzyme of heme degradation, has potent antioxidant and anti-inflammatory effects and is an emerging therapeutic target for the treatment of cardiovascular disease.	Heme	85-89	heme oxygenase 1	Homo sapiens	0-21
20594940-3	2010	To further investigate the statin-specific HO-1 regulation, we examined HO-1 gene expression by simvastatin in cell cultures of human endothelial cells.	Simvastatin	96-107	heme oxygenase 1	Homo sapiens	72-76
20594940-4	2010	Simvastatin-dependent HO-1 gene activation was significantly reduced by pharmacological inhibition of the p38 MAPK and phosphotidylinositol-3-kinase (PI3K)/Akt pathways.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	22-26
20594940-5	2010	Although HO-1 is considered to be primarily regulated at the transcriptional level, simvastatin induced activity of a human HO-1 promoter gene construct only to a minor extent.	Simvastatin	84-95	heme oxygenase 1	Homo sapiens	124-128
20594940-6	2010	By contrast, studies with actinomycin D indicated that the half-life of HO-1 mRNA was significantly prolonged in the presence of simvastatin suggesting a post-transcriptional mode of HO-1 regulation.	Dactinomycin	26-39	heme oxygenase 1	Homo sapiens	72-76
20594940-6	2010	By contrast, studies with actinomycin D indicated that the half-life of HO-1 mRNA was significantly prolonged in the presence of simvastatin suggesting a post-transcriptional mode of HO-1 regulation.	Dactinomycin	26-39	heme oxygenase 1	Homo sapiens	183-187
20594940-6	2010	By contrast, studies with actinomycin D indicated that the half-life of HO-1 mRNA was significantly prolonged in the presence of simvastatin suggesting a post-transcriptional mode of HO-1 regulation.	Simvastatin	129-140	heme oxygenase 1	Homo sapiens	72-76
20594940-6	2010	By contrast, studies with actinomycin D indicated that the half-life of HO-1 mRNA was significantly prolonged in the presence of simvastatin suggesting a post-transcriptional mode of HO-1 regulation.	Simvastatin	129-140	heme oxygenase 1	Homo sapiens	183-187
20822529-3	2010	Deleterious free heme is degraded by HO-1 to carbon monoxide, iron and biliverdin, which have potent anti-oxidant and anti-inflammatory properties.	Heme	17-21	heme oxygenase 1	Homo sapiens	37-41
20822529-3	2010	Deleterious free heme is degraded by HO-1 to carbon monoxide, iron and biliverdin, which have potent anti-oxidant and anti-inflammatory properties.	Carbon Monoxide	45-60	heme oxygenase 1	Homo sapiens	37-41
20822529-3	2010	Deleterious free heme is degraded by HO-1 to carbon monoxide, iron and biliverdin, which have potent anti-oxidant and anti-inflammatory properties.	Iron	62-66	heme oxygenase 1	Homo sapiens	37-41
20822529-10	2010	Pretreatment with hemin alone substantially induced both HO-1 mRNA and protein expression, and HO-1 mRNA expression was further enhanced when hemin was combined with IL-1beta treatment.	Hemin	18-23	heme oxygenase 1	Homo sapiens	57-61
20822529-3	2010	Deleterious free heme is degraded by HO-1 to carbon monoxide, iron and biliverdin, which have potent anti-oxidant and anti-inflammatory properties.	Biliverdine	71-81	heme oxygenase 1	Homo sapiens	37-41
20822529-12	2010	When pretreated with SnPP, the inhibitory effect of hemin on IL-1beta-induced NO production and iNOS expression was reversed, suggesting the involvement of HO-1.	S-Nitroso-N-propionyl-D,L-penicillamine	21-25	heme oxygenase 1	Homo sapiens	156-160
20558128-0	2010	Piceatannol induces heme oxygenase-1 expression in human mammary epithelial cells through activation of ARE-driven Nrf2 signaling.	3,3',4,5'-tetrahydroxystilbene	0-11	heme oxygenase 1	Homo sapiens	20-36
20558128-12	2010	The thiol reducing agents, dithiothreitol (100 microM) or beta-mercaptoethanol (1.4 microM), attenuated piceatannol-induced Nrf2 activation and HO-1 expression.	Sulfhydryl Compounds	4-9	heme oxygenase 1	Homo sapiens	144-148
20478284-0	2010	High selenium status in individuals exposed to arsenic through coal-burning in Shaanxi (PR of China) modulates antioxidant enzymes, heme oxygenase-1 and DNA damage.	Selenium	5-13	heme oxygenase 1	Homo sapiens	132-148
20478284-0	2010	High selenium status in individuals exposed to arsenic through coal-burning in Shaanxi (PR of China) modulates antioxidant enzymes, heme oxygenase-1 and DNA damage.	Arsenic	47-54	heme oxygenase 1	Homo sapiens	132-148
20478284-4	2010	RESULTS: High selenium status was correlated with elevated activities of serum superoxide dismutase, glutathione peroxidase, catalase, and reduced levels of malondialdehyde, and increased RNA and protein expression of heme oxygenase-1 in peripheral blood mononuclear cells (PBMC) of individuals in the high arsenic group.	Selenium	14-22	heme oxygenase 1	Homo sapiens	218-234
20478284-4	2010	RESULTS: High selenium status was correlated with elevated activities of serum superoxide dismutase, glutathione peroxidase, catalase, and reduced levels of malondialdehyde, and increased RNA and protein expression of heme oxygenase-1 in peripheral blood mononuclear cells (PBMC) of individuals in the high arsenic group.	Arsenic	307-314	heme oxygenase 1	Homo sapiens	218-234
20558128-12	2010	The thiol reducing agents, dithiothreitol (100 microM) or beta-mercaptoethanol (1.4 microM), attenuated piceatannol-induced Nrf2 activation and HO-1 expression.	Dithiothreitol	27-41	heme oxygenase 1	Homo sapiens	144-148
20558128-12	2010	The thiol reducing agents, dithiothreitol (100 microM) or beta-mercaptoethanol (1.4 microM), attenuated piceatannol-induced Nrf2 activation and HO-1 expression.	Mercaptoethanol	58-78	heme oxygenase 1	Homo sapiens	144-148
20558128-12	2010	The thiol reducing agents, dithiothreitol (100 microM) or beta-mercaptoethanol (1.4 microM), attenuated piceatannol-induced Nrf2 activation and HO-1 expression.	3,3',4,5'-tetrahydroxystilbene	104-115	heme oxygenase 1	Homo sapiens	144-148
20558128-13	2010	It is hence likely that piceatannol modifies specific cysteine residues of Keap1, which allows Nrf2 to translocate into the nucleus and bind to ARE, leading to enhancement of the expression of HO-1.	3,3',4,5'-tetrahydroxystilbene	24-35	heme oxygenase 1	Homo sapiens	193-197
20558128-13	2010	It is hence likely that piceatannol modifies specific cysteine residues of Keap1, which allows Nrf2 to translocate into the nucleus and bind to ARE, leading to enhancement of the expression of HO-1.	Cysteine	54-62	heme oxygenase 1	Homo sapiens	193-197
20558128-14	2010	The characteristic catechol moiety of piceatannol appears to be critical for induction of Nrf2 activation and subsequent upregulation of HO-1.	catechol	19-27	heme oxygenase 1	Homo sapiens	137-141
20558128-14	2010	The characteristic catechol moiety of piceatannol appears to be critical for induction of Nrf2 activation and subsequent upregulation of HO-1.	3,3',4,5'-tetrahydroxystilbene	38-49	heme oxygenase 1	Homo sapiens	137-141
20558128-3	2010	In the present study, we found that piceatannol treatment (30 microM) significantly upregulated the expression of the antioxidant enzyme heme oxygenase-1 (HO-1) and its mRNA transcript at 6h and 3h, respectively in human breast epithelial (MCF10A) cells.	3,3',4,5'-tetrahydroxystilbene	36-47	heme oxygenase 1	Homo sapiens	137-153
20558128-3	2010	In the present study, we found that piceatannol treatment (30 microM) significantly upregulated the expression of the antioxidant enzyme heme oxygenase-1 (HO-1) and its mRNA transcript at 6h and 3h, respectively in human breast epithelial (MCF10A) cells.	3,3',4,5'-tetrahydroxystilbene	36-47	heme oxygenase 1	Homo sapiens	155-159
20558128-6	2010	Upregulation of HO-1 expression by piceatannol through direct binding of Nrf2 to antioxidant response element (ARE) was verified by the chromatin immunoprecipitation (ChIP) assay.	3,3',4,5'-tetrahydroxystilbene	35-46	heme oxygenase 1	Homo sapiens	16-20
20558128-7	2010	siRNA knock down of Nrf2 gene abolished piceatannol-induced HO-1 expression.	3,3',4,5'-tetrahydroxystilbene	40-51	heme oxygenase 1	Homo sapiens	60-64
20558128-8	2010	In addition, piceatannol-induced activation of Nrf2 and/or HO-1 expression was abrogated by the pharmacological inhibitor (LY294002) as well as the kinase-dead form of Akt.	3,3',4,5'-tetrahydroxystilbene	13-24	heme oxygenase 1	Homo sapiens	59-63
20558128-8	2010	In addition, piceatannol-induced activation of Nrf2 and/or HO-1 expression was abrogated by the pharmacological inhibitor (LY294002) as well as the kinase-dead form of Akt.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	123-131	heme oxygenase 1	Homo sapiens	59-63
20558128-9	2010	In an attempt to elucidate the molecular mechanisms underlying cytoprotective or chemoprotective activity exerted by piceatannol, we examined its effect on the signaling pathways responsible for induction of HO-1 expression.	3,3',4,5'-tetrahydroxystilbene	117-128	heme oxygenase 1	Homo sapiens	208-212
20580464-3	2010	A different iron metabolism gene signature was detected in both macrophage types, with the heme regulatory molecules CD163 and Heme Oxygenase-1 (HO-1) being preferentially expressed by M2 (M-CSF) macrophages.	Iron	12-16	heme oxygenase 1	Homo sapiens	145-149
20580464-3	2010	A different iron metabolism gene signature was detected in both macrophage types, with the heme regulatory molecules CD163 and Heme Oxygenase-1 (HO-1) being preferentially expressed by M2 (M-CSF) macrophages.	Heme	91-95	heme oxygenase 1	Homo sapiens	145-149
20580464-6	2010	In contrast to the HO-1 inhibitor tin protoporphyrin (SnPP), the administration of cobalt protoporphyrin (CoPP), a potent inducer of HO-1 resulted in increased LPS-triggered IL-10 release from M2 (M-CSF) macrophages.	cobaltiprotoporphyrin	83-104	heme oxygenase 1	Homo sapiens	133-137
20644008-10	2010	We conclude that estradiol via ER-alpha promotes EPC-mediated capillary formation by a mechanism that involves nongenomic activation of RTKs and HO-1 activation.	Estradiol	17-26	heme oxygenase 1	Homo sapiens	145-149
20580464-6	2010	In contrast to the HO-1 inhibitor tin protoporphyrin (SnPP), the administration of cobalt protoporphyrin (CoPP), a potent inducer of HO-1 resulted in increased LPS-triggered IL-10 release from M2 (M-CSF) macrophages.	cobaltiprotoporphyrin	106-110	heme oxygenase 1	Homo sapiens	133-137
20644008-2	2010	Because estradiol augments vascular repair, we hypothesize that estradiol increases EPC proliferation and capillary formation via RTK activation and induction of HO-1.	Estradiol	8-17	heme oxygenase 1	Homo sapiens	162-166
20644008-2	2010	Because estradiol augments vascular repair, we hypothesize that estradiol increases EPC proliferation and capillary formation via RTK activation and induction of HO-1.	Estradiol	64-73	heme oxygenase 1	Homo sapiens	162-166
20644008-7	2010	Estradiol increased HO-1 expression by 2- to 3-fold, an effect blocked by SU5416, and PPT mimicked the effects of estradiol on HO-1.	Estradiol	0-9	heme oxygenase 1	Homo sapiens	20-24
20551909-8	2010	At 24 hours postinjury, despite equivalent levels of tubular necrosis, apoptosis, and capillary density between groups, the injection of Ad-HO-1 M phi resulted in preserved renal function (serum creatinine reduced by 46%), and reduced microvascular platelet deposition.	Creatinine	195-205	heme oxygenase 1	Homo sapiens	140-144
20644008-7	2010	Estradiol increased HO-1 expression by 2- to 3-fold, an effect blocked by SU5416, and PPT mimicked the effects of estradiol on HO-1.	4,4',4''-(4-propyl-((1)H)-pyrazole-1,3,5-triyl) tris-phenol	86-89	heme oxygenase 1	Homo sapiens	127-131
20644008-7	2010	Estradiol increased HO-1 expression by 2- to 3-fold, an effect blocked by SU5416, and PPT mimicked the effects of estradiol on HO-1.	Estradiol	114-123	heme oxygenase 1	Homo sapiens	127-131
20644008-8	2010	The ability of estradiol to enhance capillary formation, increase expression of HO-1, and augment phosphorylation of extracellular signal-regulated kinase 1/2, Akt, and vascular endothelial growth factor receptor 2 was mimicked by its cell-impermeable analog BSA estradiol.	Estradiol	15-24	heme oxygenase 1	Homo sapiens	80-84
20502928-2	2010	Two heme oxygenase isoforms, HO-1 and HO-2, exist that differ in several ways, including a complete lack of Cys residues in HO-1 and the presence of three Cys residues as part of heme-regulatory motifs (HRMs) in HO-2.	Cysteine	108-111	heme oxygenase 1	Homo sapiens	29-42
20502928-2	2010	Two heme oxygenase isoforms, HO-1 and HO-2, exist that differ in several ways, including a complete lack of Cys residues in HO-1 and the presence of three Cys residues as part of heme-regulatory motifs (HRMs) in HO-2.	Cysteine	108-111	heme oxygenase 1	Homo sapiens	29-33
20502928-2	2010	Two heme oxygenase isoforms, HO-1 and HO-2, exist that differ in several ways, including a complete lack of Cys residues in HO-1 and the presence of three Cys residues as part of heme-regulatory motifs (HRMs) in HO-2.	Cysteine	155-158	heme oxygenase 1	Homo sapiens	29-42
20502928-2	2010	Two heme oxygenase isoforms, HO-1 and HO-2, exist that differ in several ways, including a complete lack of Cys residues in HO-1 and the presence of three Cys residues as part of heme-regulatory motifs (HRMs) in HO-2.	Cysteine	155-158	heme oxygenase 1	Homo sapiens	29-33
20502928-8	2010	These findings are consistent with the presence of a hydrogen-bonding network at the heme"s distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1.	Hydrogen	53-61	heme oxygenase 1	Homo sapiens	198-202
20502928-8	2010	These findings are consistent with the presence of a hydrogen-bonding network at the heme"s distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1.	Heme	85-89	heme oxygenase 1	Homo sapiens	198-202
20536682-9	2010	The neuroprotective effect was prevented by chelerythrine, LY294002, and Sn (IV) protoporphyrin IX dichloride (SnPP), indicating the participation of the PKC/PI3K/Akt activation and induction of the antioxidant enzyme heme oxygenase-1.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	59-67	heme oxygenase 1	Homo sapiens	218-234
20536682-9	2010	The neuroprotective effect was prevented by chelerythrine, LY294002, and Sn (IV) protoporphyrin IX dichloride (SnPP), indicating the participation of the PKC/PI3K/Akt activation and induction of the antioxidant enzyme heme oxygenase-1.	S-Nitroso-N-propionyl-D,L-penicillamine	111-115	heme oxygenase 1	Homo sapiens	218-234
20838567-6	2010	In addition, Western blots showed that ATX elevated of heme oxygenase-1 (HO-1; Hsp32) and Hsp70 protein levels in in vitro.	astaxanthine	39-42	heme oxygenase 1	Homo sapiens	55-77
20838567-6	2010	In addition, Western blots showed that ATX elevated of heme oxygenase-1 (HO-1; Hsp32) and Hsp70 protein levels in in vitro.	astaxanthine	39-42	heme oxygenase 1	Homo sapiens	79-84
20551909-6	2010	In vitro Ad-HO-1 M phi showed an anti-inflammatory phenotype with increased phagocytosis of apoptotic cells (ACs) and increased interleukin (IL)-10 but reduced TNF-alpha and nitric oxide (NO) following lipopolysaccharide/interferon-gamma (IFN gamma) stimulation compared to control transduced or unmodified M phi.	Nitric Oxide	174-186	heme oxygenase 1	Homo sapiens	12-16
20638469-7	2010	An induction of HO-1 expression was observed from concentrations above 5 microM of 4-HNE.	4-hydroxy-2-nonenal	83-88	heme oxygenase 1	Homo sapiens	16-20
20539916-3	2010	One of the proteins important for neovascularisation is heme oxygenase-1 (HO-1), an enzyme degrading heme.	Heme	56-60	heme oxygenase 1	Homo sapiens	74-78
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Heme	88-92	heme oxygenase 1	Homo sapiens	12-28
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Heme	88-92	heme oxygenase 1	Homo sapiens	30-34
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	12-28
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	30-34
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Bilirubin	115-124	heme oxygenase 1	Homo sapiens	12-28
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Bilirubin	115-124	heme oxygenase 1	Homo sapiens	30-34
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Iron	135-139	heme oxygenase 1	Homo sapiens	12-28
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Iron	135-139	heme oxygenase 1	Homo sapiens	30-34
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Iron	141-143	heme oxygenase 1	Homo sapiens	12-28
20689484-1	2010	OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe).	Iron	141-143	heme oxygenase 1	Homo sapiens	30-34
20689484-4	2010	METHODS: Changes in the HO-1 activity after AMI were analyzed by measuring serum levels of bilirubin and Fe.	Bilirubin	91-100	heme oxygenase 1	Homo sapiens	24-28
20689484-9	2010	Furthermore, the serum HO-1 protein level was elevated, and its change was significantly correlated with the change in bilirubin level (r = 0.82, P &lt; 0.005).	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	23-27
20796278-0	2010	GT-repeat polymorphism in the heme oxygenase-1 gene promoter and the risk of carotid atherosclerosis related to arsenic exposure.	Arsenic	112-119	heme oxygenase 1	Homo sapiens	30-46
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Heme	67-71	heme oxygenase 1	Homo sapiens	12-28
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Heme	67-71	heme oxygenase 1	Homo sapiens	30-34
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Carbon Monoxide	77-92	heme oxygenase 1	Homo sapiens	12-28
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Carbon Monoxide	77-92	heme oxygenase 1	Homo sapiens	30-34
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Biliverdine	94-104	heme oxygenase 1	Homo sapiens	12-28
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Biliverdine	94-104	heme oxygenase 1	Homo sapiens	30-34
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Iron	115-119	heme oxygenase 1	Homo sapiens	12-28
20832528-1	2010	BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron.	Iron	115-119	heme oxygenase 1	Homo sapiens	30-34
20796278-1	2010	BACKGROUND: Arsenic is a strong stimulus of heme oxygenase (HO)-1 expression in experimental studies in response to oxidative stress caused by a stimulus.	Arsenic	12-19	heme oxygenase 1	Homo sapiens	44-65
20796278-5	2010	In this study, we investigated the relationship between HO-1 genetic polymorphism and the risk of atherosclerosis related to arsenic.	Arsenic	125-132	heme oxygenase 1	Homo sapiens	56-60
20796278-13	2010	CONCLUSIONS: This exploratory study suggests that at a relatively high level of arsenic exposure, carriers of the short (GT)n allele (&lt; 27 repeats) in the HO-1 gene promoter had a lower probability of developing carotid atherosclerosis than non-carriers of the allele after long-term arsenic exposure via ground water.	Arsenic	80-87	heme oxygenase 1	Homo sapiens	158-162
20796278-13	2010	CONCLUSIONS: This exploratory study suggests that at a relatively high level of arsenic exposure, carriers of the short (GT)n allele (&lt; 27 repeats) in the HO-1 gene promoter had a lower probability of developing carotid atherosclerosis than non-carriers of the allele after long-term arsenic exposure via ground water.	Arsenic	287-294	heme oxygenase 1	Homo sapiens	158-162
20796278-13	2010	CONCLUSIONS: This exploratory study suggests that at a relatively high level of arsenic exposure, carriers of the short (GT)n allele (&lt; 27 repeats) in the HO-1 gene promoter had a lower probability of developing carotid atherosclerosis than non-carriers of the allele after long-term arsenic exposure via ground water.	Water	315-320	heme oxygenase 1	Homo sapiens	158-162
20796278-14	2010	The short (GT)n repeat in the HO-1 gene promoter may provide protective effects against carotid atherosclerosis in individuals with a high level of arsenic exposure.	Arsenic	148-155	heme oxygenase 1	Homo sapiens	30-34
20511222-6	2010	Treatment with hydrogen peroxide (H(2)O(2)) enhances the nuclear colocalization of NRF2 and NRP/B and induces heme oxygenase 1 (HO1).	Hydrogen Peroxide	15-32	heme oxygenase 1	Homo sapiens	110-126
20811623-5	2010	Plasma HO-1 concentrations were significantly correlated with plasma glucose concentrations, HOMA-beta and HOMA-IR (P&lt;0.001).	Glucose	69-76	heme oxygenase 1	Homo sapiens	7-11
20511222-6	2010	Treatment with hydrogen peroxide (H(2)O(2)) enhances the nuclear colocalization of NRF2 and NRP/B and induces heme oxygenase 1 (HO1).	Hydrogen Peroxide	15-32	heme oxygenase 1	Homo sapiens	128-131
20511222-6	2010	Treatment with hydrogen peroxide (H(2)O(2)) enhances the nuclear colocalization of NRF2 and NRP/B and induces heme oxygenase 1 (HO1).	Hydrogen Peroxide	34-42	heme oxygenase 1	Homo sapiens	110-126
20511222-6	2010	Treatment with hydrogen peroxide (H(2)O(2)) enhances the nuclear colocalization of NRF2 and NRP/B and induces heme oxygenase 1 (HO1).	Hydrogen Peroxide	34-42	heme oxygenase 1	Homo sapiens	128-131
20515663-4	2010	Zinc protoporphyrin IX (ZnPP IX), a HO-1 inhibitor, attenuated thrombin-induced injury of cortical cells in a concentration-dependent manner (0.3-3 microM) and tended to inhibit shrinkage of the striatal tissue at 0.3 microM.	zinc protoporphyrin	0-22	heme oxygenase 1	Homo sapiens	36-40
20515663-4	2010	Zinc protoporphyrin IX (ZnPP IX), a HO-1 inhibitor, attenuated thrombin-induced injury of cortical cells in a concentration-dependent manner (0.3-3 microM) and tended to inhibit shrinkage of the striatal tissue at 0.3 microM.	zinc protoporphyrin	24-31	heme oxygenase 1	Homo sapiens	36-40
20515663-6	2010	The increase of HO-1 protein was suppressed by a p38 MAPK inhibitor SB203580, and early activation of p38 MAPK after thrombin treatment was observed in neurons and microglia in the striatum.	SB 203580	68-76	heme oxygenase 1	Homo sapiens	16-20
20515663-10	2010	Thrombin-induced cortical injury may be also regulated by the expression of HO-1 and the resultant production of heme degradation products such as carbon monoxide.	Carbon Monoxide	147-162	heme oxygenase 1	Homo sapiens	76-80
20430097-6	2010	Pretreatment with the mitogen-activated protein kinase kinase 1/2 (MEK1/2) inhibitor, U0126, inhibited CaMKII-induced stimulation of HO-1 promoter activity, suggesting that ERK1/2 is a downstream mediator of CaMKII in BDMC signaling to HO-1 expression.	U 0126	86-91	heme oxygenase 1	Homo sapiens	133-137
20504881-0	2010	Parenteral iron formulations differentially affect MCP-1, HO-1, and NGAL gene expression and renal responses to injury.	Iron	11-15	heme oxygenase 1	Homo sapiens	58-62
20504881-12	2010	We conclude that 1) parenteral iron formulations that stimulate redox signaling can evoke cyto/nephrotoxicity; 2) secondary adaptive responses to this injury (e.g., HO-1/NGAL induction) can initiate a renal tubular cytoresistant state; this suggests a potential new clinical application for intravenous Fe therapy; and 3) FMX is bioneutral regarding these responses.	Iron	31-35	heme oxygenase 1	Homo sapiens	165-169
20508205-5	2010	The presence of the S allele led to higher basal HO-1 expression and stronger induction in response to cobalt protoporphyrin, prostaglandin-J(2), hydrogen peroxide, and lipopolysaccharide.	Hydrogen Peroxide	146-163	heme oxygenase 1	Homo sapiens	49-53
20806083-0	2010	Resveratrol protects human lens epithelial cells against H2O2-induced oxidative stress by increasing catalase, SOD-1, and HO-1 expression.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	122-126
20806083-0	2010	Resveratrol protects human lens epithelial cells against H2O2-induced oxidative stress by increasing catalase, SOD-1, and HO-1 expression.	Hydrogen Peroxide	57-61	heme oxygenase 1	Homo sapiens	122-126
20806083-9	2010	RESULTS: Resveratrol clearly reduced H(2)O(2) induced cell apoptosis and ROS accumulation; protected HLEB-3 cells from H(2)O(2) induced oxidative damage, and increased the expression levels of SOD-1, catalase, and HO-1.	Resveratrol	9-20	heme oxygenase 1	Homo sapiens	214-218
20430097-0	2010	Up-regulation of heme oxygenase-1 expression through CaMKII-ERK1/2-Nrf2 signaling mediates the anti-inflammatory effect of bisdemethoxycurcumin in LPS-stimulated macrophages.	bisdemethoxycurcumin	123-143	heme oxygenase 1	Homo sapiens	17-33
20430097-1	2010	We have identified a novel anti-inflammatory signaling pathway that leads to the expression of heme oxygenase-1 (HO-1) in response to bisdemethoxycurcumin (BDMC), an analog of curcumin.	bisdemethoxycurcumin	134-154	heme oxygenase 1	Homo sapiens	95-111
20430097-1	2010	We have identified a novel anti-inflammatory signaling pathway that leads to the expression of heme oxygenase-1 (HO-1) in response to bisdemethoxycurcumin (BDMC), an analog of curcumin.	bisdemethoxycurcumin	134-154	heme oxygenase 1	Homo sapiens	113-117
20430097-6	2010	Pretreatment with the mitogen-activated protein kinase kinase 1/2 (MEK1/2) inhibitor, U0126, inhibited CaMKII-induced stimulation of HO-1 promoter activity, suggesting that ERK1/2 is a downstream mediator of CaMKII in BDMC signaling to HO-1 expression.	U 0126	86-91	heme oxygenase 1	Homo sapiens	236-240
20430097-1	2010	We have identified a novel anti-inflammatory signaling pathway that leads to the expression of heme oxygenase-1 (HO-1) in response to bisdemethoxycurcumin (BDMC), an analog of curcumin.	bisdemethoxycurcumin	156-160	heme oxygenase 1	Homo sapiens	95-111
20430097-6	2010	Pretreatment with the mitogen-activated protein kinase kinase 1/2 (MEK1/2) inhibitor, U0126, inhibited CaMKII-induced stimulation of HO-1 promoter activity, suggesting that ERK1/2 is a downstream mediator of CaMKII in BDMC signaling to HO-1 expression.	bisdemethoxycurcumin	218-222	heme oxygenase 1	Homo sapiens	133-137
20430097-1	2010	We have identified a novel anti-inflammatory signaling pathway that leads to the expression of heme oxygenase-1 (HO-1) in response to bisdemethoxycurcumin (BDMC), an analog of curcumin.	bisdemethoxycurcumin	156-160	heme oxygenase 1	Homo sapiens	113-117
20430097-1	2010	We have identified a novel anti-inflammatory signaling pathway that leads to the expression of heme oxygenase-1 (HO-1) in response to bisdemethoxycurcumin (BDMC), an analog of curcumin.	Curcumin	146-154	heme oxygenase 1	Homo sapiens	95-111
20430097-9	2010	Collectively, our findings identify a Ca(2+)/calmodulin-CaMKII-ERK1/2-Nrf2 cascade as a novel anti-inflammatory pathway mediating BDMC signaling to HO-1 expression in macrophages.	bisdemethoxycurcumin	130-134	heme oxygenase 1	Homo sapiens	148-152
20430097-1	2010	We have identified a novel anti-inflammatory signaling pathway that leads to the expression of heme oxygenase-1 (HO-1) in response to bisdemethoxycurcumin (BDMC), an analog of curcumin.	Curcumin	146-154	heme oxygenase 1	Homo sapiens	113-117
20430097-4	2010	The signaling pathway involved in BDMC-mediated HO-1 induction included Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) and extracellular signal-regulated kinase 1/2 (ERK1/2).	bisdemethoxycurcumin	34-38	heme oxygenase 1	Homo sapiens	48-52
20647090-4	2010	RESULTS: HO-1 induction by cobaltic protoporphyrin IX (CoPP) in HDPCs increased cell growth and mineralization and up-regulated the messenger RNA expression of such odontoblastic markers as alkaline phosphatase, osteopontin, bone sialoprotein, dentin matrix protein-1, and dentin sialophosphoprotein.	cobaltic protoporphyrin ix	27-53	heme oxygenase 1	Homo sapiens	9-13
20722927-2	2010	We investigated the activation of HO-1 by whisky, which contains various phenolic substances.	whisky	42-48	heme oxygenase 1	Homo sapiens	34-38
20647090-4	2010	RESULTS: HO-1 induction by cobaltic protoporphyrin IX (CoPP) in HDPCs increased cell growth and mineralization and up-regulated the messenger RNA expression of such odontoblastic markers as alkaline phosphatase, osteopontin, bone sialoprotein, dentin matrix protein-1, and dentin sialophosphoprotein.	copp	55-59	heme oxygenase 1	Homo sapiens	9-13
20647090-6	2010	CONCLUSIONS: CoPP treatment results in dental pulp cell proliferation and odontoblast differentiation that appears partly mediated by HO-1.	copp	13-17	heme oxygenase 1	Homo sapiens	134-138
20722927-4	2010	To determine the compounds with potent HO-1-inducing activity among the whisky congeners, several chemicals that had been reported to exist in whisky or oak barrels were screened, and coniferyl aldehyde and sinapyl aldehyde showed the activity.	coniferaldehyde	184-202	heme oxygenase 1	Homo sapiens	39-43
20722927-4	2010	To determine the compounds with potent HO-1-inducing activity among the whisky congeners, several chemicals that had been reported to exist in whisky or oak barrels were screened, and coniferyl aldehyde and sinapyl aldehyde showed the activity.	sinapyl aldehyde	207-223	heme oxygenase 1	Homo sapiens	39-43
20430037-0	2010	Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin.	Biliverdine	14-24	heme oxygenase 1	Homo sapiens	108-124
20430037-0	2010	Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin.	Bilirubin	28-37	heme oxygenase 1	Homo sapiens	108-124
20430037-0	2010	Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin.	Bilirubin	181-190	heme oxygenase 1	Homo sapiens	108-124
20430037-2	2010	HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS).	Bilirubin	13-22	heme oxygenase 1	Homo sapiens	0-4
20430037-2	2010	HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS).	reactive oxygen and nitrogen species	52-88	heme oxygenase 1	Homo sapiens	0-4
20430037-2	2010	HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS).	rons	90-94	heme oxygenase 1	Homo sapiens	0-4
20430037-3	2010	It remains to determine whether conversion of biliverdin to bilirubin is an essential step for HO-1-conferred protection of endothelial cells.	Biliverdine	46-56	heme oxygenase 1	Homo sapiens	95-99
20486808-5	2010	HO-1 was induced by infection with a recombinant adenovirus carrying the human HO-1 gene or an inducer of HO-1 activity, cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	121-145	heme oxygenase 1	Homo sapiens	0-4
20430037-3	2010	It remains to determine whether conversion of biliverdin to bilirubin is an essential step for HO-1-conferred protection of endothelial cells.	Bilirubin	60-69	heme oxygenase 1	Homo sapiens	95-99
20430037-7	2010	HO-1- and BVR-silenced cells have increased levels of oxidative stress and bilirubin but not biliverdin increased expression of the protective protein GTP-cyclohydrolase.	Bilirubin	75-84	heme oxygenase 1	Homo sapiens	0-4
20430037-8	2010	Moreover, protection by hemin-induced HO-1 expression or biliverdin-triggered bilirubin formation was impaired upon silencing of the HO-1 or BVR gene, respectively.	Biliverdine	57-67	heme oxygenase 1	Homo sapiens	133-137
20430037-8	2010	Moreover, protection by hemin-induced HO-1 expression or biliverdin-triggered bilirubin formation was impaired upon silencing of the HO-1 or BVR gene, respectively.	Bilirubin	78-87	heme oxygenase 1	Homo sapiens	133-137
20486808-5	2010	HO-1 was induced by infection with a recombinant adenovirus carrying the human HO-1 gene or an inducer of HO-1 activity, cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	147-151	heme oxygenase 1	Homo sapiens	0-4
20471992-9	2010	The HO-1 competitive inhibitor zinc protoporphyrin partially but significantly restored the sensitivity of precultured monocytes to CBD-mediated apoptosis.	zinc protoporphyrin	31-50	heme oxygenase 1	Homo sapiens	4-8
20536138-7	2010	In parallel, andrographolide significantly induced the expression of HO-1 in a concentration-dependent fashion (p &lt; 0.05).	andrographolide	13-28	heme oxygenase 1	Homo sapiens	69-73
20501657-3	2010	Oxidative stress induced by H(2)O(2) led to an increase in MARE activity and expression of heme oxygenase-1 (HO-1), an inducible antioxidant defense enzyme.	Hydrogen Peroxide	28-36	heme oxygenase 1	Homo sapiens	91-107
20501657-3	2010	Oxidative stress induced by H(2)O(2) led to an increase in MARE activity and expression of heme oxygenase-1 (HO-1), an inducible antioxidant defense enzyme.	Hydrogen Peroxide	28-36	heme oxygenase 1	Homo sapiens	109-113
20501657-6	2010	In contrast, Bach1 overexpression abolished HO-1 induction by H(2)O(2), which led to increased reactive oxygen species accumulation.	Hydrogen Peroxide	62-70	heme oxygenase 1	Homo sapiens	44-48
20501657-6	2010	In contrast, Bach1 overexpression abolished HO-1 induction by H(2)O(2), which led to increased reactive oxygen species accumulation.	Reactive Oxygen Species	95-118	heme oxygenase 1	Homo sapiens	44-48
20599745-0	2010	Celastrol suppresses IFN-gamma-induced ICAM-1 expression and subsequent monocyte adhesiveness via the induction of heme oxygenase-1 in the HaCaT cells.	celastrol	0-9	heme oxygenase 1	Homo sapiens	115-131
20599745-3	2010	We found that celastrol induced mRNA and protein expression of heme oxygenase-1 (HO-1) in the human keratinocyte cell line HaCaT.	celastrol	14-23	heme oxygenase 1	Homo sapiens	63-79
20599745-3	2010	We found that celastrol induced mRNA and protein expression of heme oxygenase-1 (HO-1) in the human keratinocyte cell line HaCaT.	celastrol	14-23	heme oxygenase 1	Homo sapiens	81-85
20599745-4	2010	Treatment of HaCaT cells with tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, reversed the suppressive effect of celastrol on IFN-gamma-induced protein and mRNA expression of ICAM-1.	tin protoporphyrin IX	30-51	heme oxygenase 1	Homo sapiens	84-88
20599745-4	2010	Treatment of HaCaT cells with tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, reversed the suppressive effect of celastrol on IFN-gamma-induced protein and mRNA expression of ICAM-1.	S-Nitroso-N-propionyl-D,L-penicillamine	53-57	heme oxygenase 1	Homo sapiens	84-88
20599745-4	2010	Treatment of HaCaT cells with tin protoporphyrin IX (SnPP), a specific inhibitor of HO-1, reversed the suppressive effect of celastrol on IFN-gamma-induced protein and mRNA expression of ICAM-1.	celastrol	125-134	heme oxygenase 1	Homo sapiens	84-88
20599745-5	2010	HO-1 knockdown using small interfering RNA (siRNA) led to reverse inhibition of IFN-gamma-induced up-regulation of ICAM-1 by celastrol.	celastrol	125-134	heme oxygenase 1	Homo sapiens	0-4
20599745-7	2010	Furthermore, blockage of HO-1 activity by SnPP and HO-1 siRNA reversed the inhibitory effect of celastrol on IFN-gamma-induced adhesion of monocytes to keratinocytes.	S-Nitroso-N-propionyl-D,L-penicillamine	42-46	heme oxygenase 1	Homo sapiens	25-29
20599745-7	2010	Furthermore, blockage of HO-1 activity by SnPP and HO-1 siRNA reversed the inhibitory effect of celastrol on IFN-gamma-induced adhesion of monocytes to keratinocytes.	celastrol	96-105	heme oxygenase 1	Homo sapiens	25-29
20599745-7	2010	Furthermore, blockage of HO-1 activity by SnPP and HO-1 siRNA reversed the inhibitory effect of celastrol on IFN-gamma-induced adhesion of monocytes to keratinocytes.	celastrol	96-105	heme oxygenase 1	Homo sapiens	51-55
20498371-8	2010	Also, 8-nitro-cGMP caused S-guanylation of KEAP1 in cells, which led to Nrf2 activation and subsequent induction of antioxidant enzymes, including heme oxygenase-1; thus, 8-nitro-cGMP protected cells against cytotoxic effects of hydrogen peroxide.	8-nitroguanosine 3',5'-cyclic monophosphate	6-18	heme oxygenase 1	Homo sapiens	147-163
20498371-8	2010	Also, 8-nitro-cGMP caused S-guanylation of KEAP1 in cells, which led to Nrf2 activation and subsequent induction of antioxidant enzymes, including heme oxygenase-1; thus, 8-nitro-cGMP protected cells against cytotoxic effects of hydrogen peroxide.	8-nitroguanosine 3',5'-cyclic monophosphate	171-183	heme oxygenase 1	Homo sapiens	147-163
20498371-8	2010	Also, 8-nitro-cGMP caused S-guanylation of KEAP1 in cells, which led to Nrf2 activation and subsequent induction of antioxidant enzymes, including heme oxygenase-1; thus, 8-nitro-cGMP protected cells against cytotoxic effects of hydrogen peroxide.	Hydrogen Peroxide	229-246	heme oxygenase 1	Homo sapiens	147-163
20676377-2	2010	However, HO-1 protein levels are increased in dopaminergic neurons of Parkinson"s disease (PD) patients, suggesting its participation in free-iron deposition, oxidative stress and neurotoxicity.	Iron	142-146	heme oxygenase 1	Homo sapiens	9-13
20599745-8	2010	These results suggest that celastrol may exert anti-inflammatory responses by suppressing IFN-gamma-induced expression of ICAM-1 and subsequent monocyte adhesion via expression of HO-1 in the keratinocytes.	celastrol	27-36	heme oxygenase 1	Homo sapiens	180-184
20536138-9	2010	Transfection with HO-1-specific small interfering RNA knocked down HO-1 expression, and the inhibition of expression of ICAM-1 by andrographolide was significantly reversed.	andrographolide	130-145	heme oxygenase 1	Homo sapiens	18-22
20536138-10	2010	These results suggest that stimulation of Nrf2-dependent HO-1 expression is involved in the suppression of TNF-alpha-induced ICAM-1 expression exerted by andrographolide.	andrographolide	154-169	heme oxygenase 1	Homo sapiens	57-61
20618971-9	2010	Pretreatment of cells with wortmannin inhibited translocation of Nrf2 and induction of HMOX1.	Wortmannin	27-37	heme oxygenase 1	Homo sapiens	87-92
20618971-10	2010	Wortmannin pretreatment was also able to diminish adaphostin induction of HMOX1, and as a consequence, enhance the toxicity of adaphostin to NCI-H522.	Wortmannin	0-10	heme oxygenase 1	Homo sapiens	74-79
20618971-10	2010	Wortmannin pretreatment was also able to diminish adaphostin induction of HMOX1, and as a consequence, enhance the toxicity of adaphostin to NCI-H522.	NSC 680410	50-60	heme oxygenase 1	Homo sapiens	74-79
20618971-11	2010	CONCLUSIONS: Adaphostin-induced oxidative stress in NCI-H522 was mediated through nuclear translocation of Nrf2 leading to upregulation of HMOX1.	NSC 680410	13-23	heme oxygenase 1	Homo sapiens	139-144
20593496-1	2010	Heme oxygenase (HO)-1 is the inducible isoform of the first and rate-limiting enzyme of heme degradation.	Heme	88-92	heme oxygenase 1	Homo sapiens	0-21
20461740-0	2010	Resveratrol inhibits human lung adenocarcinoma cell metastasis by suppressing heme oxygenase 1-mediated nuclear factor-kappaB pathway and subsequently downregulating expression of matrix metalloproteinases.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	78-94
20378845-5	2010	In the interactions between hemoglobin and atheroma lipids, hemoglobin and heme promote further lipid oxidation and subsequently endothelial reactions such as upregulation of heme oxygenase-1 and cytotoxicity to endothelium.	Heme	75-79	heme oxygenase 1	Homo sapiens	175-191
20664735-6	2010	After 24 h exposure of Huh7 cells to GLA, we identified several genes encoding the antioxidant proteins to be upregulated: heme oxygenase-1 (HO-1), aldo-keto reductase 1 family C1 (AKR1C1), C4 (AKR1C4), and thioredoxin (Trx).	gamma-Linolenic Acid	37-40	heme oxygenase 1	Homo sapiens	123-139
20664735-6	2010	After 24 h exposure of Huh7 cells to GLA, we identified several genes encoding the antioxidant proteins to be upregulated: heme oxygenase-1 (HO-1), aldo-keto reductase 1 family C1 (AKR1C1), C4 (AKR1C4), and thioredoxin (Trx).	gamma-Linolenic Acid	37-40	heme oxygenase 1	Homo sapiens	141-145
20664735-7	2010	The HO-1 protein levels were overexpressed in Huh7 cells after GLA exposure using a Western blot analysis.	gamma-Linolenic Acid	63-66	heme oxygenase 1	Homo sapiens	4-8
20664735-9	2010	GLA treatment has induced cell growth inhibition, ROS generation including lipid peroxidation, and HO-1 production for antioxidant protection against oxidative stress caused by GLA in Huh7 cells.	gamma-Linolenic Acid	0-3	heme oxygenase 1	Homo sapiens	99-103
20664735-9	2010	GLA treatment has induced cell growth inhibition, ROS generation including lipid peroxidation, and HO-1 production for antioxidant protection against oxidative stress caused by GLA in Huh7 cells.	gamma-Linolenic Acid	177-180	heme oxygenase 1	Homo sapiens	99-103
20155807-4	2010	MG-132, a proteasome inhibitor, increased the amount of HO-1 protein mainly in astrocytes of primary mesencephalic cultures.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-6	heme oxygenase 1	Homo sapiens	56-60
20155807-5	2010	Quantitative RT-PCR analysis revealed that lactacystin upregulated HO-1 mRNA expression.	lactacystin	43-54	heme oxygenase 1	Homo sapiens	67-71
20155807-6	2010	Proteasome inhibition with MG132 also increased the cytomegalovirus promoter-driven expression of Flag-HO-1 protein and resulted in an accumulation of ubiquitinated Flag-HO-1 in Flag-HO-1-overexpressing PC12 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	27-32	heme oxygenase 1	Homo sapiens	103-107
20155807-6	2010	Proteasome inhibition with MG132 also increased the cytomegalovirus promoter-driven expression of Flag-HO-1 protein and resulted in an accumulation of ubiquitinated Flag-HO-1 in Flag-HO-1-overexpressing PC12 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	27-32	heme oxygenase 1	Homo sapiens	170-174
20155807-6	2010	Proteasome inhibition with MG132 also increased the cytomegalovirus promoter-driven expression of Flag-HO-1 protein and resulted in an accumulation of ubiquitinated Flag-HO-1 in Flag-HO-1-overexpressing PC12 cells.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	27-32	heme oxygenase 1	Homo sapiens	170-174
20155807-7	2010	In addition, a cycloheximide chase assay demonstrated that the degradation of Flag-HO-1 protein was slowed by MG-132.	Cycloheximide	15-28	heme oxygenase 1	Homo sapiens	83-87
20155807-7	2010	In addition, a cycloheximide chase assay demonstrated that the degradation of Flag-HO-1 protein was slowed by MG-132.	Magnesium	110-112	heme oxygenase 1	Homo sapiens	83-87
20155807-9	2010	Proteasome inhibitors protected dopaminergic neurons from 6-hydroxydopamine (6-OHDA)-induced toxicity and this neuroprotection was abrogated by co-treatment with zinc protoporphyrin IX, a HO-1 inhibitor.	Oxidopamine	58-75	heme oxygenase 1	Homo sapiens	188-192
20155807-9	2010	Proteasome inhibitors protected dopaminergic neurons from 6-hydroxydopamine (6-OHDA)-induced toxicity and this neuroprotection was abrogated by co-treatment with zinc protoporphyrin IX, a HO-1 inhibitor.	Oxidopamine	77-83	heme oxygenase 1	Homo sapiens	188-192
20155807-9	2010	Proteasome inhibitors protected dopaminergic neurons from 6-hydroxydopamine (6-OHDA)-induced toxicity and this neuroprotection was abrogated by co-treatment with zinc protoporphyrin IX, a HO-1 inhibitor.	zinc protoporphyrin	162-184	heme oxygenase 1	Homo sapiens	188-192
20155807-10	2010	Furthermore, 6-OHDA-induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO-1-catalyzed degradation of heme.	Oxidopamine	13-19	heme oxygenase 1	Homo sapiens	99-103
20155807-10	2010	Furthermore, 6-OHDA-induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO-1-catalyzed degradation of heme.	Bilirubin	52-61	heme oxygenase 1	Homo sapiens	99-103
20155807-10	2010	Furthermore, 6-OHDA-induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO-1-catalyzed degradation of heme.	Carbon Monoxide	66-81	heme oxygenase 1	Homo sapiens	99-103
20155807-10	2010	Furthermore, 6-OHDA-induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO-1-catalyzed degradation of heme.	Heme	129-133	heme oxygenase 1	Homo sapiens	99-103
20461740-7	2010	Resveratrol significantly inhibited HO-1-mediated MMP-9 (35% inhibition) and MMP-2 (28% inhibition) expression in lung cancer cells.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	36-40
20461740-10	2010	Our results suggest that resveratrol inhibited HO-1 and subsequently MMP-9 and MMP-2 expression in lung cancer cells.	Resveratrol	25-36	heme oxygenase 1	Homo sapiens	47-51
20461740-11	2010	The inhibitory effects of resveratrol on MMP expression and invasion of lung cancer cells are, in part, associated with the HO-1-mediated NF-kappaB pathway.	Resveratrol	26-37	heme oxygenase 1	Homo sapiens	124-128
20307651-8	2010	In Pin1-VSMCs, heme oxygenase-1 (HO-1) induction in response to nitric oxide donor was suppressed compared to control VSMCs.	Nitric Oxide	64-76	heme oxygenase 1	Homo sapiens	15-31
20692427-0	2010	The in vitro protection of human decay accelerating factor and hDAF/heme oxygenase-1 transgenes in porcine aortic endothelial cells against sera of Formosan macaques.	formosan	148-156	heme oxygenase 1	Homo sapiens	68-84
20307651-8	2010	In Pin1-VSMCs, heme oxygenase-1 (HO-1) induction in response to nitric oxide donor was suppressed compared to control VSMCs.	vsmcs	8-13	heme oxygenase 1	Homo sapiens	15-31
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Heme	43-47	heme oxygenase 1	Homo sapiens	0-16
20303947-1	2010	Heme oxygenase-1 (HO-1), a known cytoprotective enzyme implicated also in the cell cycle regulation and angiogenesis, exerts many of its beneficial effects through carbon monoxide (CO).	Carbon Monoxide	164-179	heme oxygenase 1	Homo sapiens	0-16
20303947-1	2010	Heme oxygenase-1 (HO-1), a known cytoprotective enzyme implicated also in the cell cycle regulation and angiogenesis, exerts many of its beneficial effects through carbon monoxide (CO).	Carbon Monoxide	164-179	heme oxygenase 1	Homo sapiens	18-22
20226179-0	2010	Structure-activity relationships in the cytoprotective effect of caffeic acid phenethyl ester (CAPE) and fluorinated derivatives: effects on heme oxygenase-1 induction and antioxidant activities.	caffeic acid phenethyl ester	65-93	heme oxygenase 1	Homo sapiens	141-157
20226179-0	2010	Structure-activity relationships in the cytoprotective effect of caffeic acid phenethyl ester (CAPE) and fluorinated derivatives: effects on heme oxygenase-1 induction and antioxidant activities.	caffeic acid phenethyl ester	95-99	heme oxygenase 1	Homo sapiens	141-157
20226179-0	2010	Structure-activity relationships in the cytoprotective effect of caffeic acid phenethyl ester (CAPE) and fluorinated derivatives: effects on heme oxygenase-1 induction and antioxidant activities.	fluorinated	105-116	heme oxygenase 1	Homo sapiens	141-157
20226179-2	2010	To ascertain the involvement of HO-1 induction in the cytoprotective effects of CAPE analogues, their ability to induce HO-1 at 20microM was determined by reverse transcriptase polymerase chain reaction, western blotting and the use of HO-1 inhibitor tin protoporphyrin IX.	caffeic acid phenethyl ester	80-84	heme oxygenase 1	Homo sapiens	32-36
20226179-2	2010	To ascertain the involvement of HO-1 induction in the cytoprotective effects of CAPE analogues, their ability to induce HO-1 at 20microM was determined by reverse transcriptase polymerase chain reaction, western blotting and the use of HO-1 inhibitor tin protoporphyrin IX.	caffeic acid phenethyl ester	80-84	heme oxygenase 1	Homo sapiens	120-124
20226179-2	2010	To ascertain the involvement of HO-1 induction in the cytoprotective effects of CAPE analogues, their ability to induce HO-1 at 20microM was determined by reverse transcriptase polymerase chain reaction, western blotting and the use of HO-1 inhibitor tin protoporphyrin IX.	caffeic acid phenethyl ester	80-84	heme oxygenase 1	Homo sapiens	120-124
20226179-3	2010	There was significant induction of HO-1 by CAPE derivatives.	caffeic acid phenethyl ester	43-47	heme oxygenase 1	Homo sapiens	35-39
20226179-6	2010	The maintenance of at least one hydroxyl group on the CAPE catechol ring and the phenethyl ester portion was required for HO-1 induction.	Bis(ethylphenyl)ether	81-96	heme oxygenase 1	Homo sapiens	122-126
20226179-10	2010	These results indicate that the induction of HO-1 plays a more important role in the cytoprotective activity of CAPE derivatives than their direct antioxidant activity.	caffeic acid phenethyl ester	112-116	heme oxygenase 1	Homo sapiens	45-49
20385560-6	2010	Covalent modification at two conserved cysteine residues, corresponding to Cys(261) and Cys(273) in HDAC1, coincided with attenuation of histone deacetylase activity, changes in histone H3 and H4 acetylation patterns, derepression of a LEF1.beta-catenin model system, and transcription of HDAC-repressed genes, e.g. heme oxygenase-1 (HO-1), Gadd45, and HSP70.	Cysteine	39-47	heme oxygenase 1	Homo sapiens	316-332
20385560-6	2010	Covalent modification at two conserved cysteine residues, corresponding to Cys(261) and Cys(273) in HDAC1, coincided with attenuation of histone deacetylase activity, changes in histone H3 and H4 acetylation patterns, derepression of a LEF1.beta-catenin model system, and transcription of HDAC-repressed genes, e.g. heme oxygenase-1 (HO-1), Gadd45, and HSP70.	Cysteine	75-78	heme oxygenase 1	Homo sapiens	316-332
20385560-6	2010	Covalent modification at two conserved cysteine residues, corresponding to Cys(261) and Cys(273) in HDAC1, coincided with attenuation of histone deacetylase activity, changes in histone H3 and H4 acetylation patterns, derepression of a LEF1.beta-catenin model system, and transcription of HDAC-repressed genes, e.g. heme oxygenase-1 (HO-1), Gadd45, and HSP70.	Cysteine	88-91	heme oxygenase 1	Homo sapiens	316-332
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Heme	43-47	heme oxygenase 1	Homo sapiens	18-22
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	0-16
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	18-22
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Biliverdine	86-96	heme oxygenase 1	Homo sapiens	0-16
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Biliverdine	86-96	heme oxygenase 1	Homo sapiens	18-22
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Bilirubin	97-106	heme oxygenase 1	Homo sapiens	0-16
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Bilirubin	97-106	heme oxygenase 1	Homo sapiens	18-22
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Iron	116-120	heme oxygenase 1	Homo sapiens	0-16
20518085-1	2010	Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron.	Iron	116-120	heme oxygenase 1	Homo sapiens	18-22
20345481-5	2010	When U937 cells were treated with phorbol myristate acetate (PHA) or gamma-interferon, they significantly expressed both HO-1 and Bach1, like primary AML cells.	Tetradecanoylphorbol Acetate	34-59	heme oxygenase 1	Homo sapiens	121-125
20523338-0	2010	Neferine inhibits angiotensin II-stimulated proliferation in vascular smooth muscle cells through heme oxygenase-1.	neferine	0-8	heme oxygenase 1	Homo sapiens	98-114
20651363-0	2010	Inhibition of heme oxygenase-1 enhances the cytotoxic effect of gemcitabine in urothelial cancer cells.	gemcitabine	64-75	heme oxygenase 1	Homo sapiens	14-30
20370320-2	2010	Several clinical and epidemiological studies have been carried out on key enzymes generating and eliminating bilirubin (heme oxygenase-1 and UDP-glucuronosyltransferase UGT1A1, respectively) and their regulation by the AhR.	Bilirubin	109-118	heme oxygenase 1	Homo sapiens	120-136
20370564-3	2010	Cell treatment with H(2)O(2) (0.5 mM) resulted in a time- and dose-dependent response of HOX-1 and COX-2 mRNA and protein levels, with ERK1/2, p38-MAPK and MSK1 found to mediate these effects.	Hydrogen Peroxide	20-28	heme oxygenase 1	Homo sapiens	89-94
20349048-9	2010	Finally, it was observed that the nitric oxide (NO) anti-inflammatory effects on ICAM-1 expression appear to be indirectly mediated by HO-1 activation, since the inhibition of HO-1 prevented the inhibitory effect of the NO donor (S-nitroso-N-acetylpenicillamine) on LPS-induced ICAM-1 expression.	Nitric Oxide	34-46	heme oxygenase 1	Homo sapiens	135-139
21179939-4	2010	We examine here the effects of multiwalled carbon nanotubes of different sizes on monocytic THP-1 cells, with regard to their ability to stimulate increased expression of the HO-1 and GST genes and their ability to produce nuclear translocation of the transcription factor, Nrf2, as well as the release of several pro-inflammatory cytokines and mediators of inflammation.	Carbon	43-49	heme oxygenase 1	Homo sapiens	175-179
21179939-5	2010	Our results suggest that long (50 microm) carbon nanotubes (62.5 microg/ml for 4 hours) produce increased nuclear translocation of Nrf2 and increased HO-1 gene expression compared with shorter entangled nanotubes.	Carbon	42-48	heme oxygenase 1	Homo sapiens	150-154
20519851-0	2010	Reduction of arsenic-induced cytotoxicity through Nrf2/HO-1 signaling in HepG2 cells.	Arsenic	13-20	heme oxygenase 1	Homo sapiens	55-59
20526373-8	2010	Silencing RNA experiments confirmed that HIF-1alpha nuclear translocation was responsible for HO-1, BVR and H-ferritin induction mediated by CS and hypoxia/reoxygenation.	Cesium	141-143	heme oxygenase 1	Homo sapiens	94-98
20353835-5	2010	To our knowledge, our results were the first to show that: (a) SIN pretreatment was able to induce HO-1 expression in donor livers in a dose dependent manner; (b) SIN pretreatment protected the liver graft from cold I/R injury; and (c) the protective effect of SIN was, at least in part, mediated by HO-1, as proved by the fact that inhibiting HO-1 activity with zinc protoporphyrin (ZnPP) reduced the protection.	sinomenine	63-66	heme oxygenase 1	Homo sapiens	99-103
20353835-5	2010	To our knowledge, our results were the first to show that: (a) SIN pretreatment was able to induce HO-1 expression in donor livers in a dose dependent manner; (b) SIN pretreatment protected the liver graft from cold I/R injury; and (c) the protective effect of SIN was, at least in part, mediated by HO-1, as proved by the fact that inhibiting HO-1 activity with zinc protoporphyrin (ZnPP) reduced the protection.	sinomenine	63-66	heme oxygenase 1	Homo sapiens	300-304
20353835-5	2010	To our knowledge, our results were the first to show that: (a) SIN pretreatment was able to induce HO-1 expression in donor livers in a dose dependent manner; (b) SIN pretreatment protected the liver graft from cold I/R injury; and (c) the protective effect of SIN was, at least in part, mediated by HO-1, as proved by the fact that inhibiting HO-1 activity with zinc protoporphyrin (ZnPP) reduced the protection.	sinomenine	63-66	heme oxygenase 1	Homo sapiens	300-304
20351094-1	2010	HO-1 (heme oxygenase-1) is an inducible microsomal enzyme that catalyzes the degradation of pro-oxidant heme.	Heme	6-10	heme oxygenase 1	Homo sapiens	0-4
20351094-8	2010	Sp1 small interfering RNA and mithramycin A, a Sp1 binding site inhibitor, resulted in loss of the loop formation between the intronic enhancer and the distal HO-1 promoter by the chromosome conformation capture assay.	mithramycin A	30-43	heme oxygenase 1	Homo sapiens	159-163
20349048-9	2010	Finally, it was observed that the nitric oxide (NO) anti-inflammatory effects on ICAM-1 expression appear to be indirectly mediated by HO-1 activation, since the inhibition of HO-1 prevented the inhibitory effect of the NO donor (S-nitroso-N-acetylpenicillamine) on LPS-induced ICAM-1 expression.	Nitric Oxide	34-46	heme oxygenase 1	Homo sapiens	176-180
20349048-9	2010	Finally, it was observed that the nitric oxide (NO) anti-inflammatory effects on ICAM-1 expression appear to be indirectly mediated by HO-1 activation, since the inhibition of HO-1 prevented the inhibitory effect of the NO donor (S-nitroso-N-acetylpenicillamine) on LPS-induced ICAM-1 expression.	S-Nitroso-N-Acetylpenicillamine	230-261	heme oxygenase 1	Homo sapiens	135-139
20349048-9	2010	Finally, it was observed that the nitric oxide (NO) anti-inflammatory effects on ICAM-1 expression appear to be indirectly mediated by HO-1 activation, since the inhibition of HO-1 prevented the inhibitory effect of the NO donor (S-nitroso-N-acetylpenicillamine) on LPS-induced ICAM-1 expression.	S-Nitroso-N-Acetylpenicillamine	230-261	heme oxygenase 1	Homo sapiens	176-180
20061555-5	2010	Inhibition of HIV-1 replication was associated with PKC-dependent induction of HO-1, a cytoprotective enzyme known to catabolize heme.	Heme	129-133	heme oxygenase 1	Homo sapiens	79-83
20121710-5	2010	However, the patients with short (&lt;24 GT) dinucleotide repeat in the HO-1 gene promoter on either allele had significantly higher prolonged unconjugated hyperbilirubinaemia than the healthy newborns.	Dinucleoside Phosphates	45-57	heme oxygenase 1	Homo sapiens	72-76
20127796-7	2010	The effects of miR-196 mimic on Bach1, HMOX1, and HCV RNA, and protein levels were measured by way of quantitative real-time polymerase chain reaction (qRT-PCR) and Western blotting, respectively.	mir-196	15-22	heme oxygenase 1	Homo sapiens	39-44
20127796-9	2010	miR-196 mimic significantly down-regulated Bach1 and up-regulated HMOX1 gene expression and inhibited HCV expression.	mir-196	0-7	heme oxygenase 1	Homo sapiens	66-71
20127796-12	2010	CONCLUSION: miR-196 directly acts on the 3"-UTR of Bach1 messenger RNA and translationally represses the expression of this protein, and up-regulates HMOX1.	mir-196	12-19	heme oxygenase 1	Homo sapiens	150-155
20188821-8	2010	These results demonstrate that CSPE-induced ROS generation is mediated through a c-Src/NADPH oxidase/MAPK pathway and in turn initiates the activation of Nrf2 and ultimately induces HO-1 expression in HTSMCs.	ros	44-47	heme oxygenase 1	Homo sapiens	182-186
20188822-6	2010	When a competitive HO-1 inhibitor, tin mesoporphyrin, was applied to HepG2 cells or the cells were transfected with siRNA for HO-1 there was a partial restoration of the inhibition of TCDD-mediated induction of CYP1A1 catalytic activity.	tin mesoporphyrin	35-52	heme oxygenase 1	Homo sapiens	19-23
20188822-6	2010	When a competitive HO-1 inhibitor, tin mesoporphyrin, was applied to HepG2 cells or the cells were transfected with siRNA for HO-1 there was a partial restoration of the inhibition of TCDD-mediated induction of CYP1A1 catalytic activity.	tin mesoporphyrin	35-52	heme oxygenase 1	Homo sapiens	126-130
20188822-6	2010	When a competitive HO-1 inhibitor, tin mesoporphyrin, was applied to HepG2 cells or the cells were transfected with siRNA for HO-1 there was a partial restoration of the inhibition of TCDD-mediated induction of CYP1A1 catalytic activity.	Polychlorinated Dibenzodioxins	184-188	heme oxygenase 1	Homo sapiens	19-23
20188822-6	2010	When a competitive HO-1 inhibitor, tin mesoporphyrin, was applied to HepG2 cells or the cells were transfected with siRNA for HO-1 there was a partial restoration of the inhibition of TCDD-mediated induction of CYP1A1 catalytic activity.	Polychlorinated Dibenzodioxins	184-188	heme oxygenase 1	Homo sapiens	126-130
20188822-8	2010	On the other hand, cobalt protoporphyrin increased HO-1 mRNA, with a concomitant decrease in CYP1A1 activity, without affecting CYP1A1 mRNA, which was reversed by HO-1 siRNA transfection.	cobaltiprotoporphyrin	19-40	heme oxygenase 1	Homo sapiens	51-55
20404253-8	2010	In isolated mitochondria, mitochondrial permeability transition was inhibited by HO-1 in a carbon monoxide (CO)-dependent manner and was recapitulated by the CO donor tricarbonylchloro(glycinato)ruthenium(II) (CORM-3).	Carbon Monoxide	91-106	heme oxygenase 1	Homo sapiens	81-85
20404253-8	2010	In isolated mitochondria, mitochondrial permeability transition was inhibited by HO-1 in a carbon monoxide (CO)-dependent manner and was recapitulated by the CO donor tricarbonylchloro(glycinato)ruthenium(II) (CORM-3).	Carbon Monoxide	108-111	heme oxygenase 1	Homo sapiens	81-85
20404253-8	2010	In isolated mitochondria, mitochondrial permeability transition was inhibited by HO-1 in a carbon monoxide (CO)-dependent manner and was recapitulated by the CO donor tricarbonylchloro(glycinato)ruthenium(II) (CORM-3).	tricarbonylchloro(glycinato)ruthenium(II)	167-207	heme oxygenase 1	Homo sapiens	81-85
19924377-6	2010	On addition of a cobalt compound, the resultant induction of HO-1 decreases adipogenesis.	Cobalt	17-23	heme oxygenase 1	Homo sapiens	61-65
20378668-7	2010	The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin.	Iron	95-99	heme oxygenase 1	Homo sapiens	37-40
20378668-7	2010	The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin.	Reactive Oxygen Species	113-136	heme oxygenase 1	Homo sapiens	37-40
20378668-7	2010	The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin.	Reactive Oxygen Species	138-141	heme oxygenase 1	Homo sapiens	37-40
20378668-7	2010	The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin.	Abscisic Acid	144-157	heme oxygenase 1	Homo sapiens	37-40
20378668-7	2010	The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin.	Abscisic Acid	159-162	heme oxygenase 1	Homo sapiens	37-40
20378668-7	2010	The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin.	Hemin	169-177	heme oxygenase 1	Homo sapiens	37-40
20336713-6	2010	The attenuation of iron-induced augmentation of heme oxygenase-1 was also confirmed in HepG2 cells expressing the core protein.	Iron	19-23	heme oxygenase 1	Homo sapiens	48-64
20061555-6	2010	Pretreatment with the PKC inhibitor Go 6976 not only substantially inhibited LPS-mediated induction of HO-1 but also attenuated LPS-induced suppression of HIV replication.	Go 6976	36-43	heme oxygenase 1	Homo sapiens	103-107
20061555-8	2010	Specificity of HO-1 was confirmed by substantial reversal of LPS-induced viral replication by pretreatment of cells with SnPP IX, an inhibitor of HO-1 enzyme activity.	tin protoporphyrin IX	121-128	heme oxygenase 1	Homo sapiens	15-19
20061555-8	2010	Specificity of HO-1 was confirmed by substantial reversal of LPS-induced viral replication by pretreatment of cells with SnPP IX, an inhibitor of HO-1 enzyme activity.	tin protoporphyrin IX	121-128	heme oxygenase 1	Homo sapiens	146-150
20110250-6	2010	HO-1 was induced by cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	20-44	heme oxygenase 1	Homo sapiens	0-4
20106603-4	2010	In this context, it has been shown that the rate limiting enzyme heme oxygenase I (HO-1), responsible for the catabolism of the free heme in the body, is an important resistance factor in malaria and is also important in the physiopathology of haemolytic diseases.	Heme	65-69	heme oxygenase 1	Homo sapiens	83-87
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Mesalamine	59-80	heme oxygenase 1	Homo sapiens	210-226
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Mesalamine	59-80	heme oxygenase 1	Homo sapiens	228-232
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Mesalamine	82-87	heme oxygenase 1	Homo sapiens	210-226
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Mesalamine	82-87	heme oxygenase 1	Homo sapiens	228-232
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Aminosalicylic Acid	123-138	heme oxygenase 1	Homo sapiens	210-226
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Aminosalicylic Acid	123-138	heme oxygenase 1	Homo sapiens	228-232
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Sulfasalazine	160-173	heme oxygenase 1	Homo sapiens	210-226
20631420-2	2010	Recent in vivo and in vitro studies have demonstrated that 5-aminosalicylic acid (5-ASA), regarded as the active moiety in aminosalicylate preparations such as sulfasalazine, can induce the heat shock protein, heme oxygenase-1 (HO-1) and up-regulate HO enzyme activity in the colon.	Sulfasalazine	160-173	heme oxygenase 1	Homo sapiens	228-232
20631420-3	2010	As HO-1 can produce endogenous anti-oxidant and anti-inflammatory moieties such as bilirubin and carbon monoxide (CO), these findings suggest a novel mechanism of action for aminosalicylates, acting as anti-colitic agents through the up-regulation of HO-1 enzyme expression and activity.	Bilirubin	83-92	heme oxygenase 1	Homo sapiens	3-7
20631420-3	2010	As HO-1 can produce endogenous anti-oxidant and anti-inflammatory moieties such as bilirubin and carbon monoxide (CO), these findings suggest a novel mechanism of action for aminosalicylates, acting as anti-colitic agents through the up-regulation of HO-1 enzyme expression and activity.	Carbon Monoxide	97-112	heme oxygenase 1	Homo sapiens	3-7
20631420-3	2010	As HO-1 can produce endogenous anti-oxidant and anti-inflammatory moieties such as bilirubin and carbon monoxide (CO), these findings suggest a novel mechanism of action for aminosalicylates, acting as anti-colitic agents through the up-regulation of HO-1 enzyme expression and activity.	Carbon Monoxide	114-116	heme oxygenase 1	Homo sapiens	3-7
20631420-3	2010	As HO-1 can produce endogenous anti-oxidant and anti-inflammatory moieties such as bilirubin and carbon monoxide (CO), these findings suggest a novel mechanism of action for aminosalicylates, acting as anti-colitic agents through the up-regulation of HO-1 enzyme expression and activity.	Carbon Monoxide	114-116	heme oxygenase 1	Homo sapiens	251-255
20110250-6	2010	HO-1 was induced by cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	46-50	heme oxygenase 1	Homo sapiens	0-4
20110250-11	2010	RESULTS: Induction of HO-1 by CoPP in the presence of IL-1beta decreased the expression of MMP-1 and -3, and MMP activity.	cobaltiprotoporphyrin	30-34	heme oxygenase 1	Homo sapiens	22-26
20083128-0	2010	Arsenic promotes angiogenesis in vitro via a heme oxygenase-1-dependent mechanism.	Arsenic	0-7	heme oxygenase 1	Homo sapiens	45-61
20083128-4	2010	The present study investigates the role of heme oxygenase-1 (HO-1) in sodium arsenite-mediated angiogenesis in vitro.	sodium arsenite	70-85	heme oxygenase 1	Homo sapiens	43-59
20083128-4	2010	The present study investigates the role of heme oxygenase-1 (HO-1) in sodium arsenite-mediated angiogenesis in vitro.	sodium arsenite	70-85	heme oxygenase 1	Homo sapiens	61-65
20083128-8	2010	Arsenite induced HO-1 mRNA and protein expression.	arsenite	0-8	heme oxygenase 1	Homo sapiens	17-21
20083128-9	2010	Knock down of HO-1 expression decreased arsenite-induced VEGF expression, cell migration, and tube formation.	arsenite	40-48	heme oxygenase 1	Homo sapiens	14-18
20083128-10	2010	We showed that arsenite promoted dissociation of Bach1 (a transcriptional repressor) from the HO-1 enhancers and increased Nrf2 binding to these elements.	arsenite	15-23	heme oxygenase 1	Homo sapiens	94-98
20083128-11	2010	Site directed mutagenesis assay identified that Bach1 cysteine residues 557 and 574 were essential for the induction of HO-1 gene in response to arsenite.	Cysteine	54-62	heme oxygenase 1	Homo sapiens	120-124
20083128-11	2010	Site directed mutagenesis assay identified that Bach1 cysteine residues 557 and 574 were essential for the induction of HO-1 gene in response to arsenite.	arsenite	145-153	heme oxygenase 1	Homo sapiens	120-124
20083128-12	2010	These findings demonstrate a role for HO-1 in arsenite-mediated angiogenesis in vitro.	arsenite	46-54	heme oxygenase 1	Homo sapiens	38-42
20368435-7	2010	Our results show that compounds containing alpha-beta unsaturated carbonyls, sulfhydryl reactive metals, and isothiocyanates are strong activators of Nrf2 in a reporter assay system and in primary human CLL based on increased expression of the Nrf2 target heme oxygenase-1.	alpha-beta unsaturated carbonyls	43-75	heme oxygenase 1	Homo sapiens	256-272
20368435-7	2010	Our results show that compounds containing alpha-beta unsaturated carbonyls, sulfhydryl reactive metals, and isothiocyanates are strong activators of Nrf2 in a reporter assay system and in primary human CLL based on increased expression of the Nrf2 target heme oxygenase-1.	Isothiocyanates	109-124	heme oxygenase 1	Homo sapiens	256-272
19890094-5	2010	The protective effect was specific for HO-1 because it was reproduced on administration of the end products of HO-1 activity, carbon monoxide, and bilirubin, and prevented by the pharmacologic inhibition of HO-1 using tin mesoporphyrin IX.	Carbon Monoxide	126-141	heme oxygenase 1	Homo sapiens	39-43
20083195-8	2010	Furthermore, celecoxib-induced HO-1 was inhibited by dominant-negative Nrf2.	Celecoxib	13-22	heme oxygenase 1	Homo sapiens	31-35
20083195-9	2010	The functional significance of HO-1 induction was revealed by celecoxib-mediated inhibition of VCAM-1 expression, a response reversed by the HO-1 antagonist zinc protoporphyrin.	Celecoxib	62-71	heme oxygenase 1	Homo sapiens	31-35
20083195-9	2010	The functional significance of HO-1 induction was revealed by celecoxib-mediated inhibition of VCAM-1 expression, a response reversed by the HO-1 antagonist zinc protoporphyrin.	Celecoxib	62-71	heme oxygenase 1	Homo sapiens	141-145
20083195-9	2010	The functional significance of HO-1 induction was revealed by celecoxib-mediated inhibition of VCAM-1 expression, a response reversed by the HO-1 antagonist zinc protoporphyrin.	zinc protoporphyrin	157-176	heme oxygenase 1	Homo sapiens	31-35
20083195-9	2010	The functional significance of HO-1 induction was revealed by celecoxib-mediated inhibition of VCAM-1 expression, a response reversed by the HO-1 antagonist zinc protoporphyrin.	zinc protoporphyrin	157-176	heme oxygenase 1	Homo sapiens	141-145
20083195-10	2010	HO-1 induction provides a molecular mechanism for clinical observations indicating relative freedom from atherothrombotic complications in patients taking celecoxib compared to other NSAIDs with comparable anti-inflammatory activity.	Celecoxib	155-164	heme oxygenase 1	Homo sapiens	0-4
20083195-0	2010	Celecoxib activates PI-3K/Akt and mitochondrial redox signaling to enhance heme oxygenase-1-mediated anti-inflammatory activity in vascular endothelium.	Celecoxib	0-9	heme oxygenase 1	Homo sapiens	75-91
20083195-3	2010	This led us to the hypothesis that celecoxib induces the vasculoprotective enzyme heme oxygenase-1 (HO-1).	Celecoxib	35-44	heme oxygenase 1	Homo sapiens	82-98
20083195-3	2010	This led us to the hypothesis that celecoxib induces the vasculoprotective enzyme heme oxygenase-1 (HO-1).	Celecoxib	35-44	heme oxygenase 1	Homo sapiens	100-104
20083195-4	2010	In human umbilical vein and aortic endothelial cells, 24-48 h treatment with celecoxib induced HO-1 mRNA and protein expression and increased HO-1 enzyme activity.	Celecoxib	77-86	heme oxygenase 1	Homo sapiens	95-99
20083195-4	2010	In human umbilical vein and aortic endothelial cells, 24-48 h treatment with celecoxib induced HO-1 mRNA and protein expression and increased HO-1 enzyme activity.	Celecoxib	77-86	heme oxygenase 1	Homo sapiens	142-146
20223678-5	2010	It was shown that inhibition of HO-1 activity by zinc protoporphyrin IX increased PDT-induced cytotoxicity in a dose-dependent manner.	zinc protoporphyrin	49-71	heme oxygenase 1	Homo sapiens	32-36
20223678-9	2010	This is supported by the fact that during PDT ferritin is readily up-regulated, able to bind excess iron formed by the HO-1 action.	Iron	100-104	heme oxygenase 1	Homo sapiens	119-123
19890094-5	2010	The protective effect was specific for HO-1 because it was reproduced on administration of the end products of HO-1 activity, carbon monoxide, and bilirubin, and prevented by the pharmacologic inhibition of HO-1 using tin mesoporphyrin IX.	mesoporphyrin IX	222-238	heme oxygenase 1	Homo sapiens	111-115
19890094-5	2010	The protective effect was specific for HO-1 because it was reproduced on administration of the end products of HO-1 activity, carbon monoxide, and bilirubin, and prevented by the pharmacologic inhibition of HO-1 using tin mesoporphyrin IX.	Bilirubin	147-156	heme oxygenase 1	Homo sapiens	39-43
19890094-5	2010	The protective effect was specific for HO-1 because it was reproduced on administration of the end products of HO-1 activity, carbon monoxide, and bilirubin, and prevented by the pharmacologic inhibition of HO-1 using tin mesoporphyrin IX.	mesoporphyrin IX	222-238	heme oxygenase 1	Homo sapiens	39-43
19890094-5	2010	The protective effect was specific for HO-1 because it was reproduced on administration of the end products of HO-1 activity, carbon monoxide, and bilirubin, and prevented by the pharmacologic inhibition of HO-1 using tin mesoporphyrin IX.	mesoporphyrin IX	222-238	heme oxygenase 1	Homo sapiens	111-115
20470258-0	2010	Heme oxygenase-1 mediates nicotine- and lipopolysaccharide-induced expression of cyclooxygenase-2 and inducible nitric oxide synthase in human periodontal ligament cells.	Nicotine	26-34	heme oxygenase 1	Homo sapiens	0-16
19885829-5	2010	Following exposure of cells to EA, heme oxygenase-1, a marker protein of oxidative stress, was strongly induced.	Ethacrynic Acid	31-33	heme oxygenase 1	Homo sapiens	35-51
20470258-2	2010	This study aimed to identify the effects of HO-1 on the proinflammatory mediators activated by nicotine and lipopolysaccharide (LPS) stimulation in human periodontal ligament (PDL) cells.	Nicotine	95-103	heme oxygenase 1	Homo sapiens	44-48
20470258-5	2010	RESULTS: Lipopolysaccharide and nicotine synergistically induced the production of NO and PGE(2) and increased the protein expression of iNOS, COX-2 and HO-1.	Nicotine	32-40	heme oxygenase 1	Homo sapiens	153-157
20470258-6	2010	Treatment with an HO-1 inhibitor and HO-1 small interfering RNAs blocked the LPS- and nicotine-stimulated NO and PGE(2) release as well as the expression of iNOS and COX-2.	Nicotine	86-94	heme oxygenase 1	Homo sapiens	18-22
20470258-6	2010	Treatment with an HO-1 inhibitor and HO-1 small interfering RNAs blocked the LPS- and nicotine-stimulated NO and PGE(2) release as well as the expression of iNOS and COX-2.	Nicotine	86-94	heme oxygenase 1	Homo sapiens	37-41
20470258-6	2010	Treatment with an HO-1 inhibitor and HO-1 small interfering RNAs blocked the LPS- and nicotine-stimulated NO and PGE(2) release as well as the expression of iNOS and COX-2.	Dinoprostone	113-119	heme oxygenase 1	Homo sapiens	18-22
20470258-6	2010	Treatment with an HO-1 inhibitor and HO-1 small interfering RNAs blocked the LPS- and nicotine-stimulated NO and PGE(2) release as well as the expression of iNOS and COX-2.	Dinoprostone	113-119	heme oxygenase 1	Homo sapiens	37-41
20470258-7	2010	CONCLUSION: Our data suggest that the nicotine- and LPS-induced inflammatory effects on PDL cells may act through a novel mechanism involving the action of HO-1.	Nicotine	38-46	heme oxygenase 1	Homo sapiens	156-160
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Cholesterol	54-65	heme oxygenase 1	Homo sapiens	0-16
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Cholesterol	54-65	heme oxygenase 1	Homo sapiens	18-22
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Oxysterols	69-79	heme oxygenase 1	Homo sapiens	0-16
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Oxysterols	69-79	heme oxygenase 1	Homo sapiens	18-22
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Oxysterols	69-78	heme oxygenase 1	Homo sapiens	0-16
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Oxysterols	69-78	heme oxygenase 1	Homo sapiens	18-22
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Cholesterol	273-284	heme oxygenase 1	Homo sapiens	0-16
18597895-2	2010	Heme oxygenase-1 (HO-1) stimulates oxidation of glial cholesterol to oxysterols, and increased oxysterol concentrations may protect neural tissues by activation of liver X receptor-beta (LXR-beta), which induces transcription of genes associated with reduction of cellular cholesterol concentrations and decrease of Abeta formation.	Cholesterol	273-284	heme oxygenase 1	Homo sapiens	18-22
18597895-3	2010	Underexpression of HO-1 in concert with underexpression of LXR-beta would result in increased cholesterol accumulation, induction of Abeta production, and increased AD risk.	Cholesterol	94-105	heme oxygenase 1	Homo sapiens	19-23
20131233-12	2010	Cilostazol- and CoPP-induced HO-1 expression was diminished in cells transfected with Nrf2 siRNA.	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	29-33
20170153-0	2010	Hesperidin upregulates heme oxygenase-1 to attenuate hydrogen peroxide-induced cell damage in hepatic L02 cells.	Hydrogen Peroxide	53-70	heme oxygenase 1	Homo sapiens	23-39
20170153-4	2010	Real-time quantitative polymerase chain reaction, Western blot, and enzyme activity assay demonstrated that hesperidin upregulated heme oxygenase-1 (HO-1) expression to protect hepatocytes against oxidative stress.	Hesperidin	108-118	heme oxygenase 1	Homo sapiens	131-147
20170153-4	2010	Real-time quantitative polymerase chain reaction, Western blot, and enzyme activity assay demonstrated that hesperidin upregulated heme oxygenase-1 (HO-1) expression to protect hepatocytes against oxidative stress.	Hesperidin	108-118	heme oxygenase 1	Homo sapiens	149-153
20170153-7	2010	Besides, ERK1/2 inhibitor significantly inhibited hesperidin-mediated HO-1 upregulation and Nrf2 nuclear translocation.	Hesperidin	50-60	heme oxygenase 1	Homo sapiens	70-74
20170153-8	2010	Taken together, the above findings suggested that hesperidin augmented cellular antioxidant defense capacity through the induction of HO-1 via ERK/Nrf2 signaling.	Hesperidin	50-60	heme oxygenase 1	Homo sapiens	134-138
20118244-1	2010	Heme oxygenases (HOs) -1 and -2 catalyze the breakdown of heme to release carbon monoxide, biliverdin, and ferrous iron, which may preserve cell function during oxidative stress.	Heme	58-62	heme oxygenase 1	Homo sapiens	0-31
20118244-1	2010	Heme oxygenases (HOs) -1 and -2 catalyze the breakdown of heme to release carbon monoxide, biliverdin, and ferrous iron, which may preserve cell function during oxidative stress.	Carbon Monoxide	74-89	heme oxygenase 1	Homo sapiens	0-31
20118244-1	2010	Heme oxygenases (HOs) -1 and -2 catalyze the breakdown of heme to release carbon monoxide, biliverdin, and ferrous iron, which may preserve cell function during oxidative stress.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	0-31
20118244-1	2010	Heme oxygenases (HOs) -1 and -2 catalyze the breakdown of heme to release carbon monoxide, biliverdin, and ferrous iron, which may preserve cell function during oxidative stress.	Iron	115-119	heme oxygenase 1	Homo sapiens	0-31
20131233-0	2010	Cilostazol enhances apoptosis of synovial cells from rheumatoid arthritis patients with inhibition of cytokine formation via Nrf2-linked heme oxygenase 1 induction.	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	137-153
20131233-6	2010	Cilostazol (10 microM) and cobalt protoporphyrin IX (CoPP) increased HO-1 messenger RNA and protein expression.	Cilostazol	0-10	heme oxygenase 1	Homo sapiens	69-73
20131233-6	2010	Cilostazol (10 microM) and cobalt protoporphyrin IX (CoPP) increased HO-1 messenger RNA and protein expression.	cobaltiprotoporphyrin	27-51	heme oxygenase 1	Homo sapiens	69-73
20131233-12	2010	Cilostazol- and CoPP-induced HO-1 expression was diminished in cells transfected with Nrf2 siRNA.	cobaltiprotoporphyrin	16-20	heme oxygenase 1	Homo sapiens	29-33
20131233-6	2010	Cilostazol (10 microM) and cobalt protoporphyrin IX (CoPP) increased HO-1 messenger RNA and protein expression.	cobaltiprotoporphyrin	53-57	heme oxygenase 1	Homo sapiens	69-73
20131233-13	2010	CONCLUSION: Cilostazol suppressed proliferation of synovial cells from RA patients by enhancing apoptosis, and also inhibited cytokine production via mediation of cAMP-dependent protein kinase activation-coupled Nrf2-linked HO-1 expression.	Cilostazol	12-22	heme oxygenase 1	Homo sapiens	224-228
20131233-7	2010	These effects were suppressed by zinc protoporphyrin IX (ZnPP), an HO-1 inhibitor.	zinc protoporphyrin	33-55	heme oxygenase 1	Homo sapiens	67-71
20131233-7	2010	These effects were suppressed by zinc protoporphyrin IX (ZnPP), an HO-1 inhibitor.	zinc protoporphyrin	57-61	heme oxygenase 1	Homo sapiens	67-71
20131233-13	2010	CONCLUSION: Cilostazol suppressed proliferation of synovial cells from RA patients by enhancing apoptosis, and also inhibited cytokine production via mediation of cAMP-dependent protein kinase activation-coupled Nrf2-linked HO-1 expression.	Cyclic AMP	163-167	heme oxygenase 1	Homo sapiens	224-228
20091384-1	2010	Heme oxygenase (HO)-1, a heme-degrading enzyme inducible by various stimuli, plays a key role in the regulation of inflammatory response in monocytes/macrophages.	Heme	25-29	heme oxygenase 1	Homo sapiens	0-21
20124108-5	2010	Overexpression of heme oxygenase 1 and its gaseous product, carbon monoxide, decreased PAR-2-stimulated sVEGFR-1 release from human umbilical vein endothelial cells.	Carbon Monoxide	60-75	heme oxygenase 1	Homo sapiens	18-34
20124108-6	2010	Simvastatin, which upregulates heme oxygenase 1, also suppressed PAR-2-mediated sVEGFR-1 release.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	31-47
20020468-1	2010	Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin.	Heme	139-143	heme oxygenase 1	Homo sapiens	0-16
20020468-1	2010	Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin.	Heme	139-143	heme oxygenase 1	Homo sapiens	18-22
20020468-1	2010	Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	0-16
20020468-1	2010	Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	18-22
20020468-1	2010	Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin.	Biliverdine	169-179	heme oxygenase 1	Homo sapiens	0-16
20020468-1	2010	Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin.	Biliverdine	169-179	heme oxygenase 1	Homo sapiens	18-22
20020468-6	2010	Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1.	Bilirubin	42-51	heme oxygenase 1	Homo sapiens	36-40
20171361-0	2010	Simvastatin promotes odontoblastic differentiation and expression of angiogenic factors via heme oxygenase-1 in primary cultured human dental pulp cells.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	92-108
20020468-6	2010	Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1.	Bilirubin	42-51	heme oxygenase 1	Homo sapiens	121-125
20171361-7	2010	The inducing effect of simvastatin on odontoblastic differentiation and angiogenesis was nullified by an HO-1 inhibitor and a carbon monoxide (CO) scavenger.	Simvastatin	23-34	heme oxygenase 1	Homo sapiens	105-109
20020468-6	2010	Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1.	Carbon Monoxide	53-68	heme oxygenase 1	Homo sapiens	121-125
20171361-8	2010	CONCLUSIONS: These results suggested that simvastatin exerts its odontoblastic differentiation and angiogenesis-inducing effects in HDPCs through a mechanism that involves the action of HO-1 and its product CO.	Simvastatin	42-53	heme oxygenase 1	Homo sapiens	186-190
20020468-6	2010	Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1.	Iron	74-78	heme oxygenase 1	Homo sapiens	121-125
20020468-8	2010	In addition, endogenous PPARgamma ligand, 15-deoxy-Delta(12,14)-prostaglandin-J2 (15d-PGJ2) markedly increased both mRNA and protein levels of HO-1 in osteoblasts via PI3K-Akt and MAPK pathways.	15-deoxy-delta(	42-57	heme oxygenase 1	Homo sapiens	143-147
19917515-0	2010	Structural characterization of human heme oxygenase-1 in complex with azole-based inhibitors.	Azoles	70-75	heme oxygenase 1	Homo sapiens	37-53
20020468-8	2010	In addition, endogenous PPARgamma ligand, 15-deoxy-Delta(12,14)-prostaglandin-J2 (15d-PGJ2) markedly increased both mRNA and protein levels of HO-1 in osteoblasts via PI3K-Akt and MAPK pathways.	9-deoxy-delta-9-prostaglandin D2	63-80	heme oxygenase 1	Homo sapiens	143-147
20333281-0	2010	Possible role of heme oxygenase-1 and prostaglandins in the pathogenesis of cerebral malaria: heme oxygenase-1 induction by prostaglandin D(2) and metabolite by a human astrocyte cell line.	Prostaglandins	38-52	heme oxygenase 1	Homo sapiens	94-110
20333281-0	2010	Possible role of heme oxygenase-1 and prostaglandins in the pathogenesis of cerebral malaria: heme oxygenase-1 induction by prostaglandin D(2) and metabolite by a human astrocyte cell line.	Prostaglandins D	124-139	heme oxygenase 1	Homo sapiens	94-110
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Heme	48-52	heme oxygenase 1	Homo sapiens	0-16
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Heme	48-52	heme oxygenase 1	Homo sapiens	18-22
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Iron	82-86	heme oxygenase 1	Homo sapiens	0-16
20217200-7	2010	On the other hand, heme oxygenase-1 (HO-1) and inducible nitric oxide synthase (iNOS) expression were significantly increased by exposure to both ammonia and proinflammatory mediators and although modest, these effects were additive suggestive of a synergistic mechanism.	Ammonia	146-153	heme oxygenase 1	Homo sapiens	19-35
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Iron	82-86	heme oxygenase 1	Homo sapiens	18-22
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	0-16
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	18-22
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	0-16
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Biliverdine	109-119	heme oxygenase 1	Homo sapiens	18-22
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Bilirubin	120-129	heme oxygenase 1	Homo sapiens	0-16
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Bilirubin	120-129	heme oxygenase 1	Homo sapiens	18-22
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Iron	149-153	heme oxygenase 1	Homo sapiens	0-16
20333281-4	2010	Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites.	Iron	149-153	heme oxygenase 1	Homo sapiens	18-22
20203419-0	2010	4-Methylcatechol-induced heme oxygenase-1 exerts a protective effect against oxidative stress in cultured neural stem/progenitor cells via PI3 kinase/Akt pathway.	4-methylcatechol	0-16	heme oxygenase 1	Homo sapiens	25-41
19961840-0	2010	Senkyunolides reduce hydrogen peroxide-induced oxidative damage in human liver HepG2 cells via induction of heme oxygenase-1.	3-N-butyl-4,5-dihydrophthalide	0-13	heme oxygenase 1	Homo sapiens	108-124
19961840-0	2010	Senkyunolides reduce hydrogen peroxide-induced oxidative damage in human liver HepG2 cells via induction of heme oxygenase-1.	Hydrogen Peroxide	21-38	heme oxygenase 1	Homo sapiens	108-124
19961840-2	2010	To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron.	Heme	122-126	heme oxygenase 1	Homo sapiens	140-144
19961840-2	2010	To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron.	Biliverdine	221-231	heme oxygenase 1	Homo sapiens	140-144
19961840-2	2010	To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron.	Carbon Monoxide	233-248	heme oxygenase 1	Homo sapiens	122-138
19961840-2	2010	To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron.	Carbon Monoxide	233-248	heme oxygenase 1	Homo sapiens	140-144
19961840-2	2010	To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron.	Iron	258-262	heme oxygenase 1	Homo sapiens	122-138
19961840-2	2010	To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron.	Iron	258-262	heme oxygenase 1	Homo sapiens	140-144
19961840-9	2010	Thus, this study demonstrated that senkyunolide-H and -I attenuated oxidative damage via activation of HO-1 pathway.	3-N-butyl-4,5-dihydrophthalide	35-47	heme oxygenase 1	Homo sapiens	103-107
19965783-2	2010	Tissues from sickle patients express heme oxygenase-1 (HO-1), the enzyme that degrades free heme/hemoglobin to the signaling molecule carbon monoxide, and the antioxidants biliverdin/bilirubin.	Carbon Monoxide	134-149	heme oxygenase 1	Homo sapiens	37-53
19965783-2	2010	Tissues from sickle patients express heme oxygenase-1 (HO-1), the enzyme that degrades free heme/hemoglobin to the signaling molecule carbon monoxide, and the antioxidants biliverdin/bilirubin.	Carbon Monoxide	134-149	heme oxygenase 1	Homo sapiens	55-59
19965783-8	2010	HO-1 induction, exogenous biliverdin, or carbon monoxide markedly decreased adhesion of sickle blood to the endothelium, and sickle red cells partially inhibited relaxation mediated by carbon monoxide in isolated aortas.	Carbon Monoxide	185-200	heme oxygenase 1	Homo sapiens	0-4
20203419-1	2010	4-Methylcatechol (4MC), a stimulator of the synthesis of neurotrophin family members in various cells, was able to up-regulate the expression of heme oxygenase (HO)-1, a redox-sensitive inducible stress protein, in neural stem/progenitor cells (NS/PCs).	4-methylcatechol	0-16	heme oxygenase 1	Homo sapiens	145-166
20203419-1	2010	4-Methylcatechol (4MC), a stimulator of the synthesis of neurotrophin family members in various cells, was able to up-regulate the expression of heme oxygenase (HO)-1, a redox-sensitive inducible stress protein, in neural stem/progenitor cells (NS/PCs).	4-methylcatechol	18-21	heme oxygenase 1	Homo sapiens	145-166
20203419-2	2010	RT-PCR analysis showed that 4MC induced HO-1 mRNA expression in a dose- and a time-dependent manner.	4-methylcatechol	28-31	heme oxygenase 1	Homo sapiens	40-44
20203419-6	2010	Pretreatment of cultures with a selective inhibitor of PI3 kinase (PI3K)/Akt, but not with one of MAPK/ERK, inhibited both the 4MCinduced HO-1 expression and neuroprotective effect, demonstrating that PI3K/Akt signaling pathway played a significant role in 4MC-induced HO-1 induction and neuroprotection.	4-methylcatechol	127-130	heme oxygenase 1	Homo sapiens	138-142
20203419-6	2010	Pretreatment of cultures with a selective inhibitor of PI3 kinase (PI3K)/Akt, but not with one of MAPK/ERK, inhibited both the 4MCinduced HO-1 expression and neuroprotective effect, demonstrating that PI3K/Akt signaling pathway played a significant role in 4MC-induced HO-1 induction and neuroprotection.	4-methylcatechol	127-130	heme oxygenase 1	Homo sapiens	269-273
20203419-7	2010	Taken together, our results suggest that 4MC activates the expression of HO-1 through the PI3K/Akt signaling pathway and that the HO-1 protein inhibits the death of NS/PCs induced by oxidative stress.	4-methylcatechol	41-44	heme oxygenase 1	Homo sapiens	73-77
19956091-1	2010	Heme oxygenase (HO)-1 degrades heme and protects against oxidative stress, but it has not been pharmacologically induced in humans.	Heme	31-35	heme oxygenase 1	Homo sapiens	0-21
19956091-2	2010	In this randomized study of 10 healthy volunteers, hemin (3 mg/kg intravenously in 25% albumin) was shown to increase plasma HO-1 protein concentration four- to fivefold and HO-1 activity ~15-fold relative to baseline at 24 and 48 h (placebo -56.41 +/- 6.31 (baseline), 69.79 +/- 13.00 (24 h), 77.44 +/- 10.62 (48 h) vs. hemin -71.70 +/- 9.20 (baseline), 1,126.20 +/- 293.30 (24 h), 1,192.20 +/- 333.30 (48 h)) in four of five subjects as compared with albumin alone (P &lt;/= 0.03).	Hemin	51-56	heme oxygenase 1	Homo sapiens	125-129
19956091-2	2010	In this randomized study of 10 healthy volunteers, hemin (3 mg/kg intravenously in 25% albumin) was shown to increase plasma HO-1 protein concentration four- to fivefold and HO-1 activity ~15-fold relative to baseline at 24 and 48 h (placebo -56.41 +/- 6.31 (baseline), 69.79 +/- 13.00 (24 h), 77.44 +/- 10.62 (48 h) vs. hemin -71.70 +/- 9.20 (baseline), 1,126.20 +/- 293.30 (24 h), 1,192.20 +/- 333.30 (48 h)) in four of five subjects as compared with albumin alone (P &lt;/= 0.03).	Hemin	51-56	heme oxygenase 1	Homo sapiens	174-178
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Heme	117-121	heme oxygenase 1	Homo sapiens	0-16
19558496-6	2010	Induction of Nrf2 due to SFN was accompanied by an increase in mRNA and protein levels of NADPH quinone oxidoreductase 1, heme oxygenase 1 and gamma-glutamylcysteine-synthetase.	sulforaphane	25-28	heme oxygenase 1	Homo sapiens	122-138
19797297-1	2010	HO-1 is the only inducible one of three isoenzymes that catalyzes the oxidative degradation of heme.	Heme	95-99	heme oxygenase 1	Homo sapiens	0-4
19797297-7	2010	HO-1 modulation by SnPP treatment of T(regs) or PGJ(2) treatment of CD4(+)CD25(-) T cells neither suppressed nor induced immune-modulatory function in these cells, respectively, as measured by responder-cell proliferation and/or IL-2 production.	2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE	48-51	heme oxygenase 1	Homo sapiens	0-4
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Heme	117-121	heme oxygenase 1	Homo sapiens	18-22
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Carbon Monoxide	125-140	heme oxygenase 1	Homo sapiens	0-16
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Carbon Monoxide	125-140	heme oxygenase 1	Homo sapiens	18-22
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Carbon Monoxide	142-144	heme oxygenase 1	Homo sapiens	0-16
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Carbon Monoxide	142-144	heme oxygenase 1	Homo sapiens	18-22
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Iron	147-151	heme oxygenase 1	Homo sapiens	0-16
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Iron	147-151	heme oxygenase 1	Homo sapiens	18-22
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Bilirubin	156-165	heme oxygenase 1	Homo sapiens	0-16
19925812-1	2010	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin.	Bilirubin	156-165	heme oxygenase 1	Homo sapiens	18-22
19925812-13	2010	These results indicate that the downstream products of HO-1, i.e. bilirubin and CO, modulate BDNF and GDNF expression in neuron and astrocyte.	Bilirubin	66-75	heme oxygenase 1	Homo sapiens	55-59
19937094-0	2010	Kaempferol suppresses cisplatin-induced apoptosis via inductions of heme oxygenase-1 and glutamate-cysteine ligase catalytic subunit in HEI-OC1 cell.	kaempferol	0-10	heme oxygenase 1	Homo sapiens	68-84
19937094-0	2010	Kaempferol suppresses cisplatin-induced apoptosis via inductions of heme oxygenase-1 and glutamate-cysteine ligase catalytic subunit in HEI-OC1 cell.	Cisplatin	22-31	heme oxygenase 1	Homo sapiens	68-84
19937094-7	2010	Kaempferol-induced HO-1 expression protected against cell death though the c-Jun N-terminal kinase (JNK) pathway and by the aid of Nrf2 translocation.	kaempferol	0-10	heme oxygenase 1	Homo sapiens	19-23
19937094-10	2010	CONCLUSION: The expression of HO-1 by kaempferol inhibits cisplatin-induced apoptosis in HEI-OC1 cells, and the mechanism of protective effect is also associated with its inductive effect of GCLC expression.	kaempferol	38-48	heme oxygenase 1	Homo sapiens	30-34
19833168-0	2010	Rottlerin induces heme oxygenase-1 (HO-1) up-regulation through reactive oxygen species (ROS) dependent and PKC delta-independent pathway in human colon cancer HT29 cells.	rottlerin	0-9	heme oxygenase 1	Homo sapiens	18-34
19937094-10	2010	CONCLUSION: The expression of HO-1 by kaempferol inhibits cisplatin-induced apoptosis in HEI-OC1 cells, and the mechanism of protective effect is also associated with its inductive effect of GCLC expression.	Cisplatin	58-67	heme oxygenase 1	Homo sapiens	30-34
20656217-4	2010	Heme oxygenase 1 (HO-1) protein expression is specifically increased in lesions with a vulnerable plaque phenotype resembling TCFAs and correlates with a rise in expression levels of intimal proinflammatory markers.	tcfas	126-131	heme oxygenase 1	Homo sapiens	0-16
20656217-4	2010	Heme oxygenase 1 (HO-1) protein expression is specifically increased in lesions with a vulnerable plaque phenotype resembling TCFAs and correlates with a rise in expression levels of intimal proinflammatory markers.	tcfas	126-131	heme oxygenase 1	Homo sapiens	18-22
21081219-6	2010	In the past, attempts to avoid nitrate-induced side effects have focused on administration schedules that would allow a "nitrate-free interval"; in the future, the role of co-therapies with antioxidant compounds and of activation of endogeneous protective pathways such as the heme oxygenase 1 (HO-1) will need to be explored.	Nitrates	31-38	heme oxygenase 1	Homo sapiens	277-293
19833168-10	2010	These results suggest that rottlerin induces up-regulation of HO-1 via PKC delta-independent pathway.	rottlerin	27-36	heme oxygenase 1	Homo sapiens	62-66
19833168-11	2010	Taken together, the present study identified rottlerin as a novel inducer of HO-1 expression and identified the mechanisms involved in this process.	rottlerin	45-54	heme oxygenase 1	Homo sapiens	77-81
19833168-0	2010	Rottlerin induces heme oxygenase-1 (HO-1) up-regulation through reactive oxygen species (ROS) dependent and PKC delta-independent pathway in human colon cancer HT29 cells.	rottlerin	0-9	heme oxygenase 1	Homo sapiens	36-40
19833168-0	2010	Rottlerin induces heme oxygenase-1 (HO-1) up-regulation through reactive oxygen species (ROS) dependent and PKC delta-independent pathway in human colon cancer HT29 cells.	Reactive Oxygen Species	64-87	heme oxygenase 1	Homo sapiens	18-34
19833168-0	2010	Rottlerin induces heme oxygenase-1 (HO-1) up-regulation through reactive oxygen species (ROS) dependent and PKC delta-independent pathway in human colon cancer HT29 cells.	Reactive Oxygen Species	64-87	heme oxygenase 1	Homo sapiens	36-40
19833168-0	2010	Rottlerin induces heme oxygenase-1 (HO-1) up-regulation through reactive oxygen species (ROS) dependent and PKC delta-independent pathway in human colon cancer HT29 cells.	Reactive Oxygen Species	89-92	heme oxygenase 1	Homo sapiens	18-34
19833168-0	2010	Rottlerin induces heme oxygenase-1 (HO-1) up-regulation through reactive oxygen species (ROS) dependent and PKC delta-independent pathway in human colon cancer HT29 cells.	Reactive Oxygen Species	89-92	heme oxygenase 1	Homo sapiens	36-40
19833168-1	2010	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by its substrate heme and diverse stimuli.	Heme	78-82	heme oxygenase 1	Homo sapiens	0-16
19833168-1	2010	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by its substrate heme and diverse stimuli.	Heme	78-82	heme oxygenase 1	Homo sapiens	18-22
19833168-3	2010	In this study, the effect of rottlerin, a putative PKC delta inhibitor, on HO-1 expression in HT29 human colon cancer cells was investigated.	rottlerin	29-38	heme oxygenase 1	Homo sapiens	75-79
19833168-4	2010	Rottlerin-induced HO-1 at both protein and mRNA levels in a dose- and time-dependent manner.	rottlerin	0-9	heme oxygenase 1	Homo sapiens	18-22
19833168-5	2010	Rottlerin-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine (NAC) or glutathione (GSH).	rottlerin	0-9	heme oxygenase 1	Homo sapiens	19-23
19833168-5	2010	Rottlerin-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine (NAC) or glutathione (GSH).	Acetylcysteine	67-83	heme oxygenase 1	Homo sapiens	19-23
19833168-5	2010	Rottlerin-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine (NAC) or glutathione (GSH).	Acetylcysteine	85-88	heme oxygenase 1	Homo sapiens	19-23
19833168-5	2010	Rottlerin-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine (NAC) or glutathione (GSH).	Glutathione	93-104	heme oxygenase 1	Homo sapiens	19-23
19833168-5	2010	Rottlerin-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine (NAC) or glutathione (GSH).	Glutathione	106-109	heme oxygenase 1	Homo sapiens	19-23
19833168-8	2010	The pharmacological inhibition of ERK and p38 MAPK inhibited rottlerin-induced HO-1 up-regulation.	rottlerin	61-70	heme oxygenase 1	Homo sapiens	79-83
21048309-0	2010	Geniposide induces the expression of heme oxygenase-1 via PI3K/Nrf2-signaling to enhance the antioxidant capacity in primary hippocampal neurons.	geniposide	0-10	heme oxygenase 1	Homo sapiens	37-53
21048309-5	2010	Taken together, the novel cytoprotective mechanism of geniposide to antagonize oxidative stress may be involved in PI3K- and Nrf2-mediated upregulation of the antioxidative enzyme HO-1.	geniposide	54-64	heme oxygenase 1	Homo sapiens	180-184
21048309-3	2010	In this study, geniposide upregulates the expression of heme oxygenase-1 (HO-1) to attenuate the cell apoptosis induced by 3-morpholinosydnonimine hydrochloride (SIN-1) in primary cultured hippocampal neurons.	geniposide	15-25	heme oxygenase 1	Homo sapiens	56-72
21048309-3	2010	In this study, geniposide upregulates the expression of heme oxygenase-1 (HO-1) to attenuate the cell apoptosis induced by 3-morpholinosydnonimine hydrochloride (SIN-1) in primary cultured hippocampal neurons.	geniposide	15-25	heme oxygenase 1	Homo sapiens	74-78
21048309-3	2010	In this study, geniposide upregulates the expression of heme oxygenase-1 (HO-1) to attenuate the cell apoptosis induced by 3-morpholinosydnonimine hydrochloride (SIN-1) in primary cultured hippocampal neurons.	linsidomine	123-160	heme oxygenase 1	Homo sapiens	56-72
21048309-3	2010	In this study, geniposide upregulates the expression of heme oxygenase-1 (HO-1) to attenuate the cell apoptosis induced by 3-morpholinosydnonimine hydrochloride (SIN-1) in primary cultured hippocampal neurons.	linsidomine	123-160	heme oxygenase 1	Homo sapiens	74-78
21048309-4	2010	Furthermore, geniposide induces the nuclear translocation of nuclear factor-E2-related factor 2 (Nrf2) and activation of phosphatidylinositol 3"-kinase (PI3K) in the presence of oxidative stress, and both LY294002 (a specific inhibitor of PI3K) and Zinc protoporphyrin (ZnPP, an inhibitor of HO-1) decrease the cytoprotective action of geniposide in hippocampal neurons.	geniposide	13-23	heme oxygenase 1	Homo sapiens	292-296
20054154-4	2010	CdCl(2) induced effects following either apical or basolateral exposure were evaluated by Neutral Red Uptake (NRU), Trans-Epithelial Electrical Resistance (TEER), and alteration in Metallothionein 1X (MT1X), Heat shock protein 70 (HSP70), and Heme oxygenase 1 (HMOX-1) genes.	cdcl	0-4	heme oxygenase 1	Homo sapiens	243-259
20378994-0	2010	Oligosaccharides from agar inhibit pro-inflammatory mediator release by inducing heme oxygenase 1.	Oligosaccharides	0-16	heme oxygenase 1	Homo sapiens	81-97
20378994-0	2010	Oligosaccharides from agar inhibit pro-inflammatory mediator release by inducing heme oxygenase 1.	Agar	22-26	heme oxygenase 1	Homo sapiens	81-97
20378994-3	2010	We also demonstrate that those effects of agaro-oligosaccharides on activated monocytes and macrophages may have been caused by heme oxygenase-1 induction.	agaro-oligosaccharides	42-64	heme oxygenase 1	Homo sapiens	128-144
20054154-7	2010	Co-administration of N-Acetylcysteine (NAC) exerted a strong protective effect against CdCl(2) induced barrier damage and stress related genes, while other antioxidants only attenuated CdCl(2) induced HSP70 and HMOX-1 and showed no protective effect on the barrier collapse.	Acetylcysteine	39-42	heme oxygenase 1	Homo sapiens	211-217
20054154-9	2010	The protective effect of NAC against CdCl(2) induced MT1X, HSP70 and HMOX-1 genes, demonstrates an anti-oxidant effect of NAC in addition to Cd chelation.	Acetylcysteine	25-28	heme oxygenase 1	Homo sapiens	69-75
20054154-9	2010	The protective effect of NAC against CdCl(2) induced MT1X, HSP70 and HMOX-1 genes, demonstrates an anti-oxidant effect of NAC in addition to Cd chelation.	cdcl	37-41	heme oxygenase 1	Homo sapiens	69-75
20054154-9	2010	The protective effect of NAC against CdCl(2) induced MT1X, HSP70 and HMOX-1 genes, demonstrates an anti-oxidant effect of NAC in addition to Cd chelation.	Acetylcysteine	122-125	heme oxygenase 1	Homo sapiens	69-75
20054154-9	2010	The protective effect of NAC against CdCl(2) induced MT1X, HSP70 and HMOX-1 genes, demonstrates an anti-oxidant effect of NAC in addition to Cd chelation.	Cadmium	37-39	heme oxygenase 1	Homo sapiens	69-75
20054154-4	2010	CdCl(2) induced effects following either apical or basolateral exposure were evaluated by Neutral Red Uptake (NRU), Trans-Epithelial Electrical Resistance (TEER), and alteration in Metallothionein 1X (MT1X), Heat shock protein 70 (HSP70), and Heme oxygenase 1 (HMOX-1) genes.	cdcl	0-4	heme oxygenase 1	Homo sapiens	261-267
20054154-5	2010	CdCl(2) exposure resulted in a collapse of barrier function and the induction of MT1X, HMOX-1 and HSP70 genes, prior to alterations in cell viability.	Cadmium Chloride	0-7	heme oxygenase 1	Homo sapiens	87-93
20054154-7	2010	Co-administration of N-Acetylcysteine (NAC) exerted a strong protective effect against CdCl(2) induced barrier damage and stress related genes, while other antioxidants only attenuated CdCl(2) induced HSP70 and HMOX-1 and showed no protective effect on the barrier collapse.	Acetylcysteine	21-37	heme oxygenase 1	Homo sapiens	211-217
20184791-3	2010	Compared to HO-2, which is constitutively expressed, HO-1 is a stressresponsive protein that is highly induced by many agents, including cytokines, endotoxin, heavy metals, nitric oxide and its own substrate heme.	Nitric Oxide	173-185	heme oxygenase 1	Homo sapiens	53-57
20064636-0	2010	Induction of heme oxygenase-1 in normal and malignant B lymphocytes by 15-deoxy-Delta(12,14)-prostaglandin J(2) requires Nrf2.	15-deoxy-delta(12,14)-prostaglandin j	71-108	heme oxygenase 1	Homo sapiens	13-29
20064636-5	2010	15d-PGJ(2) potently induced HO-1 protein expression in normal and malignant B cells.	15d-pgj	0-7	heme oxygenase 1	Homo sapiens	28-32
20184791-3	2010	Compared to HO-2, which is constitutively expressed, HO-1 is a stressresponsive protein that is highly induced by many agents, including cytokines, endotoxin, heavy metals, nitric oxide and its own substrate heme.	Heme	208-212	heme oxygenase 1	Homo sapiens	53-57
19954435-1	2010	X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone.	4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone	66-111	heme oxygenase 1	Homo sapiens	33-49
20184791-5	2010	Over the past decade, compelling evidence has revealed that the induction of HO-1 represents an important defensive mechanism against further oxidative injury in tissues and cells following various insults; this occurs by virtue of the anti-inflammatory and antioxidant capacities of CO, biliverdin, and the subsequent metabolite of biliverdin, bilirubin.	Carbon Monoxide	284-286	heme oxygenase 1	Homo sapiens	77-81
19954435-2	2010	A series of 1-azolyl-4-phenyl-2-butanones was designed and synthesized for the inhibition of heme oxygenases (heme oxygenase-1 and heme oxygenase-2).	1-azolyl-4-phenyl-2-butanones	12-41	heme oxygenase 1	Homo sapiens	110-147
20184791-5	2010	Over the past decade, compelling evidence has revealed that the induction of HO-1 represents an important defensive mechanism against further oxidative injury in tissues and cells following various insults; this occurs by virtue of the anti-inflammatory and antioxidant capacities of CO, biliverdin, and the subsequent metabolite of biliverdin, bilirubin.	Biliverdine	288-298	heme oxygenase 1	Homo sapiens	77-81
19954435-7	2010	The first reported X-ray crystal structure of human heme oxygenase-1 in complex with a 1,2,4-triazole-based inhibitor, namely 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone, was also determined.	1,2,4-triazole	87-101	heme oxygenase 1	Homo sapiens	52-68
20184791-5	2010	Over the past decade, compelling evidence has revealed that the induction of HO-1 represents an important defensive mechanism against further oxidative injury in tissues and cells following various insults; this occurs by virtue of the anti-inflammatory and antioxidant capacities of CO, biliverdin, and the subsequent metabolite of biliverdin, bilirubin.	Biliverdine	333-343	heme oxygenase 1	Homo sapiens	77-81
19954435-7	2010	The first reported X-ray crystal structure of human heme oxygenase-1 in complex with a 1,2,4-triazole-based inhibitor, namely 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone, was also determined.	4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone	126-171	heme oxygenase 1	Homo sapiens	52-68
20184791-5	2010	Over the past decade, compelling evidence has revealed that the induction of HO-1 represents an important defensive mechanism against further oxidative injury in tissues and cells following various insults; this occurs by virtue of the anti-inflammatory and antioxidant capacities of CO, biliverdin, and the subsequent metabolite of biliverdin, bilirubin.	Bilirubin	345-354	heme oxygenase 1	Homo sapiens	77-81
19954435-8	2010	The inhibitor binds to the human heme oxygenase-1 distal pocket through the coordination of heme iron by the N4 in the triazole moiety, whereas the phenyl group is stabilized by hydrophobic interactions from residues within the binding pocket.	Iron	97-101	heme oxygenase 1	Homo sapiens	33-49
19954435-8	2010	The inhibitor binds to the human heme oxygenase-1 distal pocket through the coordination of heme iron by the N4 in the triazole moiety, whereas the phenyl group is stabilized by hydrophobic interactions from residues within the binding pocket.	Folic Acid	109-111	heme oxygenase 1	Homo sapiens	33-49
21525764-9	2010	RESULTS: Ethanol and TGF-beta rapidly increase ROI and reduce GSH in hHeps, causing apoptosis with a release of approximately 40% total LDH after 72 h. Similar to incubation with hemin preincubation and co-incubation of cells with nifedipine, verapamil and quercetin significantly reduce oxidative stress and resulting cellular damage, in a dose-dependent manner, by initiating nuclear translocation of Nrf2 which in turn induces HO-1 under the control of p38 and ERK.	Ethanol	9-16	heme oxygenase 1	Homo sapiens	430-434
19954435-8	2010	The inhibitor binds to the human heme oxygenase-1 distal pocket through the coordination of heme iron by the N4 in the triazole moiety, whereas the phenyl group is stabilized by hydrophobic interactions from residues within the binding pocket.	Triazoles	119-127	heme oxygenase 1	Homo sapiens	33-49
21525764-10	2010	Blocking of HO-1 activity with ZNPP9 reverses the protective effect of all three substances.	zinc protoporphyrin	31-36	heme oxygenase 1	Homo sapiens	12-16
21525764-12	2010	As polyphenols have great potential to induce HO-1 expression, they may play an important role for future therapeutic strategies to protect liver from oxidative stress-dependent damage observed during chronic alcohol consumption.	Polyphenols	3-14	heme oxygenase 1	Homo sapiens	46-50
21525764-12	2010	As polyphenols have great potential to induce HO-1 expression, they may play an important role for future therapeutic strategies to protect liver from oxidative stress-dependent damage observed during chronic alcohol consumption.	Alcohols	209-216	heme oxygenase 1	Homo sapiens	46-50
19720622-3	2010	We have recently shown that UVA-1 oxidized the abundant membrane phospholipid 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (PAPC), which then induced the stress-response protein heme oxygenase 1 (HO-1) in dermal fibroblasts.	phospholipid 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine	65-135	heme oxygenase 1	Homo sapiens	191-207
19720622-3	2010	We have recently shown that UVA-1 oxidized the abundant membrane phospholipid 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (PAPC), which then induced the stress-response protein heme oxygenase 1 (HO-1) in dermal fibroblasts.	phospholipid 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine	65-135	heme oxygenase 1	Homo sapiens	209-213
20700711-3	2010	Quantitative PCR analysis as well as Western blotting demonstrated a specific upregulation of Hsp70 mRNA and protein after heat shock, while heme oxygenase 1 (HO1 or Hsp32) mRNA and protein was specifically upregulated following H2O2-induced oxidative stress.	Hydrogen Peroxide	229-233	heme oxygenase 1	Homo sapiens	141-157
20388101-4	2010	The mechanisms through which dietary supplementation with antioxidants may be useful to prevent free radical-related diseases is related to their ability to counteract toxic production of both reactive oxygen and nitrogen species, along with the up-regulation of vitagenes, such as members of the heat shock protein (Hsp) family heme oxygenase-1 and Hsp70.	Free Radicals	96-108	heme oxygenase 1	Homo sapiens	329-345
19375813-3	2010	We found that treatment with cisplatin further augmented HO-1 expression, which was associated with activation of the epidermal growth factor receptor (EGFR) mediated signaling pathway and subsequent nuclear translocation of NF-kappaB.	Cisplatin	29-38	heme oxygenase 1	Homo sapiens	57-61
19375813-4	2010	In concordance with the findings, treatment with EGFR-selective tyrosine kinase inhibitor (AG1478) or an Akt inhibitor, which interfere with the post-EGFR signaling pathway, suppressed cisplatin induced HO-1 expression.	RTKI cpd	91-97	heme oxygenase 1	Homo sapiens	203-207
19375813-4	2010	In concordance with the findings, treatment with EGFR-selective tyrosine kinase inhibitor (AG1478) or an Akt inhibitor, which interfere with the post-EGFR signaling pathway, suppressed cisplatin induced HO-1 expression.	Cisplatin	185-194	heme oxygenase 1	Homo sapiens	203-207
19375813-7	2010	Collectively, the results indicate that resistance to cisplatin in A549 cells is associated with HO-1 through EGFR mediated signaling pathway including activation of the PI3k/Akt and NF-kappaB systems.	Cisplatin	54-63	heme oxygenase 1	Homo sapiens	97-101
21504135-11	2010	Consequently, the expression of heme oxygenase-1 and gamma-glutamyl-cysteine-synthase were elevated after 24 hrs of acrolein treatment.	Acrolein	116-124	heme oxygenase 1	Homo sapiens	32-48
19375813-2	2010	We investigated involvement of HO-1 in chemoresistance of cisplatin in human lung epithelial adenocarcinoma cell line, A549, which constitutively expressed HO-1.	Cisplatin	58-67	heme oxygenase 1	Homo sapiens	31-35
20072927-0	2010	Characterization of the antioxidant properties of pentaerithrityl tetranitrate (PETN)-induction of the intrinsic antioxidative system heme oxygenase-1 (HO-1).	Pentaerythritol Tetranitrate	50-78	heme oxygenase 1	Homo sapiens	134-150
20700711-3	2010	Quantitative PCR analysis as well as Western blotting demonstrated a specific upregulation of Hsp70 mRNA and protein after heat shock, while heme oxygenase 1 (HO1 or Hsp32) mRNA and protein was specifically upregulated following H2O2-induced oxidative stress.	Hydrogen Peroxide	229-233	heme oxygenase 1	Homo sapiens	159-162
20072927-0	2010	Characterization of the antioxidant properties of pentaerithrityl tetranitrate (PETN)-induction of the intrinsic antioxidative system heme oxygenase-1 (HO-1).	Pentaerythritol Tetranitrate	80-84	heme oxygenase 1	Homo sapiens	134-150
20700711-3	2010	Quantitative PCR analysis as well as Western blotting demonstrated a specific upregulation of Hsp70 mRNA and protein after heat shock, while heme oxygenase 1 (HO1 or Hsp32) mRNA and protein was specifically upregulated following H2O2-induced oxidative stress.	Hydrogen Peroxide	229-233	heme oxygenase 1	Homo sapiens	166-171
20072927-6	2010	Some of these effects are related to special pharmacokinetics of PETN, but upon chronic administration, PETN also induces antioxidative pathways at the genomic level, resulting in increased expression of heme oxygenase-1 (HO-1) and ferritin, both possessing highly protective properties.	Pentaerythritol Tetranitrate	104-108	heme oxygenase 1	Homo sapiens	204-220
19591088-0	2010	Protective effect of sauchinone by upregulating heme oxygenase-1 via the P38 MAPK and Nrf2/ARE pathways in HepG2 cells.	sauchinone	21-31	heme oxygenase 1	Homo sapiens	48-64
19895178-2	2010	In this study, the correlation between the HO-1 gene promoter polymorphism and alcohol, along with the risk of ESCC on Chinese males, was analyzed.The case-control study was performed in 143 ESCC patients and 264 cancer-free controls.	Alcohols	79-86	heme oxygenase 1	Homo sapiens	43-47
20062840-4	2010	Furthermore, a reduction of free heme levels led to a strong decrease in UVA-induced Nrf2 and HO-1 protein levels confirming a clear role for heme in the UV-mediated stress response.	Heme	33-37	heme oxygenase 1	Homo sapiens	94-98
20062840-4	2010	Furthermore, a reduction of free heme levels led to a strong decrease in UVA-induced Nrf2 and HO-1 protein levels confirming a clear role for heme in the UV-mediated stress response.	Heme	142-146	heme oxygenase 1	Homo sapiens	94-98
19591088-4	2010	This study investigated the potency of sauchinone as a hepatic heme oxygenase (HO)-1 inducer and its protective effects in HepG2 cells.	sauchinone	39-49	heme oxygenase 1	Homo sapiens	63-84
20199188-5	2010	Interestingly, inhibition of HO-1 induction (by zinc protoporphyrin, ZnP) was associated with an accelerated mitogenic response to EGF and HGF in MCs.	zinc protoporphyrin	48-67	heme oxygenase 1	Homo sapiens	29-33
21062534-4	2010	In fact, it has been demonstrated that the activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in various animal intestinal injury models induced by ischemia-reperfusion, indomethacin, lipopolysaccharide-associated sepsis, trinitrobenzene sulfonic acid or dextran sulfate sodium.	Indomethacin	224-236	heme oxygenase 1	Homo sapiens	57-61
21062534-4	2010	In fact, it has been demonstrated that the activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in various animal intestinal injury models induced by ischemia-reperfusion, indomethacin, lipopolysaccharide-associated sepsis, trinitrobenzene sulfonic acid or dextran sulfate sodium.	Trinitrobenzenesulfonic Acid	276-305	heme oxygenase 1	Homo sapiens	57-61
21062534-4	2010	In fact, it has been demonstrated that the activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in various animal intestinal injury models induced by ischemia-reperfusion, indomethacin, lipopolysaccharide-associated sepsis, trinitrobenzene sulfonic acid or dextran sulfate sodium.	Dextran Sulfate	309-331	heme oxygenase 1	Homo sapiens	57-61
21062534-5	2010	In addition, carbon monoxide (CO) derived from HO-1 has been shown to be involved in the regulation of intestinal inflammation.	Carbon Monoxide	13-28	heme oxygenase 1	Homo sapiens	47-51
21062534-5	2010	In addition, carbon monoxide (CO) derived from HO-1 has been shown to be involved in the regulation of intestinal inflammation.	Carbon Monoxide	30-32	heme oxygenase 1	Homo sapiens	47-51
20199188-5	2010	Interestingly, inhibition of HO-1 induction (by zinc protoporphyrin, ZnP) was associated with an accelerated mitogenic response to EGF and HGF in MCs.	pyrithione zinc	69-72	heme oxygenase 1	Homo sapiens	29-33
19781563-0	2010	Ginsenoside Rb1 protects against 6-hydroxydopamine-induced oxidative stress by increasing heme oxygenase-1 expression through an estrogen receptor-related PI3K/Akt/Nrf2-dependent pathway in human dopaminergic cells.	Oxidopamine	33-50	heme oxygenase 1	Homo sapiens	90-106
19781563-5	2010	In this study, we demonstrate that the phytoestrogen Rb1 inhibits 6-hydroxydopamine (6-OHDA)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	Oxidopamine	66-83	heme oxygenase 1	Homo sapiens	158-174
20172305-2	2010	The mechanisms responsible for this effective graft protection against ischemia-reperfusion injury are pivotal actions on generation of nitric oxide a diffusible molecule with vasodilator properties, that facilitates the up-regulation of other well-known cytoprotective genes, such as hypoxia-inducible factor-1 alpha (HIF-1alpha) and heme-oxygenase 1 (HO-1).	Nitric Oxide	136-148	heme oxygenase 1	Homo sapiens	335-351
20172305-2	2010	The mechanisms responsible for this effective graft protection against ischemia-reperfusion injury are pivotal actions on generation of nitric oxide a diffusible molecule with vasodilator properties, that facilitates the up-regulation of other well-known cytoprotective genes, such as hypoxia-inducible factor-1 alpha (HIF-1alpha) and heme-oxygenase 1 (HO-1).	Nitric Oxide	136-148	heme oxygenase 1	Homo sapiens	353-357
19781563-5	2010	In this study, we demonstrate that the phytoestrogen Rb1 inhibits 6-hydroxydopamine (6-OHDA)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	Oxidopamine	85-91	heme oxygenase 1	Homo sapiens	158-174
20172305-3	2010	During normoxic reperfusion, the presence of nitric oxide permits HIF-1alpha accumulation to inhibit prolyl-hydoxylases, thus promoting an additional overexpression of the HO-1 in steatotic and nonsteatotic graft livers preserved in IGL-1.	Nitric Oxide	45-57	heme oxygenase 1	Homo sapiens	172-176
20175232-7	2010	CONCLUSION: DRB and alpha-Amanitin can down-regulate the expression of Nrf2 and its targeting proteins HO-1, AKR1C and NQO1, but may have no effect on the localization of Nrf2.	Alpha-Amanitin	20-34	heme oxygenase 1	Homo sapiens	103-114
20193368-1	2009	OBJECTIVE: To investigate the effects of alpha-zearalanol on the expression of heme oxygenase-1 (HO-1) gene and cytosolic free calcium level in the tumor necrosis factor alpha (TNF-alpha)-stimulated human umbilical vein endothelial cell (HUVEC) and the mechanisms involved.	Zeranol	41-57	heme oxygenase 1	Homo sapiens	79-95
20193368-1	2009	OBJECTIVE: To investigate the effects of alpha-zearalanol on the expression of heme oxygenase-1 (HO-1) gene and cytosolic free calcium level in the tumor necrosis factor alpha (TNF-alpha)-stimulated human umbilical vein endothelial cell (HUVEC) and the mechanisms involved.	Zeranol	41-57	heme oxygenase 1	Homo sapiens	97-101
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	Zeranol	169-185	heme oxygenase 1	Homo sapiens	29-33
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	Zeranol	169-185	heme oxygenase 1	Homo sapiens	144-148
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	Zeranol	169-185	heme oxygenase 1	Homo sapiens	144-148
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	Zeranol	169-185	heme oxygenase 1	Homo sapiens	144-148
20733275-6	2010	In our analysis of 16 cases treated by intravesical administration of anthracyclines, the positive expression of HO-1 correlated with poor disease-free survival (p = 0.015).	Anthracyclines	70-84	heme oxygenase 1	Homo sapiens	113-117
20733275-7	2010	In in vitro experiments using urothelial cancer cell lines, HO-1 upregulation was observed by exposure to doxorubicin.	Doxorubicin	106-117	heme oxygenase 1	Homo sapiens	60-64
20733275-8	2010	Moreover, siRNA-mediated suppression of HO-1 upregulation sensitized the urothelial cancer cells to doxorubicin.	Doxorubicin	100-111	heme oxygenase 1	Homo sapiens	40-44
20733275-9	2010	CONCLUSIONS: Our findings suggested that resistance against anthracyclines correlated with HO-1 and expression analysis of HO-1 may be a useful predictive marker for intravesical administration of anthracyclines.	Anthracyclines	60-74	heme oxygenase 1	Homo sapiens	91-95
20733275-9	2010	CONCLUSIONS: Our findings suggested that resistance against anthracyclines correlated with HO-1 and expression analysis of HO-1 may be a useful predictive marker for intravesical administration of anthracyclines.	Anthracyclines	197-211	heme oxygenase 1	Homo sapiens	123-127
20193368-0	2009	[Effect of alpha-zearalanol upon the expression of HO-1 gene and the cytosolic free calcium level in tumor necrosis factor alpha-stimulated human endothelial cell].	Zeranol	11-27	heme oxygenase 1	Homo sapiens	51-55
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	alpha-zal	270-279	heme oxygenase 1	Homo sapiens	29-33
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	alpha-zal	270-279	heme oxygenase 1	Homo sapiens	144-148
19952508-2	2009	CdCl(2), heme, and diclofenac sodium salt (diclofenac) were used as inducers of HO-1.	Cadmium Chloride	0-7	heme oxygenase 1	Homo sapiens	80-84
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	alpha-zal	270-279	heme oxygenase 1	Homo sapiens	144-148
20193368-8	2009	TNF-alpha stimulation caused HO-1 mRNA increased by 145% of control (0.88 +/- 0.10 vs 0.36 +/- 0.11, P &lt; 0.01), and also obviously increased HO-1 protein expression; alpha-zearalanol inhibited the expression of HO-1 mRNA in a dose-dependent manner; Pretreatment with alpha-ZAL and p47(phox) siRNA both attenuated TNFalpha-induced HO-1 protein expression.	alpha-zal	270-279	heme oxygenase 1	Homo sapiens	144-148
20193368-10	2009	CONCLUSION: ROS only partly mediated HO-1; expression in the TNF-alpha-stimulated HUVEC; alpha-ZAL has a potent inhibitory effect on the HO-1 expression and cytosolic free calcium level in the TNF-alpha-stimulated HUVEC, mainly through the inhibition of ROS generation derived from NADPH oxidase.	ros	12-15	heme oxygenase 1	Homo sapiens	37-41
20193368-10	2009	CONCLUSION: ROS only partly mediated HO-1; expression in the TNF-alpha-stimulated HUVEC; alpha-ZAL has a potent inhibitory effect on the HO-1 expression and cytosolic free calcium level in the TNF-alpha-stimulated HUVEC, mainly through the inhibition of ROS generation derived from NADPH oxidase.	ros	12-15	heme oxygenase 1	Homo sapiens	137-141
20193368-10	2009	CONCLUSION: ROS only partly mediated HO-1; expression in the TNF-alpha-stimulated HUVEC; alpha-ZAL has a potent inhibitory effect on the HO-1 expression and cytosolic free calcium level in the TNF-alpha-stimulated HUVEC, mainly through the inhibition of ROS generation derived from NADPH oxidase.	alpha-zal	89-98	heme oxygenase 1	Homo sapiens	37-41
20193368-10	2009	CONCLUSION: ROS only partly mediated HO-1; expression in the TNF-alpha-stimulated HUVEC; alpha-ZAL has a potent inhibitory effect on the HO-1 expression and cytosolic free calcium level in the TNF-alpha-stimulated HUVEC, mainly through the inhibition of ROS generation derived from NADPH oxidase.	alpha-zal	89-98	heme oxygenase 1	Homo sapiens	137-141
19909254-5	2009	HO-1 (haem oxygenase-1), an anti-inflammatory enzyme, and its metabolite, CO (carbon monoxide), exert protective effects in several organs against oxidative stimuli.	Carbon Monoxide	74-76	heme oxygenase 1	Homo sapiens	0-4
19909254-5	2009	HO-1 (haem oxygenase-1), an anti-inflammatory enzyme, and its metabolite, CO (carbon monoxide), exert protective effects in several organs against oxidative stimuli.	Carbon Monoxide	74-76	heme oxygenase 1	Homo sapiens	6-22
19909254-5	2009	HO-1 (haem oxygenase-1), an anti-inflammatory enzyme, and its metabolite, CO (carbon monoxide), exert protective effects in several organs against oxidative stimuli.	Carbon Monoxide	78-93	heme oxygenase 1	Homo sapiens	0-4
19909254-5	2009	HO-1 (haem oxygenase-1), an anti-inflammatory enzyme, and its metabolite, CO (carbon monoxide), exert protective effects in several organs against oxidative stimuli.	Carbon Monoxide	78-93	heme oxygenase 1	Homo sapiens	6-22
19735655-4	2009	Chemical inhibition of HO-1 with zinc protoporphyrin-IX prevents neuroprotection by MGF24 against the three neurotoxins.	zinc protoporphyrin	33-55	heme oxygenase 1	Homo sapiens	23-27
19961388-0	2009	The anti-inflammatory role of heme oxygenase-1 in lipopolysaccharide and cytokine-stimulated inducible nitric oxide synthase and nitric oxide production in human periodontal ligament cells.	Nitric Oxide	103-115	heme oxygenase 1	Homo sapiens	30-46
19961388-2	2009	Therefore, the aim of this study is to investigate the anti-inflammatory properties of HO-1 in lipopolysaccharide (LPS)- and proinflammatory cytokine-stimulated inducible nitric oxide synthase (iNOS) expression and nitric oxide (NO) production in human periodontal ligament (PDL) cells.	Nitric Oxide	171-183	heme oxygenase 1	Homo sapiens	87-91
20608094-4	2009	Expressions of biopyrrins and heme oxygenase-1 (HO-1), a stress-responsive bilirubin-producing enzyme, in heart, aorta, kidney, liver and lung were immunostained with autopsied specimens.	Bilirubin	75-84	heme oxygenase 1	Homo sapiens	30-46
20608094-4	2009	Expressions of biopyrrins and heme oxygenase-1 (HO-1), a stress-responsive bilirubin-producing enzyme, in heart, aorta, kidney, liver and lung were immunostained with autopsied specimens.	Bilirubin	75-84	heme oxygenase 1	Homo sapiens	48-52
20608094-12	2009	Induction of anti-oxidative enzyme HO-1 seemed to be involved in the activation of bilirubin/biopyrrin pathway.	Bilirubin	83-92	heme oxygenase 1	Homo sapiens	35-39
20608094-12	2009	Induction of anti-oxidative enzyme HO-1 seemed to be involved in the activation of bilirubin/biopyrrin pathway.	biopyrrin	93-102	heme oxygenase 1	Homo sapiens	35-39
19952508-2	2009	CdCl(2), heme, and diclofenac sodium salt (diclofenac) were used as inducers of HO-1.	Diclofenac	19-41	heme oxygenase 1	Homo sapiens	80-84
19952508-2	2009	CdCl(2), heme, and diclofenac sodium salt (diclofenac) were used as inducers of HO-1.	Diclofenac	19-29	heme oxygenase 1	Homo sapiens	80-84
19952508-6	2009	HO-1 levels were increased by CdCl(2) (7.5 microM), heme (10, 100 microM), and stannic mesoporphyrin (SnMP) (10 microM), but were not changed by AAP, and were decreased by diclofenac.	cdcl	30-34	heme oxygenase 1	Homo sapiens	0-4
19952508-6	2009	HO-1 levels were increased by CdCl(2) (7.5 microM), heme (10, 100 microM), and stannic mesoporphyrin (SnMP) (10 microM), but were not changed by AAP, and were decreased by diclofenac.	Heme	52-56	heme oxygenase 1	Homo sapiens	0-4
19952508-6	2009	HO-1 levels were increased by CdCl(2) (7.5 microM), heme (10, 100 microM), and stannic mesoporphyrin (SnMP) (10 microM), but were not changed by AAP, and were decreased by diclofenac.	mesoporphyrin IX	87-100	heme oxygenase 1	Homo sapiens	0-4
19952508-6	2009	HO-1 levels were increased by CdCl(2) (7.5 microM), heme (10, 100 microM), and stannic mesoporphyrin (SnMP) (10 microM), but were not changed by AAP, and were decreased by diclofenac.	tin mesoporphyrin	102-106	heme oxygenase 1	Homo sapiens	0-4
19952508-6	2009	HO-1 levels were increased by CdCl(2) (7.5 microM), heme (10, 100 microM), and stannic mesoporphyrin (SnMP) (10 microM), but were not changed by AAP, and were decreased by diclofenac.	Diclofenac	172-182	heme oxygenase 1	Homo sapiens	0-4
19952508-7	2009	HO-1 levels were increased by diclofenac (300 microM), and CP (36 microM), but were unaffected by AAP because of low sensitivity in HepG2 cells.	Diclofenac	30-40	heme oxygenase 1	Homo sapiens	0-4
19734319-7	2009	Upregulation of HO-1 is not inhibited by Trolox, a non-thiol antioxidant, and does not involve the transcription factors AP-1 or Nrf2.	Sulfhydryl Compounds	55-60	heme oxygenase 1	Homo sapiens	16-20
19797172-10	2009	Transfection of HAECs with mTOR (mammalian target of rapamycin) short hairpin RNA and with Akt2 small interfering RNA significantly inhibited RSG-mediated transcriptional upregulation of heme oxygenase-1, a PPARgamma target gene.	Rosiglitazone	142-145	heme oxygenase 1	Homo sapiens	187-203
19822148-3	2009	CS exposure led to increased HO-1 and nuclear Nrf2 expression (6 h) followed by decreased HO-1 expression concomitantly with nuclear Nrf2/Bach1 ratio decrease (72h).	Cesium	0-2	heme oxygenase 1	Homo sapiens	29-33
19822148-3	2009	CS exposure led to increased HO-1 and nuclear Nrf2 expression (6 h) followed by decreased HO-1 expression concomitantly with nuclear Nrf2/Bach1 ratio decrease (72h).	Cesium	0-2	heme oxygenase 1	Homo sapiens	90-94
19822148-5	2009	Extracellular-signal-regulated kinase(1/2) (ERK(1/2)) and c-Jun NH2-terminal kinase (JNK) inhibition completely abrogated CS effects on HO-1 expression and nuclear Nrf2/Bach1 translocation.	Cesium	122-124	heme oxygenase 1	Homo sapiens	136-140
19822148-6	2009	These results suggest that ERK(1/2) and JNK are involved in CS-induced biphasic HO-1 expression by a specific regulation of Nrf2/Keap1-Bach1.	Cesium	60-62	heme oxygenase 1	Homo sapiens	80-84
19615435-3	2009	Comparison of the in vitro neurotoxicity data with general cytotoxicity data generated in a non-neuronal cell line and with in vivo data such as acute human lethal blood concentration, revealed that GABA(A) receptor function, acetylcholine esterase activity, cell membrane potential, glucose uptake, total RNA expression and altered gene expression of NF-H, GFAP, MBP, HSP32 and caspase-3 were the best endpoints to use for further testing with 36 additional chemicals.	gamma-Aminobutyric Acid	199-203	heme oxygenase 1	Homo sapiens	369-374
19797172-11	2009	Chromatin immunoprecipitation assay demonstrated sirolimus interferes with binding of PPARgamma to its response elements in heme oxygenase-1 promoter.	Sirolimus	49-58	heme oxygenase 1	Homo sapiens	124-140
19734319-0	2009	Peroxisome proliferator-activated receptor-gamma ligands induce heme oxygenase-1 in lung fibroblasts by a PPARgamma-independent, glutathione-dependent mechanism.	Glutathione	129-140	heme oxygenase 1	Homo sapiens	64-80
19734319-4	2009	We report here that the PPARgamma ligands 15d-PGJ2 and 2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid (CDDO), which have potent antifibrotic effects in vitro, also strongly induce HO-1 expression in primary human lung fibroblasts.	15-deoxyprostaglandin J2	42-50	heme oxygenase 1	Homo sapiens	178-182
19734319-10	2009	These data suggest that in human lung fibroblasts, 15d-PGJ2 and CDDO induce HO-1 via a GSH-dependent mechanism involving the formation of covalent bonds between 15d-PGJ2 or CDDO and GSH.	15-deoxyprostaglandin J2	51-59	heme oxygenase 1	Homo sapiens	76-80
19734319-4	2009	We report here that the PPARgamma ligands 15d-PGJ2 and 2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid (CDDO), which have potent antifibrotic effects in vitro, also strongly induce HO-1 expression in primary human lung fibroblasts.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	55-99	heme oxygenase 1	Homo sapiens	178-182
19734319-4	2009	We report here that the PPARgamma ligands 15d-PGJ2 and 2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid (CDDO), which have potent antifibrotic effects in vitro, also strongly induce HO-1 expression in primary human lung fibroblasts.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	101-105	heme oxygenase 1	Homo sapiens	178-182
19734319-6	2009	Upregulation of HO-1 coincides with decreased intracellular glutathione (GSH) levels and can be inhibited by N-acetyl cysteine (NAC), a thiol antioxidant and GSH precursor.	Glutathione	60-71	heme oxygenase 1	Homo sapiens	16-20
19734319-6	2009	Upregulation of HO-1 coincides with decreased intracellular glutathione (GSH) levels and can be inhibited by N-acetyl cysteine (NAC), a thiol antioxidant and GSH precursor.	Glutathione	73-76	heme oxygenase 1	Homo sapiens	16-20
19734319-6	2009	Upregulation of HO-1 coincides with decreased intracellular glutathione (GSH) levels and can be inhibited by N-acetyl cysteine (NAC), a thiol antioxidant and GSH precursor.	Acetylcysteine	109-126	heme oxygenase 1	Homo sapiens	16-20
19734319-6	2009	Upregulation of HO-1 coincides with decreased intracellular glutathione (GSH) levels and can be inhibited by N-acetyl cysteine (NAC), a thiol antioxidant and GSH precursor.	Acetylcysteine	128-131	heme oxygenase 1	Homo sapiens	16-20
19734319-6	2009	Upregulation of HO-1 coincides with decreased intracellular glutathione (GSH) levels and can be inhibited by N-acetyl cysteine (NAC), a thiol antioxidant and GSH precursor.	Sulfhydryl Compounds	136-141	heme oxygenase 1	Homo sapiens	16-20
19734319-6	2009	Upregulation of HO-1 coincides with decreased intracellular glutathione (GSH) levels and can be inhibited by N-acetyl cysteine (NAC), a thiol antioxidant and GSH precursor.	Glutathione	158-161	heme oxygenase 1	Homo sapiens	16-20
19734319-10	2009	These data suggest that in human lung fibroblasts, 15d-PGJ2 and CDDO induce HO-1 via a GSH-dependent mechanism involving the formation of covalent bonds between 15d-PGJ2 or CDDO and GSH.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	64-68	heme oxygenase 1	Homo sapiens	76-80
19734319-10	2009	These data suggest that in human lung fibroblasts, 15d-PGJ2 and CDDO induce HO-1 via a GSH-dependent mechanism involving the formation of covalent bonds between 15d-PGJ2 or CDDO and GSH.	Glutathione	87-90	heme oxygenase 1	Homo sapiens	76-80
19734319-10	2009	These data suggest that in human lung fibroblasts, 15d-PGJ2 and CDDO induce HO-1 via a GSH-dependent mechanism involving the formation of covalent bonds between 15d-PGJ2 or CDDO and GSH.	15-deoxyprostaglandin J2	161-169	heme oxygenase 1	Homo sapiens	76-80
19734319-10	2009	These data suggest that in human lung fibroblasts, 15d-PGJ2 and CDDO induce HO-1 via a GSH-dependent mechanism involving the formation of covalent bonds between 15d-PGJ2 or CDDO and GSH.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	173-177	heme oxygenase 1	Homo sapiens	76-80
19734319-10	2009	These data suggest that in human lung fibroblasts, 15d-PGJ2 and CDDO induce HO-1 via a GSH-dependent mechanism involving the formation of covalent bonds between 15d-PGJ2 or CDDO and GSH.	Glutathione	182-185	heme oxygenase 1	Homo sapiens	76-80
19734319-11	2009	Inhibiting HO-1 upregulation with NAC has only a small effect on the antifibrotic properties of 15d-PGJ2 and CDDO in vitro.	Acetylcysteine	34-37	heme oxygenase 1	Homo sapiens	11-15
19734319-11	2009	Inhibiting HO-1 upregulation with NAC has only a small effect on the antifibrotic properties of 15d-PGJ2 and CDDO in vitro.	15-deoxyprostaglandin J2	96-104	heme oxygenase 1	Homo sapiens	11-15
19734319-11	2009	Inhibiting HO-1 upregulation with NAC has only a small effect on the antifibrotic properties of 15d-PGJ2 and CDDO in vitro.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	109-113	heme oxygenase 1	Homo sapiens	11-15
19729077-3	2009	MATERIALS AND METHODS: Western blotting was used to examine the effect of apigenin (10-40 microM) on the LPS- and nicotine-induced expression of cyclooxygenase-2 (COX-2), inducible nitric oxide synthase (iNOS), and heme oxygenase-1 (HO-1), as well as the phosphorylation of mitogen-activated protein kinases (MAPKs), in hPDL cells.	Nicotine	114-122	heme oxygenase 1	Homo sapiens	215-231
19397697-10	2009	Induction of HMOX-1 expression by pantothenol and pantothenic acid in dermal cells was confirmed on the protein level using immunoblots.	dexpanthenol	34-45	heme oxygenase 1	Homo sapiens	13-19
19397697-10	2009	Induction of HMOX-1 expression by pantothenol and pantothenic acid in dermal cells was confirmed on the protein level using immunoblots.	Pantothenic Acid	50-66	heme oxygenase 1	Homo sapiens	13-19
19729077-3	2009	MATERIALS AND METHODS: Western blotting was used to examine the effect of apigenin (10-40 microM) on the LPS- and nicotine-induced expression of cyclooxygenase-2 (COX-2), inducible nitric oxide synthase (iNOS), and heme oxygenase-1 (HO-1), as well as the phosphorylation of mitogen-activated protein kinases (MAPKs), in hPDL cells.	Nicotine	114-122	heme oxygenase 1	Homo sapiens	233-237
19729077-0	2009	Anti-inflammatory effects of apigenin on nicotine- and lipopolysaccharide-stimulated human periodontal ligament cells via heme oxygenase-1.	Apigenin	29-37	heme oxygenase 1	Homo sapiens	122-138
19729077-5	2009	RESULTS: Incubation of hPDL cells with apigenin decreased LPS- and nicotine-induced HO-1 protein expression and activity.	Nicotine	67-75	heme oxygenase 1	Homo sapiens	84-88
19729077-7	2009	Hemin, a selective HO-1 inducer, reversed the apigenin-mediated suppression of nicotine- and LPS-induced NO, PGE2 and cytokine production.	Nicotine	79-87	heme oxygenase 1	Homo sapiens	19-23
19536150-2	2009	We showed by real-time PCR, western blotting, and ELISA that HO-1 mRNA and protein expression by cultured normal human keratinocytes was upregulated during epidermal differentiation induced by a high-calcium medium.	Calcium	200-207	heme oxygenase 1	Homo sapiens	61-65
19903769-3	2009	Heme oxygenase 1 (HO-1), the inducible isoform of the rate-limiting enzyme in heme degradation, counteracts oxidative and inflammatory damage.	Heme	78-82	heme oxygenase 1	Homo sapiens	0-16
19903769-3	2009	Heme oxygenase 1 (HO-1), the inducible isoform of the rate-limiting enzyme in heme degradation, counteracts oxidative and inflammatory damage.	Heme	78-82	heme oxygenase 1	Homo sapiens	18-22
19903769-7	2009	Hemin treatment increased HO-1 at both protein and mRNA levels in all cell lines and decreased cell proliferation and invasion.	Hemin	0-5	heme oxygenase 1	Homo sapiens	26-30
19625608-0	2009	Hypochlorous acid-induced heme oxygenase-1 gene expression promotes human endothelial cell survival.	Hypochlorous Acid	0-17	heme oxygenase 1	Homo sapiens	26-42
19679656-4	2009	Elevations in mRNA and protein levels of HIF-dependent genes heme oxygenase-1 (Ho-1) and manganese superoxide dismutase (Mnsod) following DHB pretreatment alone are also maintained in the presence of MPTP.	3,4-dihydroxybenzoate	138-141	heme oxygenase 1	Homo sapiens	61-77
19679656-4	2009	Elevations in mRNA and protein levels of HIF-dependent genes heme oxygenase-1 (Ho-1) and manganese superoxide dismutase (Mnsod) following DHB pretreatment alone are also maintained in the presence of MPTP.	3,4-dihydroxybenzoate	138-141	heme oxygenase 1	Homo sapiens	79-83
19679656-4	2009	Elevations in mRNA and protein levels of HIF-dependent genes heme oxygenase-1 (Ho-1) and manganese superoxide dismutase (Mnsod) following DHB pretreatment alone are also maintained in the presence of MPTP.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	200-204	heme oxygenase 1	Homo sapiens	61-77
19679656-4	2009	Elevations in mRNA and protein levels of HIF-dependent genes heme oxygenase-1 (Ho-1) and manganese superoxide dismutase (Mnsod) following DHB pretreatment alone are also maintained in the presence of MPTP.	1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine	200-204	heme oxygenase 1	Homo sapiens	79-83
19686725-0	2009	Synergistic induction of heme oxygenase-1 by nicaraven after subarachnoid hemorrhage to prevent delayed cerebral vasospasm.	nicaraven	45-54	heme oxygenase 1	Homo sapiens	25-41
19686725-7	2009	Antisense HO-1 oligodeoxynucleotides abrogated this HO-1 induction and the antivasospastic effect of nicaraven.	nicaraven	101-110	heme oxygenase 1	Homo sapiens	10-14
19686725-8	2009	In vitro study using Hela cells, nicaraven enhanced the human HO-1 promoter (-4.5 kbp) activity, which was pre-activated with the blood component oxyhemoglobin to mimic the ability of subarachnoid hemorrhage.	nicaraven	33-42	heme oxygenase 1	Homo sapiens	62-66
19686725-9	2009	These results suggest that this enhanced HO-1 expression through a combination of pathological state and pharmacological agent could be an effective strategy to improve the prognosis of heme- and oxidative stress-induced diseases, such as delayed cerebral vasospasm.	Heme	186-190	heme oxygenase 1	Homo sapiens	41-45
19625608-3	2009	Treatment of human endothelial cells with the myeloperoxidase product HOCl stimulated a concentration- and time-dependent increase in HO-1 protein that resulted in a significant rise in carbon monoxide (CO) production.	Carbon Monoxide	186-201	heme oxygenase 1	Homo sapiens	134-138
19625608-3	2009	Treatment of human endothelial cells with the myeloperoxidase product HOCl stimulated a concentration- and time-dependent increase in HO-1 protein that resulted in a significant rise in carbon monoxide (CO) production.	Carbon Monoxide	203-205	heme oxygenase 1	Homo sapiens	134-138
19625608-5	2009	In addition, HOCl induced a significant rise in HO-1 promoter activity that was blocked by mutating the antioxidant response element (ARE) in the promoter or by overexpressing a dominant-negative mutant of Nrf2.	Hypochlorous Acid	13-17	heme oxygenase 1	Homo sapiens	48-52
19625608-6	2009	The HOCl-mediated induction of Nrf2 or HO-1 was blocked by the glutathione donor N-acetyl-l-cysteine but was unaffected by ascorbic or uric acid.	Hypochlorous Acid	4-8	heme oxygenase 1	Homo sapiens	39-43
19625608-6	2009	The HOCl-mediated induction of Nrf2 or HO-1 was blocked by the glutathione donor N-acetyl-l-cysteine but was unaffected by ascorbic or uric acid.	Glutathione	63-74	heme oxygenase 1	Homo sapiens	39-43
19625608-6	2009	The HOCl-mediated induction of Nrf2 or HO-1 was blocked by the glutathione donor N-acetyl-l-cysteine but was unaffected by ascorbic or uric acid.	Acetylcysteine	81-100	heme oxygenase 1	Homo sapiens	39-43
19625608-7	2009	Finally, treatment of endothelial cells with HOCl stimulated mitochondrial dysfunction, caspase-3 activation, and cell death that was potentiated by the HO inhibitor, tin protoporphyrin-IX, or by the knockdown of HO-1, and reversed by the exogenous administration of biliverdin, bilirubin, or CO.	Hypochlorous Acid	45-49	heme oxygenase 1	Homo sapiens	213-217
19625608-7	2009	Finally, treatment of endothelial cells with HOCl stimulated mitochondrial dysfunction, caspase-3 activation, and cell death that was potentiated by the HO inhibitor, tin protoporphyrin-IX, or by the knockdown of HO-1, and reversed by the exogenous administration of biliverdin, bilirubin, or CO.	Biliverdine	267-277	heme oxygenase 1	Homo sapiens	213-217
19625608-7	2009	Finally, treatment of endothelial cells with HOCl stimulated mitochondrial dysfunction, caspase-3 activation, and cell death that was potentiated by the HO inhibitor, tin protoporphyrin-IX, or by the knockdown of HO-1, and reversed by the exogenous administration of biliverdin, bilirubin, or CO.	Bilirubin	279-288	heme oxygenase 1	Homo sapiens	213-217
19625608-8	2009	These results demonstrate that HOCl induces HO-1 gene transcription via the activation of the Nrf2/ARE pathway to counteract HOCl-mediated mitochondrial dysfunction and cell death.	Hypochlorous Acid	31-35	heme oxygenase 1	Homo sapiens	44-48
19625608-8	2009	These results demonstrate that HOCl induces HO-1 gene transcription via the activation of the Nrf2/ARE pathway to counteract HOCl-mediated mitochondrial dysfunction and cell death.	Hypochlorous Acid	125-129	heme oxygenase 1	Homo sapiens	44-48
19625608-9	2009	The ability of HOCl to activate HO-1 gene expression may represent a critical adaptive response to maintain endothelial cell viability at sites of vascular inflammation and atherosclerosis.	Hypochlorous Acid	15-19	heme oxygenase 1	Homo sapiens	32-36
19576919-0	2009	Methamphetamine induces heme oxygenase-1 expression in cortical neurons and glia to prevent its toxicity.	Methamphetamine	0-15	heme oxygenase 1	Homo sapiens	24-40
19576919-3	2009	We used primary cortical neuron/glia cocultures to explore the role of HO-1 in METH-induced toxicity.	Methamphetamine	79-83	heme oxygenase 1	Homo sapiens	71-75
19576919-8	2009	Inhibition of the p38 mitogen-activated protein kinase pathway significantly blocked HO-1 induction by METH and aggravated METH neurotoxicity.	Methamphetamine	103-107	heme oxygenase 1	Homo sapiens	85-89
19576919-10	2009	However, prior induction of HO-1 using cobalt protoporphyrine IX partially protected neurons from METH toxicity.	cobalt protoporphyrine ix	39-64	heme oxygenase 1	Homo sapiens	28-32
19576919-10	2009	However, prior induction of HO-1 using cobalt protoporphyrine IX partially protected neurons from METH toxicity.	Methamphetamine	98-102	heme oxygenase 1	Homo sapiens	28-32
19576919-11	2009	Taken together, our results suggest that induction of HO-1 by METH via the p38 signaling pathway may be protective, albeit insufficient to completely protect cortical neurons from METH toxicity.	Methamphetamine	62-66	heme oxygenase 1	Homo sapiens	54-58
19683516-6	2009	Depletion of glutathione in the cells or loading the cells with ascorbate greatly increased heme oxygenase-1 induction in the presence of copper.	Glutathione	13-24	heme oxygenase 1	Homo sapiens	92-108
19683516-6	2009	Depletion of glutathione in the cells or loading the cells with ascorbate greatly increased heme oxygenase-1 induction in the presence of copper.	Ascorbic Acid	64-73	heme oxygenase 1	Homo sapiens	92-108
19683516-6	2009	Depletion of glutathione in the cells or loading the cells with ascorbate greatly increased heme oxygenase-1 induction in the presence of copper.	Copper	138-144	heme oxygenase 1	Homo sapiens	92-108
19855245-14	2009	Moreover, treatment with TAK-779 (a) decreased alloantigen-specific T-lymphocyte proliferation and number of IFN-gamma producing cells and (b) increased HO-1 gene transcript level in the allografts.	TAK 779	25-32	heme oxygenase 1	Homo sapiens	153-157
19855245-17	2009	The beneficial effects of TAK-779 may be because of (a) reduction in CCR5 and CXCR3 T-lymphocyte subset infiltration into the graft, (b) attenuation of alloantigen-specific T-lymphocyte proliferative response and IFN-gamma production, and (c) induction of HO-1 gene.	TAK 779	26-33	heme oxygenase 1	Homo sapiens	256-260
19808972-6	2009	The effect of ho-1 silencing on these oncogenic features was mimicked by exposure of cells to a novel selective small-molecule HO-1 inhibitor referred to as OB-24.	OB-24 HCl	157-162	heme oxygenase 1	Homo sapiens	14-18
19808972-6	2009	The effect of ho-1 silencing on these oncogenic features was mimicked by exposure of cells to a novel selective small-molecule HO-1 inhibitor referred to as OB-24.	OB-24 HCl	157-162	heme oxygenase 1	Homo sapiens	127-131
19808972-7	2009	OB-24 selectively inhibited HO-1 activity in PCA cells, which correlated with a reduction of protein carbonylation and reactive oxygen species formation.	OB-24 HCl	0-5	heme oxygenase 1	Homo sapiens	28-32
19625608-3	2009	Treatment of human endothelial cells with the myeloperoxidase product HOCl stimulated a concentration- and time-dependent increase in HO-1 protein that resulted in a significant rise in carbon monoxide (CO) production.	Hypochlorous Acid	70-74	heme oxygenase 1	Homo sapiens	134-138
19602432-2	2009	Silica nanoparticles-induced oxidative stress was assessed by examining the formation of reactive oxygen species (ROS) and induction of antioxidant enzymes, such as superoxide dismutase (SOD) and heme oxygenase-1 (HO-1).	Silicon Dioxide	0-6	heme oxygenase 1	Homo sapiens	196-212
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Carbon Monoxide	102-117	heme oxygenase 1	Homo sapiens	18-22
19874266-5	2009	Induction of the astroglial ho-1 gene may constitute a "common pathway" leading to pathological brain iron deposition, intracellular oxidative damage and bioenergetic failure in AD and other human CNS disorders.	Iron	102-106	heme oxygenase 1	Homo sapiens	28-32
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Heme	68-72	heme oxygenase 1	Homo sapiens	0-16
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Heme	68-72	heme oxygenase 1	Homo sapiens	18-22
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Biliverdine	76-86	heme oxygenase 1	Homo sapiens	0-16
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Biliverdine	76-86	heme oxygenase 1	Homo sapiens	18-22
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Iron	93-97	heme oxygenase 1	Homo sapiens	0-16
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Iron	93-97	heme oxygenase 1	Homo sapiens	18-22
19874266-2	2009	Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide.	Carbon Monoxide	102-117	heme oxygenase 1	Homo sapiens	0-16
19364390-8	2009	Sublethal concentrations of arecoline upregulated the expression of the following stress-responsive genes: heme oxygenase-1; ferritin light chain; glucose-6-phosphate dehydrogenase; glutamate-cysteine ligase catalytic subunit; and glutathione reductase.	Arecoline	28-37	heme oxygenase 1	Homo sapiens	107-123
19602432-2	2009	Silica nanoparticles-induced oxidative stress was assessed by examining the formation of reactive oxygen species (ROS) and induction of antioxidant enzymes, such as superoxide dismutase (SOD) and heme oxygenase-1 (HO-1).	Silicon Dioxide	0-6	heme oxygenase 1	Homo sapiens	214-218
19602432-4	2009	From the overall results, silica nanoparticles exerted toxicity via oxidative stress, which lead to the induction of HO-1 via the Nrf-2-ERK MAP kinase signaling pathway; cells exposed to porous silica nanoparticles showed a more sensitive response than those exposed to fumed silica.	Silicon Dioxide	26-32	heme oxygenase 1	Homo sapiens	117-121
19602432-4	2009	From the overall results, silica nanoparticles exerted toxicity via oxidative stress, which lead to the induction of HO-1 via the Nrf-2-ERK MAP kinase signaling pathway; cells exposed to porous silica nanoparticles showed a more sensitive response than those exposed to fumed silica.	Silicon Dioxide	194-200	heme oxygenase 1	Homo sapiens	117-121
19602432-4	2009	From the overall results, silica nanoparticles exerted toxicity via oxidative stress, which lead to the induction of HO-1 via the Nrf-2-ERK MAP kinase signaling pathway; cells exposed to porous silica nanoparticles showed a more sensitive response than those exposed to fumed silica.	Silicon Dioxide	194-200	heme oxygenase 1	Homo sapiens	117-121
19777608-0	2009	Iron increases HMOX1 and decreases hepatitis C viral expression in HCV-expressing cells.	Iron	0-4	heme oxygenase 1	Homo sapiens	15-20
19540194-5	2009	C18-DOM increased the expression of anti-atherogenic molecule namely heme oxygenase-1 in endothelial cells and all these data showed that C18-DOM is exhibiting aspirin-like effects.	Aspirin	160-167	heme oxygenase 1	Homo sapiens	69-85
19617398-1	2009	Heme oxygenase-1 (HO-1), a ubiquitous inducible stress-response protein, serves a major metabolic function in heme turnover.	Heme	110-114	heme oxygenase 1	Homo sapiens	0-16
19617398-1	2009	Heme oxygenase-1 (HO-1), a ubiquitous inducible stress-response protein, serves a major metabolic function in heme turnover.	Heme	110-114	heme oxygenase 1	Homo sapiens	18-22
19694439-2	2009	In humans, heme oxygenase-1 (hHO-1) is overexpressed in tumor tissues, where it helps to protect cancer cells from anticancer agents, while HOs in fungal pathogens, such as Candida albicans, function as the primary means of iron acquisition.	Iron	224-228	heme oxygenase 1	Homo sapiens	11-27
19694439-2	2009	In humans, heme oxygenase-1 (hHO-1) is overexpressed in tumor tissues, where it helps to protect cancer cells from anticancer agents, while HOs in fungal pathogens, such as Candida albicans, function as the primary means of iron acquisition.	Iron	224-228	heme oxygenase 1	Homo sapiens	29-34
19694439-4	2009	In this study, we have examined the equilibrium binding of three isocyanides, isopropyl, n-butyl, and benzyl, to the two major human HO isoforms (hHO-1 and hHO-2), Candida albicans HO (CaHmx1), and human cytochrome P450 CYP3A4 using electronic absorption spectroscopy.	Cyanides	65-76	heme oxygenase 1	Homo sapiens	146-151
19694439-7	2009	Because the dissociation constants (KD) of the ligands for ferrous heme-hHO-1 were below the limit of accuracy for equilibrium titrations, stopped-flow kinetic experiments were used to measure the binding parameters of the isocyanides to ferrous hHO-1.	Cyanides	223-234	heme oxygenase 1	Homo sapiens	72-77
19694439-7	2009	Because the dissociation constants (KD) of the ligands for ferrous heme-hHO-1 were below the limit of accuracy for equilibrium titrations, stopped-flow kinetic experiments were used to measure the binding parameters of the isocyanides to ferrous hHO-1.	Cyanides	223-234	heme oxygenase 1	Homo sapiens	246-251
19694439-8	2009	Steady-state activity assays showed that benzyl isocyanide was the most potent uncompetitive inhibitor with respect to heme with a KI = 0.15 microM for hHO-1.	Benzyl isocyanide	41-58	heme oxygenase 1	Homo sapiens	152-157
19694439-8	2009	Steady-state activity assays showed that benzyl isocyanide was the most potent uncompetitive inhibitor with respect to heme with a KI = 0.15 microM for hHO-1.	Heme	119-123	heme oxygenase 1	Homo sapiens	152-157
19761582-13	2009	Ag-np induced stress resulted in the up regulation of metallothionein and heme oxygenase -1 genes.	ag-np	0-5	heme oxygenase 1	Homo sapiens	74-91
19563780-2	2009	We identified the protein kinase C delta (PKCdelta) inhibitor rottlerin as the only compound that reduced NO-induced ARE-luciferase reporter activity and diminished NO-induced up-regulation of two Nrf2/ARE-regulated proteins - NAD(P)H:quinone oxidoreductase-1 (NQO1) and hemeoxygenase-1 (HO-1) in SH-Sy5y cells.	rottlerin	62-71	heme oxygenase 1	Homo sapiens	271-292
19570893-0	2009	Membrane depolarization induces calcium-dependent upregulation of Hsp70 and Hmox-1 in skeletal muscle cells.	Calcium	32-39	heme oxygenase 1	Homo sapiens	76-82
19570893-4	2009	The aim of this work was to investigate the involvement of calcium in Hsp70 and Hmox-1 expression upon depolarization of skeletal muscle cells.	Calcium	59-66	heme oxygenase 1	Homo sapiens	80-86
19570893-8	2009	Here we demonstrated that inhibition of IP(3)-dependent calcium signals decreased both Hsp70 mRNA induction and Hsp70 and Hmox-1 protein expression.	Inositol 1,4,5-Trisphosphate	40-45	heme oxygenase 1	Homo sapiens	122-128
19570893-8	2009	Here we demonstrated that inhibition of IP(3)-dependent calcium signals decreased both Hsp70 mRNA induction and Hsp70 and Hmox-1 protein expression.	Calcium	56-63	heme oxygenase 1	Homo sapiens	122-128
19681826-7	2009	HO-1 inhibition by the specific inhibitor, SnPP, completely abolished T-cell suppression and IL-10 production.	S-Nitroso-N-propionyl-D,L-penicillamine	43-47	heme oxygenase 1	Homo sapiens	0-4
19777608-4	2009	RESULTS: Iron, in the form of ferric nitrilotriacetate, increased oxidative stress and up-regulated HMOX1 gene expression.	Iron	9-13	heme oxygenase 1	Homo sapiens	100-105
19777608-4	2009	RESULTS: Iron, in the form of ferric nitrilotriacetate, increased oxidative stress and up-regulated HMOX1 gene expression.	ferric nitrilotriacetate	30-54	heme oxygenase 1	Homo sapiens	100-105
19777608-6	2009	Silencing the up-regulation of HMOX1 nuclear factor-erythroid 2-related factor 2 (Nrf2) by Nrf2-siRNA decreased FeNTA-mediated up-regulation of HMOX1 mRNA levels.	ferric nitrilotriacetate	112-117	heme oxygenase 1	Homo sapiens	31-36
19777608-6	2009	Silencing the up-regulation of HMOX1 nuclear factor-erythroid 2-related factor 2 (Nrf2) by Nrf2-siRNA decreased FeNTA-mediated up-regulation of HMOX1 mRNA levels.	ferric nitrilotriacetate	112-117	heme oxygenase 1	Homo sapiens	144-149
19777608-9	2009	CONCLUSION: Excess iron up-regulates HMOX1 and down-regulates HCV gene expression in hepatoma cells.	Iron	19-23	heme oxygenase 1	Homo sapiens	37-42
18774956-1	2009	Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism.	Iron	40-44	heme oxygenase 1	Homo sapiens	0-16
18774956-1	2009	Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism.	Iron	40-44	heme oxygenase 1	Homo sapiens	18-22
18774956-1	2009	Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism.	Iron	101-105	heme oxygenase 1	Homo sapiens	0-16
18774956-1	2009	Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism.	Iron	101-105	heme oxygenase 1	Homo sapiens	18-22
18774956-1	2009	Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism.	Iron	101-105	heme oxygenase 1	Homo sapiens	0-16
18774956-1	2009	Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism.	Iron	101-105	heme oxygenase 1	Homo sapiens	18-22
18774956-4	2009	Here we postulated that HO-1 is critical in the regulation of ferroportin, the major cellular iron exporter, and hepcidin, the key regulator of iron homeostasis central in the pathogenesis of anemia of inflammation.	Iron	94-98	heme oxygenase 1	Homo sapiens	24-28
18774956-4	2009	Here we postulated that HO-1 is critical in the regulation of ferroportin, the major cellular iron exporter, and hepcidin, the key regulator of iron homeostasis central in the pathogenesis of anemia of inflammation.	Iron	144-148	heme oxygenase 1	Homo sapiens	24-28
18774956-5	2009	Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling.	Iron	79-83	heme oxygenase 1	Homo sapiens	66-70
18774956-5	2009	Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling.	Iron	79-83	heme oxygenase 1	Homo sapiens	153-157
18774956-5	2009	Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling.	Iron	161-165	heme oxygenase 1	Homo sapiens	66-70
18774956-5	2009	Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling.	Iron	161-165	heme oxygenase 1	Homo sapiens	153-157
18774956-12	2009	This study therefore shows a crucial role for HO-1 in maintaining body iron balance.	Iron	71-75	heme oxygenase 1	Homo sapiens	46-50
19794918-7	2009	The amount of heme oxygenase-1 (HO-1) protein in the intestinal mucosa was significantly increased by lansoprazole, but not by omeprazole.	Lansoprazole	102-114	heme oxygenase 1	Homo sapiens	14-30
19556236-1	2009	Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin.	Heme	245-249	heme oxygenase 1	Homo sapiens	0-16
19794918-7	2009	The amount of heme oxygenase-1 (HO-1) protein in the intestinal mucosa was significantly increased by lansoprazole, but not by omeprazole.	Lansoprazole	102-114	heme oxygenase 1	Homo sapiens	32-36
19794918-8	2009	These results suggest that lansoprazole, but not omeprazole, ameliorates indomethacin-induced small intestinal ulceration through upregulation of HO-1/carbon monoxide.	Lansoprazole	27-39	heme oxygenase 1	Homo sapiens	146-150
19653226-0	2009	Protective effect of sulforaphane on indomethacin-induced cytotoxicity via heme oxygenase-1 expression in human intestinal Int 407 cells.	sulforaphane	21-33	heme oxygenase 1	Homo sapiens	75-91
19653226-0	2009	Protective effect of sulforaphane on indomethacin-induced cytotoxicity via heme oxygenase-1 expression in human intestinal Int 407 cells.	Indomethacin	37-49	heme oxygenase 1	Homo sapiens	75-91
19653226-2	2009	In the present study, we investigated the effect of sulforaphane on the expression of heme oxygenase-1 (HO-1) in human intestinal Int 407 cells.	sulforaphane	52-64	heme oxygenase 1	Homo sapiens	86-102
19653226-2	2009	In the present study, we investigated the effect of sulforaphane on the expression of heme oxygenase-1 (HO-1) in human intestinal Int 407 cells.	sulforaphane	52-64	heme oxygenase 1	Homo sapiens	104-108
19653226-3	2009	RT-PCR and Western blot data revealed that sulforaphane induced an increase in HO-1 expression at the mRNA and protein levels, respectively.	sulforaphane	43-55	heme oxygenase 1	Homo sapiens	79-83
19653226-5	2009	Actinomycin D (an RNA synthesis inhibitor) and cycloheximide (a protein synthesis inhibitor) inhibited sulforaphane-responsive HO-1 mRNA expression, indicating that sulforaphane is a requirement for transcription and de novo protein synthesis.	Dactinomycin	0-13	heme oxygenase 1	Homo sapiens	127-131
19653226-5	2009	Actinomycin D (an RNA synthesis inhibitor) and cycloheximide (a protein synthesis inhibitor) inhibited sulforaphane-responsive HO-1 mRNA expression, indicating that sulforaphane is a requirement for transcription and de novo protein synthesis.	Cycloheximide	47-60	heme oxygenase 1	Homo sapiens	127-131
19653226-5	2009	Actinomycin D (an RNA synthesis inhibitor) and cycloheximide (a protein synthesis inhibitor) inhibited sulforaphane-responsive HO-1 mRNA expression, indicating that sulforaphane is a requirement for transcription and de novo protein synthesis.	sulforaphane	103-115	heme oxygenase 1	Homo sapiens	127-131
19653226-5	2009	Actinomycin D (an RNA synthesis inhibitor) and cycloheximide (a protein synthesis inhibitor) inhibited sulforaphane-responsive HO-1 mRNA expression, indicating that sulforaphane is a requirement for transcription and de novo protein synthesis.	sulforaphane	165-177	heme oxygenase 1	Homo sapiens	127-131
19653226-7	2009	We also found that U0126, an ERK kinase inhibitor, suppressed the sulforaphane-induced HO-1 expression and nuclear translocation of Nrf2.	U 0126	19-24	heme oxygenase 1	Homo sapiens	87-91
19653226-7	2009	We also found that U0126, an ERK kinase inhibitor, suppressed the sulforaphane-induced HO-1 expression and nuclear translocation of Nrf2.	sulforaphane	66-78	heme oxygenase 1	Homo sapiens	87-91
19653226-8	2009	Moreover, the cytoprotective effect of sulforaphane on indomethancin-induced cytotoxicity was partially blocked by ERK and HO-1 inhibitors, further demonstrating that sulforaphane attenuated oxidative stress through a pathway that involved ERK and HO-1.	sulforaphane	39-51	heme oxygenase 1	Homo sapiens	123-127
19653226-8	2009	Moreover, the cytoprotective effect of sulforaphane on indomethancin-induced cytotoxicity was partially blocked by ERK and HO-1 inhibitors, further demonstrating that sulforaphane attenuated oxidative stress through a pathway that involved ERK and HO-1.	sulforaphane	39-51	heme oxygenase 1	Homo sapiens	248-252
19653226-8	2009	Moreover, the cytoprotective effect of sulforaphane on indomethancin-induced cytotoxicity was partially blocked by ERK and HO-1 inhibitors, further demonstrating that sulforaphane attenuated oxidative stress through a pathway that involved ERK and HO-1.	Indomethacin	55-68	heme oxygenase 1	Homo sapiens	123-127
19653226-8	2009	Moreover, the cytoprotective effect of sulforaphane on indomethancin-induced cytotoxicity was partially blocked by ERK and HO-1 inhibitors, further demonstrating that sulforaphane attenuated oxidative stress through a pathway that involved ERK and HO-1.	Indomethacin	55-68	heme oxygenase 1	Homo sapiens	248-252
19653226-8	2009	Moreover, the cytoprotective effect of sulforaphane on indomethancin-induced cytotoxicity was partially blocked by ERK and HO-1 inhibitors, further demonstrating that sulforaphane attenuated oxidative stress through a pathway that involved ERK and HO-1.	sulforaphane	167-179	heme oxygenase 1	Homo sapiens	123-127
19653226-8	2009	Moreover, the cytoprotective effect of sulforaphane on indomethancin-induced cytotoxicity was partially blocked by ERK and HO-1 inhibitors, further demonstrating that sulforaphane attenuated oxidative stress through a pathway that involved ERK and HO-1.	sulforaphane	167-179	heme oxygenase 1	Homo sapiens	248-252
19556236-1	2009	Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin.	Biliverdine	212-222	heme oxygenase 1	Homo sapiens	0-16
19556236-1	2009	Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin.	Biliverdine	212-222	heme oxygenase 1	Homo sapiens	18-22
19556236-1	2009	Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin.	Bilirubin	296-305	heme oxygenase 1	Homo sapiens	0-16
19556236-1	2009	Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin.	Bilirubin	296-305	heme oxygenase 1	Homo sapiens	18-22
19556236-1	2009	Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin.	Heme	245-249	heme oxygenase 1	Homo sapiens	18-22
19608869-3	2009	In this study, we report that HO-1 was induced in cultured human tracheal smooth muscle cells after either treatment with a potent inducer of HO-1 activity, cobalt protoporphyrin IX, or infection with a recombinant adenovirus that carries the human HO-1 gene.	cobaltiprotoporphyrin	157-181	heme oxygenase 1	Homo sapiens	30-34
19781175-1	2009	OBJECTIVE: To study the protective effect of islet xenograft and its possible mechanism of high expression of heme oxygenase-1 (HO-1) in donor pancreas islet induced by cobalt protoporphyrin (CoPP).	cobaltiprotoporphyrin	169-190	heme oxygenase 1	Homo sapiens	110-126
19781175-1	2009	OBJECTIVE: To study the protective effect of islet xenograft and its possible mechanism of high expression of heme oxygenase-1 (HO-1) in donor pancreas islet induced by cobalt protoporphyrin (CoPP).	cobaltiprotoporphyrin	169-190	heme oxygenase 1	Homo sapiens	128-132
19781175-1	2009	OBJECTIVE: To study the protective effect of islet xenograft and its possible mechanism of high expression of heme oxygenase-1 (HO-1) in donor pancreas islet induced by cobalt protoporphyrin (CoPP).	cobaltiprotoporphyrin	192-196	heme oxygenase 1	Homo sapiens	110-126
19781175-1	2009	OBJECTIVE: To study the protective effect of islet xenograft and its possible mechanism of high expression of heme oxygenase-1 (HO-1) in donor pancreas islet induced by cobalt protoporphyrin (CoPP).	cobaltiprotoporphyrin	192-196	heme oxygenase 1	Homo sapiens	128-132
19534727-0	2009	Human haem oxygenase-1 induction by nitro-linoleic acid is mediated by cAMP, AP-1 and E-box response element interactions.	10-nitro-9,12-octadecadienoic acid	36-55	heme oxygenase 1	Homo sapiens	6-22
19534727-0	2009	Human haem oxygenase-1 induction by nitro-linoleic acid is mediated by cAMP, AP-1 and E-box response element interactions.	Cyclic AMP	71-75	heme oxygenase 1	Homo sapiens	6-22
19534727-2	2009	LNO2 (nitrolinoleic acid) induces expression of HO-1 (haem oxygenase-1), an enzyme that catabolizes haem into products exhibiting potent anti-inflammatory properties.	10-Nitrolinoleic acid	0-4	heme oxygenase 1	Homo sapiens	48-70
19534727-2	2009	LNO2 (nitrolinoleic acid) induces expression of HO-1 (haem oxygenase-1), an enzyme that catabolizes haem into products exhibiting potent anti-inflammatory properties.	10-nitro-9,12-octadecadienoic acid	6-24	heme oxygenase 1	Homo sapiens	48-70
19534727-6	2009	Site-directed mutagenesis of a CRE (cAMP-response element) or of a downstream NF-E2/AP-1 (activating protein-1) element, individually, within this 500 bp region modestly reduced activation of the HO-1 promoter by LNO2.	Cyclic AMP	36-40	heme oxygenase 1	Homo sapiens	196-200
19608869-6	2009	HO-1 overexpression also attenuated TNF-alpha-induced oxidative stress, which was abrogated in the presence of both the HO-1 inhibitor, zinc protoporphyrin IX, as well as a carbon monoxide scavenger.	zinc protoporphyrin	136-158	heme oxygenase 1	Homo sapiens	0-4
19608869-6	2009	HO-1 overexpression also attenuated TNF-alpha-induced oxidative stress, which was abrogated in the presence of both the HO-1 inhibitor, zinc protoporphyrin IX, as well as a carbon monoxide scavenger.	zinc protoporphyrin	136-158	heme oxygenase 1	Homo sapiens	120-124
19608869-6	2009	HO-1 overexpression also attenuated TNF-alpha-induced oxidative stress, which was abrogated in the presence of both the HO-1 inhibitor, zinc protoporphyrin IX, as well as a carbon monoxide scavenger.	Carbon Monoxide	173-188	heme oxygenase 1	Homo sapiens	0-4
19608869-8	2009	These results suggest that HO-1 functions as a suppressor of TNF-alpha signaling, not only by inhibiting the expression of adhesion molecules and generation of interleukin-6, but also by diminishing intracellular reactive oxygen species production and nuclear factor-kappaB activation in both cultured human tracheal smooth muscle cells and the airways of mice.	Reactive Oxygen Species	213-236	heme oxygenase 1	Homo sapiens	27-31
19508170-7	2009	Interestingly, several of the drug partners, when applied as single agents, induced the expression of Hsp32 in neoplastic cells, suggesting that synergistic effects resulted from SMA-ZnPP-induced ablation of a Hsp32-mediated survival-pathway that is otherwise used by tumor cells to escape drug-induced apoptosis.	zinc protoporphyrin	183-187	heme oxygenase 1	Homo sapiens	102-107
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Heme	57-61	heme oxygenase 1	Homo sapiens	75-79
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Biliverdine	168-178	heme oxygenase 1	Homo sapiens	57-73
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Biliverdine	168-178	heme oxygenase 1	Homo sapiens	75-79
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Iron	185-189	heme oxygenase 1	Homo sapiens	57-73
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Iron	185-189	heme oxygenase 1	Homo sapiens	75-79
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	57-73
19727608-3	2009	One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	75-79
19652369-0	2009	Nitric oxide modulates osteoblastic differentiation with heme oxygenase-1 via the mitogen activated protein kinase and nuclear factor-kappaB pathways in human periodontal ligament cells.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	57-73
19640789-3	2009	Heme oxygenase-1 (HO-1) is a key enzyme that is indispensable for the temporal and spatial regulation of host response and, together with its essential metabolite carbon monoxide (CO), is crucial for maintaining homeostasis, inhibition of inflammation and the preservation of function and life.	Carbon Monoxide	163-178	heme oxygenase 1	Homo sapiens	0-16
19640789-3	2009	Heme oxygenase-1 (HO-1) is a key enzyme that is indispensable for the temporal and spatial regulation of host response and, together with its essential metabolite carbon monoxide (CO), is crucial for maintaining homeostasis, inhibition of inflammation and the preservation of function and life.	Carbon Monoxide	163-178	heme oxygenase 1	Homo sapiens	18-22
19640789-3	2009	Heme oxygenase-1 (HO-1) is a key enzyme that is indispensable for the temporal and spatial regulation of host response and, together with its essential metabolite carbon monoxide (CO), is crucial for maintaining homeostasis, inhibition of inflammation and the preservation of function and life.	Carbon Monoxide	180-182	heme oxygenase 1	Homo sapiens	0-16
19640789-3	2009	Heme oxygenase-1 (HO-1) is a key enzyme that is indispensable for the temporal and spatial regulation of host response and, together with its essential metabolite carbon monoxide (CO), is crucial for maintaining homeostasis, inhibition of inflammation and the preservation of function and life.	Carbon Monoxide	180-182	heme oxygenase 1	Homo sapiens	18-22
19508170-7	2009	Interestingly, several of the drug partners, when applied as single agents, induced the expression of Hsp32 in neoplastic cells, suggesting that synergistic effects resulted from SMA-ZnPP-induced ablation of a Hsp32-mediated survival-pathway that is otherwise used by tumor cells to escape drug-induced apoptosis.	zinc protoporphyrin	183-187	heme oxygenase 1	Homo sapiens	210-215
19522732-0	2009	Brain sterol dysregulation in sporadic AD and MCI: relationship to heme oxygenase-1.	Sterols	6-12	heme oxygenase 1	Homo sapiens	67-83
18830972-0	2009	GSH-dependent iNOS and HO-1 mediated apoptosis of human Jurkat cells induced by nickel(II).	Glutathione	0-3	heme oxygenase 1	Homo sapiens	23-27
18830972-0	2009	GSH-dependent iNOS and HO-1 mediated apoptosis of human Jurkat cells induced by nickel(II).	Nickel(2+)	80-90	heme oxygenase 1	Homo sapiens	23-27
18830972-7	2009	A significant increase in HO-1 mRNA levels was detected in nickel treated cells.	Nickel	59-65	heme oxygenase 1	Homo sapiens	26-30
18830972-9	2009	Expression changes of HO-1 and iNOS were markedly blocked when Jurkat cells were preincubated with NAC, suggesting that ROS resulted in HO-1 and iNOS dysfunction in Jurkat cells.	Acetylcysteine	99-102	heme oxygenase 1	Homo sapiens	22-26
18830972-9	2009	Expression changes of HO-1 and iNOS were markedly blocked when Jurkat cells were preincubated with NAC, suggesting that ROS resulted in HO-1 and iNOS dysfunction in Jurkat cells.	Acetylcysteine	99-102	heme oxygenase 1	Homo sapiens	136-140
18830972-9	2009	Expression changes of HO-1 and iNOS were markedly blocked when Jurkat cells were preincubated with NAC, suggesting that ROS resulted in HO-1 and iNOS dysfunction in Jurkat cells.	Reactive Oxygen Species	120-123	heme oxygenase 1	Homo sapiens	22-26
18830972-9	2009	Expression changes of HO-1 and iNOS were markedly blocked when Jurkat cells were preincubated with NAC, suggesting that ROS resulted in HO-1 and iNOS dysfunction in Jurkat cells.	Reactive Oxygen Species	120-123	heme oxygenase 1	Homo sapiens	136-140
18830972-10	2009	We supposed that the immune toxicity of nickel(II) was mainly due to GSH depletion and finally led to apoptosis, probably via changing the expression levels of HO-1 and iNOS in human T lymphocytes.	Nickel	40-46	heme oxygenase 1	Homo sapiens	160-164
19522732-3	2009	We recently determined that HO-1 over-expression suppresses total CH levels by augmenting liver X receptor-mediated CH efflux and enhances oxysterol formation in cultured astroglia.	Oxysterols	139-148	heme oxygenase 1	Homo sapiens	28-32
19522732-6	2009	The relationships of sterol/oxysterol levels to HO-1 protein expression and clinical/demographic variables were determined by multivariable regression and non-parametric statistical analyses.	Sterols	21-27	heme oxygenase 1	Homo sapiens	48-52
19522732-6	2009	The relationships of sterol/oxysterol levels to HO-1 protein expression and clinical/demographic variables were determined by multivariable regression and non-parametric statistical analyses.	Oxysterols	28-37	heme oxygenase 1	Homo sapiens	48-52
19401559-0	2009	Identification of crassin acetate as a new immunosuppressant triggering heme oxygenase-1 expression in dendritic cells.	crassin acetate	18-33	heme oxygenase 1	Homo sapiens	72-88
19656028-5	2009	Nicotine induced the synthesis of the transcription factor NF-E2-related factor-2 (Nrf2) as well as a number of cellular antioxidants and phase II enzymes, such as heme oxygenase-1.	Nicotine	0-8	heme oxygenase 1	Homo sapiens	164-180
20021945-6	2009	The relative survival rate of HepG2 cells under hypoxia was significantly decreased after the HO-1 protein overexpression was inhibited by ZnPPIX (P &lt; 0.01).	zinc protoporphyrin	139-145	heme oxygenase 1	Homo sapiens	94-98
20021945-7	2009	The total SOD activity of cells was significantly increased after cells were treated by hypoxia for 16 hours (P &lt; 0.05), while decreased significantly by HO-1 inhibitor ZnPPIX treatment (P &lt; 0.01).	zinc protoporphyrin	172-178	heme oxygenase 1	Homo sapiens	157-161
20021945-9	2009	In addition, the HO-1 overexpression under hypoxia was decreased by HIF-1alpha inhibitor, while the HIF-1alpha expression level under hypoxia was not significantly changed after HO-1 expression was inhibited by ZnPPIX.	zinc protoporphyrin	211-217	heme oxygenase 1	Homo sapiens	178-182
19457866-6	2009	Synergy was observed between laminar shear stress and atorvastatin, resulting in optimal expression of heme oxygenase-1 and resistance to oxidative stress, a response inhibited by heme oxygenase-1 small interfering RNA.	Atorvastatin	54-66	heme oxygenase 1	Homo sapiens	103-119
19457866-6	2009	Synergy was observed between laminar shear stress and atorvastatin, resulting in optimal expression of heme oxygenase-1 and resistance to oxidative stress, a response inhibited by heme oxygenase-1 small interfering RNA.	Atorvastatin	54-66	heme oxygenase 1	Homo sapiens	180-196
19457866-9	2009	In contrast, heme oxygenase-1 induction by atorvastatin in endothelial cells exposed to oscillatory flow was markedly attenuated.	Atorvastatin	43-55	heme oxygenase 1	Homo sapiens	13-29
19457866-10	2009	We have identified a novel relationship between laminar shear stress and statins, demonstrating that atorvastatin-mediated heme oxygenase-1-dependent antioxidant effects are laminar shear stress-dependent, proving the principle that biomechanical signaling contributes significantly to endothelial responsiveness to pharmacological agents.	Atorvastatin	101-113	heme oxygenase 1	Homo sapiens	123-139
19401559-4	2009	Treatment with CRA at nontoxic doses induced heme oxygenase-1 (HO-1) mRNA/protein expression and HO-1 enzymatic activity in DCs, suggesting a unique mechanism of action.	crassin acetate	15-18	heme oxygenase 1	Homo sapiens	45-61
19401559-4	2009	Treatment with CRA at nontoxic doses induced heme oxygenase-1 (HO-1) mRNA/protein expression and HO-1 enzymatic activity in DCs, suggesting a unique mechanism of action.	crassin acetate	15-18	heme oxygenase 1	Homo sapiens	63-67
19401559-4	2009	Treatment with CRA at nontoxic doses induced heme oxygenase-1 (HO-1) mRNA/protein expression and HO-1 enzymatic activity in DCs, suggesting a unique mechanism of action.	crassin acetate	15-18	heme oxygenase 1	Homo sapiens	97-101
19457084-7	2009	Likewise, treatment of HO-1 over-expressing cells with the HO-1 inhibitor, tin mesoporphyrin, the iron chelator deferoxamine or antagonist of CO-dependent cGMP activation, methylene blue, mitigated the HO-1-induced reduction in alpha-synuclein levels.	Deferoxamine	112-124	heme oxygenase 1	Homo sapiens	23-27
18619522-8	2009	Heme oxygenase 1 (HO1) is an important component of the system for mobilization of iron from macrophages.	Iron	83-87	heme oxygenase 1	Homo sapiens	0-16
18619522-8	2009	Heme oxygenase 1 (HO1) is an important component of the system for mobilization of iron from macrophages.	Iron	83-87	heme oxygenase 1	Homo sapiens	18-21
19702533-2	2009	Naturally occurring substances that upregulate the inducible isoform of HO (HO-1) have therefore been proposed as potential new drugs for the treatment of free radical-induced disease.	Free Radicals	155-167	heme oxygenase 1	Homo sapiens	76-80
19453654-0	2009	High extracellular induced sputum haem oxygenase-1 in sarcoidosis and chronic beryllium disease.	Beryllium	78-87	heme oxygenase 1	Homo sapiens	34-50
19362144-3	2009	HO-1 serves a vital metabolic function as the rate-limiting step in the heme degradation pathway and in the maintenance of iron homeostasis.	Heme	72-76	heme oxygenase 1	Homo sapiens	0-4
19362144-3	2009	HO-1 serves a vital metabolic function as the rate-limiting step in the heme degradation pathway and in the maintenance of iron homeostasis.	Iron	123-127	heme oxygenase 1	Homo sapiens	0-4
19362144-5	2009	The cytoprotective functions of HO-1 may be attributed to heme turnover, as well as to beneficial properties of its enzymatic reaction products: biliverdin-IXalpha, iron, and carbon monoxide (CO).	Biliverdine	145-163	heme oxygenase 1	Homo sapiens	32-36
19362144-5	2009	The cytoprotective functions of HO-1 may be attributed to heme turnover, as well as to beneficial properties of its enzymatic reaction products: biliverdin-IXalpha, iron, and carbon monoxide (CO).	Iron	165-169	heme oxygenase 1	Homo sapiens	32-36
19362144-5	2009	The cytoprotective functions of HO-1 may be attributed to heme turnover, as well as to beneficial properties of its enzymatic reaction products: biliverdin-IXalpha, iron, and carbon monoxide (CO).	Carbon Monoxide	175-190	heme oxygenase 1	Homo sapiens	32-36
19362144-5	2009	The cytoprotective functions of HO-1 may be attributed to heme turnover, as well as to beneficial properties of its enzymatic reaction products: biliverdin-IXalpha, iron, and carbon monoxide (CO).	Carbon Monoxide	192-194	heme oxygenase 1	Homo sapiens	32-36
19475336-3	2009	Therefore, it is tempting that the iron-releasing key enzyme in heme catabolism, heme oxygenase-1 (HO-1), may represent a candidate for a genetic susceptibility to PD.	Iron	35-39	heme oxygenase 1	Homo sapiens	81-97
19475336-3	2009	Therefore, it is tempting that the iron-releasing key enzyme in heme catabolism, heme oxygenase-1 (HO-1), may represent a candidate for a genetic susceptibility to PD.	Iron	35-39	heme oxygenase 1	Homo sapiens	99-103
19475336-3	2009	Therefore, it is tempting that the iron-releasing key enzyme in heme catabolism, heme oxygenase-1 (HO-1), may represent a candidate for a genetic susceptibility to PD.	Heme	64-68	heme oxygenase 1	Homo sapiens	81-97
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Carbon Monoxide	139-154	heme oxygenase 1	Homo sapiens	29-45
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Carbon Monoxide	139-154	heme oxygenase 1	Homo sapiens	47-51
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Carbon Monoxide	139-154	heme oxygenase 1	Homo sapiens	125-129
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Carbon Monoxide	156-158	heme oxygenase 1	Homo sapiens	29-45
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Carbon Monoxide	156-158	heme oxygenase 1	Homo sapiens	47-51
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Carbon Monoxide	156-158	heme oxygenase 1	Homo sapiens	125-129
19465554-1	2009	Given that the physiology of heme oxygenase-1 (HO-1) encompasses mitochondrial biogenesis, we tested the hypothesis that the HO-1 product, carbon monoxide (CO), activates mitochondrial biogenesis in skeletal muscle and enhances maximal oxygen uptake (Vo(2max)) in humans.	Oxygen	34-40	heme oxygenase 1	Homo sapiens	47-51
19590705-0	2009	Taurine Chloramine Activates Nrf2, Increases HO-1 Expression and Protects Cells from Death Caused by Hydrogen Peroxide.	N-chlorotaurine	0-18	heme oxygenase 1	Homo sapiens	45-49
19590705-5	2009	TauCl increased the expression of peroxiredoxin-1, thioredoxin-1 and heme oxygenase (HO)-1, the anti-oxidant enzymes normally induced by activation of NF-E2-related factor-2 (Nrf2).	N-chlorotaurine	0-5	heme oxygenase 1	Homo sapiens	69-90
19590705-8	2009	Elevation of HO activity via induction of HO-1 expression within neighboring cells may provide protection from cytotoxicity caused by inflammatory oxidants like H(2)O(2).	Water	161-166	heme oxygenase 1	Homo sapiens	42-46
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Heme	49-53	heme oxygenase 1	Homo sapiens	0-16
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Heme	49-53	heme oxygenase 1	Homo sapiens	18-22
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Iron	62-66	heme oxygenase 1	Homo sapiens	0-16
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Iron	62-66	heme oxygenase 1	Homo sapiens	18-22
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	0-16
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	18-22
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Carbon Monoxide	85-87	heme oxygenase 1	Homo sapiens	0-16
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Carbon Monoxide	85-87	heme oxygenase 1	Homo sapiens	18-22
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	0-16
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	18-22
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Bilirubin	105-114	heme oxygenase 1	Homo sapiens	0-16
19457084-3	2009	Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors.	Bilirubin	105-114	heme oxygenase 1	Homo sapiens	18-22
19457084-7	2009	Likewise, treatment of HO-1 over-expressing cells with the HO-1 inhibitor, tin mesoporphyrin, the iron chelator deferoxamine or antagonist of CO-dependent cGMP activation, methylene blue, mitigated the HO-1-induced reduction in alpha-synuclein levels.	tin mesoporphyrin	75-92	heme oxygenase 1	Homo sapiens	23-27
19457084-7	2009	Likewise, treatment of HO-1 over-expressing cells with the HO-1 inhibitor, tin mesoporphyrin, the iron chelator deferoxamine or antagonist of CO-dependent cGMP activation, methylene blue, mitigated the HO-1-induced reduction in alpha-synuclein levels.	Iron	98-102	heme oxygenase 1	Homo sapiens	23-27
19475336-3	2009	Therefore, it is tempting that the iron-releasing key enzyme in heme catabolism, heme oxygenase-1 (HO-1), may represent a candidate for a genetic susceptibility to PD.	Heme	64-68	heme oxygenase 1	Homo sapiens	99-103
19457084-7	2009	Likewise, treatment of HO-1 over-expressing cells with the HO-1 inhibitor, tin mesoporphyrin, the iron chelator deferoxamine or antagonist of CO-dependent cGMP activation, methylene blue, mitigated the HO-1-induced reduction in alpha-synuclein levels.	Cyclic GMP	155-159	heme oxygenase 1	Homo sapiens	23-27
19457084-7	2009	Likewise, treatment of HO-1 over-expressing cells with the HO-1 inhibitor, tin mesoporphyrin, the iron chelator deferoxamine or antagonist of CO-dependent cGMP activation, methylene blue, mitigated the HO-1-induced reduction in alpha-synuclein levels.	Methylene Blue	172-186	heme oxygenase 1	Homo sapiens	23-27
19457084-8	2009	Furthermore, when HO-1 over-expressing cells were treated with the proteosome inhibitors, lactacystin and MG132, level of alpha-synuclein was almost completely restored.	lactacystin	90-101	heme oxygenase 1	Homo sapiens	18-22
19457084-8	2009	Furthermore, when HO-1 over-expressing cells were treated with the proteosome inhibitors, lactacystin and MG132, level of alpha-synuclein was almost completely restored.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	106-111	heme oxygenase 1	Homo sapiens	18-22
19457088-7	2009	Heme-derived free ferrous iron, CO, and biliverdin/bilirubin are biologically active substances that have been shown to either ameliorate or exacerbate neural injury contingent upon specific disease models employed, the intensity and duration of HO-1 expression and the nature of the prevailing redox microenvironment.	ferrous iron	18-30	heme oxygenase 1	Homo sapiens	246-250
19457088-7	2009	Heme-derived free ferrous iron, CO, and biliverdin/bilirubin are biologically active substances that have been shown to either ameliorate or exacerbate neural injury contingent upon specific disease models employed, the intensity and duration of HO-1 expression and the nature of the prevailing redox microenvironment.	Biliverdine	40-50	heme oxygenase 1	Homo sapiens	246-250
19457088-7	2009	Heme-derived free ferrous iron, CO, and biliverdin/bilirubin are biologically active substances that have been shown to either ameliorate or exacerbate neural injury contingent upon specific disease models employed, the intensity and duration of HO-1 expression and the nature of the prevailing redox microenvironment.	Bilirubin	51-60	heme oxygenase 1	Homo sapiens	246-250
19457088-8	2009	In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging-related neurodegenerative disorders.	Iron	100-104	heme oxygenase 1	Homo sapiens	25-29
19457088-8	2009	In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging-related neurodegenerative disorders.	Iron	171-175	heme oxygenase 1	Homo sapiens	25-29
19457088-9	2009	Glial HO-1 expression may also impact cell survival and neuroplasticity in these conditions by modulating brain sterol metabolism and proteosomal degradation of neurotoxic protein aggregates.	Sterols	112-118	heme oxygenase 1	Homo sapiens	6-10
19039664-7	2009	The regulation of both hmox1 and mt1 is prevented by the copper-chelator, bathocuproinedisulfonate (BCDS), but not uptake of heme-AlexaFluor-labeled HPX into endosomes.	bathocuproine sulfonate	74-98	heme oxygenase 1	Homo sapiens	23-28
19320847-5	2009	Targeted knockdown of HO-1 leads to decreased intracellular PpIX accumulation, resulting in a failure to enhance ALA-PDT effect in four cell lines.	protoporphyrin IX	60-64	heme oxygenase 1	Homo sapiens	22-26
19320847-8	2009	Our results suggested that (1) FECH siRNA improved the phototoxicity of ALA-PDT, (2) overexpression of HO-1 was associated with shorter (GT)n repeat of the promoter region, and (3) siRNA-mediated knockdown of HO-1 could suppress the growth of bladder cancer cells overexpressing HO-1.	Alanine	72-75	heme oxygenase 1	Homo sapiens	103-107
19320847-8	2009	Our results suggested that (1) FECH siRNA improved the phototoxicity of ALA-PDT, (2) overexpression of HO-1 was associated with shorter (GT)n repeat of the promoter region, and (3) siRNA-mediated knockdown of HO-1 could suppress the growth of bladder cancer cells overexpressing HO-1.	Alanine	72-75	heme oxygenase 1	Homo sapiens	209-213
19320847-8	2009	Our results suggested that (1) FECH siRNA improved the phototoxicity of ALA-PDT, (2) overexpression of HO-1 was associated with shorter (GT)n repeat of the promoter region, and (3) siRNA-mediated knockdown of HO-1 could suppress the growth of bladder cancer cells overexpressing HO-1.	Alanine	72-75	heme oxygenase 1	Homo sapiens	209-213
19428335-0	2009	Heme oxygenase-1 induction modulates microsomal prostaglandin E synthase-1 expression and prostaglandin E(2) production in osteoarthritic chondrocytes.	Dinoprostone	90-108	heme oxygenase 1	Homo sapiens	0-16
19428335-5	2009	Cells were stimulated with IL-1beta in the absence or presence of the HO-1 inducer cobalt protoporphyrin IX (CoPP).	cobaltiprotoporphyrin	83-107	heme oxygenase 1	Homo sapiens	70-74
19428335-9	2009	The production of PGE(2) was decreased by HO-1 induction as a result of diminished mPGES-1 protein and mRNA expression.	Dinoprostone	18-24	heme oxygenase 1	Homo sapiens	42-46
19508729-6	2009	HO-1 expression and activity was regulated by zinc (inhibition) and cobalt (induction) protoporphyrin.	Cobalt	68-74	heme oxygenase 1	Homo sapiens	0-4
19508729-6	2009	HO-1 expression and activity was regulated by zinc (inhibition) and cobalt (induction) protoporphyrin.	protoporphyrin IX	85-101	heme oxygenase 1	Homo sapiens	0-4
19508729-7	2009	Furthermore, the influence of cellular HO-1 levels and its metabolites on effects of standard chemotherapy with gemcitabine was tested in vivo and in vitro.	gemcitabine	112-123	heme oxygenase 1	Homo sapiens	39-43
19508729-9	2009	Chemoresistance to gemcitabine was increased during HO-1 induction in PaCa cells expressing low levels of HO-1.	gemcitabine	19-30	heme oxygenase 1	Homo sapiens	52-56
19508729-9	2009	Chemoresistance to gemcitabine was increased during HO-1 induction in PaCa cells expressing low levels of HO-1.	gemcitabine	19-30	heme oxygenase 1	Homo sapiens	106-110
19508729-14	2009	The metabolites biliverdin and iron seem to be involved in HO-1-mediated resistance to anticancer treatment.	Biliverdine	16-26	heme oxygenase 1	Homo sapiens	59-63
19508729-14	2009	The metabolites biliverdin and iron seem to be involved in HO-1-mediated resistance to anticancer treatment.	Iron	31-35	heme oxygenase 1	Homo sapiens	59-63
19344704-4	2009	Whereas the expression of glutathione peroxidase (GPx), catalase, Cu,Zn-superoxide dismutase (Cu,Zn-SOD) and heme oxygenase-1 (HO-1) increased with curcumin concentration and also with increase in time of incubation, the expression of Mn- superoxide dismutase (Mn-SOD) showed concentration dependant repression upon treatment with curcumin.	Curcumin	148-156	heme oxygenase 1	Homo sapiens	109-125
19344704-4	2009	Whereas the expression of glutathione peroxidase (GPx), catalase, Cu,Zn-superoxide dismutase (Cu,Zn-SOD) and heme oxygenase-1 (HO-1) increased with curcumin concentration and also with increase in time of incubation, the expression of Mn- superoxide dismutase (Mn-SOD) showed concentration dependant repression upon treatment with curcumin.	Curcumin	148-156	heme oxygenase 1	Homo sapiens	127-131
19487598-8	2009	HO-1 induction by cobalt protoporphyrin impeded lesion progression into vulnerable plaques, indicated by a reduction in necrotic core size and intraplaque lipid accumulation, whereas cap thickness and vascular smooth muscle cells were increased.	cobaltiprotoporphyrin	18-39	heme oxygenase 1	Homo sapiens	0-4
19487598-9	2009	In contrast, inhibition of HO-1 by zinc protoporphyrin augmented plaque vulnerability.	zinc protoporphyrin	35-54	heme oxygenase 1	Homo sapiens	27-31
19325051-0	2009	The protective role of HO-1 and its generated products (CO, bilirubin, and Fe) in ethanol-induced human hepatocyte damage.	Carbon Monoxide	56-58	heme oxygenase 1	Homo sapiens	23-27
19325051-0	2009	The protective role of HO-1 and its generated products (CO, bilirubin, and Fe) in ethanol-induced human hepatocyte damage.	Ethanol	82-89	heme oxygenase 1	Homo sapiens	23-27
19325051-1	2009	It has been reported that naturally occurring quercetin exerts hepatoprotective effects through heme oxygenase-1 (HO-1) induction.	Quercetin	46-55	heme oxygenase 1	Homo sapiens	96-112
19325051-1	2009	It has been reported that naturally occurring quercetin exerts hepatoprotective effects through heme oxygenase-1 (HO-1) induction.	Quercetin	46-55	heme oxygenase 1	Homo sapiens	114-118
19325051-2	2009	However, the precise mechanism of how ethanol-associated liver damage is counteracted by quercetin-enhanced HO-1 metabolism still remains unclear.	Quercetin	89-98	heme oxygenase 1	Homo sapiens	108-112
19325051-9	2009	These results suggested that quercetin virtually attenuated ethanol-derived oxidative damage via HO-1 induction.	Quercetin	29-38	heme oxygenase 1	Homo sapiens	97-101
19325051-9	2009	These results suggested that quercetin virtually attenuated ethanol-derived oxidative damage via HO-1 induction.	Ethanol	60-67	heme oxygenase 1	Homo sapiens	97-101
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Heme	0-4	heme oxygenase 1	Homo sapiens	71-87
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Heme	0-4	heme oxygenase 1	Homo sapiens	89-94
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Heme	52-56	heme oxygenase 1	Homo sapiens	71-87
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Heme	52-56	heme oxygenase 1	Homo sapiens	89-94
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Iron	114-118	heme oxygenase 1	Homo sapiens	71-87
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Iron	114-118	heme oxygenase 1	Homo sapiens	89-94
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Heme	52-56	heme oxygenase 1	Homo sapiens	71-87
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Heme	52-56	heme oxygenase 1	Homo sapiens	89-94
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Iron	168-172	heme oxygenase 1	Homo sapiens	71-87
19039664-2	2009	Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron.	Iron	168-172	heme oxygenase 1	Homo sapiens	89-94
19039664-4	2009	When heme-HPX induces HMOX1, the copper-storing metallothioneins (MTs) are also induced whereas the copper-responsive copper chaperone that delivers copper to Cu, Zn superoxide dismutase, CCS1, is decreased; both are known responses when cellular copper levels rise.	Copper	33-39	heme oxygenase 1	Homo sapiens	22-27
19039664-4	2009	When heme-HPX induces HMOX1, the copper-storing metallothioneins (MTs) are also induced whereas the copper-responsive copper chaperone that delivers copper to Cu, Zn superoxide dismutase, CCS1, is decreased; both are known responses when cellular copper levels rise.	Copper	100-106	heme oxygenase 1	Homo sapiens	22-27
19039664-4	2009	When heme-HPX induces HMOX1, the copper-storing metallothioneins (MTs) are also induced whereas the copper-responsive copper chaperone that delivers copper to Cu, Zn superoxide dismutase, CCS1, is decreased; both are known responses when cellular copper levels rise.	Copper	100-106	heme oxygenase 1	Homo sapiens	22-27
19039664-4	2009	When heme-HPX induces HMOX1, the copper-storing metallothioneins (MTs) are also induced whereas the copper-responsive copper chaperone that delivers copper to Cu, Zn superoxide dismutase, CCS1, is decreased; both are known responses when cellular copper levels rise.	Copper	100-106	heme oxygenase 1	Homo sapiens	22-27
19039664-4	2009	When heme-HPX induces HMOX1, the copper-storing metallothioneins (MTs) are also induced whereas the copper-responsive copper chaperone that delivers copper to Cu, Zn superoxide dismutase, CCS1, is decreased; both are known responses when cellular copper levels rise.	Copper	100-106	heme oxygenase 1	Homo sapiens	22-27
19039664-7	2009	The regulation of both hmox1 and mt1 is prevented by the copper-chelator, bathocuproinedisulfonate (BCDS), but not uptake of heme-AlexaFluor-labeled HPX into endosomes.	bathocuproine sulfonate	100-104	heme oxygenase 1	Homo sapiens	23-28
19039664-5	2009	Endocytosis of heme-HPX is needed to regulate CCS1 since the signaling ligand cobalt-protoporphyrin (CoPP)-HPX, which does not induce HMOX1 but does co-localize with heme-HPX in endosomes, also decreased CCS1.	heme-hpx	15-23	heme oxygenase 1	Homo sapiens	134-139
19039664-7	2009	The regulation of both hmox1 and mt1 is prevented by the copper-chelator, bathocuproinedisulfonate (BCDS), but not uptake of heme-AlexaFluor-labeled HPX into endosomes.	Copper	57-63	heme oxygenase 1	Homo sapiens	23-28
19039664-8	2009	Supporting a role for copper in HMOX1 regulation by heme-HPX, nutritional copper deficiency generated by tetraethylene pentamine or 232 tetraamine prevented HMOX1 induction.	Copper	22-28	heme oxygenase 1	Homo sapiens	32-37
19039664-8	2009	Supporting a role for copper in HMOX1 regulation by heme-HPX, nutritional copper deficiency generated by tetraethylene pentamine or 232 tetraamine prevented HMOX1 induction.	Copper	22-28	heme oxygenase 1	Homo sapiens	157-162
19039664-8	2009	Supporting a role for copper in HMOX1 regulation by heme-HPX, nutritional copper deficiency generated by tetraethylene pentamine or 232 tetraamine prevented HMOX1 induction.	tetraethylenepentamine	105-128	heme oxygenase 1	Homo sapiens	157-162
19039664-8	2009	Supporting a role for copper in HMOX1 regulation by heme-HPX, nutritional copper deficiency generated by tetraethylene pentamine or 232 tetraamine prevented HMOX1 induction.	tetraamine	136-146	heme oxygenase 1	Homo sapiens	32-37
19039664-8	2009	Supporting a role for copper in HMOX1 regulation by heme-HPX, nutritional copper deficiency generated by tetraethylene pentamine or 232 tetraamine prevented HMOX1 induction.	tetraamine	136-146	heme oxygenase 1	Homo sapiens	157-162
19039664-10	2009	A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX.	Copper	30-36	heme oxygenase 1	Homo sapiens	178-183
19039664-10	2009	A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX.	Copper	30-36	heme oxygenase 1	Homo sapiens	287-292
19039664-10	2009	A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX.	Heme	71-75	heme oxygenase 1	Homo sapiens	178-183
19039664-10	2009	A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX.	Heme	71-75	heme oxygenase 1	Homo sapiens	287-292
19039664-10	2009	A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX.	Heme	111-115	heme oxygenase 1	Homo sapiens	178-183
19039664-10	2009	A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX.	Heme	111-115	heme oxygenase 1	Homo sapiens	287-292
19063990-0	2009	Heme oxygenase-1 induction prevents neuronal damage triggered during mitochondrial inhibition: role of CO and bilirubin.	Carbon Monoxide	103-105	heme oxygenase 1	Homo sapiens	0-16
19373083-7	2009	SUMMARY: The development of derivatives of probucol targeting anti-inflammatory and antioxidant processes, perhaps via induction of heme oxygenase-1, may add to the armamentarium of current agents used in treatment of atherosclerotic disease and diabetes.	Probucol	43-51	heme oxygenase 1	Homo sapiens	132-148
19063990-0	2009	Heme oxygenase-1 induction prevents neuronal damage triggered during mitochondrial inhibition: role of CO and bilirubin.	Bilirubin	110-119	heme oxygenase 1	Homo sapiens	0-16
19063990-2	2009	A protective role of the inducible isoform, HO-1, has been described in pathological conditions associated with reactive oxygen species (ROS) and oxidative damage.	Reactive Oxygen Species	112-135	heme oxygenase 1	Homo sapiens	44-48
19063990-2	2009	A protective role of the inducible isoform, HO-1, has been described in pathological conditions associated with reactive oxygen species (ROS) and oxidative damage.	Reactive Oxygen Species	137-140	heme oxygenase 1	Homo sapiens	44-48
19063990-3	2009	The aim of this study was to investigate the role of HO-1 in the neurotoxicity induced by the mitochondrial toxin 3-nitropropionic acid (3-NP) in primary cultures of cerebellar granule neurons (CGNs).	3-nitropropionic acid	114-135	heme oxygenase 1	Homo sapiens	53-57
19063990-3	2009	The aim of this study was to investigate the role of HO-1 in the neurotoxicity induced by the mitochondrial toxin 3-nitropropionic acid (3-NP) in primary cultures of cerebellar granule neurons (CGNs).	3-nitropropionic acid	137-141	heme oxygenase 1	Homo sapiens	53-57
19063990-6	2009	In addition, HO-1 up-regulation induced by the exposure to cobalt protoporphyrin (CoPP) before the incubation with 3-NP, prevented the cell death and the increase in ROS induced by 3-NP.	cobaltiprotoporphyrin	59-80	heme oxygenase 1	Homo sapiens	13-17
19063990-6	2009	In addition, HO-1 up-regulation induced by the exposure to cobalt protoporphyrin (CoPP) before the incubation with 3-NP, prevented the cell death and the increase in ROS induced by 3-NP.	cobaltiprotoporphyrin	82-86	heme oxygenase 1	Homo sapiens	13-17
19063990-6	2009	In addition, HO-1 up-regulation induced by the exposure to cobalt protoporphyrin (CoPP) before the incubation with 3-NP, prevented the cell death and the increase in ROS induced by 3-NP.	3-nitropropionic acid	115-119	heme oxygenase 1	Homo sapiens	13-17
19063990-6	2009	In addition, HO-1 up-regulation induced by the exposure to cobalt protoporphyrin (CoPP) before the incubation with 3-NP, prevented the cell death and the increase in ROS induced by 3-NP.	Reactive Oxygen Species	166-169	heme oxygenase 1	Homo sapiens	13-17
19063990-6	2009	In addition, HO-1 up-regulation induced by the exposure to cobalt protoporphyrin (CoPP) before the incubation with 3-NP, prevented the cell death and the increase in ROS induced by 3-NP.	3-nitropropionic acid	181-185	heme oxygenase 1	Homo sapiens	13-17
19420259-5	2009	In Tsc2-deficient neurons, the expression of stress markers such as CHOP and HO-1 is increased, and this increase is completely reversed by the mTOR inhibitor rapamycin both in vitro and in vivo.	Sirolimus	159-168	heme oxygenase 1	Homo sapiens	77-81
19350554-7	2009	In contrast, N-acetylcysteine, a potent cysteine reductive compound, significantly prevents up-regulation of HMOX1, GCLM, and CXCL2 genes, and repression of MMP9 and CCL22 genes induced by As(2)O(3).	Acetylcysteine	13-29	heme oxygenase 1	Homo sapiens	109-114
19350554-7	2009	In contrast, N-acetylcysteine, a potent cysteine reductive compound, significantly prevents up-regulation of HMOX1, GCLM, and CXCL2 genes, and repression of MMP9 and CCL22 genes induced by As(2)O(3).	Cysteine	21-29	heme oxygenase 1	Homo sapiens	109-114
19121922-1	2009	OBJECTIVE: We tested the hypothesis that lycopene supplementation reduces the expression of oxidant-responsive heme oxygenase-1 (HO-1) in basal conditions and in response to an oxidant challenge and determined whether this is temporally associated with increased cell viability.	Lycopene	41-49	heme oxygenase 1	Homo sapiens	111-127
19121922-1	2009	OBJECTIVE: We tested the hypothesis that lycopene supplementation reduces the expression of oxidant-responsive heme oxygenase-1 (HO-1) in basal conditions and in response to an oxidant challenge and determined whether this is temporally associated with increased cell viability.	Lycopene	41-49	heme oxygenase 1	Homo sapiens	129-133
19121922-2	2009	METHODS: We determined basal and stimulated ex vivo expression of HO-1 and cell viability in lymphocytes from volunteers after lycopene supplementation.	Lycopene	127-135	heme oxygenase 1	Homo sapiens	66-70
19484149-10	2009	In contrast to annexin A11, HMOX1 immunoreactivity positively correlated with in vitro cisplatin resistance in ovarian cancers.	Cisplatin	87-96	heme oxygenase 1	Homo sapiens	28-33
19429248-3	2009	The overall results suggest that CeO(2) nanoparticles may exert their toxicity through oxidative stress, as they cause significant increases in the cellular reactive oxygen species (ROS) concentrations, subsequently leading to the strong induction of heme oxygenase-1 (HO-1) via the p38-Nrf-2 signaling pathway.	Reactive Oxygen Species	157-180	heme oxygenase 1	Homo sapiens	251-267
19429248-3	2009	The overall results suggest that CeO(2) nanoparticles may exert their toxicity through oxidative stress, as they cause significant increases in the cellular reactive oxygen species (ROS) concentrations, subsequently leading to the strong induction of heme oxygenase-1 (HO-1) via the p38-Nrf-2 signaling pathway.	Reactive Oxygen Species	182-185	heme oxygenase 1	Homo sapiens	251-267
19349368-5	2009	Incubating human microvascular endothelial cells with the sphingosine-1-phosphate type 1 receptor (S1P(1)) inhibitor VPC23019 or performing small interfering RNA knockdown of S1P(1) blocked arsenic-stimulated HMVEC angiogenic gene expression and tube formation, but did not affect induction of either HMOX1 or IL8.	Arsenic	190-197	heme oxygenase 1	Homo sapiens	301-306
19251588-9	2009	In contrast, heme oxygenase-1 was strongly suppressed by DFO, both in the absence and presence of LPS or iron.	Deferoxamine	57-60	heme oxygenase 1	Homo sapiens	13-29
19251588-9	2009	In contrast, heme oxygenase-1 was strongly suppressed by DFO, both in the absence and presence of LPS or iron.	Iron	105-109	heme oxygenase 1	Homo sapiens	13-29
19384082-2	2009	Excess free heme catalyzes the formation of reactive oxygen species, which leads to endothelial cell (EC) dysfunction as seen in numerous pathologic vascular conditions including systemic hypertension and diabetes, as well as in ischemia/reperfusion injury.The up-regulation of HO-1 can be achieved through the use of pharmaceutical agents such as metalloporphyrins and statins.	Reactive Oxygen Species	44-67	heme oxygenase 1	Homo sapiens	278-282
19384082-3	2009	In addition, atrial natriuretic peptide and nitric oxide donors are important modulators of the heme-HO system, either through induction of HO-1 or the increased biologic activity of its products.	Nitric Oxide	44-56	heme oxygenase 1	Homo sapiens	140-144
19384082-6	2009	Delivery of human HO-1 to hyperglycemic rats significantly lowers superoxide levels and prevents EC damage and sloughing of vascular EC into the circulation.	Superoxides	66-76	heme oxygenase 1	Homo sapiens	18-22
19244544-2	2009	Since HO-1 exerts potent antioxidant effects, we hypothesized that this enzyme inhibits ROS-induced cardiomyocyte hypertrophy.	Reactive Oxygen Species	88-91	heme oxygenase 1	Homo sapiens	6-10
19117929-3	2009	METHODS: The ability of eriodictyol to activate Nrf2 and to induce the phase 2 proteins heme-oxygenase (HO)-1 and NAD(P)H:quinone oxidoreductase (NQO)-1, and the cellular antioxidant glutathione (GSH) were analyzed.	eriodictyol	24-35	heme oxygenase 1	Homo sapiens	88-109
19245827-10	2009	In summary, these findings suggest that induction of HO-1 through a Smad-dependent mechanism is responsible for the cytoprotective effect of BMP6 in H(2)O(2)-mediated renal cell injury.	Hydrogen Peroxide	149-157	heme oxygenase 1	Homo sapiens	53-57
19526463-0	2009	Investigations of the posttranslational mechanism of arsenite-mediated downregulation of human cytochrome P4501A1 levels: the role of heme oxygenase-1.	arsenite	53-61	heme oxygenase 1	Homo sapiens	134-150
19526463-3	2009	We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1.	arsenite	20-28	heme oxygenase 1	Homo sapiens	37-53
19526463-7	2009	Together these findings demonstrate that a posttranslational mechanism involving decreases in the cellular heme pool by arsenite-induced HO-1 may contribute to arsenite-mediated downregulation of CYP1A1.	arsenite	160-168	heme oxygenase 1	Homo sapiens	137-141
19526463-3	2009	We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1.	arsenite	20-28	heme oxygenase 1	Homo sapiens	55-59
19526463-3	2009	We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1.	Heme	37-41	heme oxygenase 1	Homo sapiens	55-59
19526463-3	2009	We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1.	Heme	87-91	heme oxygenase 1	Homo sapiens	37-53
19526463-3	2009	We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1.	Heme	87-91	heme oxygenase 1	Homo sapiens	55-59
19526463-4	2009	Arsenite (5 microM), in HepG2 cells, induced HO-1 mRNA 7.4-fold over the 48 h observation period, and it upregulated HO-1 protein expression.	arsenite	0-8	heme oxygenase 1	Homo sapiens	45-49
19526463-4	2009	Arsenite (5 microM), in HepG2 cells, induced HO-1 mRNA 7.4-fold over the 48 h observation period, and it upregulated HO-1 protein expression.	arsenite	0-8	heme oxygenase 1	Homo sapiens	117-121
19526463-5	2009	Arsenite decreased the induction of CYP1A1 by a PAH, benzo[k]fluoranthene (BKF), by 50%; and transfection of HepG2 cells with siRNA targeting the human HO-1 gene, reduced the arsenite downregulation of BKF-induced CYP1A1 from 54% to 27%, relative to untransfected cells.	arsenite	0-8	heme oxygenase 1	Homo sapiens	152-156
19526463-5	2009	Arsenite decreased the induction of CYP1A1 by a PAH, benzo[k]fluoranthene (BKF), by 50%; and transfection of HepG2 cells with siRNA targeting the human HO-1 gene, reduced the arsenite downregulation of BKF-induced CYP1A1 from 54% to 27%, relative to untransfected cells.	Polycyclic Aromatic Hydrocarbons	48-51	heme oxygenase 1	Homo sapiens	152-156
19526463-5	2009	Arsenite decreased the induction of CYP1A1 by a PAH, benzo[k]fluoranthene (BKF), by 50%; and transfection of HepG2 cells with siRNA targeting the human HO-1 gene, reduced the arsenite downregulation of BKF-induced CYP1A1 from 54% to 27%, relative to untransfected cells.	benzo(k)fluoranthene	53-73	heme oxygenase 1	Homo sapiens	152-156
19526463-5	2009	Arsenite decreased the induction of CYP1A1 by a PAH, benzo[k]fluoranthene (BKF), by 50%; and transfection of HepG2 cells with siRNA targeting the human HO-1 gene, reduced the arsenite downregulation of BKF-induced CYP1A1 from 54% to 27%, relative to untransfected cells.	benzo(k)fluoranthene	75-78	heme oxygenase 1	Homo sapiens	152-156
19526463-5	2009	Arsenite decreased the induction of CYP1A1 by a PAH, benzo[k]fluoranthene (BKF), by 50%; and transfection of HepG2 cells with siRNA targeting the human HO-1 gene, reduced the arsenite downregulation of BKF-induced CYP1A1 from 54% to 27%, relative to untransfected cells.	arsenite	175-183	heme oxygenase 1	Homo sapiens	152-156
19526463-5	2009	Arsenite decreased the induction of CYP1A1 by a PAH, benzo[k]fluoranthene (BKF), by 50%; and transfection of HepG2 cells with siRNA targeting the human HO-1 gene, reduced the arsenite downregulation of BKF-induced CYP1A1 from 54% to 27%, relative to untransfected cells.	benzo(k)fluoranthene	202-205	heme oxygenase 1	Homo sapiens	152-156
19526463-7	2009	Together these findings demonstrate that a posttranslational mechanism involving decreases in the cellular heme pool by arsenite-induced HO-1 may contribute to arsenite-mediated downregulation of CYP1A1.	Heme	107-111	heme oxygenase 1	Homo sapiens	137-141
19526463-7	2009	Together these findings demonstrate that a posttranslational mechanism involving decreases in the cellular heme pool by arsenite-induced HO-1 may contribute to arsenite-mediated downregulation of CYP1A1.	arsenite	120-128	heme oxygenase 1	Homo sapiens	137-141
19250338-0	2009	HO-1-mediated macroautophagy: a mechanism for unregulated iron deposition in aging and degenerating neural tissues.	Iron	58-62	heme oxygenase 1	Homo sapiens	0-4
19250338-2	2009	We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria.	Iron	140-144	heme oxygenase 1	Homo sapiens	32-48
19250338-6	2009	Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways.	Iron	92-96	heme oxygenase 1	Homo sapiens	6-10
19250338-6	2009	Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways.	Iron	137-141	heme oxygenase 1	Homo sapiens	6-10
19250338-7	2009	Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron.	Iron	143-147	heme oxygenase 1	Homo sapiens	6-10
19250338-2	2009	We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria.	Iron	140-144	heme oxygenase 1	Homo sapiens	50-54
19250338-5	2009	HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity.	Iron	39-43	heme oxygenase 1	Homo sapiens	0-4
19250338-5	2009	HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity.	Sulfur	48-54	heme oxygenase 1	Homo sapiens	0-4
19289500-0	2009	Analysis of nitric oxide-stabilized mRNAs in human fibroblasts reveals HuR-dependent heme oxygenase 1 upregulation.	Nitric Oxide	12-24	heme oxygenase 1	Homo sapiens	85-101
19289500-1	2009	We previously observed that nitric oxide (NO) exposure increases the stability of mRNAs encoding heme oxygenase 1 (HO-1) and TIEG-1 in human and mouse fibroblasts.	Nitric Oxide	28-40	heme oxygenase 1	Homo sapiens	97-113
19289500-1	2009	We previously observed that nitric oxide (NO) exposure increases the stability of mRNAs encoding heme oxygenase 1 (HO-1) and TIEG-1 in human and mouse fibroblasts.	Nitric Oxide	28-40	heme oxygenase 1	Homo sapiens	115-119
19323979-5	2009	Treatment of HUVEC with ATN-224 caused increased superoxide levels, phospho-ERK signalling, nuclear NRF1 expression, HO-1 expression and induction of the anti-apoptotic proteins P21, BCL2 and BCLXL.	tetrathiomolybdate	24-31	heme oxygenase 1	Homo sapiens	117-121
19388153-9	2009	Arecoline was also found to elevate HO-1 mRNA and protein expression in a dose-dependent manner (P &lt; 0.05).	Arecoline	0-9	heme oxygenase 1	Homo sapiens	36-40
19388153-10	2009	CONCLUSIONS: Taken together, the data presented here demonstrated that HO-1 expression is significantly upregulated in OSF from areca quid chewers, and arecoline may be responsible for the enhanced HO-1 expression in vivo.	Arecoline	152-161	heme oxygenase 1	Homo sapiens	198-202
18485456-0	2009	Upregulation of heme oxygenase-1 as a host mechanism for protection against nitric oxide-induced damage in human renal epithelial cells.	Nitric Oxide	76-88	heme oxygenase 1	Homo sapiens	16-32
19651797-5	2009	Two electrophiles, 4-hydroxynonenal (HNE) and acrolein, induced the expression of phase II genes (GCLC, GCLM, NQO1, NQO2, HO-1, and GSTM-1).	4-hydroxy-2-nonenal	19-35	heme oxygenase 1	Homo sapiens	122-126
19651797-5	2009	Two electrophiles, 4-hydroxynonenal (HNE) and acrolein, induced the expression of phase II genes (GCLC, GCLM, NQO1, NQO2, HO-1, and GSTM-1).	Acrolein	46-54	heme oxygenase 1	Homo sapiens	122-126
18485456-2	2009	METHODS: Heme oxygenase-1 expression was investigated in the human renal epithelial cell line A498 in response to the uropathogenic Escherichia coli (UPEC) strain IA2, the NO-donor DETA/NONOate (DETA/NO), and proinflammatory cytokines (interleukin-1beta, tumor necrosis factor-alpha, and interferon-gamma) using reverse transcriptase polymerase chain reaction and Western blot analysis.	DEET	181-185	heme oxygenase 1	Homo sapiens	9-25
18485456-2	2009	METHODS: Heme oxygenase-1 expression was investigated in the human renal epithelial cell line A498 in response to the uropathogenic Escherichia coli (UPEC) strain IA2, the NO-donor DETA/NONOate (DETA/NO), and proinflammatory cytokines (interleukin-1beta, tumor necrosis factor-alpha, and interferon-gamma) using reverse transcriptase polymerase chain reaction and Western blot analysis.	pelargonic acid	186-193	heme oxygenase 1	Homo sapiens	9-25
19243105-1	2009	The active site electronic structure of the azide complex of substrate-bound human heme oxygenase 1 (hHO) has been investigated by (1)H NMR spectroscopy to shed light on the orbital/spin ground state as an indicator of the unique distal pocket environment of the enzyme.	Azides	44-49	heme oxygenase 1	Homo sapiens	83-99
18485456-2	2009	METHODS: Heme oxygenase-1 expression was investigated in the human renal epithelial cell line A498 in response to the uropathogenic Escherichia coli (UPEC) strain IA2, the NO-donor DETA/NONOate (DETA/NO), and proinflammatory cytokines (interleukin-1beta, tumor necrosis factor-alpha, and interferon-gamma) using reverse transcriptase polymerase chain reaction and Western blot analysis.	DEET	195-199	heme oxygenase 1	Homo sapiens	9-25
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	Hemin	26-31	heme oxygenase 1	Homo sapiens	13-17
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	Hemin	26-31	heme oxygenase 1	Homo sapiens	54-58
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	Hemin	26-31	heme oxygenase 1	Homo sapiens	54-58
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	DEET	36-40	heme oxygenase 1	Homo sapiens	54-58
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	DEET	36-40	heme oxygenase 1	Homo sapiens	54-58
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	Glutathione	89-100	heme oxygenase 1	Homo sapiens	13-17
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	DEET	160-164	heme oxygenase 1	Homo sapiens	13-17
18485456-4	2009	RESULTS: The HO-1 inducer hemin and DETA/NO increased HO-1 expression in A498 cells, and glutathione depletion further increased HO-1 expression in response to DETA/NO and hemin.	Hemin	172-177	heme oxygenase 1	Homo sapiens	13-17
18485456-9	2009	CONCLUSIONS: The expression of HO-1 increased in human renal epithelial cells in response to NO, and the expression was further enhanced in glutathione-depleted cells.	Glutathione	140-151	heme oxygenase 1	Homo sapiens	31-35
19389234-1	2009	BACKGROUND: Heme oxygenase-1 is an inducible cytoprotective enzyme which handles oxidative stress by generating anti-oxidant bilirubin and vasodilating carbon monoxide.	Bilirubin	125-134	heme oxygenase 1	Homo sapiens	12-28
19389234-1	2009	BACKGROUND: Heme oxygenase-1 is an inducible cytoprotective enzyme which handles oxidative stress by generating anti-oxidant bilirubin and vasodilating carbon monoxide.	Carbon Monoxide	152-167	heme oxygenase 1	Homo sapiens	12-28
19389234-2	2009	A (GT)n dinucleotide repeat and a -413A&gt;T single nucleotide polymorphism have been reported in the promoter region of HMOX1 to both influence the occurrence of coronary artery disease and myocardial infarction.	(gt)n dinucleotide	2-20	heme oxygenase 1	Homo sapiens	121-126
19239904-0	2009	Sofalcone, an anti-ulcer chalcone derivative, suppresses inflammatory crosstalk between macrophages and adipocytes and adipocyte differentiation: implication of heme-oxygenase-1 induction.	sofalcone	0-9	heme oxygenase 1	Homo sapiens	161-177
19239904-4	2009	The suppressive effect of sofalcone on NO production was attenuated by treatment with tin-protoporphyrin (SnPP), a heme-oxygenase (HO)-1 inhibitor.	sofalcone	26-35	heme oxygenase 1	Homo sapiens	115-136
19239904-4	2009	The suppressive effect of sofalcone on NO production was attenuated by treatment with tin-protoporphyrin (SnPP), a heme-oxygenase (HO)-1 inhibitor.	tin protoporphyrin IX	86-104	heme oxygenase 1	Homo sapiens	115-136
19239904-4	2009	The suppressive effect of sofalcone on NO production was attenuated by treatment with tin-protoporphyrin (SnPP), a heme-oxygenase (HO)-1 inhibitor.	S-Nitroso-N-propionyl-D,L-penicillamine	106-110	heme oxygenase 1	Homo sapiens	115-136
19371606-0	2009	Induction of heme oxygenase 1 by arsenite inhibits cytokine-induced monocyte adhesion to human endothelial cells.	arsenite	33-41	heme oxygenase 1	Homo sapiens	13-29
19371606-2	2009	Arsenite, as an oxidative stressor, is a potent inducer of HO-1 in human and rodent cells.	arsenite	0-8	heme oxygenase 1	Homo sapiens	59-63
19371606-3	2009	In this study, we investigated the mechanistic role of arsenite-induced HO-1 in modulating tumor necrosis factor alpha (TNF-alpha) induced monocyte adhesion to human umbilical vein endothelial cells (HUVEC).	arsenite	55-63	heme oxygenase 1	Homo sapiens	72-76
19371606-4	2009	Arsenite pretreatment, which upregulated HO-1 in a time- and concentration-dependent manner, inhibited TNF-alpha-induced monocyte adhesion to HUVEC and intercellular adhesion molecule 1 protein expression by 50% and 40%, respectively.	arsenite	0-8	heme oxygenase 1	Homo sapiens	41-45
19371606-5	2009	Importantly, knockdown of HO-1 by small interfering RNA abolished the arsenite-induced inhibitory effects.	arsenite	70-78	heme oxygenase 1	Homo sapiens	26-30
19371606-6	2009	These results indicate that induction of HO-1 by arsenite inhibits the cytokine-induced monocyte adhesion to HUVEC by suppressing adhesion molecule expression.	arsenite	49-57	heme oxygenase 1	Homo sapiens	41-45
19371606-7	2009	These findings established an important mechanistic link between the functional monocyte adhesion properties of HUVEC and the induction of HO-1 by arsenite.	arsenite	147-155	heme oxygenase 1	Homo sapiens	139-143
19336889-1	2009	We previously reported that eupatilin (5,7-dihydroxy-3,4,6-trimethoxyflavone) extracted from Artemisia asiaitica, augmented the cellular antioxidant defense capacity through induction of the antioxidant protein heme oxygenase-1 (HO-1), thereby protecting ileal smooth muscle cells from nonsteroidal anti-inflammatory drug (NSAID)-induced intestinal toxicity.	eupatilin	28-37	heme oxygenase 1	Homo sapiens	211-227
19336889-10	2009	We confirmed that ZnPP, an HO-1 inhibitor, repressed eupatilin-induced HO-1 activity and showed the protective effect of eupatilin against indomethacin-induced cell injury.	eupatilin	53-62	heme oxygenase 1	Homo sapiens	71-75
19336889-1	2009	We previously reported that eupatilin (5,7-dihydroxy-3,4,6-trimethoxyflavone) extracted from Artemisia asiaitica, augmented the cellular antioxidant defense capacity through induction of the antioxidant protein heme oxygenase-1 (HO-1), thereby protecting ileal smooth muscle cells from nonsteroidal anti-inflammatory drug (NSAID)-induced intestinal toxicity.	eupatilin	28-37	heme oxygenase 1	Homo sapiens	229-233
19336889-11	2009	The data suggested that HO-1 was partly responsible for the eupatilin-mediated protective action of esophageal epithelial cells against indomethacin via both ERKs and PI3K/Akt pathways as well as Nrf2 translocation.	eupatilin	60-69	heme oxygenase 1	Homo sapiens	24-28
19336889-1	2009	We previously reported that eupatilin (5,7-dihydroxy-3,4,6-trimethoxyflavone) extracted from Artemisia asiaitica, augmented the cellular antioxidant defense capacity through induction of the antioxidant protein heme oxygenase-1 (HO-1), thereby protecting ileal smooth muscle cells from nonsteroidal anti-inflammatory drug (NSAID)-induced intestinal toxicity.	eupatilin	39-76	heme oxygenase 1	Homo sapiens	211-227
19336889-11	2009	The data suggested that HO-1 was partly responsible for the eupatilin-mediated protective action of esophageal epithelial cells against indomethacin via both ERKs and PI3K/Akt pathways as well as Nrf2 translocation.	Indomethacin	136-148	heme oxygenase 1	Homo sapiens	24-28
19336889-1	2009	We previously reported that eupatilin (5,7-dihydroxy-3,4,6-trimethoxyflavone) extracted from Artemisia asiaitica, augmented the cellular antioxidant defense capacity through induction of the antioxidant protein heme oxygenase-1 (HO-1), thereby protecting ileal smooth muscle cells from nonsteroidal anti-inflammatory drug (NSAID)-induced intestinal toxicity.	eupatilin	39-76	heme oxygenase 1	Homo sapiens	229-233
19336889-7	2009	Eupatilin-induced HO-1 expression and Nrf2 were partly attenuated by MEK inhibitor PD98059 and almost completely by phosphatidyl-inactiol 3 kinase (PI3K) inhibitor LY294002, but not by c-Jun N-terminal kinase (JNK) inhibitor SP600125 or p38 mitogen activated protein kinase (MAPK) inhibitor SB202190.	eupatilin	0-9	heme oxygenase 1	Homo sapiens	18-22
19336889-7	2009	Eupatilin-induced HO-1 expression and Nrf2 were partly attenuated by MEK inhibitor PD98059 and almost completely by phosphatidyl-inactiol 3 kinase (PI3K) inhibitor LY294002, but not by c-Jun N-terminal kinase (JNK) inhibitor SP600125 or p38 mitogen activated protein kinase (MAPK) inhibitor SB202190.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	83-90	heme oxygenase 1	Homo sapiens	18-22
19336889-7	2009	Eupatilin-induced HO-1 expression and Nrf2 were partly attenuated by MEK inhibitor PD98059 and almost completely by phosphatidyl-inactiol 3 kinase (PI3K) inhibitor LY294002, but not by c-Jun N-terminal kinase (JNK) inhibitor SP600125 or p38 mitogen activated protein kinase (MAPK) inhibitor SB202190.	pyrazolanthrone	225-233	heme oxygenase 1	Homo sapiens	18-22
19336889-7	2009	Eupatilin-induced HO-1 expression and Nrf2 were partly attenuated by MEK inhibitor PD98059 and almost completely by phosphatidyl-inactiol 3 kinase (PI3K) inhibitor LY294002, but not by c-Jun N-terminal kinase (JNK) inhibitor SP600125 or p38 mitogen activated protein kinase (MAPK) inhibitor SB202190.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	291-299	heme oxygenase 1	Homo sapiens	18-22
19336889-10	2009	We confirmed that ZnPP, an HO-1 inhibitor, repressed eupatilin-induced HO-1 activity and showed the protective effect of eupatilin against indomethacin-induced cell injury.	zinc protoporphyrin	18-22	heme oxygenase 1	Homo sapiens	27-31
19336889-10	2009	We confirmed that ZnPP, an HO-1 inhibitor, repressed eupatilin-induced HO-1 activity and showed the protective effect of eupatilin against indomethacin-induced cell injury.	zinc protoporphyrin	18-22	heme oxygenase 1	Homo sapiens	71-75
19336889-10	2009	We confirmed that ZnPP, an HO-1 inhibitor, repressed eupatilin-induced HO-1 activity and showed the protective effect of eupatilin against indomethacin-induced cell injury.	eupatilin	53-62	heme oxygenase 1	Homo sapiens	27-31
19407950-9	2009	Compared with the SP600125 group, the expressions of JNK, c-Jun, P-c-Jun and HO-1 mRNA and its protein in the TXLSP+SP600125 group were significantly increased at different time points (P&lt;0.05, P&lt;0.01).	pyrazolanthrone	116-124	heme oxygenase 1	Homo sapiens	77-81
19131520-4	2009	This allows measurement of bilirubin formation after incorporation of full-length CPR and heme oxygenase-1 (HO-1) into a membrane environment.	Bilirubin	27-36	heme oxygenase 1	Homo sapiens	90-106
19131520-4	2009	This allows measurement of bilirubin formation after incorporation of full-length CPR and heme oxygenase-1 (HO-1) into a membrane environment.	Bilirubin	27-36	heme oxygenase 1	Homo sapiens	108-112
19131520-9	2009	These results not only show that HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity but also provide for a chemically defined system to be used to examine the function of full-length HO-1 in a membrane environment.	Hydrogen Peroxide	48-65	heme oxygenase 1	Homo sapiens	33-37
19131520-9	2009	These results not only show that HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity but also provide for a chemically defined system to be used to examine the function of full-length HO-1 in a membrane environment.	Hydrogen Peroxide	48-65	heme oxygenase 1	Homo sapiens	89-93
19131520-9	2009	These results not only show that HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity but also provide for a chemically defined system to be used to examine the function of full-length HO-1 in a membrane environment.	Hydrogen Peroxide	48-65	heme oxygenase 1	Homo sapiens	89-93
19243019-8	2009	Among polymorphisms in other genes, only the (GT)n repeat polymorphism in the HMOX1 promoter region showed association with TBIL levels in the Uyghur population, but not in the Han and Kazak populations.	Bilirubin	124-128	heme oxygenase 1	Homo sapiens	78-83
19136476-0	2009	15-Deoxy-Delta12,14-prostaglandin J2 upregulates the expression of heme oxygenase-1 and subsequently matrix metalloproteinase-1 in human breast cancer cells: possible roles of iron and ROS.	Iron	176-180	heme oxygenase 1	Homo sapiens	67-127
19136476-0	2009	15-Deoxy-Delta12,14-prostaglandin J2 upregulates the expression of heme oxygenase-1 and subsequently matrix metalloproteinase-1 in human breast cancer cells: possible roles of iron and ROS.	Reactive Oxygen Species	185-188	heme oxygenase 1	Homo sapiens	67-127
19136476-3	2009	Treatment of MCF-7 and MDA-MB-231 cells with 30 microM of 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) increased the expression of HO-1, which preceded the induction of matrix metalloproteinases (MMPs).	14-prostaglandin j2	75-94	heme oxygenase 1	Homo sapiens	134-138
19136476-4	2009	The 15d-PGJ2-induced upregulation of MMP-1 was abrogated by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) as well as introduction of HO-1 short interfering RNA.	15-deoxy-delta(12,14)-prostaglandin J2	4-12	heme oxygenase 1	Homo sapiens	64-68
19136476-4	2009	The 15d-PGJ2-induced upregulation of MMP-1 was abrogated by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) as well as introduction of HO-1 short interfering RNA.	15-deoxy-delta(12,14)-prostaglandin J2	4-12	heme oxygenase 1	Homo sapiens	136-140
19136476-4	2009	The 15d-PGJ2-induced upregulation of MMP-1 was abrogated by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) as well as introduction of HO-1 short interfering RNA.	zinc protoporphyrin	79-101	heme oxygenase 1	Homo sapiens	64-68
19136476-4	2009	The 15d-PGJ2-induced upregulation of MMP-1 was abrogated by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP) as well as introduction of HO-1 short interfering RNA.	zinc protoporphyrin	103-107	heme oxygenase 1	Homo sapiens	64-68
19136476-5	2009	In addition, HO-1 inducers, such as cobalt protoporphyrin IX and hemin, upregulated the expression of MMP-1.	cobaltiprotoporphyrin	36-60	heme oxygenase 1	Homo sapiens	13-17
19136476-7	2009	Treatment with the HO-1 inhibitor ZnPP abolished the migrative phenotype of 15d-PGJ2-treated MCF-7 cells.	zinc protoporphyrin	34-38	heme oxygenase 1	Homo sapiens	19-23
19136476-7	2009	Treatment with the HO-1 inhibitor ZnPP abolished the migrative phenotype of 15d-PGJ2-treated MCF-7 cells.	9-deoxy-delta-9-prostaglandin D2	80-84	heme oxygenase 1	Homo sapiens	19-23
19136476-9	2009	We hypothesize that excess iron, released as a consequence HO-1 activity induced by 15d-PGJ2, is transiently available for the stimulation of intracellular ROS generation and subsequently MMP-1 expression.	Iron	27-31	heme oxygenase 1	Homo sapiens	59-63
19136476-9	2009	We hypothesize that excess iron, released as a consequence HO-1 activity induced by 15d-PGJ2, is transiently available for the stimulation of intracellular ROS generation and subsequently MMP-1 expression.	15-deoxy-delta(12,14)-prostaglandin J2	84-92	heme oxygenase 1	Homo sapiens	59-63
19136476-9	2009	We hypothesize that excess iron, released as a consequence HO-1 activity induced by 15d-PGJ2, is transiently available for the stimulation of intracellular ROS generation and subsequently MMP-1 expression.	Reactive Oxygen Species	156-159	heme oxygenase 1	Homo sapiens	59-63
19136476-12	2009	In conclusion, 15d-PGJ2 upregulates MMP-1 expression via induction of HO-1 and subsequent production of iron capable of generating ROS, which may contribute to increased metastasis and invasiveness of the human breast cancer cells.	15-deoxy-delta(12,14)-prostaglandin J2	15-23	heme oxygenase 1	Homo sapiens	70-74
18952926-0	2009	Reactivation of optic nerve head astrocytes by TGF-beta2 and H2O2 is accompanied by increased Hsp32 and Hsp47 expression.	Hydrogen Peroxide	61-65	heme oxygenase 1	Homo sapiens	94-99
18952926-8	2009	Exposure of the cells to H(2)O(2) could increase both Hsp32 and -47.	Hydrogen Peroxide	25-33	heme oxygenase 1	Homo sapiens	54-59
18996220-0	2009	Sodium arsenite induces ROS generation, DNA oxidative damage, HO-1 and c-Myc proteins, NF-kappaB activation and cell proliferation in human breast cancer MCF-7 cells.	sodium arsenite	0-15	heme oxygenase 1	Homo sapiens	62-66
19238116-2	2009	This study investigated the genetic variants of four bilirubin metabolism genes--heme oxygenase-1 (HMOX1), biliverdin reductase A (BLVRA), solute carrier organic anion transporter family member 1B1 (SLCO1B1), and uridine diphosphate glycosyltransferase 1A1 (UGT1A1)--in relation to TBIL levels and CAD.	Bilirubin	53-62	heme oxygenase 1	Homo sapiens	99-104
18996220-5	2009	ROS-mediated DNA damage as measured by the presence of 8-OHdG DNA-adducts in their nuclei, IkappaB phosphorylation, NF-kappaB activation and increases in c-Myc and HO-1 protein levels were also observed, suggesting that these factors play a relevant role in the arsenite induced MCF-7 cell recruitment into the S-phase of the cell cycle and cell proliferation observed.	ros	0-3	heme oxygenase 1	Homo sapiens	164-168
19374863-6	2009	Together with AG-126, structurally related benzylidenemalononitrile tyrphostins AG-9, AG-10, AG-18, and AG-1288 were able to up-regulate the expression of HO-1 and several other genes, although with relatively less efficacy.	Benzylidenemalononitrile	43-67	heme oxygenase 1	Homo sapiens	155-159
19174156-0	2009	KB-34, a newly synthesized chalcone derivative, inhibits lipopolysaccharide-stimulated nitric oxide production in RAW 264.7 macrophages via heme oxygenase-1 induction and blockade of activator protein-1.	kb-34	0-5	heme oxygenase 1	Homo sapiens	140-156
19174156-7	2009	Treatment with SnPP, a selective inhibitor of HO-1, reversed the KB-34-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by KB-34.	S-Nitroso-N-propionyl-D,L-penicillamine	15-19	heme oxygenase 1	Homo sapiens	46-50
19174156-7	2009	Treatment with SnPP, a selective inhibitor of HO-1, reversed the KB-34-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by KB-34.	S-Nitroso-N-propionyl-D,L-penicillamine	15-19	heme oxygenase 1	Homo sapiens	130-134
19174156-7	2009	Treatment with SnPP, a selective inhibitor of HO-1, reversed the KB-34-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by KB-34.	kb-34	65-70	heme oxygenase 1	Homo sapiens	46-50
19174156-7	2009	Treatment with SnPP, a selective inhibitor of HO-1, reversed the KB-34-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by KB-34.	kb-34	65-70	heme oxygenase 1	Homo sapiens	130-134
19174156-7	2009	Treatment with SnPP, a selective inhibitor of HO-1, reversed the KB-34-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by KB-34.	Nitrites	94-101	heme oxygenase 1	Homo sapiens	46-50
19174156-7	2009	Treatment with SnPP, a selective inhibitor of HO-1, reversed the KB-34-mediated inhibition of nitrite production, suggesting that HO-1 plays an important role in the suppression of NO production by KB-34.	Nitrites	94-101	heme oxygenase 1	Homo sapiens	130-134
19154785-8	2009	UFP also up-regulated heme oxygenase-1 (HO-1) and tissue factor (TF) mRNA expression, and pretreatment with the antioxidant N-acetylcysteine significantly decreased their expression.	Acetylcysteine	124-140	heme oxygenase 1	Homo sapiens	22-38
19154785-10	2009	Treatment with the JNK inhibitor SP600125 and silencing of both JNK1 and JNK2 with siRNA inhibited UFP-stimulated O(2)(-) production and mRNA expression of HO-1 and TF.	pyrazolanthrone	33-41	heme oxygenase 1	Homo sapiens	156-167
19374863-6	2009	Together with AG-126, structurally related benzylidenemalononitrile tyrphostins AG-9, AG-10, AG-18, and AG-1288 were able to up-regulate the expression of HO-1 and several other genes, although with relatively less efficacy.	Tyrphostins	68-79	heme oxygenase 1	Homo sapiens	155-159
19135260-0	2009	Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand.	Heme	9-13	heme oxygenase 1	Homo sapiens	49-65
19100829-7	2009	OxLDL-mediated induction of the oxidative stress responsive gene, heme oxygenase-1, was also abolished by H(2)S.	Hydrogen Sulfide	106-111	heme oxygenase 1	Homo sapiens	66-82
19299217-5	2009	According to our previous study, AVF failure was associated with a longer dinucleotide (GT)n repeat (n &gt; or = 30) in the promoter of the heme oxygenase-1 (HO-1) gene.	Dinucleoside Phosphates	74-86	heme oxygenase 1	Homo sapiens	140-156
19299217-5	2009	According to our previous study, AVF failure was associated with a longer dinucleotide (GT)n repeat (n &gt; or = 30) in the promoter of the heme oxygenase-1 (HO-1) gene.	Dinucleoside Phosphates	74-86	heme oxygenase 1	Homo sapiens	158-162
19236154-3	2009	Data generated by various groups indicate that Nrf2 induces the expression of a group of cytoprotective, antixenobiotic and antioxidant enzymes that include heme oxygenase-1, NAD(P)H:quinone oxidoreductase and enzymes of glutathione (GSH) metabolism such as gamma-glutamyl cysteine ligase, GSH transferases and so on.	Glutathione	221-232	heme oxygenase 1	Homo sapiens	157-173
19236154-3	2009	Data generated by various groups indicate that Nrf2 induces the expression of a group of cytoprotective, antixenobiotic and antioxidant enzymes that include heme oxygenase-1, NAD(P)H:quinone oxidoreductase and enzymes of glutathione (GSH) metabolism such as gamma-glutamyl cysteine ligase, GSH transferases and so on.	Glutathione	234-237	heme oxygenase 1	Homo sapiens	157-173
19212657-1	2009	Human heme oxygenase-1 (hHO-1) is a rate-limiting enzyme in heme metabolism.	Heme	6-10	heme oxygenase 1	Homo sapiens	24-29
19212657-3	2009	Site-directed mutagenesis studies indicate that the proximal residue histidine 25 (His25) plays a key role in hHO-1 activity.	Histidine	69-78	heme oxygenase 1	Homo sapiens	110-115
19212657-10	2009	By supplementing imidazole, the HO-1 activity was restored approximately 90% to its normal level.	imidazole	17-26	heme oxygenase 1	Homo sapiens	32-36
19135260-0	2009	Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand.	Selenocysteine	71-85	heme oxygenase 1	Homo sapiens	49-65
19135260-0	2009	Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand.	Iron	115-119	heme oxygenase 1	Homo sapiens	49-65
19135260-1	2009	To characterize heme oxygenase with a selenocysteine (SeCys) as the proximal iron ligand, we have expressed truncated human heme oxygenase-1 (hHO-1) His25Cys, in which Cys-25 is the only cysteine, in the Escherichia coli cysteine auxotroph strain BL21(DE3)cys.	Selenocysteine	38-52	heme oxygenase 1	Homo sapiens	124-140
19135260-1	2009	To characterize heme oxygenase with a selenocysteine (SeCys) as the proximal iron ligand, we have expressed truncated human heme oxygenase-1 (hHO-1) His25Cys, in which Cys-25 is the only cysteine, in the Escherichia coli cysteine auxotroph strain BL21(DE3)cys.	Selenocysteine	38-52	heme oxygenase 1	Homo sapiens	142-147
19135260-5	2009	The heme-His25SeCys hHO-1 complex could be prepared by either (a) supplementing the overexpression medium with heme, or (b) reconstituting the purified apoprotein with heme.	Heme	4-8	heme oxygenase 1	Homo sapiens	20-25
19135260-5	2009	The heme-His25SeCys hHO-1 complex could be prepared by either (a) supplementing the overexpression medium with heme, or (b) reconstituting the purified apoprotein with heme.	Heme	111-115	heme oxygenase 1	Homo sapiens	20-25
19135260-11	2009	47 (2008) 3480-3482 ], indicate that a selenyl radical is formed in the hHO-1 His25SeCys mutant that adds to a heme vinyl group.	selenyl radical	39-54	heme oxygenase 1	Homo sapiens	72-77
19135260-11	2009	47 (2008) 3480-3482 ], indicate that a selenyl radical is formed in the hHO-1 His25SeCys mutant that adds to a heme vinyl group.	Heme	111-115	heme oxygenase 1	Homo sapiens	72-77
19122175-0	2009	Induction of prostacyclin by steady laminar shear stress suppresses tumor necrosis factor-alpha biosynthesis via heme oxygenase-1 in human endothelial cells.	Epoprostenol	13-25	heme oxygenase 1	Homo sapiens	113-129
19129475-5	2009	Although the first phase of HO-1 induction at 6 h was accomplished by AC-derived sphingosine-1-phosphate (S1P) acting via S1P receptor 1, the second wave of HO-1 induction at 24 h was attributed to autocrine signaling of vascular endothelial growth factor A (VEGFA), whose expression and release were facilitated by S1P.	Charcoal	70-72	heme oxygenase 1	Homo sapiens	28-32
19129475-5	2009	Although the first phase of HO-1 induction at 6 h was accomplished by AC-derived sphingosine-1-phosphate (S1P) acting via S1P receptor 1, the second wave of HO-1 induction at 24 h was attributed to autocrine signaling of vascular endothelial growth factor A (VEGFA), whose expression and release were facilitated by S1P.	sphingosine 1-phosphate	81-104	heme oxygenase 1	Homo sapiens	28-32
19417726-3	2009	It has been clinically demonstrated that the immunoreactivities of intrarenal heme oxygenase-1 (HO-1) and 4-hydroxy-2-nonenal (4-HNE) markers of reactive oxygen species (ROS) and those of intrarenal angiotensinogen (AGT) and angiotensin II (Ang II) markers of renin angiotensin system (RAS) in IgA nephropathy patients were significantly increased as compared to those of control subjects.	Reactive Oxygen Species	145-168	heme oxygenase 1	Homo sapiens	78-94
19417726-3	2009	It has been clinically demonstrated that the immunoreactivities of intrarenal heme oxygenase-1 (HO-1) and 4-hydroxy-2-nonenal (4-HNE) markers of reactive oxygen species (ROS) and those of intrarenal angiotensinogen (AGT) and angiotensin II (Ang II) markers of renin angiotensin system (RAS) in IgA nephropathy patients were significantly increased as compared to those of control subjects.	Reactive Oxygen Species	170-173	heme oxygenase 1	Homo sapiens	78-94
19122175-8	2009	Carbacyclin, an agonist of IP, induced HO-1.	carboprostacyclin	0-11	heme oxygenase 1	Homo sapiens	39-43
19122175-9	2009	Similarly to inhibition of prostacyclin biosynthesis or activity, the novel imidazole-based HO-1 inhibitor QC15 reversed TNF-alpha reduction by LSS.	imidazole	76-85	heme oxygenase 1	Homo sapiens	92-96
19122175-10	2009	These findings suggest that inhibition of COX-2-dependent prostacyclin might contribute to acceleration of atherogenesis in patients taking traditional nonsteroidal antiinflammatory drugs (NSAIDs) and NSAIDs selective for COX-2 through downregulation of HO-1, which halts TNF-alpha generation in human endothelial cells.	Epoprostenol	58-70	heme oxygenase 1	Homo sapiens	254-258
19033392-9	2009	A significant inhibition of the expression of hmox1 and nqo1 mRNAs and CD86 expression was found in 1-chloro 2,4-dinitrobenzene-treated THP-1 cells preincubated with N-acetyl cysteine, a glutathione precursor.	Dinitrochlorobenzene	100-127	heme oxygenase 1	Homo sapiens	46-51
18842672-11	2009	CONCLUSIONS: Collectively, we suggest that HO-1 induced by TMP might, at least in part, protect against gentamicin-induced nephrotoxicity through antiapoptotic and anti-inflammatory mechanisms, and that it may have therapeutic potential for patients with renal disease.	tetramethylpyrazine	59-62	heme oxygenase 1	Homo sapiens	43-47
18842672-11	2009	CONCLUSIONS: Collectively, we suggest that HO-1 induced by TMP might, at least in part, protect against gentamicin-induced nephrotoxicity through antiapoptotic and anti-inflammatory mechanisms, and that it may have therapeutic potential for patients with renal disease.	Gentamicins	104-114	heme oxygenase 1	Homo sapiens	43-47
19036700-0	2009	Heme oxygenase-1 expression enhances vascular endothelial resistance to complement-mediated injury through induction of decay-accelerating factor: a role for increased bilirubin and ferritin.	Bilirubin	168-177	heme oxygenase 1	Homo sapiens	0-16
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Heme	19-23	heme oxygenase 1	Homo sapiens	27-43
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Heme	19-23	heme oxygenase 1	Homo sapiens	45-49
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Carbon Monoxide	61-76	heme oxygenase 1	Homo sapiens	27-43
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Carbon Monoxide	61-76	heme oxygenase 1	Homo sapiens	45-49
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Biliverdine	78-88	heme oxygenase 1	Homo sapiens	27-43
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Biliverdine	78-88	heme oxygenase 1	Homo sapiens	45-49
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Iron	99-103	heme oxygenase 1	Homo sapiens	27-43
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Iron	99-103	heme oxygenase 1	Homo sapiens	45-49
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Iron	105-107	heme oxygenase 1	Homo sapiens	27-43
19036700-1	2009	Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe).	Iron	105-107	heme oxygenase 1	Homo sapiens	45-49
19036700-5	2009	In contrast, HO-1 agonists hemin and cobalt protoporphyrin IX significantly increased DAF protein expression, reflecting an increase in transcription and steady-state mRNA.	Cobalt	37-43	heme oxygenase 1	Homo sapiens	13-17
19036700-5	2009	In contrast, HO-1 agonists hemin and cobalt protoporphyrin IX significantly increased DAF protein expression, reflecting an increase in transcription and steady-state mRNA.	protoporphyrin IX	44-61	heme oxygenase 1	Homo sapiens	13-17
19036700-6	2009	Adenoviral-mediated overexpression of HO-1 increased DAF expression, enhancing protection against C3 deposition and complement-mediated lysis, and this was reversed by DAF inhibitory monoclonal antibody (mAb) 1H4.	1H4	209-212	heme oxygenase 1	Homo sapiens	38-42
18845641-6	2009	Real-time PCR analyses, Western blotting, and immunofluorescence of first trimester placentae and differentiating villous explant cultures demonstrated down-regulation of HO-1 in invasive EVTs as compared with CTBs.	evts	188-192	heme oxygenase 1	Homo sapiens	171-175
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Heme	130-134	heme oxygenase 1	Homo sapiens	0-21
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Iron	140-152	heme oxygenase 1	Homo sapiens	0-21
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Carbon Monoxide	154-169	heme oxygenase 1	Homo sapiens	0-21
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Carbon Monoxide	171-173	heme oxygenase 1	Homo sapiens	0-21
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Biliverdine	180-190	heme oxygenase 1	Homo sapiens	0-21
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Biliverdine	192-194	heme oxygenase 1	Homo sapiens	0-21
20107533-1	2009	Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR).	Bilirubin	242-251	heme oxygenase 1	Homo sapiens	0-21
18757839-6	2009	We hypothesized that PMET activation by Ox-PAPC causes intracellular NAD(P)H depletion, which leads to the increased oxidative stress and HO-1 induction.	nad(p)h	69-76	heme oxygenase 1	Homo sapiens	138-142
18757839-7	2009	Supporting this hypothesis, cotreatment of cells with exogenous NAD(P)H and Ox-PAPC significantly decreased oxidative stress and HO-1 induction by Ox-PAPC.	nad(p)h	64-71	heme oxygenase 1	Homo sapiens	129-133
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Heme	76-80	heme oxygenase 1	Homo sapiens	0-16
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Heme	76-80	heme oxygenase 1	Homo sapiens	18-22
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	0-16
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	18-22
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Iron	103-107	heme oxygenase 1	Homo sapiens	0-16
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Iron	103-107	heme oxygenase 1	Homo sapiens	18-22
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Iron	166-170	heme oxygenase 1	Homo sapiens	0-16
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Iron	166-170	heme oxygenase 1	Homo sapiens	18-22
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Biliverdine	197-207	heme oxygenase 1	Homo sapiens	0-16
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Biliverdine	197-207	heme oxygenase 1	Homo sapiens	18-22
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Bilirubin	231-240	heme oxygenase 1	Homo sapiens	0-16
19162549-1	2009	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase).	Bilirubin	231-240	heme oxygenase 1	Homo sapiens	18-22
19162549-2	2009	Over the past few years it has become apparent that these "arms" of the HO-1 system can act protectively in a variety of experimental models of disease; there is also evidence that HO-1 and bilirubin have protective actions in humans.	Bilirubin	190-199	heme oxygenase 1	Homo sapiens	72-76
19162549-3	2009	Here, we present a model for the beneficial actions of the products of heme degradation, and we discuss the potential clinical applications of enhancing the HO-1 system.	Heme	71-75	heme oxygenase 1	Homo sapiens	157-161
18812229-7	2009	Both inducible nitric oxide synthase (NOS-2) and hemoxygenase-1 (HO-1) gene expression were increased by tBH and reduced by both RES and SM pretreatments.	tert-Butylhydroperoxide	105-108	heme oxygenase 1	Homo sapiens	49-69
19033392-9	2009	A significant inhibition of the expression of hmox1 and nqo1 mRNAs and CD86 expression was found in 1-chloro 2,4-dinitrobenzene-treated THP-1 cells preincubated with N-acetyl cysteine, a glutathione precursor.	Acetylcysteine	166-183	heme oxygenase 1	Homo sapiens	46-51
19033392-9	2009	A significant inhibition of the expression of hmox1 and nqo1 mRNAs and CD86 expression was found in 1-chloro 2,4-dinitrobenzene-treated THP-1 cells preincubated with N-acetyl cysteine, a glutathione precursor.	Glutathione	187-198	heme oxygenase 1	Homo sapiens	46-51
18996444-7	2009	ODQ and KT5823 decreased, whereas 8-bromo-cyclic GMP increased, the number of dopaminergic neurons expressing HO-1 after IFN-gamma/LPS challenge, without parallel changes in HO-1 expression in other cell populations.	1H-(1,2,4)oxadiazolo(4,3-a)quinoxalin-1-one	0-3	heme oxygenase 1	Homo sapiens	110-114
18996444-0	2009	Nitric oxide-cyclic GMP signaling pathway limits inflammatory degeneration of midbrain dopaminergic neurons: cell type-specific regulation of heme oxygenase-1 expression.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	142-158
18996444-8	2009	An NO donor 3-(4-morpholinyl)sydnonimine hydrochloride also induced HO-1 expression in dopaminergic neurons, which was abolished by ODQ and augmented by 8-bromo-cyclic GMP.	3-(4-morpholinyl)sydnonimine hydrochloride	12-54	heme oxygenase 1	Homo sapiens	68-72
18996444-8	2009	An NO donor 3-(4-morpholinyl)sydnonimine hydrochloride also induced HO-1 expression in dopaminergic neurons, which was abolished by ODQ and augmented by 8-bromo-cyclic GMP.	1H-(1,2,4)oxadiazolo(4,3-a)quinoxalin-1-one	132-135	heme oxygenase 1	Homo sapiens	68-72
18996444-9	2009	Moreover, IFN-gamma/LPS-induced dopaminergic cell death was augmented by zinc protoporphyrin IX, an HO-1 inhibitor.	zinc protoporphyrin	73-95	heme oxygenase 1	Homo sapiens	100-104
18845130-0	2009	Reactive oxygen species-independent apoptosis in doxorubicin-treated H9c2 cardiomyocytes: role for heme oxygenase-1 down-modulation.	Doxorubicin	49-60	heme oxygenase 1	Homo sapiens	99-115
19292935-4	2009	It is now generally recognized that nitric oxide (NO) and carbon monoxide (CO), two gaso-transmitters synthesized by inducible NO synthase (iNOS) and heme-oxygenase-1 (HO-1) respectively, play important roles in the compensatory regulation of the blood pressure during the development of hypertension.	Nitric Oxide	36-48	heme oxygenase 1	Homo sapiens	150-166
18992762-5	2009	CDDP significantly increased renal abundances of HO-1, HSP60, HSP72 and HSP90 at days 1, 3, and 5.	Cisplatin	0-4	heme oxygenase 1	Homo sapiens	49-53
19092646-6	2009	Both HO-1 and ferritin have been identified as targets of, and inducible by, aspirin and, in the case of HO-1, aspirin-triggered lipoxins.	Aspirin	77-84	heme oxygenase 1	Homo sapiens	5-9
19092646-6	2009	Both HO-1 and ferritin have been identified as targets of, and inducible by, aspirin and, in the case of HO-1, aspirin-triggered lipoxins.	Aspirin	111-118	heme oxygenase 1	Homo sapiens	5-9
19092646-6	2009	Both HO-1 and ferritin have been identified as targets of, and inducible by, aspirin and, in the case of HO-1, aspirin-triggered lipoxins.	Aspirin	111-118	heme oxygenase 1	Homo sapiens	105-109
19092646-6	2009	Both HO-1 and ferritin have been identified as targets of, and inducible by, aspirin and, in the case of HO-1, aspirin-triggered lipoxins.	Lipoxins	129-137	heme oxygenase 1	Homo sapiens	5-9
19092646-6	2009	Both HO-1 and ferritin have been identified as targets of, and inducible by, aspirin and, in the case of HO-1, aspirin-triggered lipoxins.	Lipoxins	129-137	heme oxygenase 1	Homo sapiens	105-109
19092646-8	2009	HO-1 and its antioxidant product bilirubin have been reported to be not only involved in vasoprotection, but to have a similar function in gastric tissue.	Bilirubin	33-42	heme oxygenase 1	Homo sapiens	0-4
19183882-0	2009	NS398 protects cells from sodium nitroprusside-mediated cytotoxicity through enhancing HO-1 induction independent of COX-2 inhibition.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	0-5	heme oxygenase 1	Homo sapiens	87-91
19183882-0	2009	NS398 protects cells from sodium nitroprusside-mediated cytotoxicity through enhancing HO-1 induction independent of COX-2 inhibition.	Nitroprusside	26-46	heme oxygenase 1	Homo sapiens	87-91
19183882-3	2009	Recently, however, salicylate the active metabolite of aspirin showed COX-independent anti-inflammatory effects through induction of HO-1.	Salicylates	19-29	heme oxygenase 1	Homo sapiens	133-137
19183882-3	2009	Recently, however, salicylate the active metabolite of aspirin showed COX-independent anti-inflammatory effects through induction of HO-1.	Aspirin	55-62	heme oxygenase 1	Homo sapiens	133-137
19183882-4	2009	Thus, we hypothesized that HO-1 are induced as an adaptive response to sodium nitroprusside (SNP) and play a protective role against cytotoxicity.	Nitroprusside	71-91	heme oxygenase 1	Homo sapiens	27-31
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Heme	63-67	heme oxygenase 1	Homo sapiens	0-16
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Heme	63-67	heme oxygenase 1	Homo sapiens	18-22
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Heme	63-67	heme oxygenase 1	Homo sapiens	157-161
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Biliverdine	71-81	heme oxygenase 1	Homo sapiens	0-16
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Biliverdine	71-81	heme oxygenase 1	Homo sapiens	18-22
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Biliverdine	71-81	heme oxygenase 1	Homo sapiens	157-161
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	0-16
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	18-22
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	157-161
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Iron	109-113	heme oxygenase 1	Homo sapiens	0-16
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Iron	109-113	heme oxygenase 1	Homo sapiens	18-22
19123922-1	2009	Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR).	Iron	109-113	heme oxygenase 1	Homo sapiens	157-161
19292935-4	2009	It is now generally recognized that nitric oxide (NO) and carbon monoxide (CO), two gaso-transmitters synthesized by inducible NO synthase (iNOS) and heme-oxygenase-1 (HO-1) respectively, play important roles in the compensatory regulation of the blood pressure during the development of hypertension.	Nitric Oxide	36-48	heme oxygenase 1	Homo sapiens	168-172
19292935-4	2009	It is now generally recognized that nitric oxide (NO) and carbon monoxide (CO), two gaso-transmitters synthesized by inducible NO synthase (iNOS) and heme-oxygenase-1 (HO-1) respectively, play important roles in the compensatory regulation of the blood pressure during the development of hypertension.	Carbon Monoxide	58-73	heme oxygenase 1	Homo sapiens	150-166
19292935-4	2009	It is now generally recognized that nitric oxide (NO) and carbon monoxide (CO), two gaso-transmitters synthesized by inducible NO synthase (iNOS) and heme-oxygenase-1 (HO-1) respectively, play important roles in the compensatory regulation of the blood pressure during the development of hypertension.	Carbon Monoxide	58-73	heme oxygenase 1	Homo sapiens	168-172
19292935-4	2009	It is now generally recognized that nitric oxide (NO) and carbon monoxide (CO), two gaso-transmitters synthesized by inducible NO synthase (iNOS) and heme-oxygenase-1 (HO-1) respectively, play important roles in the compensatory regulation of the blood pressure during the development of hypertension.	Carbon Monoxide	75-77	heme oxygenase 1	Homo sapiens	150-166
19292935-4	2009	It is now generally recognized that nitric oxide (NO) and carbon monoxide (CO), two gaso-transmitters synthesized by inducible NO synthase (iNOS) and heme-oxygenase-1 (HO-1) respectively, play important roles in the compensatory regulation of the blood pressure during the development of hypertension.	Carbon Monoxide	75-77	heme oxygenase 1	Homo sapiens	168-172
19888908-5	2009	Exposure of HepG2 and Hep3B cells to Cu2+ inhibited the enzymes PBGD and ALAD of the heme synthesis pathway and, in parallel, upregulated heme oxygenase-1 (HO-1).	cupric ion	37-41	heme oxygenase 1	Homo sapiens	138-154
19794825-6	2009	In addition, LAS0811 induced expression of heme oxygenase 1 (HO1), which is an ARE-regulated enzyme with anti-inflammatory activity.	las0811	13-20	heme oxygenase 1	Homo sapiens	43-59
19794825-6	2009	In addition, LAS0811 induced expression of heme oxygenase 1 (HO1), which is an ARE-regulated enzyme with anti-inflammatory activity.	las0811	13-20	heme oxygenase 1	Homo sapiens	61-64
19177192-0	2009	Dimethoxycurcumin, a Synthetic Curcumin Analogue, Induces Heme Oxygenase-1 Expression through Nrf2 Activation in RAW264.7 Macrophages.	dimethoxycurcumin	0-17	heme oxygenase 1	Homo sapiens	58-74
19177192-0	2009	Dimethoxycurcumin, a Synthetic Curcumin Analogue, Induces Heme Oxygenase-1 Expression through Nrf2 Activation in RAW264.7 Macrophages.	Curcumin	31-39	heme oxygenase 1	Homo sapiens	58-74
19177192-2	2009	The aim of this study was to investigate whether dimethoxycurcumin [1,7-bis(4,3-dimethoxyphenyl)-1,6-heptadiene-3,5-dione], a synthetic curcumin analogue with higher metabolic stability over curcumin, could induce HO-1 expression to the same extent as curcumin in RAW264.7 macrophages.	dimethoxycurcumin	49-66	heme oxygenase 1	Homo sapiens	214-218
19177192-2	2009	The aim of this study was to investigate whether dimethoxycurcumin [1,7-bis(4,3-dimethoxyphenyl)-1,6-heptadiene-3,5-dione], a synthetic curcumin analogue with higher metabolic stability over curcumin, could induce HO-1 expression to the same extent as curcumin in RAW264.7 macrophages.	1,7-bis(4,3-dimethoxyphenyl)-1,6-heptadiene-3,5-dione	68-121	heme oxygenase 1	Homo sapiens	214-218
19177192-2	2009	The aim of this study was to investigate whether dimethoxycurcumin [1,7-bis(4,3-dimethoxyphenyl)-1,6-heptadiene-3,5-dione], a synthetic curcumin analogue with higher metabolic stability over curcumin, could induce HO-1 expression to the same extent as curcumin in RAW264.7 macrophages.	Curcumin	58-66	heme oxygenase 1	Homo sapiens	214-218
19177192-3	2009	Dimethoxycurcumin and curcumin, but not tetrahydrocurcumin, induced HO-1 expression and Nrf2 nuclear translocation, suggesting that the unsaturated nature of the diarylheptanoid chain of the compounds are crucial for HO-1 expression and Nrf2 activation.	dimethoxycurcumin	0-17	heme oxygenase 1	Homo sapiens	68-72
19177192-3	2009	Dimethoxycurcumin and curcumin, but not tetrahydrocurcumin, induced HO-1 expression and Nrf2 nuclear translocation, suggesting that the unsaturated nature of the diarylheptanoid chain of the compounds are crucial for HO-1 expression and Nrf2 activation.	dimethoxycurcumin	0-17	heme oxygenase 1	Homo sapiens	217-221
19177192-3	2009	Dimethoxycurcumin and curcumin, but not tetrahydrocurcumin, induced HO-1 expression and Nrf2 nuclear translocation, suggesting that the unsaturated nature of the diarylheptanoid chain of the compounds are crucial for HO-1 expression and Nrf2 activation.	Curcumin	9-17	heme oxygenase 1	Homo sapiens	68-72
19177192-3	2009	Dimethoxycurcumin and curcumin, but not tetrahydrocurcumin, induced HO-1 expression and Nrf2 nuclear translocation, suggesting that the unsaturated nature of the diarylheptanoid chain of the compounds are crucial for HO-1 expression and Nrf2 activation.	Curcumin	9-17	heme oxygenase 1	Homo sapiens	217-221
19177192-4	2009	Blockage of Nrf2 synthesis by small interfering RNA abolished HO-1 expression by dimethoxycurcumin, indicating that dimethoxycurcumin may induce HO-1 expression via Nrf2 activation.	dimethoxycurcumin	81-98	heme oxygenase 1	Homo sapiens	62-66
19177192-4	2009	Blockage of Nrf2 synthesis by small interfering RNA abolished HO-1 expression by dimethoxycurcumin, indicating that dimethoxycurcumin may induce HO-1 expression via Nrf2 activation.	dimethoxycurcumin	81-98	heme oxygenase 1	Homo sapiens	145-149
19177192-4	2009	Blockage of Nrf2 synthesis by small interfering RNA abolished HO-1 expression by dimethoxycurcumin, indicating that dimethoxycurcumin may induce HO-1 expression via Nrf2 activation.	dimethoxycurcumin	116-133	heme oxygenase 1	Homo sapiens	62-66
19177192-4	2009	Blockage of Nrf2 synthesis by small interfering RNA abolished HO-1 expression by dimethoxycurcumin, indicating that dimethoxycurcumin may induce HO-1 expression via Nrf2 activation.	dimethoxycurcumin	116-133	heme oxygenase 1	Homo sapiens	145-149
19177192-5	2009	In comparison, dimethoxycurcumin and curcumin had about the same effect on HO-1 expression, suggesting that dimethoxycurcumin retains the HO-1-inducing activity of its parent compound curcumin in RAW264.7 macrophages.	dimethoxycurcumin	15-32	heme oxygenase 1	Homo sapiens	75-79
19177192-5	2009	In comparison, dimethoxycurcumin and curcumin had about the same effect on HO-1 expression, suggesting that dimethoxycurcumin retains the HO-1-inducing activity of its parent compound curcumin in RAW264.7 macrophages.	Curcumin	24-32	heme oxygenase 1	Homo sapiens	75-79
19177192-5	2009	In comparison, dimethoxycurcumin and curcumin had about the same effect on HO-1 expression, suggesting that dimethoxycurcumin retains the HO-1-inducing activity of its parent compound curcumin in RAW264.7 macrophages.	dimethoxycurcumin	108-125	heme oxygenase 1	Homo sapiens	75-79
19177192-5	2009	In comparison, dimethoxycurcumin and curcumin had about the same effect on HO-1 expression, suggesting that dimethoxycurcumin retains the HO-1-inducing activity of its parent compound curcumin in RAW264.7 macrophages.	dimethoxycurcumin	108-125	heme oxygenase 1	Homo sapiens	138-142
19177192-5	2009	In comparison, dimethoxycurcumin and curcumin had about the same effect on HO-1 expression, suggesting that dimethoxycurcumin retains the HO-1-inducing activity of its parent compound curcumin in RAW264.7 macrophages.	Curcumin	37-45	heme oxygenase 1	Homo sapiens	75-79
19355962-6	2009	The anti-inflammatory activity of chalcones has been correlated with the induction of heme oxygenase-1 while phlorotannins have been found to inhibit matrix metalloproteinase, which is implicated in arthritis, chronic inflammation, and wrinkle formation.	Chalcones	34-43	heme oxygenase 1	Homo sapiens	86-102
19263288-1	2009	Heme oxygenases (HO-1 and HO-2) are responsible for the production of carbon monoxide, a vasodilator.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	0-30
19177185-3	2009	Cells counteract this by rapidly inducing the rate-limiting enzyme in heme breakdown, heme oxygenase-1 (HO-1), which is a low-molecular-weight stress protein.	Heme	70-74	heme oxygenase 1	Homo sapiens	86-102
19177185-3	2009	Cells counteract this by rapidly inducing the rate-limiting enzyme in heme breakdown, heme oxygenase-1 (HO-1), which is a low-molecular-weight stress protein.	Heme	70-74	heme oxygenase 1	Homo sapiens	104-108
19177185-4	2009	The enzymatic HO-1 reaction removes heme.	Heme	36-40	heme oxygenase 1	Homo sapiens	14-18
19888908-5	2009	Exposure of HepG2 and Hep3B cells to Cu2+ inhibited the enzymes PBGD and ALAD of the heme synthesis pathway and, in parallel, upregulated heme oxygenase-1 (HO-1).	cupric ion	37-41	heme oxygenase 1	Homo sapiens	156-160
21152244-9	2009	VEGF, MMP9 and HO-1 transcript levels were increased in ARPE19 cells under H(2)O(2) - induced oxidative stress.	Hydrogen Peroxide	75-83	heme oxygenase 1	Homo sapiens	15-19
19046352-3	2009	In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia.	Iron	91-95	heme oxygenase 1	Homo sapiens	51-55
19046352-3	2009	In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia.	ammonium ferrous sulfate	97-103	heme oxygenase 1	Homo sapiens	51-55
19046352-3	2009	In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia.	Carbon Monoxide	106-121	heme oxygenase 1	Homo sapiens	51-55
19046352-3	2009	In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia.	Carbon Monoxide	123-125	heme oxygenase 1	Homo sapiens	51-55
19046352-3	2009	In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia.	Bilirubin	131-140	heme oxygenase 1	Homo sapiens	51-55
19046352-3	2009	In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia.	Oxysterols	175-184	heme oxygenase 1	Homo sapiens	51-55
18983509-0	2009	15-deoxy-Delta12,14 prostaglandin J2-induced heme oxygenase-1 in megakaryocytes regulates thrombopoiesis.	9-deoxy-delta-9-prostaglandin D2	20-36	heme oxygenase 1	Homo sapiens	45-61
18983509-10	2009	15d-PGJ(2)-induced HO-1 was independent of PPARgamma, but could be replicated using other electrophilic prostaglandins, suggesting that the electrophilic properties of 15d-PGJ(2) were important for HO-1 induction.	15d-pgj	0-7	heme oxygenase 1	Homo sapiens	19-23
18983509-10	2009	15d-PGJ(2)-induced HO-1 was independent of PPARgamma, but could be replicated using other electrophilic prostaglandins, suggesting that the electrophilic properties of 15d-PGJ(2) were important for HO-1 induction.	15d-pgj	0-7	heme oxygenase 1	Homo sapiens	198-202
18983509-10	2009	15d-PGJ(2)-induced HO-1 was independent of PPARgamma, but could be replicated using other electrophilic prostaglandins, suggesting that the electrophilic properties of 15d-PGJ(2) were important for HO-1 induction.	15d-pgj	168-175	heme oxygenase 1	Homo sapiens	19-23
18983509-11	2009	Interestingly, inhibiting HO-1 activity enhanced ROS generation and augmented 15d-PGJ(2)-induced platelet production, which could be attenuated by antioxidants.	Reactive Oxygen Species	49-52	heme oxygenase 1	Homo sapiens	26-30
18983509-11	2009	Interestingly, inhibiting HO-1 activity enhanced ROS generation and augmented 15d-PGJ(2)-induced platelet production, which could be attenuated by antioxidants.	15-deoxyprostaglandin J2	78-88	heme oxygenase 1	Homo sapiens	26-30
18983509-12	2009	These new data reveal that HO-1 negatively regulates thrombopoiesis by inhibiting ROS.	Reactive Oxygen Species	82-85	heme oxygenase 1	Homo sapiens	27-31
19468257-0	2009	Pretreatment with glutamine attenuates anoxia/reoxygenation injury of human proximal renal tubular epithelial cells via induction of heme oxygenase-1.	Glutamine	18-27	heme oxygenase 1	Homo sapiens	133-149
19468257-1	2009	BACKGROUND/AIMS: Glutamine showed potential cytoprotective activity probably due to induction of heme oxygenase-1 (HO-1).	Glutamine	17-26	heme oxygenase 1	Homo sapiens	97-113
19468257-1	2009	BACKGROUND/AIMS: Glutamine showed potential cytoprotective activity probably due to induction of heme oxygenase-1 (HO-1).	Glutamine	17-26	heme oxygenase 1	Homo sapiens	115-119
19307691-10	2009	We close this review by focusing on the protective properties of the organic nitrate pentaerithrityl tetranitrate, which upregulates enzymes that have strong antioxidative activity, such as heme oxygenase-1 and ferritin, thereby preventing the development of tolerance and endothelial dysfunction.	organic	69-76	heme oxygenase 1	Homo sapiens	190-219
19468257-5	2009	RESULTS: A/R significantly induced apoptosis of HK-2 cells, which was inhibited by glutamine, during which HO-1 was upregulated significantly, but nullified by p38MAPK inhibitor.	Glutamine	83-92	heme oxygenase 1	Homo sapiens	107-111
19468257-8	2009	CONCLUSION: Glutamine prevents A/R injury of HK-2 cells through induction of HO-1 via a p38MAPK-dependent pathway, which plays a key role in the cytoprotective effect of glutamine.	Glutamine	12-21	heme oxygenase 1	Homo sapiens	77-81
19307691-10	2009	We close this review by focusing on the protective properties of the organic nitrate pentaerithrityl tetranitrate, which upregulates enzymes that have strong antioxidative activity, such as heme oxygenase-1 and ferritin, thereby preventing the development of tolerance and endothelial dysfunction.	nitrate pentaerithrityl tetranitrate	77-113	heme oxygenase 1	Homo sapiens	190-219
19468257-8	2009	CONCLUSION: Glutamine prevents A/R injury of HK-2 cells through induction of HO-1 via a p38MAPK-dependent pathway, which plays a key role in the cytoprotective effect of glutamine.	Glutamine	170-179	heme oxygenase 1	Homo sapiens	77-81
18957281-9	2008	Thus, PGD(2) induces HO-1 mRNA expression through DP2 receptor, linking the PGD(2)-DP2 signaling with heme homeostasis.	Prostaglandin D2	6-12	heme oxygenase 1	Homo sapiens	21-25
18923065-5	2009	However, the YC-1-mediated induction of HO-1 was inhibited by the phosphatidylinositol-3-kinase (PI3K) inhibitors wortmannin and 2-(4-morpholinyl)-8-phenyl-1(4H)-benzopyran-4-one hydrochloride (LY294002).	Wortmannin	114-124	heme oxygenase 1	Homo sapiens	40-44
18923065-5	2009	However, the YC-1-mediated induction of HO-1 was inhibited by the phosphatidylinositol-3-kinase (PI3K) inhibitors wortmannin and 2-(4-morpholinyl)-8-phenyl-1(4H)-benzopyran-4-one hydrochloride (LY294002).	LY-294,002 hydrochloride	129-192	heme oxygenase 1	Homo sapiens	40-44
18923065-5	2009	However, the YC-1-mediated induction of HO-1 was inhibited by the phosphatidylinositol-3-kinase (PI3K) inhibitors wortmannin and 2-(4-morpholinyl)-8-phenyl-1(4H)-benzopyran-4-one hydrochloride (LY294002).	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	194-202	heme oxygenase 1	Homo sapiens	40-44
18923065-8	2009	The ability of YC-1 to sensitize sGC to gaseous monoxides and simultaneously stimulate their production through the induction of HO-1 and iNOS provides a potent mechanism by which the cGMP-dependent and -independent biological actions of this agent are amplified.	Cyclic GMP	184-188	heme oxygenase 1	Homo sapiens	129-133
18829152-4	2009	When N-acetyl-L-cysteine or glutathione-monoethyl ester, a potent antioxidant, was added to cell culture, hmox-1 upregulation was attenuated, suggesting that oxidative stress caused by sonication is involved in this process.	Acetylcysteine	5-24	heme oxygenase 1	Homo sapiens	106-112
18829152-4	2009	When N-acetyl-L-cysteine or glutathione-monoethyl ester, a potent antioxidant, was added to cell culture, hmox-1 upregulation was attenuated, suggesting that oxidative stress caused by sonication is involved in this process.	S-ethyl glutathione	28-55	heme oxygenase 1	Homo sapiens	106-112
18957281-0	2008	Prostaglandin D2 induces heme oxygenase-1 mRNA expression through the DP2 receptor.	Prostaglandin D2	0-16	heme oxygenase 1	Homo sapiens	25-41
18957281-2	2008	We have shown that PGD(2) induces the expression of heme oxygenase-1 (HO-1) in the retinal pigment epithelium (RPE) that is essential for survival of photoreceptors.	Prostaglandin D2	19-25	heme oxygenase 1	Homo sapiens	52-68
18957281-2	2008	We have shown that PGD(2) induces the expression of heme oxygenase-1 (HO-1) in the retinal pigment epithelium (RPE) that is essential for survival of photoreceptors.	Prostaglandin D2	19-25	heme oxygenase 1	Homo sapiens	70-74
18957281-9	2008	Thus, PGD(2) induces HO-1 mRNA expression through DP2 receptor, linking the PGD(2)-DP2 signaling with heme homeostasis.	Prostaglandin D2	76-82	heme oxygenase 1	Homo sapiens	21-25
18957281-3	2008	HO-1 is a key enzyme in physiological heme degradation.	Heme	38-42	heme oxygenase 1	Homo sapiens	0-4
18845176-7	2008	Moreover, puerarin induced Nrf2 nuclear translocation, which is upstream of puerarin-induced HO-1 expression, and PI3K activation, a pathway that is involved in induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	puerarin	10-18	heme oxygenase 1	Homo sapiens	93-97
18957281-4	2008	Here, we explored the mechanism for the PGD(2)-mediated induction of HO-1 expression using ARPE-19 human RPE cells.	Prostaglandin D2	40-46	heme oxygenase 1	Homo sapiens	69-73
18957281-6	2008	Treatment with a DP2 agonist, 15(R)-15-methyl-PGD(2) or DK-PGD(2), increased HO-1 mRNA expression, and pretreatment with a DP2 antagonist, CAY10471, decreased the magnitude of the PGD(2)-mediated HO-1 induction.	15(r)-15-methyl-pgd	30-49	heme oxygenase 1	Homo sapiens	77-81
18957281-6	2008	Treatment with a DP2 agonist, 15(R)-15-methyl-PGD(2) or DK-PGD(2), increased HO-1 mRNA expression, and pretreatment with a DP2 antagonist, CAY10471, decreased the magnitude of the PGD(2)-mediated HO-1 induction.	15(r)-15-methyl-pgd	30-49	heme oxygenase 1	Homo sapiens	196-200
18957281-6	2008	Treatment with a DP2 agonist, 15(R)-15-methyl-PGD(2) or DK-PGD(2), increased HO-1 mRNA expression, and pretreatment with a DP2 antagonist, CAY10471, decreased the magnitude of the PGD(2)-mediated HO-1 induction.	Prostaglandins D	46-49	heme oxygenase 1	Homo sapiens	77-81
18845176-4	2008	In this study, we demonstrate that the phytoestrogen puerarin inhibits tert-butyl hydroperoxide (t-BHP)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	puerarin	53-61	heme oxygenase 1	Homo sapiens	169-185
18845176-7	2008	Moreover, puerarin induced Nrf2 nuclear translocation, which is upstream of puerarin-induced HO-1 expression, and PI3K activation, a pathway that is involved in induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	puerarin	10-18	heme oxygenase 1	Homo sapiens	197-201
18845176-4	2008	In this study, we demonstrate that the phytoestrogen puerarin inhibits tert-butyl hydroperoxide (t-BHP)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	puerarin	53-61	heme oxygenase 1	Homo sapiens	187-191
18845176-7	2008	Moreover, puerarin induced Nrf2 nuclear translocation, which is upstream of puerarin-induced HO-1 expression, and PI3K activation, a pathway that is involved in induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	puerarin	76-84	heme oxygenase 1	Homo sapiens	93-97
18845176-4	2008	In this study, we demonstrate that the phytoestrogen puerarin inhibits tert-butyl hydroperoxide (t-BHP)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	tert-Butylhydroperoxide	71-95	heme oxygenase 1	Homo sapiens	169-185
18845176-4	2008	In this study, we demonstrate that the phytoestrogen puerarin inhibits tert-butyl hydroperoxide (t-BHP)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	tert-Butylhydroperoxide	71-95	heme oxygenase 1	Homo sapiens	187-191
18845176-8	2008	Puerarin-induced up-regulation of HO-1 and cytoprotection against t-BHP were abolished by silencing Nrf2 expression with specific siRNA.	puerarin	0-8	heme oxygenase 1	Homo sapiens	34-38
18845176-4	2008	In this study, we demonstrate that the phytoestrogen puerarin inhibits tert-butyl hydroperoxide (t-BHP)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	tert-Butylhydroperoxide	97-102	heme oxygenase 1	Homo sapiens	169-185
18845176-9	2008	Also, puerarin-mediated increases in PI3K activation and HO-1 induction were reversed by co-treatment with ICI 182,780 and pertussis toxin.	puerarin	6-14	heme oxygenase 1	Homo sapiens	57-61
18845176-4	2008	In this study, we demonstrate that the phytoestrogen puerarin inhibits tert-butyl hydroperoxide (t-BHP)-induced oxidative injury via an ER-dependent Gbeta1/PI3K/Akt and heme oxygenase-1 (HO-1) pathway.	tert-Butylhydroperoxide	97-102	heme oxygenase 1	Homo sapiens	187-191
18845176-10	2008	Taken together, these results suggest that puerarin augments cellular antioxidant defense capacity through ER-dependent HO-1 induction via the Gbeta1/PI3K/Akt-Nrf2 signaling pathway, thereby protecting cells from oxidative stress.	puerarin	43-51	heme oxygenase 1	Homo sapiens	120-124
18845176-6	2008	Also, puerarin up-regulated HO-1 expression and this expression conferred cytoprotection against oxidative injury induced by t-BHP.	tert-Butylhydroperoxide	125-130	heme oxygenase 1	Homo sapiens	28-32
18852027-0	2008	Nordihydroguaiaretic acid activates the antioxidant pathway Nrf2/HO-1 and protects cerebellar granule neurons against oxidative stress.	Masoprocol	0-25	heme oxygenase 1	Homo sapiens	65-69
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	Masoprocol	14-39	heme oxygenase 1	Homo sapiens	129-150
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	Masoprocol	14-39	heme oxygenase 1	Homo sapiens	152-156
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	Masoprocol	41-45	heme oxygenase 1	Homo sapiens	129-150
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	Masoprocol	41-45	heme oxygenase 1	Homo sapiens	152-156
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	Water	214-219	heme oxygenase 1	Homo sapiens	129-150
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	Water	214-219	heme oxygenase 1	Homo sapiens	152-156
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	3-nitropropionic acid	226-247	heme oxygenase 1	Homo sapiens	129-150
18852027-2	2008	We found that nordihydroguaiaretic acid (NDGA), a powerful antioxidant from Larrea tridentate, activates the antioxidant pathway Nrf2/heme oxygenase-1 (HO-1) in cerebellar granule neurons and protects them against H(2)O(2) or 3-nitropropionic acid-induced neurotoxicity.	3-nitropropionic acid	226-247	heme oxygenase 1	Homo sapiens	152-156
18852027-3	2008	The role of HO-1 in this protective effect was made evident by using an HO inhibitor, tin-mesoporphyrin.	tin mesoporphyrin	86-103	heme oxygenase 1	Homo sapiens	12-16
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	Prednisolone	128-140	heme oxygenase 1	Homo sapiens	299-303
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	Dexamethasone	146-159	heme oxygenase 1	Homo sapiens	38-42
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	11,17-dihydroxy-6-methyl-17-(1-propynyl)androsta-1,4,6-triene-3-one	119-126	heme oxygenase 1	Homo sapiens	38-42
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	Acetylcysteine	175-194	heme oxygenase 1	Homo sapiens	38-42
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	11,17-dihydroxy-6-methyl-17-(1-propynyl)androsta-1,4,6-triene-3-one	119-126	heme oxygenase 1	Homo sapiens	299-303
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	Prednisolone	128-140	heme oxygenase 1	Homo sapiens	38-42
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	Acetylcysteine	175-194	heme oxygenase 1	Homo sapiens	299-303
19548360-5	2008	The increases in reactive species and HO-1 protein are inhibited by agonists of glucocorticoid receptors (GR), such as RU28362, prednisolone, and dexamethasone, as well as by N-acetyl-L-cysteine and SB203580 (a p38 inhibitor), suggesting a role of GR in NF-induced increases in reactive species and HO-1.	SB 203580	199-207	heme oxygenase 1	Homo sapiens	38-42
19548360-6	2008	Assay-guided fractionation of NF led to three active compounds, phenethyl ferulate, bergaptol, and isoimperatorin, that were found to increase oxidative stress and HO-1 protein levels in HFHs.	phenethyl ferulate	64-82	heme oxygenase 1	Homo sapiens	164-168
19548360-6	2008	Assay-guided fractionation of NF led to three active compounds, phenethyl ferulate, bergaptol, and isoimperatorin, that were found to increase oxidative stress and HO-1 protein levels in HFHs.	bergaptol	84-93	heme oxygenase 1	Homo sapiens	164-168
19548360-6	2008	Assay-guided fractionation of NF led to three active compounds, phenethyl ferulate, bergaptol, and isoimperatorin, that were found to increase oxidative stress and HO-1 protein levels in HFHs.	isoimperatorin	99-113	heme oxygenase 1	Homo sapiens	164-168
18341478-8	2008	SnP (tin protoporphyrin), an HO-1 inhibitor, counteracted the effects of Adv-HO-1.	tin protoporphyrin IX	5-23	heme oxygenase 1	Homo sapiens	29-33
18341478-8	2008	SnP (tin protoporphyrin), an HO-1 inhibitor, counteracted the effects of Adv-HO-1.	tin protoporphyrin IX	5-23	heme oxygenase 1	Homo sapiens	77-81
19120903-2	2008	Two end products of heme degradation, carbon monoxide (CO) and bilirubin, are involved in the protective role of HO-1 against oxidative injury.	Carbon Monoxide	38-53	heme oxygenase 1	Homo sapiens	113-117
18948096-4	2008	The present study had a focus on the human retinal pigment epithelial (RPE) cell line ARPE-19 in an attempt to demonstrate a reduction in intracellular Cd(2+) effect associated with heme oxygenase-1 (HO-1) expression by co-exposure with zinc (Zn(2+)) or manganese (Mn(2+)), which is known to be a more potent inhibitor of Cd(2+) uptake than Zn(2+).	Cadmium	152-154	heme oxygenase 1	Homo sapiens	182-198
18948096-4	2008	The present study had a focus on the human retinal pigment epithelial (RPE) cell line ARPE-19 in an attempt to demonstrate a reduction in intracellular Cd(2+) effect associated with heme oxygenase-1 (HO-1) expression by co-exposure with zinc (Zn(2+)) or manganese (Mn(2+)), which is known to be a more potent inhibitor of Cd(2+) uptake than Zn(2+).	Cadmium	152-154	heme oxygenase 1	Homo sapiens	200-204
18948096-4	2008	The present study had a focus on the human retinal pigment epithelial (RPE) cell line ARPE-19 in an attempt to demonstrate a reduction in intracellular Cd(2+) effect associated with heme oxygenase-1 (HO-1) expression by co-exposure with zinc (Zn(2+)) or manganese (Mn(2+)), which is known to be a more potent inhibitor of Cd(2+) uptake than Zn(2+).	Zinc	243-245	heme oxygenase 1	Homo sapiens	200-204
18948096-4	2008	The present study had a focus on the human retinal pigment epithelial (RPE) cell line ARPE-19 in an attempt to demonstrate a reduction in intracellular Cd(2+) effect associated with heme oxygenase-1 (HO-1) expression by co-exposure with zinc (Zn(2+)) or manganese (Mn(2+)), which is known to be a more potent inhibitor of Cd(2+) uptake than Zn(2+).	Manganese	254-263	heme oxygenase 1	Homo sapiens	200-204
18948096-4	2008	The present study had a focus on the human retinal pigment epithelial (RPE) cell line ARPE-19 in an attempt to demonstrate a reduction in intracellular Cd(2+) effect associated with heme oxygenase-1 (HO-1) expression by co-exposure with zinc (Zn(2+)) or manganese (Mn(2+)), which is known to be a more potent inhibitor of Cd(2+) uptake than Zn(2+).	Cadmium	322-324	heme oxygenase 1	Homo sapiens	200-204
18948096-4	2008	The present study had a focus on the human retinal pigment epithelial (RPE) cell line ARPE-19 in an attempt to demonstrate a reduction in intracellular Cd(2+) effect associated with heme oxygenase-1 (HO-1) expression by co-exposure with zinc (Zn(2+)) or manganese (Mn(2+)), which is known to be a more potent inhibitor of Cd(2+) uptake than Zn(2+).	Zinc	341-343	heme oxygenase 1	Homo sapiens	200-204
18948096-7	2008	Mn(2+) ions as low as 2.5 microM were found to cause an increase in HO-1 mRNA expression levels in ARPE-19 cells, demonstrating for the first time that Mn(2+) is an inducer of HO-1.	Manganese(2+)	0-6	heme oxygenase 1	Homo sapiens	68-72
18948096-7	2008	Mn(2+) ions as low as 2.5 microM were found to cause an increase in HO-1 mRNA expression levels in ARPE-19 cells, demonstrating for the first time that Mn(2+) is an inducer of HO-1.	Manganese(2+)	0-6	heme oxygenase 1	Homo sapiens	176-180
18948096-7	2008	Mn(2+) ions as low as 2.5 microM were found to cause an increase in HO-1 mRNA expression levels in ARPE-19 cells, demonstrating for the first time that Mn(2+) is an inducer of HO-1.	Manganese(2+)	152-158	heme oxygenase 1	Homo sapiens	68-72
18948096-7	2008	Mn(2+) ions as low as 2.5 microM were found to cause an increase in HO-1 mRNA expression levels in ARPE-19 cells, demonstrating for the first time that Mn(2+) is an inducer of HO-1.	Manganese(2+)	152-158	heme oxygenase 1	Homo sapiens	176-180
18948096-8	2008	Mn(2+) ions at 1 microM induced HO-1 mRNA expression in the HEK293 human embryonic kidney cells.	Manganese(2+)	0-6	heme oxygenase 1	Homo sapiens	32-36
18948096-11	2008	Further, induction of HO-1 by Mn(2+) could provide RPE with some resistance to enhanced oxidative stress arising from Cd(2+) accumulation in RPE as HO-1 is one of the frontline cellular antioxidant defense mechanisms.	Manganese(2+)	30-36	heme oxygenase 1	Homo sapiens	22-26
18948096-11	2008	Further, induction of HO-1 by Mn(2+) could provide RPE with some resistance to enhanced oxidative stress arising from Cd(2+) accumulation in RPE as HO-1 is one of the frontline cellular antioxidant defense mechanisms.	Manganese(2+)	30-36	heme oxygenase 1	Homo sapiens	148-152
18301921-2	2008	The enzyme heme oxygenase-1 (HO-1) participates in cytoprotection against oxygen radical injury.	Oxygen	16-22	heme oxygenase 1	Homo sapiens	29-33
19120903-2	2008	Two end products of heme degradation, carbon monoxide (CO) and bilirubin, are involved in the protective role of HO-1 against oxidative injury.	Carbon Monoxide	55-57	heme oxygenase 1	Homo sapiens	113-117
19120903-2	2008	Two end products of heme degradation, carbon monoxide (CO) and bilirubin, are involved in the protective role of HO-1 against oxidative injury.	Bilirubin	63-72	heme oxygenase 1	Homo sapiens	113-117
18799798-0	2008	Overexpression of heme oxygenase-1 protects dopaminergic neurons against 1-methyl-4-phenylpyridinium-induced neurotoxicity.	1-Methyl-4-phenylpyridinium	73-100	heme oxygenase 1	Homo sapiens	18-34
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Heme	117-121	heme oxygenase 1	Homo sapiens	0-16
18799798-6	2008	Apomorphine-induced rotation after MPP(+) treatment was also inhibited by Ad-HO-1.	Apomorphine	0-11	heme oxygenase 1	Homo sapiens	77-81
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Heme	117-121	heme oxygenase 1	Homo sapiens	18-22
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Carbon Monoxide	125-140	heme oxygenase 1	Homo sapiens	0-16
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Carbon Monoxide	125-140	heme oxygenase 1	Homo sapiens	18-22
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Carbon Monoxide	142-144	heme oxygenase 1	Homo sapiens	0-16
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Carbon Monoxide	142-144	heme oxygenase 1	Homo sapiens	18-22
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Iron	147-151	heme oxygenase 1	Homo sapiens	0-16
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Iron	147-151	heme oxygenase 1	Homo sapiens	18-22
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Bilirubin	157-166	heme oxygenase 1	Homo sapiens	0-16
18799798-1	2008	Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin.	Bilirubin	157-166	heme oxygenase 1	Homo sapiens	18-22
18799798-3	2008	We here locally injected adenovirus containing human HO-1 gene (Ad-HO-1) into rat substantia nigra concomitantly with 1-methyl-4-phenylpyridinium (MPP(+)).	1-Methyl-4-phenylpyridinium	118-145	heme oxygenase 1	Homo sapiens	53-57
18799798-3	2008	We here locally injected adenovirus containing human HO-1 gene (Ad-HO-1) into rat substantia nigra concomitantly with 1-methyl-4-phenylpyridinium (MPP(+)).	1-Methyl-4-phenylpyridinium	118-145	heme oxygenase 1	Homo sapiens	67-71
18799798-3	2008	We here locally injected adenovirus containing human HO-1 gene (Ad-HO-1) into rat substantia nigra concomitantly with 1-methyl-4-phenylpyridinium (MPP(+)).	mangion-purified polysaccharide (Candida albicans)	147-150	heme oxygenase 1	Homo sapiens	53-57
18809379-0	2008	NS-398, a selective COX-2 inhibitor, inhibits proliferation of IL-1beta-stimulated vascular smooth muscle cells by induction of HO-1.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	0-6	heme oxygenase 1	Homo sapiens	128-132
18809379-4	2008	Furthermore, SnPPIX, a HO-1 inhibitor, reversed the effects of NS-398 on PGE(2) production, suggesting that COX-2 activity can be affected by HO-1.	Dinoprostone	73-79	heme oxygenase 1	Homo sapiens	142-146
18809379-1	2008	We investigated whether NS-398, a selective inhibitor of COX-2, induces HO-1 in IL-1beta-stimulated vascular smooth muscle cells (VSMC).	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	24-30	heme oxygenase 1	Homo sapiens	72-76
18809379-5	2008	Hemin, a HO-1 inducer, also reduced the production of PGE(2) and proliferation of IL-1beta-stimulated VSMC.	Prostaglandins E	54-57	heme oxygenase 1	Homo sapiens	9-13
18809379-4	2008	Furthermore, SnPPIX, a HO-1 inhibitor, reversed the effects of NS-398 on PGE(2) production, suggesting that COX-2 activity can be affected by HO-1.	tin protoporphyrin IX	13-19	heme oxygenase 1	Homo sapiens	23-27
18809379-8	2008	In conclusion, NS-398 inhibits proliferation of IL-1beta-stimulated VSMC by HO-1-derived CO.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	15-21	heme oxygenase 1	Homo sapiens	76-80
18809379-4	2008	Furthermore, SnPPIX, a HO-1 inhibitor, reversed the effects of NS-398 on PGE(2) production, suggesting that COX-2 activity can be affected by HO-1.	tin protoporphyrin IX	13-19	heme oxygenase 1	Homo sapiens	142-146
18809379-4	2008	Furthermore, SnPPIX, a HO-1 inhibitor, reversed the effects of NS-398 on PGE(2) production, suggesting that COX-2 activity can be affected by HO-1.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	63-69	heme oxygenase 1	Homo sapiens	23-27
18809379-4	2008	Furthermore, SnPPIX, a HO-1 inhibitor, reversed the effects of NS-398 on PGE(2) production, suggesting that COX-2 activity can be affected by HO-1.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	63-69	heme oxygenase 1	Homo sapiens	142-146
18809379-4	2008	Furthermore, SnPPIX, a HO-1 inhibitor, reversed the effects of NS-398 on PGE(2) production, suggesting that COX-2 activity can be affected by HO-1.	Dinoprostone	73-79	heme oxygenase 1	Homo sapiens	23-27
18696091-12	2008	Both cell types biosynthesize HO-1 and ferritin in response to heme.	Heme	63-67	heme oxygenase 1	Homo sapiens	30-34
18528644-10	2008	Heme oxygenase 1 expression increased and DMT1 expression decreased with higher heme Fe concentrations in the media.	Heme	80-84	heme oxygenase 1	Homo sapiens	0-16
18528644-10	2008	Heme oxygenase 1 expression increased and DMT1 expression decreased with higher heme Fe concentrations in the media.	Iron	85-87	heme oxygenase 1	Homo sapiens	0-16
18928848-3	2008	In addition, treatment with N-acetylcysteine, indomethacin, and heme oxygenase-1 inhibitors blocked reactive oxygen species production, antioxidant response element (ARE) gene expression, and Nrf2 accumulation that occurred in response to mechanical stress.	Reactive Oxygen Species	100-123	heme oxygenase 1	Homo sapiens	64-80
18778734-10	2008	While induction of heme oxygenase-1 was implicated in the cytoprotection by 15d-PGJ(2) under some experimental conditions, additional experiments indicated that this enzyme was not involved in the cytoprotection observed in this system.	15d-pgj	76-83	heme oxygenase 1	Homo sapiens	19-35
18985801-6	2008	However, in recent years a possible novel aspect in the mode of action of these compounds has been suggested; that is, the ultimate stimulation of the heme oxygenase-1 (HO-1) pathway is likely to account for the established and powerful antioxidant/anti-inflammatory properties of these polyphenols.	Polyphenols	287-298	heme oxygenase 1	Homo sapiens	151-167
18985801-6	2008	However, in recent years a possible novel aspect in the mode of action of these compounds has been suggested; that is, the ultimate stimulation of the heme oxygenase-1 (HO-1) pathway is likely to account for the established and powerful antioxidant/anti-inflammatory properties of these polyphenols.	Polyphenols	287-298	heme oxygenase 1	Homo sapiens	169-173
18798608-0	2008	X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors.	1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone	66-113	heme oxygenase 1	Homo sapiens	33-49
18798608-0	2008	X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors.	1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone	66-113	heme oxygenase 1	Homo sapiens	157-173
18798608-0	2008	X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors.	imidazole	141-150	heme oxygenase 1	Homo sapiens	33-49
18798608-0	2008	X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors.	imidazole	141-150	heme oxygenase 1	Homo sapiens	157-173
18975324-1	2008	OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress.	guanine-thymidine	15-32	heme oxygenase 1	Homo sapiens	53-58
18975324-1	2008	OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress.	guanine-thymidine	15-32	heme oxygenase 1	Homo sapiens	131-147
18975324-1	2008	OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress.	guanine-thymidine	15-32	heme oxygenase 1	Homo sapiens	149-153
18975324-1	2008	OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress.	Heme	109-113	heme oxygenase 1	Homo sapiens	53-58
18975324-1	2008	OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress.	Heme	109-113	heme oxygenase 1	Homo sapiens	131-147
18975324-1	2008	OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress.	Heme	109-113	heme oxygenase 1	Homo sapiens	149-153
18824663-3	2008	Although the HO-1 gene promoter contains consensus binding sites for proinflammatory/oxidative transcription factors like nuclear factor-kappaB, activating protein (AP)-1, and AP-2, the effects of HO inducers on these transcription factors in cardiac lesions of deoxycorticosterone acetate hypertension are not fully understood.	Desoxycorticosterone Acetate	262-289	heme oxygenase 1	Homo sapiens	13-17
18824663-5	2008	The cardioprotection by hemin was accompanied by increased HO-1, HO activity, cGMP, superoxide dismutase, catalase, the total antioxidant capacity alongside the reduction of 8-isoprostane, AP-1, AP-2, nuclear factor-kappaB, and c-Jun-NH(2)-terminal kinase, whereas chromium mesoporphyrin abolished the hemin effects.	Hemin	24-29	heme oxygenase 1	Homo sapiens	59-63
18799519-0	2008	A prolyl-hydroxylase inhibitor, ethyl-3,4-dihydroxybenzoate, induces haem oxygenase-1 expression in human cells through a mechanism independent of hypoxia-inducible factor-1alpha.	ethyl protocatechuate	32-59	heme oxygenase 1	Homo sapiens	69-85
18799519-4	2008	Under hypoxia (1% O(2)), the expression of HO-1 mRNA was decreased in HeLa cells, increased in D407 cells, and unchanged in ARPE-19 cells, while HIF-1alpha protein was accumulated in these cell lines.	o(2)	18-22	heme oxygenase 1	Homo sapiens	43-47
18799519-7	2008	Treatment with EDHB (250-500 microM) increased HIF-1alpha protein levels in HeLa and D407 cells, but not in ARPE-19 cells, whereas EDHB at lower concentrations (50-100 microM) consistently induced HO-1 mRNA expression (about 20-fold) in these three cell lines.	ethyl protocatechuate	15-19	heme oxygenase 1	Homo sapiens	197-201
18799519-7	2008	Treatment with EDHB (250-500 microM) increased HIF-1alpha protein levels in HeLa and D407 cells, but not in ARPE-19 cells, whereas EDHB at lower concentrations (50-100 microM) consistently induced HO-1 mRNA expression (about 20-fold) in these three cell lines.	ethyl protocatechuate	131-135	heme oxygenase 1	Homo sapiens	197-201
18799519-8	2008	Moreover, EDHB increased the HO-1 gene promoter activity via the enhancer that lacks a HIF-1-binding site.	ethyl protocatechuate	10-14	heme oxygenase 1	Homo sapiens	29-33
18799519-9	2008	In conclusion, the signals evoked by hypoxia and after EDHB treatment differentially regulate HO-1 mRNA expression through HIF-1alpha-independent mechanisms.	ethyl protocatechuate	55-59	heme oxygenase 1	Homo sapiens	94-98
18524839-10	2008	A stronger estimated effect of O(3) on FEV(1) was found in subjects carrying both the GSTP1 105Val variant and the HMOX1 long (GT)n repeat (-1.94%, 95% CI: -2.89% to -0.98%).	Ozone	31-35	heme oxygenase 1	Homo sapiens	115-120
18787101-1	2008	We investigated the role of heme oxygenase-1 (HO-1), a powerful anti-inflammatory and anti-oxidant enzyme, in modulating cigarette smoke (CS)-induced mucus secretion.	Cesium	138-140	heme oxygenase 1	Homo sapiens	28-44
18787101-1	2008	We investigated the role of heme oxygenase-1 (HO-1), a powerful anti-inflammatory and anti-oxidant enzyme, in modulating cigarette smoke (CS)-induced mucus secretion.	Cesium	138-140	heme oxygenase 1	Homo sapiens	46-50
18787101-4	2008	In French participants to the European Community Respiratory Health Survey II (n = 210, 30 to 53 years of age, 50% males) exposed to CS, a significant increase in the percentage of participants with chronic sputum was observed in those harboring at least one allele with a long (GT)(n) in the HO-1 promoter gene (&gt;33 repeats), which is associated with a low level of HO-1 protein expression, compared with those with a short number of (GT)n repeats (21.7% versus 8.6%, P = 0.047).	Cesium	133-135	heme oxygenase 1	Homo sapiens	293-297
18787101-4	2008	In French participants to the European Community Respiratory Health Survey II (n = 210, 30 to 53 years of age, 50% males) exposed to CS, a significant increase in the percentage of participants with chronic sputum was observed in those harboring at least one allele with a long (GT)(n) in the HO-1 promoter gene (&gt;33 repeats), which is associated with a low level of HO-1 protein expression, compared with those with a short number of (GT)n repeats (21.7% versus 8.6%, P = 0.047).	Cesium	133-135	heme oxygenase 1	Homo sapiens	370-374
18787101-6	2008	We conclude that HO-1 has a significant protective effect against airway mucus hypersecretion in animals and humans exposed to CS.	Cesium	127-129	heme oxygenase 1	Homo sapiens	17-21
18696091-14	2008	The persistence of HO-1 protein implies continuous exposure of CNS to free heme or an excessively sensitive transcriptional response of the HO-1 gene.	Heme	75-79	heme oxygenase 1	Homo sapiens	19-23
18701634-5	2008	HO-1 was induced in cultured mTALH cells by treatment with cobalt protoporphyrin (CoPP, 10 microM) or hemin (50 microM) or by transfection with a plasmid containing the human HO-1 isoform.	cobaltiprotoporphyrin	59-80	heme oxygenase 1	Homo sapiens	0-4
18689604-8	2008	Treatment with the antioxidants N-acetyl-l-cysteine or GSH reduced the expression of HO-1 induced by CSE.	Glutathione	55-58	heme oxygenase 1	Homo sapiens	85-89
18689604-0	2008	Cigarette smoke-induced expression of heme oxygenase-1 in human lung fibroblasts is regulated by intracellular glutathione.	Glutathione	111-122	heme oxygenase 1	Homo sapiens	38-54
18701634-5	2008	HO-1 was induced in cultured mTALH cells by treatment with cobalt protoporphyrin (CoPP, 10 microM) or hemin (50 microM) or by transfection with a plasmid containing the human HO-1 isoform.	cobaltiprotoporphyrin	82-86	heme oxygenase 1	Homo sapiens	0-4
18689604-7	2008	This induction of HO-1 paralleled a decrease in intracellular GSH, and a sustained reduction in GSH resulted in a dramatic increase in HO-1.	Glutathione	62-65	heme oxygenase 1	Homo sapiens	18-22
18689604-13	2008	Reduction of c-Fos and c-Jun nuclear translocation by SP-600125 attenuated the CSE-induced expression of HO-1.	pyrazolanthrone	54-63	heme oxygenase 1	Homo sapiens	105-109
18701634-5	2008	HO-1 was induced in cultured mTALH cells by treatment with cobalt protoporphyrin (CoPP, 10 microM) or hemin (50 microM) or by transfection with a plasmid containing the human HO-1 isoform.	Hemin	102-107	heme oxygenase 1	Homo sapiens	0-4
18689604-7	2008	This induction of HO-1 paralleled a decrease in intracellular GSH, and a sustained reduction in GSH resulted in a dramatic increase in HO-1.	Glutathione	96-99	heme oxygenase 1	Homo sapiens	135-139
18689604-8	2008	Treatment with the antioxidants N-acetyl-l-cysteine or GSH reduced the expression of HO-1 induced by CSE.	Acetylcysteine	32-51	heme oxygenase 1	Homo sapiens	85-89
18701634-7	2008	Induction of HO-1 via CoPP, hemin, or overexpression of the human HO-1 isoform significantly reduced ANG II-induced DHE fluorescence to 64+/-5, 64+/-8, and 41+/-4 RFU/microm2, respectively.	dihydroethidium	116-119	heme oxygenase 1	Homo sapiens	13-17
18701634-7	2008	Induction of HO-1 via CoPP, hemin, or overexpression of the human HO-1 isoform significantly reduced ANG II-induced DHE fluorescence to 64+/-5, 64+/-8, and 41+/-4 RFU/microm2, respectively.	dihydroethidium	116-119	heme oxygenase 1	Homo sapiens	66-70
18544348-6	2008	HO-1 ubiquitination in HEK293 cells was enhanced by zinc chloride, but suppressed with a zinc chelator (N,N,N",N"-tetrakis(2-pyridylmethyl)ethyl-enediamine), suggesting the involvement of a RING-E3 ligase in this process.	zinc chloride	52-65	heme oxygenase 1	Homo sapiens	0-4
18576916-1	2008	Heme oxygenase-1, an enzyme degrading heme to carbon monoxide, iron, and biliverdin, has been recognized as playing a crucial role in cellular defense against stressful conditions, not only related to heme release.	Heme	38-42	heme oxygenase 1	Homo sapiens	0-16
18576916-1	2008	Heme oxygenase-1, an enzyme degrading heme to carbon monoxide, iron, and biliverdin, has been recognized as playing a crucial role in cellular defense against stressful conditions, not only related to heme release.	Carbon Monoxide	46-61	heme oxygenase 1	Homo sapiens	0-16
18576916-1	2008	Heme oxygenase-1, an enzyme degrading heme to carbon monoxide, iron, and biliverdin, has been recognized as playing a crucial role in cellular defense against stressful conditions, not only related to heme release.	Iron	63-67	heme oxygenase 1	Homo sapiens	0-16
18576916-1	2008	Heme oxygenase-1, an enzyme degrading heme to carbon monoxide, iron, and biliverdin, has been recognized as playing a crucial role in cellular defense against stressful conditions, not only related to heme release.	Biliverdine	73-83	heme oxygenase 1	Homo sapiens	0-16
18576916-1	2008	Heme oxygenase-1, an enzyme degrading heme to carbon monoxide, iron, and biliverdin, has been recognized as playing a crucial role in cellular defense against stressful conditions, not only related to heme release.	Heme	201-205	heme oxygenase 1	Homo sapiens	0-16
18769149-13	2008	Conversely, transfection of Beas-2b with ho-1 siRNA augmented CSE-induced DISC formation and increased intracellular reactive oxygen species formation.	Reactive Oxygen Species	117-140	heme oxygenase 1	Homo sapiens	41-45
18769232-1	2008	PURPOSE OF REVIEW: Heme oxygenase-1 apart from converting heme to carbon monoxide, iron and biliverdin has been shown to exert anti-inflammatory, antiapoptotic and antioxidant actions.	Heme	58-62	heme oxygenase 1	Homo sapiens	19-35
18769232-1	2008	PURPOSE OF REVIEW: Heme oxygenase-1 apart from converting heme to carbon monoxide, iron and biliverdin has been shown to exert anti-inflammatory, antiapoptotic and antioxidant actions.	Carbon Monoxide	66-81	heme oxygenase 1	Homo sapiens	19-35
18769232-1	2008	PURPOSE OF REVIEW: Heme oxygenase-1 apart from converting heme to carbon monoxide, iron and biliverdin has been shown to exert anti-inflammatory, antiapoptotic and antioxidant actions.	Iron	83-87	heme oxygenase 1	Homo sapiens	19-35
18769232-1	2008	PURPOSE OF REVIEW: Heme oxygenase-1 apart from converting heme to carbon monoxide, iron and biliverdin has been shown to exert anti-inflammatory, antiapoptotic and antioxidant actions.	Biliverdine	92-102	heme oxygenase 1	Homo sapiens	19-35
18769232-3	2008	RECENT FINDINGS: Heme oxygenase-1 has been shown to be protective against atherosclerosis via decreasing ROS generation and proinflammatory cytokine production resulting in diminished lipid uptake and foam cell formation.	ros	105-108	heme oxygenase 1	Homo sapiens	17-33
18802114-0	2008	Lipoteichoic acid induces HO-1 expression via the TLR2/MyD88/c-Src/NADPH oxidase pathway and Nrf2 in human tracheal smooth muscle cells.	lipoteichoic acid	0-17	heme oxygenase 1	Homo sapiens	26-30
18802114-1	2008	Heme oxygenase (HO)-1 is a stress-inducible rate-limiting enzyme in heme degradation that confers cytoprotection against oxidative injury and provides a vital function in maintaining tissue homeostasis.	Heme	68-72	heme oxygenase 1	Homo sapiens	0-21
18802114-7	2008	These results demonstrated that LTA-induced ROS generation was mediated through the TLR2/MyD88/TRAF6/c-Src/NADPH oxidase pathway, in turn initiates the activation of Nrf2, and ultimately induces HO-1 expression in HTSMCs.	Reactive Oxygen Species	44-47	heme oxygenase 1	Homo sapiens	195-199
18689445-6	2008	The application of the HO-1-specific inhibitor zinc protoporphyrin IX (ZnPPIX) could inhibit the above IAA and hematin responses.	zinc protoporphyrin	47-69	heme oxygenase 1	Homo sapiens	23-27
18689445-6	2008	The application of the HO-1-specific inhibitor zinc protoporphyrin IX (ZnPPIX) could inhibit the above IAA and hematin responses.	zinc protoporphyrin	71-77	heme oxygenase 1	Homo sapiens	23-27
18586083-0	2008	Role of oxidative stress in the induction of metallothionein-2A and heme oxygenase-1 gene expression by the antineoplastic agent gallium nitrate in human lymphoma cells.	gallium nitrate	129-144	heme oxygenase 1	Homo sapiens	68-84
18786476-1	2008	Hemoxygenase (HO)-1 is an inducible isoform of the first and rate-controlling enzyme of the degradation of heme into iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Heme	107-111	heme oxygenase 1	Homo sapiens	0-19
18786476-1	2008	Hemoxygenase (HO)-1 is an inducible isoform of the first and rate-controlling enzyme of the degradation of heme into iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Iron	117-121	heme oxygenase 1	Homo sapiens	0-19
18786476-1	2008	Hemoxygenase (HO)-1 is an inducible isoform of the first and rate-controlling enzyme of the degradation of heme into iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Carbon Monoxide	123-138	heme oxygenase 1	Homo sapiens	0-19
18786476-1	2008	Hemoxygenase (HO)-1 is an inducible isoform of the first and rate-controlling enzyme of the degradation of heme into iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Biliverdine	144-154	heme oxygenase 1	Homo sapiens	0-19
18786476-1	2008	Hemoxygenase (HO)-1 is an inducible isoform of the first and rate-controlling enzyme of the degradation of heme into iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin.	Bilirubin	201-210	heme oxygenase 1	Homo sapiens	0-19
18786476-3	2008	Thus, the physiological induction of HO-1 may be an adaptive and beneficial response to several possibly noxious stimuli, including heme itself, suggesting a potentially autoprotective and autodefensive role in several pathophysiological states including acute coronary syndromes and stroke.	Heme	132-136	heme oxygenase 1	Homo sapiens	37-41
18566994-4	2008	The activation of Nrf2 by apo-10"-lycopenoic acid is associated with the induction of phase II detoxifying/antioxidant enzymes including heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1, glutathione S-transferases, and glutamate-cysteine ligases in BEAS-2B cells.	apo-10'-lycopenoic acid	26-49	heme oxygenase 1	Homo sapiens	137-187
18586083-6	2008	N-Acetyl-L-cysteine blocked gallium-induced MT2A and HO-1 expression and increased gallium"s cytotoxicity.	Acetylcysteine	0-19	heme oxygenase 1	Homo sapiens	53-57
18586083-6	2008	N-Acetyl-L-cysteine blocked gallium-induced MT2A and HO-1 expression and increased gallium"s cytotoxicity.	Gallium	28-35	heme oxygenase 1	Homo sapiens	53-57
18586083-2	2008	Using a DNA microarray to examine genes induced by gallium nitrate in CCRF-CEM cells, we found that gallium increased metallothionein-2A (MT2A) and heme oxygenase-1 (HO-1) gene expression and altered the levels of other stress-related genes.	gallium nitrate	51-66	heme oxygenase 1	Homo sapiens	148-164
18586083-8	2008	Gallium nitrate increased the phosphorylation of p38 mitogen-activated protein kinase and activated Nrf-2, a regulator of HO-1 gene transcription.	gallium nitrate	0-15	heme oxygenase 1	Homo sapiens	122-126
18586083-9	2008	Gallium-induced Nrf-2 activation and HO-1 expression were diminished by a p38 MAP kinase inhibitor.	Gallium	0-7	heme oxygenase 1	Homo sapiens	37-41
18586083-2	2008	Using a DNA microarray to examine genes induced by gallium nitrate in CCRF-CEM cells, we found that gallium increased metallothionein-2A (MT2A) and heme oxygenase-1 (HO-1) gene expression and altered the levels of other stress-related genes.	gallium nitrate	51-66	heme oxygenase 1	Homo sapiens	166-170
18586083-10	2008	We conclude that gallium nitrate induces cellular oxidative stress as an early event which then triggers the expression of HO-1 and MT2A through different pathways.	gallium nitrate	17-32	heme oxygenase 1	Homo sapiens	123-127
18586083-2	2008	Using a DNA microarray to examine genes induced by gallium nitrate in CCRF-CEM cells, we found that gallium increased metallothionein-2A (MT2A) and heme oxygenase-1 (HO-1) gene expression and altered the levels of other stress-related genes.	Gallium	51-58	heme oxygenase 1	Homo sapiens	148-164
18586083-2	2008	Using a DNA microarray to examine genes induced by gallium nitrate in CCRF-CEM cells, we found that gallium increased metallothionein-2A (MT2A) and heme oxygenase-1 (HO-1) gene expression and altered the levels of other stress-related genes.	Gallium	51-58	heme oxygenase 1	Homo sapiens	166-170
18586083-3	2008	MT2A and HO-1 were increased after 6 and 16 h of incubation with gallium nitrate.	gallium nitrate	65-80	heme oxygenase 1	Homo sapiens	9-13
18573251-6	2008	Inhibition of HO-1 activity using the HO-1 inhibitor tin protoporphyrin IX (SnPPIX), resulted in loss of cytoprotection.	tin protoporphyrin IX	53-74	heme oxygenase 1	Homo sapiens	14-18
18554677-0	2008	Metallothionein-III protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a PI3K and ERK/Nrf2-dependent manner.	Oxidopamine	37-54	heme oxygenase 1	Homo sapiens	108-124
18554677-3	2008	In this study, we demonstrate that MT-III prevents the accumulation of reactive oxygen species (ROS) in dopaminergic SH-SY5Y cells challenged with the Parkinson"s disease-related neurotoxin 6-hydroxydopamine (6-OHDA) by a mechanism that involves phosphatidylinositol 3-kinase (PI3K) and ERK kinase/NF-E2-related factor 2 (Nrf2) dependent induction of the stress response protein heme oxygenase-1 (HO-1).	Oxidopamine	190-207	heme oxygenase 1	Homo sapiens	379-395
18554677-3	2008	In this study, we demonstrate that MT-III prevents the accumulation of reactive oxygen species (ROS) in dopaminergic SH-SY5Y cells challenged with the Parkinson"s disease-related neurotoxin 6-hydroxydopamine (6-OHDA) by a mechanism that involves phosphatidylinositol 3-kinase (PI3K) and ERK kinase/NF-E2-related factor 2 (Nrf2) dependent induction of the stress response protein heme oxygenase-1 (HO-1).	Oxidopamine	190-207	heme oxygenase 1	Homo sapiens	397-401
18554677-5	2008	Also, MT-III up-regulates HO-1 expression and this expression confers neuroprotection against oxidative injury induced by 6-OHDA.	Oxidopamine	122-128	heme oxygenase 1	Homo sapiens	26-30
18554677-7	2008	Taken together, these results suggest that the PI3K and ERK/Nrf2 signaling pathway controls the intracellular levels of ROS by regulating the expression of the antioxidant enzyme HO-1.	Reactive Oxygen Species	120-123	heme oxygenase 1	Homo sapiens	179-183
18586007-0	2008	Epigallocatechin activates haem oxygenase-1 expression via protein kinase Cdelta and Nrf2.	gallocatechol	0-16	heme oxygenase 1	Homo sapiens	27-43
18586007-4	2008	EGC time and dose dependently increased HO-1 mRNA and protein expression but had minimal effect on expression of other ARE-regulated genes, including NAD(P)H:quinone oxidoreductase 1, glutathione cysteine ligase and ferritin.	gallocatechol	0-3	heme oxygenase 1	Homo sapiens	40-44
18586007-5	2008	siRNA knock down of Nrf2 significantly inhibited EGC-induced HO-1 expression.	gallocatechol	49-52	heme oxygenase 1	Homo sapiens	61-65
18573251-6	2008	Inhibition of HO-1 activity using the HO-1 inhibitor tin protoporphyrin IX (SnPPIX), resulted in loss of cytoprotection.	tin protoporphyrin IX	53-74	heme oxygenase 1	Homo sapiens	38-42
18586007-6	2008	Furthermore, inhibition of PKC by Ro-31-8220 dose dependently decreased EGC-induced HO-1 mRNA expression, whereas MAP kinase and phosphatidylinositol-3-kinase pathway inhibitors had no significant effect.	Ro 31-8220	34-44	heme oxygenase 1	Homo sapiens	84-88
18573251-6	2008	Inhibition of HO-1 activity using the HO-1 inhibitor tin protoporphyrin IX (SnPPIX), resulted in loss of cytoprotection.	tin protoporphyrin IX	76-82	heme oxygenase 1	Homo sapiens	14-18
18586007-6	2008	Furthermore, inhibition of PKC by Ro-31-8220 dose dependently decreased EGC-induced HO-1 mRNA expression, whereas MAP kinase and phosphatidylinositol-3-kinase pathway inhibitors had no significant effect.	gallocatechol	72-75	heme oxygenase 1	Homo sapiens	84-88
18586007-8	2008	PKCdelta inhibition significantly decreased EGC-induced HO-1 mRNA expression, whereas PKCalpha- and beta-specific inhibitors had no significant effect.	gallocatechol	44-47	heme oxygenase 1	Homo sapiens	56-60
18586007-9	2008	These results demonstrate for the first time that EGC-induced HO-1 expression occurs via PKCdelta and Nrf2.	gallocatechol	50-53	heme oxygenase 1	Homo sapiens	62-66
18573251-6	2008	Inhibition of HO-1 activity using the HO-1 inhibitor tin protoporphyrin IX (SnPPIX), resulted in loss of cytoprotection.	tin protoporphyrin IX	76-82	heme oxygenase 1	Homo sapiens	38-42
18573251-7	2008	Carbon monoxide, one of HO-1 catabolic products appeared to play a small role in CAPE protection.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	24-28
18573251-9	2008	These findings suggest an important role of HO-1 induction in CAPE cytoprotection against oxidant stress, which may not relate to CAPE structural antioxidant activity nor to its traditional enzymatic activity in decomposing heme but to a yet to be determined activity.	caffeic acid phenethyl ester	62-66	heme oxygenase 1	Homo sapiens	44-48
18312299-4	2008	METHODS: DNA of 99 patients that underwent complete surgical resection of OSCC was analyzed for GTn-repeat polymorphism in the HMOX-1 promoter by polymerase chain reaction, capillary electrophoresis and DNA sequencing.	Nitroglycerin	96-99	heme oxygenase 1	Homo sapiens	127-133
18657588-2	2008	In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1).	Heme	17-21	heme oxygenase 1	Homo sapiens	101-117
18657588-2	2008	In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1).	Heme	17-21	heme oxygenase 1	Homo sapiens	119-123
18657588-2	2008	In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1).	Heme	43-47	heme oxygenase 1	Homo sapiens	101-117
18657588-2	2008	In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1).	Heme	43-47	heme oxygenase 1	Homo sapiens	119-123
18657588-2	2008	In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1).	Biliverdine	62-72	heme oxygenase 1	Homo sapiens	101-117
18657588-2	2008	In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1).	Biliverdine	62-72	heme oxygenase 1	Homo sapiens	119-123
18459998-1	2008	Heme oxygenase-1 (HO-1) has a microsatellite polymorphism based on the number of guanosine-thymidine nucleotide repeats (GT) repeats that regulates expression levels and could have an impact on organ survival post-injury.	guanosine-thymidine nucleotide	81-111	heme oxygenase 1	Homo sapiens	0-16
18459998-1	2008	Heme oxygenase-1 (HO-1) has a microsatellite polymorphism based on the number of guanosine-thymidine nucleotide repeats (GT) repeats that regulates expression levels and could have an impact on organ survival post-injury.	guanosine-thymidine nucleotide	81-111	heme oxygenase 1	Homo sapiens	18-22
18584244-0	2008	Evidence that cisplatin-induced auditory damage is attenuated by downregulation of pro-inflammatory cytokines via Nrf2/HO-1.	Cisplatin	14-23	heme oxygenase 1	Homo sapiens	119-123
18584244-2	2008	We report here that flunarizine markedly attenuates cisplatin-induced pro-inflammatory cytokine secretion and their messenger RNA transcription as well as cisplatin cytotoxicity through the activation of Nrf2/HO-1 and downregulation of NF-kappaB.	Flunarizine	20-31	heme oxygenase 1	Homo sapiens	209-213
18584244-2	2008	We report here that flunarizine markedly attenuates cisplatin-induced pro-inflammatory cytokine secretion and their messenger RNA transcription as well as cisplatin cytotoxicity through the activation of Nrf2/HO-1 and downregulation of NF-kappaB.	Cisplatin	52-61	heme oxygenase 1	Homo sapiens	209-213
18584244-3	2008	In HEI-OC1 cells, overexpression of Nrf2/HO-1 by gene transfer or pharmacological approaches attenuated cisplatin-induced cytotoxicity and pro-inflammatory cytokine production.	Cisplatin	104-113	heme oxygenase 1	Homo sapiens	41-45
18644421-4	2008	Furthermore, RA stimulated the antioxidant enzyme heme oxygenase-1 (HO-1).	rosmarinic acid	13-15	heme oxygenase 1	Homo sapiens	50-66
18644421-4	2008	Furthermore, RA stimulated the antioxidant enzyme heme oxygenase-1 (HO-1).	rosmarinic acid	13-15	heme oxygenase 1	Homo sapiens	68-72
18644421-5	2008	We also demonstrated that the HO-1 induction by RA was associated with the protein kinase A (PKA) and phosphatidylinositiol-3-kinase (PI3K) signaling pathways.	rosmarinic acid	48-50	heme oxygenase 1	Homo sapiens	30-34
18776993-0	2008	Up-regulation of heme oxygenase-1 by isoflurane preconditioning during tolerance against neuronal injury induced by oxygen glucose deprivation.	Isoflurane	37-47	heme oxygenase 1	Homo sapiens	17-33
18776993-2	2008	The HO-1 isozyme is induced by a variety of factors such as heat, heme, ischemia, and hydrogen peroxide.	Heme	66-70	heme oxygenase 1	Homo sapiens	4-8
18776993-2	2008	The HO-1 isozyme is induced by a variety of factors such as heat, heme, ischemia, and hydrogen peroxide.	Hydrogen Peroxide	86-103	heme oxygenase 1	Homo sapiens	4-8
18776993-5	2008	Recently, isoflurane has been shown to up-regulate HO-1 in the liver.	Isoflurane	10-20	heme oxygenase 1	Homo sapiens	51-55
18776993-7	2008	Further study by reverse transcription-polymerase chain reaction and Western blot analysis showed that isoflurane preconditioning significantly increases HO-1 expression in oxygen glucose deprivation (OGD)-induced neuronal injury.	Isoflurane	103-113	heme oxygenase 1	Homo sapiens	154-158
18776993-9	2008	These findings indicated that the neuroprotective role of isoflurane preconditioning against OGD-induced injury might be associated with its role in up-regulating HO-1 in ischemic neurons.	Isoflurane	58-68	heme oxygenase 1	Homo sapiens	163-167
18584244-4	2008	On the contrary, inhibition of Nrf2/HO-1 signaling by pharmacological inhibitors or specific small interfering RNAs significantly abolished the beneficial effects of flunarizine.	Flunarizine	166-177	heme oxygenase 1	Homo sapiens	36-40
18584244-7	2008	Finally, orally administrated Sibelium, the trade name of flunarizine, suppressed the increase of pro-inflammatory cytokines by cisplatin in both serum and cochleas of mice, whereas it increased HO-1 expression in cochleas.	Flunarizine	30-38	heme oxygenase 1	Homo sapiens	195-199
18584244-8	2008	These results indicate that flunarizine induces a protective effect against cisplatin ototoxicity through the downregulation of NF-kappaB by Nrf2/HO-1 activation and the resulting inhibition of pro-inflammatory cytokine production in vitro and in vivo.	Flunarizine	28-39	heme oxygenase 1	Homo sapiens	146-150
18584244-8	2008	These results indicate that flunarizine induces a protective effect against cisplatin ototoxicity through the downregulation of NF-kappaB by Nrf2/HO-1 activation and the resulting inhibition of pro-inflammatory cytokine production in vitro and in vivo.	Cisplatin	76-85	heme oxygenase 1	Homo sapiens	146-150
18631371-6	2008	Additionally, H(2)O(2) treatment induced upregulation of CHOP, GRP78 and several representative endoplasmic reticulum (ER) stress-responsive proteins, including heme oxygenase-1.	Hydrogen Peroxide	14-22	heme oxygenase 1	Homo sapiens	161-177
18412543-3	2008	Fluorescence correlation spectroscopy was used to investigate the mobility of hBVR in living cells and its function in the nuclear transport of haematin for induction of HO-1.	Hemin	144-152	heme oxygenase 1	Homo sapiens	170-174
18556172-9	2008	Incidentally, MT, Hsp70 and HO-1 showed similar responses to Cd exposure.	Cadmium	61-63	heme oxygenase 1	Homo sapiens	28-32
18539158-2	2008	In this study, we found that the expressions of anti-oxidant proteins (gamma-glutamylcysteine ligase heavy chain (gamma-GCL h), heme oxygenase-1, thioredoxin and peroxiredoxin1) in TAM-resistant MCF-7 (TAMR-MCF-7) cells were higher than control MCF-7 cells.	Tamoxifen	181-184	heme oxygenase 1	Homo sapiens	128-144
18556172-7	2008	It remained essentially unchanged with 2.5 microM Cd exposure of Sertoli cells; however, MT, Hsp70 and HO-1 were significantly increased by Cd exposure.	Cadmium	140-142	heme oxygenase 1	Homo sapiens	103-107
18556172-8	2008	As a result, Cd-induced MT was protected Sertoli cells against apoptosis, and Cd-induced HO-1 was involved in protection against oxidative stress.	Cadmium	78-80	heme oxygenase 1	Homo sapiens	89-93
18424257-2	2008	Here, we report that treatment of human breast epithelial (MCF10A) cells with EGCG induces the expression of glutamate-cysteine ligase, manganese superoxide dismutase (MnSOD), and heme oxygenase-1 (HO-1).	epigallocatechin gallate	78-82	heme oxygenase 1	Homo sapiens	180-196
18424257-2	2008	Here, we report that treatment of human breast epithelial (MCF10A) cells with EGCG induces the expression of glutamate-cysteine ligase, manganese superoxide dismutase (MnSOD), and heme oxygenase-1 (HO-1).	epigallocatechin gallate	78-82	heme oxygenase 1	Homo sapiens	198-202
18424257-5	2008	Silencing of Nrf2 by siRNA gene knockdown rendered the MCF10A cells less sensitive to the EGCG-induced expression of HO-1 and MnSOD.	epigallocatechin gallate	90-94	heme oxygenase 1	Homo sapiens	117-121
18550526-0	2008	BACH1 is a specific repressor of HMOX1 that is inactivated by arsenite.	arsenite	62-70	heme oxygenase 1	Homo sapiens	33-38
18550526-2	2008	To prevent accumulation, the inducible enzyme heme oxygenase-1 (HMOX1) catalyzes degradation of heme.	Heme	46-50	heme oxygenase 1	Homo sapiens	64-69
18550526-4	2008	Conversely, increased intracellular heme or sulfhydryl oxidation inactivate BACH1, permitting transcriptional induction of HMOX1.	Heme	36-40	heme oxygenase 1	Homo sapiens	123-128
18550526-6	2008	We show that BACH1 is inactivated at low micromolar arsenite concentrations and that BACH1 inactivation is necessary and sufficient for transcriptional induction of HMOX1.	arsenite	52-60	heme oxygenase 1	Homo sapiens	165-170
18550526-8	2008	The loss of BACH1 function in human keratinocytes results almost exclusively in HMOX1 induction, suggesting that BACH1 may function as a rheostat regulating levels of intracellular free heme.	Heme	186-190	heme oxygenase 1	Homo sapiens	80-85
18219551-0	2008	Heme oxygenase-1 participates in the anti-inflammatory activity of taurine chloramine.	N-chlorotaurine	67-85	heme oxygenase 1	Homo sapiens	0-16
18412543-9	2008	Experiments with nuclear localization, export signal mutants and si-hBVR [siRNA (small interfering RNA) specific to hBVR] indicate that nuclear localization of hBVR is required for induction of HO-1 by haematin.	Hemin	202-210	heme oxygenase 1	Homo sapiens	194-198
18443197-0	2008	Serum bilirubin and ferritin levels link heme oxygenase-1 gene promoter polymorphism and susceptibility to coronary artery disease in diabetic patients.	Bilirubin	6-15	heme oxygenase 1	Homo sapiens	41-57
18712632-4	2008	The results show that alpha(1)-microglobulin prevents intracellular oxidation and up-regulation of heme oxygenase-1 induced by heme, hydrogen peroxide and Fenton reaction-generated hydroxyl radicals in the culture medium.	Hydrogen Peroxide	133-150	heme oxygenase 1	Homo sapiens	99-115
18712632-4	2008	The results show that alpha(1)-microglobulin prevents intracellular oxidation and up-regulation of heme oxygenase-1 induced by heme, hydrogen peroxide and Fenton reaction-generated hydroxyl radicals in the culture medium.	Hydroxyl Radical	181-198	heme oxygenase 1	Homo sapiens	99-115
18440590-10	2008	In patients with CAF-MD, the inducible enzyme HO-1 is more expressed in the left atrial areas that show greater structural remodeling.	caf-md	17-23	heme oxygenase 1	Homo sapiens	46-50
18443197-3	2008	The aim of this study was to assess the association of the length of (GT)(n) repeats in the HO-1 gene promoter with serum bilirubin, markers of iron status, and the development of coronary artery disease (CAD).	Bilirubin	122-131	heme oxygenase 1	Homo sapiens	92-96
18443197-3	2008	The aim of this study was to assess the association of the length of (GT)(n) repeats in the HO-1 gene promoter with serum bilirubin, markers of iron status, and the development of coronary artery disease (CAD).	Iron	144-148	heme oxygenase 1	Homo sapiens	92-96
18443197-9	2008	With adjustment for both serum bilirubin and ferritin, the effect of HO-1 promoter polymorphism on susceptibility to CAD disappeared.	Bilirubin	31-40	heme oxygenase 1	Homo sapiens	69-73
18443197-10	2008	CONCLUSIONS: Length polymorphism in the HO-1 gene promoter is correlated with susceptibility to CAD in diabetic patients, and this effect might be conveyed through its influence on serum bilirubin and ferritin.	Bilirubin	187-196	heme oxygenase 1	Homo sapiens	40-44
18331200-1	2008	Heme oxygenase-1 is the rate-limiting enzyme for the degradation of the prooxidant heme.	Heme	83-87	heme oxygenase 1	Homo sapiens	0-16
18634931-0	2008	Hydrogen peroxide induces heme oxygenase-1 and dentin sialophosphoprotein mRNA in human pulp cells.	Hydrogen Peroxide	0-17	heme oxygenase 1	Homo sapiens	26-42
18634931-1	2008	Although the induction of heme oxygenase-1 (HO-1) by hydrogen peroxide (H2O2) has been reported, the HO-1 and odontoblastic differentiation-inducing effects against H2O2 have not been clarified in human pulp cells.	Hydrogen Peroxide	53-70	heme oxygenase 1	Homo sapiens	26-42
18634931-1	2008	Although the induction of heme oxygenase-1 (HO-1) by hydrogen peroxide (H2O2) has been reported, the HO-1 and odontoblastic differentiation-inducing effects against H2O2 have not been clarified in human pulp cells.	Hydrogen Peroxide	53-70	heme oxygenase 1	Homo sapiens	44-48
18634931-1	2008	Although the induction of heme oxygenase-1 (HO-1) by hydrogen peroxide (H2O2) has been reported, the HO-1 and odontoblastic differentiation-inducing effects against H2O2 have not been clarified in human pulp cells.	Hydrogen Peroxide	72-76	heme oxygenase 1	Homo sapiens	26-42
18634931-1	2008	Although the induction of heme oxygenase-1 (HO-1) by hydrogen peroxide (H2O2) has been reported, the HO-1 and odontoblastic differentiation-inducing effects against H2O2 have not been clarified in human pulp cells.	Hydrogen Peroxide	72-76	heme oxygenase 1	Homo sapiens	44-48
18634931-3	2008	H2O2 decreased cell viability but increased HO-1 and DSPP expression in a concentration- and time-dependent manner.	Hydrogen Peroxide	0-4	heme oxygenase 1	Homo sapiens	44-48
18634931-4	2008	Antioxidants and inhibitors of HO-1, phosphatidylinositol-3"-kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase blocked H2O2-induced cytotoxicity and the expression of HO-1 and DSPP mRNA in pulp cells.	Hydrogen Peroxide	157-161	heme oxygenase 1	Homo sapiens	31-35
18634931-4	2008	Antioxidants and inhibitors of HO-1, phosphatidylinositol-3"-kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase blocked H2O2-induced cytotoxicity and the expression of HO-1 and DSPP mRNA in pulp cells.	Hydrogen Peroxide	157-161	heme oxygenase 1	Homo sapiens	205-209
18634931-5	2008	These data suggest that the induction of HO-1 by H2O2 in pulp cells plays a protective role against the cytotoxic effects of H2O2 and stimulates DSPP expression, resulting in premature odontoblast differentiation through pathways that involve phosphatidylinositol-3"-kinase, p38, and extracellular signal-regulated kinase.	Hydrogen Peroxide	49-53	heme oxygenase 1	Homo sapiens	41-45
18634931-5	2008	These data suggest that the induction of HO-1 by H2O2 in pulp cells plays a protective role against the cytotoxic effects of H2O2 and stimulates DSPP expression, resulting in premature odontoblast differentiation through pathways that involve phosphatidylinositol-3"-kinase, p38, and extracellular signal-regulated kinase.	Hydrogen Peroxide	125-129	heme oxygenase 1	Homo sapiens	41-45
18636201-5	2008	In addition, combination treatment with As2O3 and sulindac increased reactive oxygen species (ROS) and oxidative stress, as evidenced by the heme oxygenase-1 (HO-1) expression and mitogen-activated protein kinase (MAPK) phosphorylation.	Arsenic Trioxide	40-45	heme oxygenase 1	Homo sapiens	141-157
18636201-5	2008	In addition, combination treatment with As2O3 and sulindac increased reactive oxygen species (ROS) and oxidative stress, as evidenced by the heme oxygenase-1 (HO-1) expression and mitogen-activated protein kinase (MAPK) phosphorylation.	Arsenic Trioxide	40-45	heme oxygenase 1	Homo sapiens	159-163
18636201-5	2008	In addition, combination treatment with As2O3 and sulindac increased reactive oxygen species (ROS) and oxidative stress, as evidenced by the heme oxygenase-1 (HO-1) expression and mitogen-activated protein kinase (MAPK) phosphorylation.	Sulindac	50-58	heme oxygenase 1	Homo sapiens	141-157
18636201-5	2008	In addition, combination treatment with As2O3 and sulindac increased reactive oxygen species (ROS) and oxidative stress, as evidenced by the heme oxygenase-1 (HO-1) expression and mitogen-activated protein kinase (MAPK) phosphorylation.	Sulindac	50-58	heme oxygenase 1	Homo sapiens	159-163
18636201-8	2008	Combination treatment with As2O3 and sulindac induced oxidative DNA damage in a time-dependent fashion, which was evaluated by H2AX phosphorylation along with HO-1 induction.	Arsenic Trioxide	27-32	heme oxygenase 1	Homo sapiens	159-163
18636201-8	2008	Combination treatment with As2O3 and sulindac induced oxidative DNA damage in a time-dependent fashion, which was evaluated by H2AX phosphorylation along with HO-1 induction.	Sulindac	37-45	heme oxygenase 1	Homo sapiens	159-163
17964723-6	2008	Human embryonic kidney (HEK) 293T cells treated with 10 microM CoPP expressed 20-fold higher HO-1 levels when compared to controls; this effect was suppressed by transfection with the dominant negative for the nuclear factor-erythroid 2-related factor 2 (Nrf2).	cobaltiprotoporphyrin	63-67	heme oxygenase 1	Homo sapiens	93-97
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Oxygen	45-47	heme oxygenase 1	Homo sapiens	6-22
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Oxygen	45-47	heme oxygenase 1	Homo sapiens	24-29
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	NADP	53-58	heme oxygenase 1	Homo sapiens	6-22
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	NADP	53-58	heme oxygenase 1	Homo sapiens	24-29
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Heme	6-10	heme oxygenase 1	Homo sapiens	24-29
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Biliverdine	90-100	heme oxygenase 1	Homo sapiens	6-22
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Biliverdine	90-100	heme oxygenase 1	Homo sapiens	24-29
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Carbon Monoxide	102-104	heme oxygenase 1	Homo sapiens	6-22
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Carbon Monoxide	102-104	heme oxygenase 1	Homo sapiens	24-29
18593583-0	2008	The coffee diterpene kahweol induces heme oxygenase-1 via the PI3K and p38/Nrf2 pathway to protect human dopaminergic neurons from 6-hydroxydopamine-derived oxidative stress.	Diterpenes	11-20	heme oxygenase 1	Homo sapiens	37-53
18593583-0	2008	The coffee diterpene kahweol induces heme oxygenase-1 via the PI3K and p38/Nrf2 pathway to protect human dopaminergic neurons from 6-hydroxydopamine-derived oxidative stress.	kahweol	21-28	heme oxygenase 1	Homo sapiens	37-53
18593583-0	2008	The coffee diterpene kahweol induces heme oxygenase-1 via the PI3K and p38/Nrf2 pathway to protect human dopaminergic neurons from 6-hydroxydopamine-derived oxidative stress.	Oxidopamine	131-148	heme oxygenase 1	Homo sapiens	37-53
18593583-3	2008	Kahweol also up-regulated heme oxygenase-1 (HO-1) expression, which conferred neuroprotection against 6-OHDA-induced oxidative injury.	Oxidopamine	102-108	heme oxygenase 1	Homo sapiens	26-42
18593583-3	2008	Kahweol also up-regulated heme oxygenase-1 (HO-1) expression, which conferred neuroprotection against 6-OHDA-induced oxidative injury.	Oxidopamine	102-108	heme oxygenase 1	Homo sapiens	44-48
18593583-4	2008	Moreover, kahweol induced PI3K and p38 activation, which are involved in the induction of Nrf2, HO-1 expression, and neuroprotection.	kahweol	10-17	heme oxygenase 1	Homo sapiens	96-100
18593583-5	2008	These results suggest that regulation of the anti-oxidant enzyme HO-1 via the PI3K and p38/Nrf2 signaling pathways controls the intracellular levels of ROS.	ros	152-155	heme oxygenase 1	Homo sapiens	65-69
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Iron	115-119	heme oxygenase 1	Homo sapiens	6-22
18487208-2	2008	Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron.	Iron	115-119	heme oxygenase 1	Homo sapiens	24-29
18487208-4	2008	Here we report spectroscopic detection of a transient intermediate during oxidation by hHO-1 of alpha-meso-phenylheme-IX, alpha-meso-(p-methylphenyl)-mesoheme-III, and alpha-meso-(p-trifluoromethylphenyl)-mesoheme-III.	alpha-meso-phenylheme-ix	96-120	heme oxygenase 1	Homo sapiens	87-92
18487208-4	2008	Here we report spectroscopic detection of a transient intermediate during oxidation by hHO-1 of alpha-meso-phenylheme-IX, alpha-meso-(p-methylphenyl)-mesoheme-III, and alpha-meso-(p-trifluoromethylphenyl)-mesoheme-III.	alpha-meso-(p-methylphenyl)-mesoheme	122-158	heme oxygenase 1	Homo sapiens	87-92
18487208-4	2008	Here we report spectroscopic detection of a transient intermediate during oxidation by hHO-1 of alpha-meso-phenylheme-IX, alpha-meso-(p-methylphenyl)-mesoheme-III, and alpha-meso-(p-trifluoromethylphenyl)-mesoheme-III.	alpha-meso-(p-trifluoromethylphenyl)-mesoheme	168-213	heme oxygenase 1	Homo sapiens	87-92
18487208-11	2008	The hHO-1-isoporphyrin complexes were found to have half-lives of 1.7 and 2.4 h for the p-trifluoromethyl- and p-methyl-substituted phenylhemes, respectively.	p-trifluoromethyl- and p-methyl-substituted phenylhemes	88-143	heme oxygenase 1	Homo sapiens	4-9
18487208-12	2008	The addition of NADPH-P450 reductase to the H2O2-generated hHO-1-isoporphyrin complex produced alpha-biliverdin, confirming its role as a reaction intermediate.	Hydrogen Peroxide	44-48	heme oxygenase 1	Homo sapiens	59-64
18487208-12	2008	The addition of NADPH-P450 reductase to the H2O2-generated hHO-1-isoporphyrin complex produced alpha-biliverdin, confirming its role as a reaction intermediate.	biliverdin	95-111	heme oxygenase 1	Homo sapiens	59-64
18487208-13	2008	Identification of an isoporphyrin intermediate in the catalytic sequence of hHO-1, the first such intermediate observed in hemoprotein catalysis, completes our understanding of the critical first step of heme oxidation.	isoporphyrin	21-33	heme oxygenase 1	Homo sapiens	76-81
18487208-13	2008	Identification of an isoporphyrin intermediate in the catalytic sequence of hHO-1, the first such intermediate observed in hemoprotein catalysis, completes our understanding of the critical first step of heme oxidation.	Heme	204-208	heme oxygenase 1	Homo sapiens	76-81
18435907-5	2008	Interestingly, the effects of tranilast on LPS-induced PGE(2), NO, TNF-alpha, and IL-1beta production were partially reversed by the HO-1 inhibitor tin protoporphyrin, suggesting that tranilast-induced HO-1 expression is at least partly responsible for the resulting anti-inflammatory effects of the drug.	protoporphyrin IX	152-166	heme oxygenase 1	Homo sapiens	133-137
18435907-5	2008	Interestingly, the effects of tranilast on LPS-induced PGE(2), NO, TNF-alpha, and IL-1beta production were partially reversed by the HO-1 inhibitor tin protoporphyrin, suggesting that tranilast-induced HO-1 expression is at least partly responsible for the resulting anti-inflammatory effects of the drug.	protoporphyrin IX	152-166	heme oxygenase 1	Homo sapiens	202-206
18452993-5	2008	In addition, L-theanine partially prevented both rotenone- and dieldrin-induced heme oxygenase-1 (HO-1) up-regulation.	theanine	13-23	heme oxygenase 1	Homo sapiens	80-96
18547064-0	2008	Structure-activity relationships of methoxychalcones as inducers of heme oxygenase-1.	methoxychalcones	36-52	heme oxygenase 1	Homo sapiens	68-84
18547064-3	2008	Recent evidence indicates that the bioactivity of hydroxy-chalcones is correlated with their intrinsic property to induce the antioxidant and cytoprotective enzyme heme oxygenase-1 (HO-1).	hydroxy-chalcones	50-67	heme oxygenase 1	Homo sapiens	164-180
18547064-3	2008	Recent evidence indicates that the bioactivity of hydroxy-chalcones is correlated with their intrinsic property to induce the antioxidant and cytoprotective enzyme heme oxygenase-1 (HO-1).	hydroxy-chalcones	50-67	heme oxygenase 1	Homo sapiens	182-186
18547064-7	2008	This study provides additional information on the structural features that methoxychalcones and natural antioxidants need to possess to be considered as therapeutic agents for maximizing HO-1 expression and activity.	methoxychalcones	75-91	heme oxygenase 1	Homo sapiens	187-191
18691515-7	2008	Dermal fibroblasts exposed to 25 micromol/L ferulic acid ethyl ester in the presence of 500 micromol/L hydrogen peroxide showed an increased level of both heme oxygenase-1 and heat shock protein-70 compared with dermal fibroblasts treated with hydrogen peroxide alone.	ethyl ferulate	44-68	heme oxygenase 1	Homo sapiens	155-197
18691515-7	2008	Dermal fibroblasts exposed to 25 micromol/L ferulic acid ethyl ester in the presence of 500 micromol/L hydrogen peroxide showed an increased level of both heme oxygenase-1 and heat shock protein-70 compared with dermal fibroblasts treated with hydrogen peroxide alone.	Hydrogen Peroxide	103-120	heme oxygenase 1	Homo sapiens	155-197
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Heme	22-26	heme oxygenase 1	Homo sapiens	40-44
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Carbon Monoxide	81-96	heme oxygenase 1	Homo sapiens	22-38
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Carbon Monoxide	81-96	heme oxygenase 1	Homo sapiens	40-44
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Carbon Monoxide	98-100	heme oxygenase 1	Homo sapiens	22-38
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Carbon Monoxide	98-100	heme oxygenase 1	Homo sapiens	40-44
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Biliverdine	106-116	heme oxygenase 1	Homo sapiens	22-38
18381758-1	2008	The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation.	Biliverdine	106-116	heme oxygenase 1	Homo sapiens	40-44
18381758-2	2008	Here we report that both HO-1 expression and activity can be highly increased in undifferentiated human mesenchymal stem cells (MSCs) treated with hemin, a known HO-1 inducer.	Hemin	147-152	heme oxygenase 1	Homo sapiens	25-29
18381758-2	2008	Here we report that both HO-1 expression and activity can be highly increased in undifferentiated human mesenchymal stem cells (MSCs) treated with hemin, a known HO-1 inducer.	Hemin	147-152	heme oxygenase 1	Homo sapiens	162-166
18381758-3	2008	However, HO-1 mRNA and protein expression gradually decrease when MSCs undergo neural differentiation in vitro, making them extremely susceptible to glutamate-mediated cytotoxicity.	Glutamic Acid	149-158	heme oxygenase 1	Homo sapiens	9-13
18460015-2	2008	A HO-1 gene promoter microsatellite (GT)(n) dinucleotide repeat polymorphism was associated with regulation of HO-1 in response to inflammatory stimuli.	(n) dinucleotide	40-56	heme oxygenase 1	Homo sapiens	2-6
18460015-2	2008	A HO-1 gene promoter microsatellite (GT)(n) dinucleotide repeat polymorphism was associated with regulation of HO-1 in response to inflammatory stimuli.	(n) dinucleotide	40-56	heme oxygenase 1	Homo sapiens	111-115
18452993-5	2008	In addition, L-theanine partially prevented both rotenone- and dieldrin-induced heme oxygenase-1 (HO-1) up-regulation.	Rotenone	49-57	heme oxygenase 1	Homo sapiens	80-96
18452993-5	2008	In addition, L-theanine partially prevented both rotenone- and dieldrin-induced heme oxygenase-1 (HO-1) up-regulation.	Dieldrin	63-71	heme oxygenase 1	Homo sapiens	80-96
17712531-8	2008	Consistent with this, when the acidification of endosomes is prevented by bafilomycin then heme oxygenase-1 induction by heme-HPX no longer occurs.	bafilomycin	74-85	heme oxygenase 1	Homo sapiens	91-107
18567745-0	2008	Enterolactone induces heme oxygenase-1 expression through nuclear factor-E2-related factor 2 activation in endothelial cells.	2,3-bis(3'-hydroxybenzyl)butyrolactone	0-13	heme oxygenase 1	Homo sapiens	22-38
18567745-3	2008	Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health.	Bilirubin	202-211	heme oxygenase 1	Homo sapiens	109-125
18567745-3	2008	Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health.	Bilirubin	202-211	heme oxygenase 1	Homo sapiens	127-131
18567745-3	2008	Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health.	Biliverdine	216-226	heme oxygenase 1	Homo sapiens	109-125
18567745-3	2008	Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health.	Biliverdine	216-226	heme oxygenase 1	Homo sapiens	127-131
18567745-3	2008	Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health.	Carbon Monoxide	238-253	heme oxygenase 1	Homo sapiens	109-125
18567745-3	2008	Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health.	Carbon Monoxide	238-253	heme oxygenase 1	Homo sapiens	127-131
18567745-4	2008	Our aim was therefore to assess whether enterolactone has indirect antioxidative effects via induction of HO-1 in endothelial cells.	2,3-bis(3'-hydroxybenzyl)butyrolactone	40-53	heme oxygenase 1	Homo sapiens	106-110
18567745-5	2008	The effect of enterolactone on HO-1 mRNA and protein expression in human umbilical vein endothelial cells (HUVEC) was analyzed by quantitative real-time PCR and western blot.	2,3-bis(3'-hydroxybenzyl)butyrolactone	14-27	heme oxygenase 1	Homo sapiens	31-35
18567745-6	2008	The role of nuclear factor-E2-related factor 2 (Nrf2) in HO-1 induction by enterolactone was studied using small interfering RNA (siRNA) and chromatin immunoprecipitation (ChIP) methods.	2,3-bis(3'-hydroxybenzyl)butyrolactone	75-88	heme oxygenase 1	Homo sapiens	57-61
18567745-7	2008	Our results showed that enterolactone induced HO-1 in HUVEC in a time- and concentration-dependent manner.	2,3-bis(3'-hydroxybenzyl)butyrolactone	24-37	heme oxygenase 1	Homo sapiens	46-50
18567745-8	2008	The induction appeared to be mediated via the transcription factor Nrf2, as Nrf2 siRNA abolished the HO-1 induction by enterolactone.	2,3-bis(3'-hydroxybenzyl)butyrolactone	119-132	heme oxygenase 1	Homo sapiens	101-105
18567745-9	2008	We also showed using ChIP that exposure to enterolactone increased the binding of Nrf2 to the promoter region of HO-1.	2,3-bis(3'-hydroxybenzyl)butyrolactone	43-56	heme oxygenase 1	Homo sapiens	113-117
18567745-10	2008	In conclusion, enterolactone increases the expression of HO-1 via Nrf2, which may contribute to its vasculoprotective effects.	2,3-bis(3'-hydroxybenzyl)butyrolactone	15-28	heme oxygenase 1	Homo sapiens	57-61
18440740-9	2008	We also found that PD98059, a MEK (MAPK/ERK kinase) inhibitor, attenuated the eupatilin-induced HO-1 expression and nuclear translocation of transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2).	eupatilin	78-87	heme oxygenase 1	Homo sapiens	96-100
18523255-1	2008	The induction of heme oxygenase 1 (HO-1) by a single treatment with cobalt protoporphyrin (CoPPIX) protects against inflammatory liver failure and ischemia reperfusion injury after allotransplantation.	cobaltiprotoporphyrin	68-89	heme oxygenase 1	Homo sapiens	17-33
18523255-1	2008	The induction of heme oxygenase 1 (HO-1) by a single treatment with cobalt protoporphyrin (CoPPIX) protects against inflammatory liver failure and ischemia reperfusion injury after allotransplantation.	cobaltiprotoporphyrin	68-89	heme oxygenase 1	Homo sapiens	35-39
18523255-1	2008	The induction of heme oxygenase 1 (HO-1) by a single treatment with cobalt protoporphyrin (CoPPIX) protects against inflammatory liver failure and ischemia reperfusion injury after allotransplantation.	coppix	91-97	heme oxygenase 1	Homo sapiens	17-33
18523255-1	2008	The induction of heme oxygenase 1 (HO-1) by a single treatment with cobalt protoporphyrin (CoPPIX) protects against inflammatory liver failure and ischemia reperfusion injury after allotransplantation.	coppix	91-97	heme oxygenase 1	Homo sapiens	35-39
18523255-3	2008	To investigate the poorly understood mechanism of CoPPIX-induced HO-1 activity in more detail, we performed gene expression analysis in murine liver, revealing the up-regulation of STAT3 after CoPPIX treatment.	coppix	50-56	heme oxygenase 1	Homo sapiens	65-69
18523255-3	2008	To investigate the poorly understood mechanism of CoPPIX-induced HO-1 activity in more detail, we performed gene expression analysis in murine liver, revealing the up-regulation of STAT3 after CoPPIX treatment.	coppix	193-199	heme oxygenase 1	Homo sapiens	65-69
18598766-6	2008	PI3K inhibitor LY294002 could block the elevation of HO-1 protein expression and reverse the protective effect of alpha-Gal silencing and GS-IB4 against CDC.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	15-23	heme oxygenase 1	Homo sapiens	53-57
18440740-7	2008	Heme oxygenase-1 (HO-1), which is known as a cytoprotective enzyme due to its anti-inflammatory actions, is a candidate protein since ZnPP, an HO-1 inhibitor, repressed the protective effect of eupatilin on indomethacin-induced cell damage in a concentration-dependent manner.	zinc protoporphyrin	134-138	heme oxygenase 1	Homo sapiens	0-16
18440740-7	2008	Heme oxygenase-1 (HO-1), which is known as a cytoprotective enzyme due to its anti-inflammatory actions, is a candidate protein since ZnPP, an HO-1 inhibitor, repressed the protective effect of eupatilin on indomethacin-induced cell damage in a concentration-dependent manner.	zinc protoporphyrin	134-138	heme oxygenase 1	Homo sapiens	18-22
18440740-7	2008	Heme oxygenase-1 (HO-1), which is known as a cytoprotective enzyme due to its anti-inflammatory actions, is a candidate protein since ZnPP, an HO-1 inhibitor, repressed the protective effect of eupatilin on indomethacin-induced cell damage in a concentration-dependent manner.	zinc protoporphyrin	134-138	heme oxygenase 1	Homo sapiens	143-147
18440740-7	2008	Heme oxygenase-1 (HO-1), which is known as a cytoprotective enzyme due to its anti-inflammatory actions, is a candidate protein since ZnPP, an HO-1 inhibitor, repressed the protective effect of eupatilin on indomethacin-induced cell damage in a concentration-dependent manner.	Indomethacin	207-219	heme oxygenase 1	Homo sapiens	0-16
18440740-7	2008	Heme oxygenase-1 (HO-1), which is known as a cytoprotective enzyme due to its anti-inflammatory actions, is a candidate protein since ZnPP, an HO-1 inhibitor, repressed the protective effect of eupatilin on indomethacin-induced cell damage in a concentration-dependent manner.	Indomethacin	207-219	heme oxygenase 1	Homo sapiens	18-22
18440740-9	2008	We also found that PD98059, a MEK (MAPK/ERK kinase) inhibitor, attenuated the eupatilin-induced HO-1 expression and nuclear translocation of transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2).	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	19-26	heme oxygenase 1	Homo sapiens	96-100
18357586-4	2008	Further, Curcumin inhibited LPS-induced IL-1 and IL-6 secretion and blockage of HO-1 expression/activity by HO-1 siRNA or HO-1 inhibitor, SnPP reversed the inhibitory effects of Curcumin on cytokines secretion.	S-Nitroso-N-propionyl-D,L-penicillamine	138-142	heme oxygenase 1	Homo sapiens	80-84
18598163-0	2008	Luteolin suppresses cisplatin-induced apoptosis in auditory cells: possible mediation through induction of heme oxygenase-1 expression.	Cisplatin	20-29	heme oxygenase 1	Homo sapiens	107-123
18598163-8	2008	These results demonstrate that the expression of HO-1 by luteolin is mediated by the ERK pathway, and also that the activating of HO-1 inhibits cisplatin-induced apoptosis in HEI-OC1 1 cells.	Cisplatin	144-153	heme oxygenase 1	Homo sapiens	49-53
18598163-8	2008	These results demonstrate that the expression of HO-1 by luteolin is mediated by the ERK pathway, and also that the activating of HO-1 inhibits cisplatin-induced apoptosis in HEI-OC1 1 cells.	Cisplatin	144-153	heme oxygenase 1	Homo sapiens	130-134
18357586-0	2008	Heme oxygenase-1 mediates the anti-inflammatory effect of Curcumin within LPS-stimulated human monocytes.	Curcumin	58-66	heme oxygenase 1	Homo sapiens	0-16
18357586-1	2008	Curcumin, a polyphenolic compound derived from plant, regulates heme oxygenase (HO-1) expression within certain cell types; however, the Curcumin-mediated signal transduction in the regulation of HO-1 expression within human monocytes/macrophages is unclear.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	80-84
18357586-1	2008	Curcumin, a polyphenolic compound derived from plant, regulates heme oxygenase (HO-1) expression within certain cell types; however, the Curcumin-mediated signal transduction in the regulation of HO-1 expression within human monocytes/macrophages is unclear.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	196-200
18357586-1	2008	Curcumin, a polyphenolic compound derived from plant, regulates heme oxygenase (HO-1) expression within certain cell types; however, the Curcumin-mediated signal transduction in the regulation of HO-1 expression within human monocytes/macrophages is unclear.	polyphenolic compound	12-33	heme oxygenase 1	Homo sapiens	80-84
18357586-1	2008	Curcumin, a polyphenolic compound derived from plant, regulates heme oxygenase (HO-1) expression within certain cell types; however, the Curcumin-mediated signal transduction in the regulation of HO-1 expression within human monocytes/macrophages is unclear.	polyphenolic compound	12-33	heme oxygenase 1	Homo sapiens	196-200
18357586-1	2008	Curcumin, a polyphenolic compound derived from plant, regulates heme oxygenase (HO-1) expression within certain cell types; however, the Curcumin-mediated signal transduction in the regulation of HO-1 expression within human monocytes/macrophages is unclear.	Curcumin	137-145	heme oxygenase 1	Homo sapiens	80-84
18357586-1	2008	Curcumin, a polyphenolic compound derived from plant, regulates heme oxygenase (HO-1) expression within certain cell types; however, the Curcumin-mediated signal transduction in the regulation of HO-1 expression within human monocytes/macrophages is unclear.	Curcumin	137-145	heme oxygenase 1	Homo sapiens	196-200
18357586-2	2008	Herein, we show that Curcumin dose dependently induced HO-1 expression and HO-1 activity through the activation of PKCalpha, PKCdelta/ERK1/2, p38alpha, and PI3-kinase.	Curcumin	21-29	heme oxygenase 1	Homo sapiens	55-59
18357586-2	2008	Herein, we show that Curcumin dose dependently induced HO-1 expression and HO-1 activity through the activation of PKCalpha, PKCdelta/ERK1/2, p38alpha, and PI3-kinase.	Curcumin	21-29	heme oxygenase 1	Homo sapiens	75-79
18357586-3	2008	In addition, H2O2 release is essential for Curcumin-mediated ERK1/2 and p38 phosphorylation and HO-1 expression.	Hydrogen Peroxide	13-17	heme oxygenase 1	Homo sapiens	96-100
18357586-3	2008	In addition, H2O2 release is essential for Curcumin-mediated ERK1/2 and p38 phosphorylation and HO-1 expression.	Curcumin	43-51	heme oxygenase 1	Homo sapiens	96-100
18498885-0	2008	Effect of mineral trioxide aggregate on dentin bridge formation and expression of dentin sialoprotein and heme oxygenase-1 in human dental pulp.	mineral trioxide	10-26	heme oxygenase 1	Homo sapiens	106-122
18357586-4	2008	Further, Curcumin inhibited LPS-induced IL-1 and IL-6 secretion and blockage of HO-1 expression/activity by HO-1 siRNA or HO-1 inhibitor, SnPP reversed the inhibitory effects of Curcumin on cytokines secretion.	S-Nitroso-N-propionyl-D,L-penicillamine	138-142	heme oxygenase 1	Homo sapiens	108-112
18357586-4	2008	Further, Curcumin inhibited LPS-induced IL-1 and IL-6 secretion and blockage of HO-1 expression/activity by HO-1 siRNA or HO-1 inhibitor, SnPP reversed the inhibitory effects of Curcumin on cytokines secretion.	S-Nitroso-N-propionyl-D,L-penicillamine	138-142	heme oxygenase 1	Homo sapiens	108-112
18357586-4	2008	Further, Curcumin inhibited LPS-induced IL-1 and IL-6 secretion and blockage of HO-1 expression/activity by HO-1 siRNA or HO-1 inhibitor, SnPP reversed the inhibitory effects of Curcumin on cytokines secretion.	Curcumin	178-186	heme oxygenase 1	Homo sapiens	80-84
18357586-4	2008	Further, Curcumin inhibited LPS-induced IL-1 and IL-6 secretion and blockage of HO-1 expression/activity by HO-1 siRNA or HO-1 inhibitor, SnPP reversed the inhibitory effects of Curcumin on cytokines secretion.	Curcumin	178-186	heme oxygenase 1	Homo sapiens	108-112
18357586-4	2008	Further, Curcumin inhibited LPS-induced IL-1 and IL-6 secretion and blockage of HO-1 expression/activity by HO-1 siRNA or HO-1 inhibitor, SnPP reversed the inhibitory effects of Curcumin on cytokines secretion.	Curcumin	178-186	heme oxygenase 1	Homo sapiens	108-112
18357586-5	2008	HO-1 over-expression produced the same inhibitory effects of Curcumin on IL-1 secretion.	Curcumin	61-69	heme oxygenase 1	Homo sapiens	0-4
18357586-6	2008	Collectively, our results suggest that Curcumin inhibits cytokines secretion within LPS-stimulated monocytes through a mechanism that involves the action of HO-1.	Curcumin	39-47	heme oxygenase 1	Homo sapiens	157-161
18332044-0	2008	Heme-oxygenase 1 gene expression is a marker for hexavalent chromium-induced stress and toxicity in human dermal fibroblasts.	Chromium	60-68	heme oxygenase 1	Homo sapiens	0-16
18332044-5	2008	The Cr(VI)-induced overexpression of heme-oxygenase 1 messenger RNA (HO-1) in the fibroblasts was significantly blocked by actinomycin D and by inhibitors of MAP kinase pathways.	Dactinomycin	123-136	heme oxygenase 1	Homo sapiens	37-53
18332044-5	2008	The Cr(VI)-induced overexpression of heme-oxygenase 1 messenger RNA (HO-1) in the fibroblasts was significantly blocked by actinomycin D and by inhibitors of MAP kinase pathways.	Dactinomycin	123-136	heme oxygenase 1	Homo sapiens	69-73
18332044-6	2008	The Cr(VI)-induced cytotoxicity and the overexpression of the HO-1 gene were dependent on the glutathione level of the fibroblasts.	Glutathione	94-105	heme oxygenase 1	Homo sapiens	62-66
18332044-7	2008	Buthionine sulfoximine-mediated GSH depletion resulted in enhanced Cr(VI) cytotoxicity and further overexpression of the HO-1 gene.	Buthionine Sulfoximine	0-22	heme oxygenase 1	Homo sapiens	121-125
18332044-7	2008	Buthionine sulfoximine-mediated GSH depletion resulted in enhanced Cr(VI) cytotoxicity and further overexpression of the HO-1 gene.	Glutathione	32-35	heme oxygenase 1	Homo sapiens	121-125
18332044-8	2008	On the other hand, elevated cellular levels of glutathione resulting from pretreating the cells with GSH significantly protected the cells against the Cr(VI)-induced cytotoxicity and blocked the HO-1 gene"s overexpression.	Glutathione	47-58	heme oxygenase 1	Homo sapiens	195-199
18332044-8	2008	On the other hand, elevated cellular levels of glutathione resulting from pretreating the cells with GSH significantly protected the cells against the Cr(VI)-induced cytotoxicity and blocked the HO-1 gene"s overexpression.	Glutathione	101-104	heme oxygenase 1	Homo sapiens	195-199
18332044-9	2008	Pretreating the fibroblasts with N-acetyl cysteine also significantly reduced the Cr(VI)-induced cytotoxicity and overexpression of the HO-1 gene.	Acetylcysteine	33-50	heme oxygenase 1	Homo sapiens	136-140
18332044-9	2008	Pretreating the fibroblasts with N-acetyl cysteine also significantly reduced the Cr(VI)-induced cytotoxicity and overexpression of the HO-1 gene.	chromium hexavalent ion	82-88	heme oxygenase 1	Homo sapiens	136-140
18376820-0	2008	Selenolate complexes of CYP101 and the heme-bound hHO-1/H25A proximal cavity mutant.	selenolate	0-10	heme oxygenase 1	Homo sapiens	50-55
18172853-6	2008	Protein levels of gamma-GCS and heme oxygenase-1 (HO-1), two MARE-containing genes, were also increased after hemin treatment.	Hemin	110-115	heme oxygenase 1	Homo sapiens	32-48
18376820-0	2008	Selenolate complexes of CYP101 and the heme-bound hHO-1/H25A proximal cavity mutant.	Heme	39-43	heme oxygenase 1	Homo sapiens	50-55
18376820-1	2008	Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy.	thiolate	0-8	heme oxygenase 1	Homo sapiens	110-126
18376820-1	2008	Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy.	thiolate	0-8	heme oxygenase 1	Homo sapiens	128-133
18376820-1	2008	Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy.	selenolate	13-23	heme oxygenase 1	Homo sapiens	110-126
18376820-1	2008	Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy.	Heme	93-97	heme oxygenase 1	Homo sapiens	110-126
18376820-1	2008	Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy.	Heme	93-97	heme oxygenase 1	Homo sapiens	128-133
18376820-3	2008	Thiolate ligands also bound to the proximal side of the heme in the cavity created by the H25A mutation in hHO-1, giving a Soret absorption similar to that of the H25C hHO-1 mutant.	thiolate	0-8	heme oxygenase 1	Homo sapiens	107-112
18376820-3	2008	Thiolate ligands also bound to the proximal side of the heme in the cavity created by the H25A mutation in hHO-1, giving a Soret absorption similar to that of the H25C hHO-1 mutant.	thiolate	0-8	heme oxygenase 1	Homo sapiens	168-173
18376820-3	2008	Thiolate ligands also bound to the proximal side of the heme in the cavity created by the H25A mutation in hHO-1, giving a Soret absorption similar to that of the H25C hHO-1 mutant.	Heme	56-60	heme oxygenase 1	Homo sapiens	107-112
18376820-3	2008	Thiolate ligands also bound to the proximal side of the heme in the cavity created by the H25A mutation in hHO-1, giving a Soret absorption similar to that of the H25C hHO-1 mutant.	Heme	56-60	heme oxygenase 1	Homo sapiens	168-173
18344023-8	2008	Both cobalt-protoporphyrin (CoPP) and CoCl2 markedly induced HO-1 expression.	cobaltiprotoporphyrin	5-26	heme oxygenase 1	Homo sapiens	61-65
18492619-11	2008	In addition, arecoline was found to elevate HO-1 mRNA in a dose-dependent manner (p &lt; 0.05).	Arecoline	13-22	heme oxygenase 1	Homo sapiens	44-48
18492619-12	2008	The addition of BaP enhanced arecolineinduced HO-1 expression (p &lt; 0.05).	Benzo(a)pyrene	16-19	heme oxygenase 1	Homo sapiens	46-50
18492619-13	2008	Moreover, addition of NAC markedly inhibited arecoline-induced HO-1 expression (p &lt; 0.05).	Arecoline	45-54	heme oxygenase 1	Homo sapiens	63-67
18492619-14	2008	CONCLUSION: Taken together, these results suggest that HO-1 expression is significantly upregulated in OSCC from areca quid chewers, and arecoline may be responsible for enhanced HO-1 expression in vivo.	Arecoline	137-146	heme oxygenase 1	Homo sapiens	179-183
18492619-16	2008	The regulation of HO-1 expression induced by arecoline is critically dependent on intracellular GSH concentration.	Arecoline	45-54	heme oxygenase 1	Homo sapiens	18-22
18492619-16	2008	The regulation of HO-1 expression induced by arecoline is critically dependent on intracellular GSH concentration.	Glutathione	96-99	heme oxygenase 1	Homo sapiens	18-22
18490853-8	2008	Antisense HO-1 and HSP 72 oligodeoxynucleotide inhibited HO-1 and HSP 72 induction, respectively, and significantly aggravated cerebral vasospasm.	Oligodeoxyribonucleotides	26-46	heme oxygenase 1	Homo sapiens	57-61
18227147-5	2008	Moreover, glutathione-depletion and cytochrome P450 (P450)-inhibition experiments have shown that the observed HO-1 induction was triggered by the electrophilic reactive metabolites produced from the problematic drugs through P450-mediated metabolic bioactivation.	Glutathione	10-21	heme oxygenase 1	Homo sapiens	111-115
18545641-4	2008	The mechanism of protective actions of HO-1 has not been completely elucidated, but recent evidence suggests that one or more of heme metabolites can mediate the protective effects of HO-1.	Heme	129-133	heme oxygenase 1	Homo sapiens	184-188
18205746-0	2008	Differential induction of heme oxygenase-1 against nicotine-induced cytotoxicity via the PI3K, MAPK, and NF-kappa B pathways in immortalized and malignant human oral keratinocytes.	Nicotine	51-59	heme oxygenase 1	Homo sapiens	26-42
18205746-1	2008	BACKGROUND: Heme oxygenase-1 (HO-1) exhibits cytoprotective effects in many different cell types and is induced by nicotine exposure in human gingival fibroblasts.	Nicotine	115-123	heme oxygenase 1	Homo sapiens	12-28
18205746-1	2008	BACKGROUND: Heme oxygenase-1 (HO-1) exhibits cytoprotective effects in many different cell types and is induced by nicotine exposure in human gingival fibroblasts.	Nicotine	115-123	heme oxygenase 1	Homo sapiens	30-34
18205746-2	2008	However, the role of HO-1 in cancer cells exposed to nicotine has not previously been described.	Nicotine	53-61	heme oxygenase 1	Homo sapiens	21-25
18205746-5	2008	RESULTS: Nicotine-induced HO-1 production and had cytotoxic effects on cells in both a concentration- and time-dependent manner.	Nicotine	9-17	heme oxygenase 1	Homo sapiens	26-30
18205746-6	2008	Nicotine-induced cytotoxicity and accumulation of HO-1 were greater in IHOK cells than in HN12 cells.	Nicotine	0-8	heme oxygenase 1	Homo sapiens	50-54
18205746-7	2008	Molecular inhibitors of the ERK, p38 MAP kinase, PI3 K, and NF-kappaB signaling pathways blocked the cytotoxic effects and induction of HO-1 expression by nicotine.	Nicotine	155-163	heme oxygenase 1	Homo sapiens	136-140
18205746-8	2008	Treatment with antioxidants (bilirubin, N-acetylcysteine) protected cells against nicotine-induced cytotoxicity and blocked the upregulation of HO-1, the effects of which were more pronounced in IHOK cells than in HN12 cells.	Bilirubin	29-38	heme oxygenase 1	Homo sapiens	144-148
18205746-8	2008	Treatment with antioxidants (bilirubin, N-acetylcysteine) protected cells against nicotine-induced cytotoxicity and blocked the upregulation of HO-1, the effects of which were more pronounced in IHOK cells than in HN12 cells.	Acetylcysteine	40-56	heme oxygenase 1	Homo sapiens	144-148
18205746-9	2008	CONCLUSIONS: Collectively, these results suggest that HO-1 plays a principal role in the protective response to nicotine in oral cancer and immortalized keratinocytes.	Nicotine	112-120	heme oxygenase 1	Homo sapiens	54-58
18483307-3	2008	Elevation of HO-1 gene expression by ferric protoporphyrin IX inhibited TPA-induced invasion of MCF-7 cells, which was blocked by adding the heme oxygenase inhibitor, tin protoporphyrin IX, or transfection of cells with HO-1 short hairpin RNA.	ferric protoporphyrin ix	37-61	heme oxygenase 1	Homo sapiens	13-17
18344023-8	2008	Both cobalt-protoporphyrin (CoPP) and CoCl2 markedly induced HO-1 expression.	cobaltiprotoporphyrin	28-32	heme oxygenase 1	Homo sapiens	61-65
18483307-3	2008	Elevation of HO-1 gene expression by ferric protoporphyrin IX inhibited TPA-induced invasion of MCF-7 cells, which was blocked by adding the heme oxygenase inhibitor, tin protoporphyrin IX, or transfection of cells with HO-1 short hairpin RNA.	ferric protoporphyrin ix	37-61	heme oxygenase 1	Homo sapiens	220-224
18344023-8	2008	Both cobalt-protoporphyrin (CoPP) and CoCl2 markedly induced HO-1 expression.	cobaltous chloride	38-43	heme oxygenase 1	Homo sapiens	61-65
18483307-3	2008	Elevation of HO-1 gene expression by ferric protoporphyrin IX inhibited TPA-induced invasion of MCF-7 cells, which was blocked by adding the heme oxygenase inhibitor, tin protoporphyrin IX, or transfection of cells with HO-1 short hairpin RNA.	Tetradecanoylphorbol Acetate	72-75	heme oxygenase 1	Homo sapiens	13-17
18483307-3	2008	Elevation of HO-1 gene expression by ferric protoporphyrin IX inhibited TPA-induced invasion of MCF-7 cells, which was blocked by adding the heme oxygenase inhibitor, tin protoporphyrin IX, or transfection of cells with HO-1 short hairpin RNA.	Tetradecanoylphorbol Acetate	72-75	heme oxygenase 1	Homo sapiens	220-224
18414232-0	2008	Hemin arginate-induced heme oxygenase 1 expression improves liver microcirculation and mediates an anti-inflammatory cytokine response after hemorrhagic shock.	L-argininate	6-14	heme oxygenase 1	Homo sapiens	23-39
18483307-3	2008	Elevation of HO-1 gene expression by ferric protoporphyrin IX inhibited TPA-induced invasion of MCF-7 cells, which was blocked by adding the heme oxygenase inhibitor, tin protoporphyrin IX, or transfection of cells with HO-1 short hairpin RNA.	protoporphyrin IX	44-61	heme oxygenase 1	Homo sapiens	13-17
18483307-3	2008	Elevation of HO-1 gene expression by ferric protoporphyrin IX inhibited TPA-induced invasion of MCF-7 cells, which was blocked by adding the heme oxygenase inhibitor, tin protoporphyrin IX, or transfection of cells with HO-1 short hairpin RNA.	protoporphyrin IX	44-61	heme oxygenase 1	Homo sapiens	220-224
18483307-4	2008	MCF-7 cells overexpressing HO-1 (MCF-7/HO-1) were established in the present study, and TPA-induced MMP-9 gene expression, tumor invasion, and colony formation were significantly reduced in MCF-7/HO-1 cells, compared with those in Neo-transfected cells.	Tetradecanoylphorbol Acetate	88-91	heme oxygenase 1	Homo sapiens	27-31
18483307-4	2008	MCF-7 cells overexpressing HO-1 (MCF-7/HO-1) were established in the present study, and TPA-induced MMP-9 gene expression, tumor invasion, and colony formation were significantly reduced in MCF-7/HO-1 cells, compared with those in Neo-transfected cells.	Tetradecanoylphorbol Acetate	88-91	heme oxygenase 1	Homo sapiens	33-43
18483307-4	2008	MCF-7 cells overexpressing HO-1 (MCF-7/HO-1) were established in the present study, and TPA-induced MMP-9 gene expression, tumor invasion, and colony formation were significantly reduced in MCF-7/HO-1 cells, compared with those in Neo-transfected cells.	Tetradecanoylphorbol Acetate	88-91	heme oxygenase 1	Homo sapiens	39-43
18483307-5	2008	Activation of protein kinase Calpha/extracellular signal-regulated kinases/AP-1 with stimulation of reactive oxygen species production was involved in TPA-induced invasion of MCF-7 cells, which was attenuated by HO-1 protein induced by ferric protoporphyrin IX or transfection of HO-1 expression vectors.	Reactive Oxygen Species	100-123	heme oxygenase 1	Homo sapiens	212-216
18483307-5	2008	Activation of protein kinase Calpha/extracellular signal-regulated kinases/AP-1 with stimulation of reactive oxygen species production was involved in TPA-induced invasion of MCF-7 cells, which was attenuated by HO-1 protein induced by ferric protoporphyrin IX or transfection of HO-1 expression vectors.	Reactive Oxygen Species	100-123	heme oxygenase 1	Homo sapiens	280-284
18483307-5	2008	Activation of protein kinase Calpha/extracellular signal-regulated kinases/AP-1 with stimulation of reactive oxygen species production was involved in TPA-induced invasion of MCF-7 cells, which was attenuated by HO-1 protein induced by ferric protoporphyrin IX or transfection of HO-1 expression vectors.	Tetradecanoylphorbol Acetate	151-154	heme oxygenase 1	Homo sapiens	212-216
18483307-5	2008	Activation of protein kinase Calpha/extracellular signal-regulated kinases/AP-1 with stimulation of reactive oxygen species production was involved in TPA-induced invasion of MCF-7 cells, which was attenuated by HO-1 protein induced by ferric protoporphyrin IX or transfection of HO-1 expression vectors.	Tetradecanoylphorbol Acetate	151-154	heme oxygenase 1	Homo sapiens	280-284
18483307-5	2008	Activation of protein kinase Calpha/extracellular signal-regulated kinases/AP-1 with stimulation of reactive oxygen species production was involved in TPA-induced invasion of MCF-7 cells, which was attenuated by HO-1 protein induced by ferric protoporphyrin IX or transfection of HO-1 expression vectors.	ferric protoporphyrin ix	236-260	heme oxygenase 1	Homo sapiens	212-216
18414232-3	2008	Hemin arginate (HAR) induces HO-1 and protects against shock-induced organ failure.	hemin arginate	0-14	heme oxygenase 1	Homo sapiens	29-33
18237271-6	2008	The consequence of this finding is that signalling initiated by electrophilic lipids differs from agonists that do not form covalent adducts with proteins because the constant generation of very lowconcentrations of 15d-PGJ2 can lead to induction of GSH or HO-1.	15-deoxy-delta(12,14)-prostaglandin J2	216-224	heme oxygenase 1	Homo sapiens	257-261
18275848-0	2008	Heme oxygenase-1 is a novel target and antioxidant mediator of S-adenosylmethionine.	S-Adenosylmethionine	63-83	heme oxygenase 1	Homo sapiens	0-16
18275848-7	2008	HO-1 upregulation by SAM was causally related to a decrease in NADPH-mediated production of oxygen radicals.	NADP	63-68	heme oxygenase 1	Homo sapiens	0-4
18275848-7	2008	HO-1 upregulation by SAM was causally related to a decrease in NADPH-mediated production of oxygen radicals.	Reactive Oxygen Species	92-107	heme oxygenase 1	Homo sapiens	0-4
18226606-3	2008	Incubation with arsenite concentration- and time-dependently increased the expression of stress proteins, heat shock protein 70, and heme oxygenase-1 in DRG explants.	arsenite	16-24	heme oxygenase 1	Homo sapiens	133-149
18048804-0	2008	Acrolein induces heme oxygenase-1 through PKC-delta and PI3K in human bronchial epithelial cells.	Acrolein	0-8	heme oxygenase 1	Homo sapiens	17-33
18237271-3	2008	Protective pathways activated by 15d-PGJ2 include those controlling the synthesis of the intracellular antioxidants GSH and the enzyme HO-1 (haem oxygenase-1).	15-deoxy-delta(12,14)-prostaglandin J2	33-41	heme oxygenase 1	Homo sapiens	135-157
18390757-0	2008	Heme oxygenase-1 is a critical regulator of nitric oxide production in enterohemorrhagic Escherichia coli-infected human enterocytes.	Nitric Oxide	44-56	heme oxygenase 1	Homo sapiens	0-16
18390757-8	2008	Knock-down of hmox-1 gene expression by small interfering RNA or the blockade of HO-1 activity by zinc protoporphyrin IX abrogated the EHEC-dependent inhibition of STAT-1 activation and iNOS mRNA expression in activated human enterocytes.	zinc protoporphyrin	98-120	heme oxygenase 1	Homo sapiens	81-85
18048804-6	2008	Acrolein-mediated HO-1 induction was significantly attenuated by pan-protein kinase C (PKC) inhibitors RO318220, staurosporine, and PKC-delta selective inhibitor rottlerin and PKC-delta small interfering RNA.	Staurosporine	113-126	heme oxygenase 1	Homo sapiens	18-22
18048804-1	2008	Heme oxygenase-1 (HO-1) catalyzes the rate limiting reaction of heme metabolism and plays critical roles in resistance to oxidative stress and other cellular functions.	Heme	64-68	heme oxygenase 1	Homo sapiens	0-16
18048804-6	2008	Acrolein-mediated HO-1 induction was significantly attenuated by pan-protein kinase C (PKC) inhibitors RO318220, staurosporine, and PKC-delta selective inhibitor rottlerin and PKC-delta small interfering RNA.	rottlerin	162-171	heme oxygenase 1	Homo sapiens	18-22
18048804-7	2008	The HO-1 induction was also decreased by phosphatidylinositol 3-kinase (PI3K) inhibitors LY294002 and wortmannin.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	89-97	heme oxygenase 1	Homo sapiens	4-8
18048804-1	2008	Heme oxygenase-1 (HO-1) catalyzes the rate limiting reaction of heme metabolism and plays critical roles in resistance to oxidative stress and other cellular functions.	Heme	64-68	heme oxygenase 1	Homo sapiens	18-22
18048804-7	2008	The HO-1 induction was also decreased by phosphatidylinositol 3-kinase (PI3K) inhibitors LY294002 and wortmannin.	Wortmannin	102-112	heme oxygenase 1	Homo sapiens	4-8
18048804-4	2008	In this investigation we studied HO-1 induction in response to acrolein and determined the signaling pathways involved in human bronchial epithelial cells (HBE1 cells).	Acrolein	63-71	heme oxygenase 1	Homo sapiens	33-37
18048804-9	2008	Furthermore, Nrf2 silencing significantly attenuated the HO-1 induction by acrolein.	Acrolein	75-83	heme oxygenase 1	Homo sapiens	57-61
18048804-6	2008	Acrolein-mediated HO-1 induction was significantly attenuated by pan-protein kinase C (PKC) inhibitors RO318220, staurosporine, and PKC-delta selective inhibitor rottlerin and PKC-delta small interfering RNA.	Acrolein	0-8	heme oxygenase 1	Homo sapiens	18-22
18048804-11	2008	Taken together, our results indicate that acrolein up-regulates HO-1 expression through both PKC-delta and PI3K pathways in HBE1 cells; PKC-delta appears to regulate HO-1 induction via modulating Nrf2 nuclear translocation, while PI3K may work through targeting on downstream signaling molecules other than Nrf2.	Acrolein	42-50	heme oxygenase 1	Homo sapiens	64-68
18048804-6	2008	Acrolein-mediated HO-1 induction was significantly attenuated by pan-protein kinase C (PKC) inhibitors RO318220, staurosporine, and PKC-delta selective inhibitor rottlerin and PKC-delta small interfering RNA.	Ro 31-8220	103-111	heme oxygenase 1	Homo sapiens	18-22
18082923-3	2008	(-)-Epigallocatechin-3-gallate (EGCG), a major green tea polyphenol, has been shown to induce expression of glutathione S-transferase, glutathione peroxidase, glutamate cysteine ligase, hemeoxygenase-1, etc.	epigallocatechin gallate	0-30	heme oxygenase 1	Homo sapiens	186-201
18371544-3	2008	HO-1, an integral component of an important cytoprotective mechanism, mediates its action through removal of heme, the generation of heme breakdown reaction products (biliverdin, free iron, and carbon monoxide), and modulation of key cellular molecules.	Heme	109-113	heme oxygenase 1	Homo sapiens	0-4
18371544-3	2008	HO-1, an integral component of an important cytoprotective mechanism, mediates its action through removal of heme, the generation of heme breakdown reaction products (biliverdin, free iron, and carbon monoxide), and modulation of key cellular molecules.	Biliverdine	167-177	heme oxygenase 1	Homo sapiens	0-4
18371544-3	2008	HO-1, an integral component of an important cytoprotective mechanism, mediates its action through removal of heme, the generation of heme breakdown reaction products (biliverdin, free iron, and carbon monoxide), and modulation of key cellular molecules.	Iron	184-188	heme oxygenase 1	Homo sapiens	0-4
18371544-3	2008	HO-1, an integral component of an important cytoprotective mechanism, mediates its action through removal of heme, the generation of heme breakdown reaction products (biliverdin, free iron, and carbon monoxide), and modulation of key cellular molecules.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	0-4
18371544-5	2008	The discovery of a functional guanosine thymine tandem repeat polymorphism in the promoter region of the human HO-1 gene has stimulated clinical investigations in a variety of diseases.	guanosine thymine	30-47	heme oxygenase 1	Homo sapiens	111-115
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	86-103	heme oxygenase 1	Homo sapiens	138-142
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	86-103	heme oxygenase 1	Homo sapiens	138-142
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	86-96	heme oxygenase 1	Homo sapiens	28-32
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	86-96	heme oxygenase 1	Homo sapiens	138-142
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	86-96	heme oxygenase 1	Homo sapiens	138-142
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	186-196	heme oxygenase 1	Homo sapiens	28-32
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	186-196	heme oxygenase 1	Homo sapiens	138-142
18206660-9	2008	The results showed that (1) HO-1 is induced in chronic cholestatic liver disease, (2) superoxide anions time- and dose-dependently induce HO-1 activity, (3) HO-1 overexpression inhibits superoxide-anions-induced apoptosis, and (4) CO blocks superoxide-anions-induced JNK phosphorylation and caspase-9, -6, -3 activation and abolishes apoptosis but does not increase necrosis.	Superoxides	186-196	heme oxygenase 1	Homo sapiens	138-142
18206660-10	2008	We conclude that HO-1 and CO protect primary hepatocytes against superoxide-anions-induced apoptosis partially via inhibition of JNK activity.	Superoxides	65-75	heme oxygenase 1	Homo sapiens	17-21
18404535-0	2008	Protection of chlorophyllin against oxidative damage by inducing HO-1 and NQO1 expression mediated by PI3K/Akt and Nrf2.	chlorophyllin	14-27	heme oxygenase 1	Homo sapiens	65-69
18082923-3	2008	(-)-Epigallocatechin-3-gallate (EGCG), a major green tea polyphenol, has been shown to induce expression of glutathione S-transferase, glutathione peroxidase, glutamate cysteine ligase, hemeoxygenase-1, etc.	epigallocatechin gallate	32-36	heme oxygenase 1	Homo sapiens	186-201
18006113-0	2008	Suppression of Nrf2-driven heme oxygenase-1 enhances the chemosensitivity of lung cancer A549 cells toward cisplatin.	Cisplatin	107-116	heme oxygenase 1	Homo sapiens	27-43
18286266-4	2008	Induction of HO-1 may confer protection by controlling intracellular levels of toxic heme, or by anti-inflammatory, anti-apoptotic, and blood flow-maintaining effects of its by-products biliverdin and CO.	Heme	85-89	heme oxygenase 1	Homo sapiens	13-17
18286266-4	2008	Induction of HO-1 may confer protection by controlling intracellular levels of toxic heme, or by anti-inflammatory, anti-apoptotic, and blood flow-maintaining effects of its by-products biliverdin and CO.	Biliverdine	186-196	heme oxygenase 1	Homo sapiens	13-17
18360685-8	2008	A minimal HO-1-inducing formulation was prepared and showed significant cytoprotection against H2O2-induced oxidative stress.	Hydrogen Peroxide	95-99	heme oxygenase 1	Homo sapiens	10-14
18006113-5	2008	A549 cells are less susceptible to cisplatin cytotoxicity than other lung cancer cell lines, concomitant with increases in HO-1 expression and MAPK phosphorylation in a time-dependent fashion.	Cisplatin	35-44	heme oxygenase 1	Homo sapiens	123-127
18006113-6	2008	Furthermore, inhibition of HO-1 by siRNA and a specific HO-1 inhibitor ZnPP augments cisplatin cytotoxicity toward A549 cells.	zinc protoporphyrin	71-75	heme oxygenase 1	Homo sapiens	27-31
18006113-6	2008	Furthermore, inhibition of HO-1 by siRNA and a specific HO-1 inhibitor ZnPP augments cisplatin cytotoxicity toward A549 cells.	zinc protoporphyrin	71-75	heme oxygenase 1	Homo sapiens	56-60
18006113-6	2008	Furthermore, inhibition of HO-1 by siRNA and a specific HO-1 inhibitor ZnPP augments cisplatin cytotoxicity toward A549 cells.	Cisplatin	85-94	heme oxygenase 1	Homo sapiens	27-31
18006113-6	2008	Furthermore, inhibition of HO-1 by siRNA and a specific HO-1 inhibitor ZnPP augments cisplatin cytotoxicity toward A549 cells.	Cisplatin	85-94	heme oxygenase 1	Homo sapiens	56-60
18006113-7	2008	Pharmacologic suppression of HO-1 activity resulted in a marked increase in the ROS generation in cisplatin-treated cells.	ros	80-83	heme oxygenase 1	Homo sapiens	29-33
18006113-7	2008	Pharmacologic suppression of HO-1 activity resulted in a marked increase in the ROS generation in cisplatin-treated cells.	Cisplatin	98-107	heme oxygenase 1	Homo sapiens	29-33
18006113-8	2008	In addition, pharmacologic inhibitors of MAPK suppressed the induction of HO-1 and Nrf2 expression by cisplatin.	Cisplatin	102-111	heme oxygenase 1	Homo sapiens	74-78
18006113-9	2008	These findings suggest that HO-1 may modulate the chemosensitivity of lung cancer A549 cells to cisplatin through the MAPK-Nrf2 pathway.	Cisplatin	96-105	heme oxygenase 1	Homo sapiens	28-32
18178725-0	2008	Heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide.	Heme	36-40	heme oxygenase 1	Homo sapiens	0-16
17657593-0	2008	Structural influence of isothiocyanates on the antioxidant response element (ARE)-mediated heme oxygenase-1 (HO-1) expression.	Isothiocyanates	24-39	heme oxygenase 1	Homo sapiens	91-107
17657593-0	2008	Structural influence of isothiocyanates on the antioxidant response element (ARE)-mediated heme oxygenase-1 (HO-1) expression.	Isothiocyanates	24-39	heme oxygenase 1	Homo sapiens	109-113
17657593-3	2008	In this study, the effects of ten structurally related isothiocyanates on the antioxidant response element (ARE)-mediated antioxidant enzyme heme oxygenase-1 (HO-1) induction in human hepatoma HepG2-C8 cells were evaluated.	Isothiocyanates	55-70	heme oxygenase 1	Homo sapiens	141-157
17657593-3	2008	In this study, the effects of ten structurally related isothiocyanates on the antioxidant response element (ARE)-mediated antioxidant enzyme heme oxygenase-1 (HO-1) induction in human hepatoma HepG2-C8 cells were evaluated.	Isothiocyanates	55-70	heme oxygenase 1	Homo sapiens	159-163
17467819-5	2008	Metoprolol increased the expression of interleukin-1alpha, cyclooxygenase-1, TNF-alpha-induced protein 3, heme oxygenase 1 and granulocyte/macrophage-colony-stimulating factor.	Metoprolol	0-10	heme oxygenase 1	Homo sapiens	106-175
18174021-0	2008	Galantamine and carbon monoxide protect brain microvascular endothelial cells by heme oxygenase-1 induction.	Galantamine	0-11	heme oxygenase 1	Homo sapiens	81-97
18174021-0	2008	Galantamine and carbon monoxide protect brain microvascular endothelial cells by heme oxygenase-1 induction.	Carbon Monoxide	16-31	heme oxygenase 1	Homo sapiens	81-97
18174021-3	2008	We hypothesized that the protective effects of galantamine would involve induction of the protective gene, heme oxygenase-1 (HO-1), in addition to enhancement of the cholinergic system.	Galantamine	47-58	heme oxygenase 1	Homo sapiens	107-123
18174021-3	2008	We hypothesized that the protective effects of galantamine would involve induction of the protective gene, heme oxygenase-1 (HO-1), in addition to enhancement of the cholinergic system.	Galantamine	47-58	heme oxygenase 1	Homo sapiens	125-129
18174021-5	2008	Galantamine significantly reduced H(2)O(2)-induced cell death of mvECs in association with HO-1 induction.	Galantamine	0-11	heme oxygenase 1	Homo sapiens	91-95
18174021-8	2008	These data suggest that the protective effects of galantamine require NF-kappaB activation and iNOS expression, in addition to HO-1.	Galantamine	50-61	heme oxygenase 1	Homo sapiens	127-131
18174021-9	2008	Likewise, carbon monoxide (CO), one of the byproducts of HO, up-regulated HO-1 and protected mvECs from oxidative stress in a similar manner.	Carbon Monoxide	10-25	heme oxygenase 1	Homo sapiens	74-78
18174021-9	2008	Likewise, carbon monoxide (CO), one of the byproducts of HO, up-regulated HO-1 and protected mvECs from oxidative stress in a similar manner.	Carbon Monoxide	27-29	heme oxygenase 1	Homo sapiens	74-78
18174021-10	2008	Our data demonstrate that galantamine mediates cytoprotective effects on mvECs through induction HO-1.	Galantamine	26-37	heme oxygenase 1	Homo sapiens	97-101
18174022-0	2008	Prostaglandin D2 induces heme oxygenase-1 in human retinal pigment epithelial cells.	Prostaglandin D2	0-16	heme oxygenase 1	Homo sapiens	25-41
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Iron	41-45	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Iron	41-45	heme oxygenase 1	Homo sapiens	18-22
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Heme	75-79	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Heme	75-79	heme oxygenase 1	Homo sapiens	18-22
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Iron	103-107	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Iron	103-107	heme oxygenase 1	Homo sapiens	18-22
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Carbon Monoxide	109-124	heme oxygenase 1	Homo sapiens	18-22
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Biliverdine	129-139	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Biliverdine	129-139	heme oxygenase 1	Homo sapiens	18-22
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Bilirubin	140-149	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Bilirubin	140-149	heme oxygenase 1	Homo sapiens	18-22
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Iron	103-107	heme oxygenase 1	Homo sapiens	0-16
18174022-4	2008	Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites.	Iron	103-107	heme oxygenase 1	Homo sapiens	18-22
18174022-7	2008	Thus, PGD(2) may contribute to the maintenance of heme homeostasis in the brain by inducing HO-1 expression.	Heme	50-54	heme oxygenase 1	Homo sapiens	92-96
18178725-0	2008	Heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide.	Nitric Oxide	120-132	heme oxygenase 1	Homo sapiens	0-16
18178725-2	2008	A 24-h organ culture with 0.1 mM cobalt chloride (CoCl2) or 30 microM Co-protoporphyrin IX was developed as a method of increasing HO-1 expression.	cobaltous chloride	33-48	heme oxygenase 1	Homo sapiens	131-135
18178725-2	2008	A 24-h organ culture with 0.1 mM cobalt chloride (CoCl2) or 30 microM Co-protoporphyrin IX was developed as a method of increasing HO-1 expression.	cobaltous chloride	50-55	heme oxygenase 1	Homo sapiens	131-135
18178725-2	2008	A 24-h organ culture with 0.1 mM cobalt chloride (CoCl2) or 30 microM Co-protoporphyrin IX was developed as a method of increasing HO-1 expression.	Cobalt protoporphyrin IX	70-90	heme oxygenase 1	Homo sapiens	131-135
18178725-4	2008	Induction of HO-1 was associated with an attenuation of pulmonary arterial relaxation to the NO-donor spermine-NONOate.	spermine nitric oxide complex	102-118	heme oxygenase 1	Homo sapiens	13-17
18178725-5	2008	The presence of a HO-1 inhibitor 30 microM chromium mesoporphyrin during the 24-h organ culture (but not acute treatment with this agent) reversed the attenuation of relaxation to NO seen in arteries co-cultured with agents that increased HO-1.	chromium mesoporphyrin	43-65	heme oxygenase 1	Homo sapiens	18-22
18178725-5	2008	The presence of a HO-1 inhibitor 30 microM chromium mesoporphyrin during the 24-h organ culture (but not acute treatment with this agent) reversed the attenuation of relaxation to NO seen in arteries co-cultured with agents that increased HO-1.	chromium mesoporphyrin	43-65	heme oxygenase 1	Homo sapiens	239-243
18178725-8	2008	However, the increase in activity seen in the presence of 1 microM spermine-NONOate was attenuated in homogenates obtained from arteries with increased HO-1.	spermine nitric oxide complex	67-83	heme oxygenase 1	Homo sapiens	152-156
18178725-9	2008	Since arteries with increased HO-1 had decreased levels of superoxide detected by the chemiluminescence of 5 microM lucigenin, superoxide did not appear to be mediating the attenuation of relaxation to NO.	Superoxides	59-69	heme oxygenase 1	Homo sapiens	30-34
18178725-10	2008	These data suggest that increasing HO-1 activity depletes heme, and this is associated with an attenuation of pulmonary artery relaxation and sGC activation responses to NO.	Heme	58-62	heme oxygenase 1	Homo sapiens	35-39
18293301-5	2008	Under subtoxic conditions, LOOH induced intracellular hydrogen peroxide production, a decrease of glutathione content, elevated expression of the AP-1 components c-fos and c-jun as well as of the anti-apoptotic enzyme heme oxygenase 1 (HO-1).	Lipid Peroxides	27-31	heme oxygenase 1	Homo sapiens	218-234
18325350-0	2008	Zinc mesoporphyrin induces rapid and marked degradation of the transcription factor Bach1 and up-regulates HO-1.	zinc mesoporphyrin	0-18	heme oxygenase 1	Homo sapiens	107-111
18325350-1	2008	Heme oxygenase 1 (HO-1) is the first and rate-controlling enzyme in heme degradation.	Heme	68-72	heme oxygenase 1	Homo sapiens	0-16
18325350-1	2008	Heme oxygenase 1 (HO-1) is the first and rate-controlling enzyme in heme degradation.	Heme	68-72	heme oxygenase 1	Homo sapiens	18-22
18325350-3	2008	To understand how zinc mesoporphyrin (ZnMP) induces the expression of HO-1, we investigated the effects of ZnMP on Bach1 mRNA and protein levels in human hepatoma Huh-7 cells by quantitative RT-PCR and Western blots.	zinc mesoporphyrin	18-36	heme oxygenase 1	Homo sapiens	70-74
18325350-3	2008	To understand how zinc mesoporphyrin (ZnMP) induces the expression of HO-1, we investigated the effects of ZnMP on Bach1 mRNA and protein levels in human hepatoma Huh-7 cells by quantitative RT-PCR and Western blots.	zinc mesoporphyrin	38-42	heme oxygenase 1	Homo sapiens	70-74
18310925-4	2008	Investigation of structure-related HO-1 inducing activity suggested that the hydroxyl group at the C-23 position in the ursane skeleton is important for this activity.	ursane	120-126	heme oxygenase 1	Homo sapiens	35-39
18216035-10	2008	CONCLUSIONS: The haemoglobin-HO-1 system may be required to ensure adequate regulation of the bioavailability of haeme, iron and oxygen in human endometrium.	haeme	113-118	heme oxygenase 1	Homo sapiens	29-33
18216035-10	2008	CONCLUSIONS: The haemoglobin-HO-1 system may be required to ensure adequate regulation of the bioavailability of haeme, iron and oxygen in human endometrium.	Iron	120-124	heme oxygenase 1	Homo sapiens	29-33
18216035-10	2008	CONCLUSIONS: The haemoglobin-HO-1 system may be required to ensure adequate regulation of the bioavailability of haeme, iron and oxygen in human endometrium.	Oxygen	129-135	heme oxygenase 1	Homo sapiens	29-33
18200630-5	2008	Up-regulation of HO-1 by cobalt protoporphyrin IX significantly reduced glycosaminoglycan degradation elicited by IL-1beta in OA cartilage explants but increased glycosaminoglycan synthesis and the expression of collagen II in OA chondrocytes in primary culture, as determined by radiometric procedures, immunoblotting and immunocytochemistry.	cobaltiprotoporphyrin	25-49	heme oxygenase 1	Homo sapiens	17-21
18200630-5	2008	Up-regulation of HO-1 by cobalt protoporphyrin IX significantly reduced glycosaminoglycan degradation elicited by IL-1beta in OA cartilage explants but increased glycosaminoglycan synthesis and the expression of collagen II in OA chondrocytes in primary culture, as determined by radiometric procedures, immunoblotting and immunocytochemistry.	Glycosaminoglycans	72-89	heme oxygenase 1	Homo sapiens	17-21
18200630-5	2008	Up-regulation of HO-1 by cobalt protoporphyrin IX significantly reduced glycosaminoglycan degradation elicited by IL-1beta in OA cartilage explants but increased glycosaminoglycan synthesis and the expression of collagen II in OA chondrocytes in primary culture, as determined by radiometric procedures, immunoblotting and immunocytochemistry.	Glycosaminoglycans	162-179	heme oxygenase 1	Homo sapiens	17-21
18325350-4	2008	We found that ZnMP markedly up-regulated HO-1 mRNA and protein levels, and rapidly and significantly decreased Bach1 protein levels by increasing degradation of Bach1 protein [half life (t(1/2)) from 19 h to 45 min], whereas ZnMP did not influence Bach1 mRNA levels.	zinc mesoporphyrin	14-18	heme oxygenase 1	Homo sapiens	41-45
18325350-7	2008	In conclusion, ZnMP produces profound post-transcriptional down-regulation of Bach1 protein levels and transcriptional up-regulation of HO-1.	zinc mesoporphyrin	15-19	heme oxygenase 1	Homo sapiens	136-140
18325350-8	2008	Our results indicate that ZnMP up-regulates HO-1 gene expression by markedly increasing Bach1 protein degradation in a proteasome-dependent manner.	zinc mesoporphyrin	26-30	heme oxygenase 1	Homo sapiens	44-48
18293301-5	2008	Under subtoxic conditions, LOOH induced intracellular hydrogen peroxide production, a decrease of glutathione content, elevated expression of the AP-1 components c-fos and c-jun as well as of the anti-apoptotic enzyme heme oxygenase 1 (HO-1).	Lipid Peroxides	27-31	heme oxygenase 1	Homo sapiens	236-240
18293301-8	2008	Application of SnPPIX, a HO-1 inhibitor, decreased the viability of HCC-1.2 cells, indicating the protective role of HO-1 induction.	tin protoporphyrin IX	15-21	heme oxygenase 1	Homo sapiens	25-29
18293301-8	2008	Application of SnPPIX, a HO-1 inhibitor, decreased the viability of HCC-1.2 cells, indicating the protective role of HO-1 induction.	tin protoporphyrin IX	15-21	heme oxygenase 1	Homo sapiens	117-121
18024796-0	2008	Targeting of heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) in leukemic cells in chronic myeloid leukemia: a novel approach to overcome resistance against imatinib.	Imatinib Mesylate	162-170	heme oxygenase 1	Homo sapiens	13-34
18071189-5	2008	Ox-PAPE-N-biotin, like Ox-PAPC, induced interleukin-8 (IL-8) protein synthesis and stimulated IL-8, low density lipoprotein receptor, heme oxygenase-1, and activating transcription factor-3 mRNA expression in HAECs.	ox-pape	0-7	heme oxygenase 1	Homo sapiens	134-189
18071189-5	2008	Ox-PAPE-N-biotin, like Ox-PAPC, induced interleukin-8 (IL-8) protein synthesis and stimulated IL-8, low density lipoprotein receptor, heme oxygenase-1, and activating transcription factor-3 mRNA expression in HAECs.	n-biotin	8-16	heme oxygenase 1	Homo sapiens	134-189
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	zinc protoporphyrine	51-71	heme oxygenase 1	Homo sapiens	20-25
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	zinc protoporphyrine	51-71	heme oxygenase 1	Homo sapiens	26-30
18024796-0	2008	Targeting of heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) in leukemic cells in chronic myeloid leukemia: a novel approach to overcome resistance against imatinib.	Imatinib Mesylate	162-170	heme oxygenase 1	Homo sapiens	36-41
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	peg-znpp	73-81	heme oxygenase 1	Homo sapiens	20-25
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	peg-znpp	73-81	heme oxygenase 1	Homo sapiens	26-30
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	2-Butenedioic acid (2Z)-, polymer with ethenylbenzene	86-105	heme oxygenase 1	Homo sapiens	20-25
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	2-Butenedioic acid (2Z)-, polymer with ethenylbenzene	86-105	heme oxygenase 1	Homo sapiens	26-30
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	sma-znpp	133-141	heme oxygenase 1	Homo sapiens	20-25
18024796-4	2008	Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells.	sma-znpp	133-141	heme oxygenase 1	Homo sapiens	26-30
18024796-7	2008	Finally, Hsp32/HO-1-targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL.	Imatinib Mesylate	76-84	heme oxygenase 1	Homo sapiens	9-14
18024796-7	2008	Finally, Hsp32/HO-1-targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL.	Imatinib Mesylate	76-84	heme oxygenase 1	Homo sapiens	15-19
18024796-7	2008	Finally, Hsp32/HO-1-targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL.	nilotinib	88-97	heme oxygenase 1	Homo sapiens	9-14
18024796-7	2008	Finally, Hsp32/HO-1-targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL.	nilotinib	88-97	heme oxygenase 1	Homo sapiens	15-19
18062931-5	2008	We have previously shown that nitric oxide and S-nitrosothiols cause nuclear accumulation of Nrf2 and upregulation of the ARE-regulated gene HO-1.	Nitric Oxide	30-42	heme oxygenase 1	Homo sapiens	141-145
18062931-5	2008	We have previously shown that nitric oxide and S-nitrosothiols cause nuclear accumulation of Nrf2 and upregulation of the ARE-regulated gene HO-1.	S-Nitrosothiols	47-62	heme oxygenase 1	Homo sapiens	141-145
18024796-7	2008	Finally, Hsp32/HO-1-targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL.	Imatinib Mesylate	132-140	heme oxygenase 1	Homo sapiens	9-14
18024796-0	2008	Targeting of heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) in leukemic cells in chronic myeloid leukemia: a novel approach to overcome resistance against imatinib.	Imatinib Mesylate	162-170	heme oxygenase 1	Homo sapiens	43-59
18024796-7	2008	Finally, Hsp32/HO-1-targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL.	Imatinib Mesylate	132-140	heme oxygenase 1	Homo sapiens	15-19
18024796-8	2008	In summary, these data show that HO-1 is a promising novel target in imatinib-resistant CML.	Imatinib Mesylate	69-77	heme oxygenase 1	Homo sapiens	33-37
18024796-0	2008	Targeting of heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) in leukemic cells in chronic myeloid leukemia: a novel approach to overcome resistance against imatinib.	Imatinib Mesylate	162-170	heme oxygenase 1	Homo sapiens	61-65
18215717-3	2008	In this study, we explored: 1) the HO-1 protein content and HO activity in human umbilical vein endothelial cells (HUVECs) exposed to different glucose concentrations, and 2) the mechanisms which account for the high glucose-induced effects on HO-1.	Glucose	217-224	heme oxygenase 1	Homo sapiens	244-248
18215717-6	2008	At 10 mM glucose, an increase of HO-1 protein expression and HO activity was observed, whereas at 20 mM, there was no change in protein content and activity relative to at 5.5 mM glucose.	Glucose	9-16	heme oxygenase 1	Homo sapiens	33-37
18215717-0	2008	Heme oxygenase-1 is an important modulator in limiting glucose-induced apoptosis in human umbilical vein endothelial cells.	Glucose	55-62	heme oxygenase 1	Homo sapiens	0-16
18215717-7	2008	HO-1 protein expression in HUVECs exposed to 20 mM of glucose was increased in the presence of 20 U/ml superoxide dismutase (SOD).	Glucose	54-61	heme oxygenase 1	Homo sapiens	0-4
18215717-3	2008	In this study, we explored: 1) the HO-1 protein content and HO activity in human umbilical vein endothelial cells (HUVECs) exposed to different glucose concentrations, and 2) the mechanisms which account for the high glucose-induced effects on HO-1.	Glucose	144-151	heme oxygenase 1	Homo sapiens	35-39
18215717-8	2008	HO-1 gene silencing augments ROS production both at 5.5 and 10 mM glucose, leading to an increased apoptosis.	Reactive Oxygen Species	29-32	heme oxygenase 1	Homo sapiens	0-4
18215717-3	2008	In this study, we explored: 1) the HO-1 protein content and HO activity in human umbilical vein endothelial cells (HUVECs) exposed to different glucose concentrations, and 2) the mechanisms which account for the high glucose-induced effects on HO-1.	Glucose	217-224	heme oxygenase 1	Homo sapiens	35-39
18215717-8	2008	HO-1 gene silencing augments ROS production both at 5.5 and 10 mM glucose, leading to an increased apoptosis.	Glucose	66-73	heme oxygenase 1	Homo sapiens	0-4
18215717-9	2008	We conclude that, in endothelial cells, the regulation of HO-1 by glucose is dependent upon levels of glucose itself.	Glucose	66-73	heme oxygenase 1	Homo sapiens	58-62
18215717-9	2008	We conclude that, in endothelial cells, the regulation of HO-1 by glucose is dependent upon levels of glucose itself.	Glucose	102-109	heme oxygenase 1	Homo sapiens	58-62
18036570-0	2008	Anti-inflammatory effects of HO-1 activity in vascular endothelial cells, commentary on "Carbon monoxide donors or heme oxygenase (HO-1) overexpression blocks interleukin-18-mediated NF-kappaB-PTEN-dependent human cardiac endothelial cell death".	Carbon Monoxide	89-104	heme oxygenase 1	Homo sapiens	29-33
18021765-6	2008	While LY294002, a non-selective phosphotidylinositol 3-kinase (PI3K) inhibitor, was able to reduce brazilin-induced phosphorylation of Akt and the subsequent induction of HO-1.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	6-14	heme oxygenase 1	Homo sapiens	171-175
18021765-10	2008	These results demonstrate that the expression of HO-1 by brazilin is mediated via the PI3K/Akt and ERK pathways, and this expression inhibits t-BHP-induced cell death in House Ear Institute-Organ of Corti 1 (HEI-OC1) cells.	brazilin	57-65	heme oxygenase 1	Homo sapiens	49-53
18021765-10	2008	These results demonstrate that the expression of HO-1 by brazilin is mediated via the PI3K/Akt and ERK pathways, and this expression inhibits t-BHP-induced cell death in House Ear Institute-Organ of Corti 1 (HEI-OC1) cells.	tert-Butylhydroperoxide	142-147	heme oxygenase 1	Homo sapiens	49-53
18070969-8	2008	One gene whose expression was affected by SbV was the heme oxygenase gene HMOX-1, and this change was observed both in the monocytic cell line THP-1 and in primary human monocyte-derived macrophages.	SBV	42-45	heme oxygenase 1	Homo sapiens	74-80
18215737-1	2008	The objective of this study was to determine whether heme oxygenase-1 (HO-1) or heme metabolites exert cytoprotective effects on interleukin-18-mediated endothelial cell (EC) death.	Heme	53-57	heme oxygenase 1	Homo sapiens	71-75
18215737-6	2008	Furthermore, hemin induced HO-1 expression, and HO-1 knockdown, HO-1 inhibition, or CO scavengers all reversed the prosurvival effects of hemin.	Hemin	13-18	heme oxygenase 1	Homo sapiens	27-31
18819247-8	2008	Dose-dependent, high-level HO-1 protein expression was achieved following culture of NPICC in medium containing either cobalt protoporphyrin (CoPP) or cobalt mesoporphyrin (CoMP).	cobaltiprotoporphyrin	119-140	heme oxygenase 1	Homo sapiens	27-31
18045827-2	2008	A functional dinucleotide repeat (GT)(n) polymorphism, within the HO-1 promoter, regulates HO-1 gene expression; a short number of repeats (S-allele &lt;25) increases transcription.	Dinucleoside Phosphates	13-25	heme oxygenase 1	Homo sapiens	66-70
18045827-2	2008	A functional dinucleotide repeat (GT)(n) polymorphism, within the HO-1 promoter, regulates HO-1 gene expression; a short number of repeats (S-allele &lt;25) increases transcription.	Dinucleoside Phosphates	13-25	heme oxygenase 1	Homo sapiens	91-95
17980396-4	2008	Exposure of RAW 264.7 macrophages to HOCl resulted in increased protein levels of Nrf2 in nuclear extractions, as well as a time- and dose-dependent increase in the expression of Nrf2 target genes, including heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1 (NQO-1), glutamate cysteine ligase catalytic subunit (GCLC), and glutathione synthetase (GS).	Hypochlorous Acid	37-41	heme oxygenase 1	Homo sapiens	208-224
18042465-3	2008	Cobalt protoporphyrin (CoPP) induced the expression of both HO-1 and p53 without significant toxicity to the cells.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	60-64
18042465-3	2008	Cobalt protoporphyrin (CoPP) induced the expression of both HO-1 and p53 without significant toxicity to the cells.	cobaltiprotoporphyrin	23-27	heme oxygenase 1	Homo sapiens	60-64
18042465-4	2008	In addition, the blockage of HO activity with the iron chelator DFO or with HO-1 siRNA inhibited the CoPP-induced expression of p53.	cobaltiprotoporphyrin	101-105	heme oxygenase 1	Homo sapiens	76-80
18195184-3	2008	Recent work has identified heme oxygenase-1 and its gaseous product, carbon monoxide, to possess potent proangiogenic properties in addition to well-recognized antiinflammatory, antioxidant, and antiapoptotic effects.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	27-43
18819247-8	2008	Dose-dependent, high-level HO-1 protein expression was achieved following culture of NPICC in medium containing either cobalt protoporphyrin (CoPP) or cobalt mesoporphyrin (CoMP).	cobaltiprotoporphyrin	142-146	heme oxygenase 1	Homo sapiens	27-31
18819247-8	2008	Dose-dependent, high-level HO-1 protein expression was achieved following culture of NPICC in medium containing either cobalt protoporphyrin (CoPP) or cobalt mesoporphyrin (CoMP).	cobalt mesoporphyrin	151-171	heme oxygenase 1	Homo sapiens	27-31
18819247-8	2008	Dose-dependent, high-level HO-1 protein expression was achieved following culture of NPICC in medium containing either cobalt protoporphyrin (CoPP) or cobalt mesoporphyrin (CoMP).	cobalt mesoporphyrin	173-177	heme oxygenase 1	Homo sapiens	27-31
18289069-3	2008	The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron.	Carbon Monoxide	161-176	heme oxygenase 1	Homo sapiens	38-42
18289069-3	2008	The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron.	Carbon Monoxide	178-180	heme oxygenase 1	Homo sapiens	38-42
18289069-3	2008	The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron.	Iron	213-217	heme oxygenase 1	Homo sapiens	38-42
18289069-3	2008	The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron.	Biliverdine	183-193	heme oxygenase 1	Homo sapiens	38-42
18289069-5	2008	There is evidence supporting that HO-1-derived CO also interacts with other gaseous molecules, such as nitric oxide (NO) and hydrogen sulfide (H2S) that may relate to either vascular protection or injury.	Nitric Oxide	103-115	heme oxygenase 1	Homo sapiens	34-38
18289069-5	2008	There is evidence supporting that HO-1-derived CO also interacts with other gaseous molecules, such as nitric oxide (NO) and hydrogen sulfide (H2S) that may relate to either vascular protection or injury.	Hydrogen Sulfide	125-141	heme oxygenase 1	Homo sapiens	34-38
18289069-3	2008	The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron.	Bilirubin	194-203	heme oxygenase 1	Homo sapiens	38-42
18289069-5	2008	There is evidence supporting that HO-1-derived CO also interacts with other gaseous molecules, such as nitric oxide (NO) and hydrogen sulfide (H2S) that may relate to either vascular protection or injury.	Hydrogen Sulfide	143-146	heme oxygenase 1	Homo sapiens	34-38
17898018-9	2008	Interestingly, sevoflurane treatment also resulted in an enhanced expression of HSP-32.	Sevoflurane	15-26	heme oxygenase 1	Homo sapiens	80-86
18289070-1	2008	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	0-16
18289070-1	2008	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	18-22
18289070-1	2008	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	0-16
18289070-1	2008	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	18-22
18289070-1	2008	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron.	Iron	107-111	heme oxygenase 1	Homo sapiens	0-16
18289070-1	2008	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron.	Iron	107-111	heme oxygenase 1	Homo sapiens	18-22
18289070-4	2008	However, experimental observations indicate that the extent of HO-1 induction may be critical because excessive heme degradation may result in toxic levels of CO, bilirubin and, more importantly, iron.	Heme	112-116	heme oxygenase 1	Homo sapiens	63-67
18289070-4	2008	However, experimental observations indicate that the extent of HO-1 induction may be critical because excessive heme degradation may result in toxic levels of CO, bilirubin and, more importantly, iron.	Carbon Monoxide	159-161	heme oxygenase 1	Homo sapiens	63-67
18289070-4	2008	However, experimental observations indicate that the extent of HO-1 induction may be critical because excessive heme degradation may result in toxic levels of CO, bilirubin and, more importantly, iron.	Bilirubin	163-172	heme oxygenase 1	Homo sapiens	63-67
18289070-4	2008	However, experimental observations indicate that the extent of HO-1 induction may be critical because excessive heme degradation may result in toxic levels of CO, bilirubin and, more importantly, iron.	Iron	196-200	heme oxygenase 1	Homo sapiens	63-67
18289072-1	2008	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme of ferroheme metabolic pathway, which has the functions of anti-oxidation, anti-inflammatory, anti-apoptosis and anti-smooth muscle hyperplasia.	Heme	55-64	heme oxygenase 1	Homo sapiens	0-16
18289072-1	2008	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme of ferroheme metabolic pathway, which has the functions of anti-oxidation, anti-inflammatory, anti-apoptosis and anti-smooth muscle hyperplasia.	Heme	55-64	heme oxygenase 1	Homo sapiens	18-22
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Heme	83-87	heme oxygenase 1	Homo sapiens	0-16
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Heme	83-87	heme oxygenase 1	Homo sapiens	18-22
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	0-16
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	18-22
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Iron	110-114	heme oxygenase 1	Homo sapiens	0-16
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Iron	110-114	heme oxygenase 1	Homo sapiens	18-22
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	0-16
18289074-1	2008	Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin.	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	18-22
20020861-6	2008	Induction of the HMOX1 was detected with a dose of arsenite at as low as 0.3 muM (0.04 ppm) and reached its maximum at 4 h after the treatment.	arsenite	51-59	heme oxygenase 1	Homo sapiens	17-22
18771089-4	2008	When HepG2 cells were incubated with non-toxic concentrations of delta-aminolevulinic acid, protoporphyrin IX, or pheophorbide a and then exposed to visible light for 90 min, the mRNA level of HO-1 began increasing markedly, reaching the maximal level in 4 h. Following the transient induction of HO-1, the mRNA level of ABCG2 gradually increased in a time-dependent manner, whereas the ABCB6 mRNA level was little affected.	Aminolevulinic Acid	65-90	heme oxygenase 1	Homo sapiens	193-197
18771089-4	2008	When HepG2 cells were incubated with non-toxic concentrations of delta-aminolevulinic acid, protoporphyrin IX, or pheophorbide a and then exposed to visible light for 90 min, the mRNA level of HO-1 began increasing markedly, reaching the maximal level in 4 h. Following the transient induction of HO-1, the mRNA level of ABCG2 gradually increased in a time-dependent manner, whereas the ABCB6 mRNA level was little affected.	protoporphyrin IX	92-109	heme oxygenase 1	Homo sapiens	193-197
18771089-4	2008	When HepG2 cells were incubated with non-toxic concentrations of delta-aminolevulinic acid, protoporphyrin IX, or pheophorbide a and then exposed to visible light for 90 min, the mRNA level of HO-1 began increasing markedly, reaching the maximal level in 4 h. Following the transient induction of HO-1, the mRNA level of ABCG2 gradually increased in a time-dependent manner, whereas the ABCB6 mRNA level was little affected.	pheophorbide a	114-128	heme oxygenase 1	Homo sapiens	193-197
18771089-4	2008	When HepG2 cells were incubated with non-toxic concentrations of delta-aminolevulinic acid, protoporphyrin IX, or pheophorbide a and then exposed to visible light for 90 min, the mRNA level of HO-1 began increasing markedly, reaching the maximal level in 4 h. Following the transient induction of HO-1, the mRNA level of ABCG2 gradually increased in a time-dependent manner, whereas the ABCB6 mRNA level was little affected.	pheophorbide a	114-128	heme oxygenase 1	Homo sapiens	297-301
18771089-6	2008	On the other hand, the mRNA level of HO-1 was remarkably enhanced by Zn(2+)-protoporphyrin IX or hemin even in the absence of light.	zn(2+)-protoporphyrin ix	69-93	heme oxygenase 1	Homo sapiens	37-41
20020861-7	2008	The arsenite-induced HMOX1 expression was attenuated by the promoted glutathione (GSH) synthesis by N-acetyl-L-cysteine (NAC).	arsenite	4-12	heme oxygenase 1	Homo sapiens	21-26
20020861-7	2008	The arsenite-induced HMOX1 expression was attenuated by the promoted glutathione (GSH) synthesis by N-acetyl-L-cysteine (NAC).	Glutathione	69-80	heme oxygenase 1	Homo sapiens	21-26
20020861-7	2008	The arsenite-induced HMOX1 expression was attenuated by the promoted glutathione (GSH) synthesis by N-acetyl-L-cysteine (NAC).	Glutathione	82-85	heme oxygenase 1	Homo sapiens	21-26
20020861-9	2008	Thus, induction of HMOX1 gene is highly sensitive and also selective against arsenite in the cells.	arsenite	77-85	heme oxygenase 1	Homo sapiens	19-24
18165777-3	2007	METHOD: We studied the impact of HO-1 induction with cobalt protoporphyrin (CoPP) in experimental pancreas transplantation with moderate (6 hr) and prolonged (20 hr) cold ischemic time (CIT).	cobaltiprotoporphyrin	53-74	heme oxygenase 1	Homo sapiens	33-37
17965015-2	2007	The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs.	Heme	35-39	heme oxygenase 1	Homo sapiens	138-142
18165777-3	2007	METHOD: We studied the impact of HO-1 induction with cobalt protoporphyrin (CoPP) in experimental pancreas transplantation with moderate (6 hr) and prolonged (20 hr) cold ischemic time (CIT).	cobaltiprotoporphyrin	76-80	heme oxygenase 1	Homo sapiens	33-37
18165777-9	2007	CoPP pretreatment markedly increased HO-1 gene expression in donor pancreas (130-fold increase) by means of quantitative reverse transcriptase -polymerase chain reaction.	cobaltiprotoporphyrin	0-4	heme oxygenase 1	Homo sapiens	37-41
18026199-10	2007	Treatment with hemin, a well-known specific inducer of HO-1, led to clear nuclear localisation of HO-1 in both cell lines and highly induced HO-1 expression in both cellular compartments.	Hemin	15-20	heme oxygenase 1	Homo sapiens	55-59
18026199-10	2007	Treatment with hemin, a well-known specific inducer of HO-1, led to clear nuclear localisation of HO-1 in both cell lines and highly induced HO-1 expression in both cellular compartments.	Hemin	15-20	heme oxygenase 1	Homo sapiens	98-102
18026199-10	2007	Treatment with hemin, a well-known specific inducer of HO-1, led to clear nuclear localisation of HO-1 in both cell lines and highly induced HO-1 expression in both cellular compartments.	Hemin	15-20	heme oxygenase 1	Homo sapiens	98-102
17883332-2	2007	We examined, in vascular endothelial cells, whether the selective expression of heme oxygenase-1 (HO-1) offers cytoprotection against glucose- and TNF-mediated cell death.	Glucose	134-141	heme oxygenase 1	Homo sapiens	80-96
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Heme	51-55	heme oxygenase 1	Homo sapiens	0-16
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Heme	51-55	heme oxygenase 1	Homo sapiens	18-22
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	89-104	heme oxygenase 1	Homo sapiens	0-16
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	89-104	heme oxygenase 1	Homo sapiens	18-22
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Iron	148-152	heme oxygenase 1	Homo sapiens	88-104
17883332-2	2007	We examined, in vascular endothelial cells, whether the selective expression of heme oxygenase-1 (HO-1) offers cytoprotection against glucose- and TNF-mediated cell death.	Glucose	134-141	heme oxygenase 1	Homo sapiens	98-102
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Iron	148-152	heme oxygenase 1	Homo sapiens	106-110
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Biliverdine	158-168	heme oxygenase 1	Homo sapiens	88-104
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Biliverdine	158-168	heme oxygenase 1	Homo sapiens	106-110
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Bilirubin	196-205	heme oxygenase 1	Homo sapiens	88-104
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Bilirubin	196-205	heme oxygenase 1	Homo sapiens	106-110
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Heme	39-43	heme oxygenase 1	Homo sapiens	57-61
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	106-108	heme oxygenase 1	Homo sapiens	0-16
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Carbon Monoxide	106-108	heme oxygenase 1	Homo sapiens	18-22
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Biliverdine	111-121	heme oxygenase 1	Homo sapiens	0-16
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Biliverdine	111-121	heme oxygenase 1	Homo sapiens	18-22
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Iron	127-139	heme oxygenase 1	Homo sapiens	0-16
17822372-1	2007	Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron.	Iron	127-139	heme oxygenase 1	Homo sapiens	18-22
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	166-168	heme oxygenase 1	Homo sapiens	57-61
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	39-55
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	57-61
17883332-6	2007	Selective expression of HO-1 prevented TNF- and hyperglycemia-mediated superoxide (O2-) formation, DNA degeneration, and upregulation of caspase, but increased the expression of pAkt and Bcl-xL, proteins responsible for endothelial dysfunction in diabetes.	Superoxides	71-81	heme oxygenase 1	Homo sapiens	24-28
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Biliverdine	171-181	heme oxygenase 1	Homo sapiens	39-55
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Biliverdine	171-181	heme oxygenase 1	Homo sapiens	57-61
17883332-6	2007	Selective expression of HO-1 prevented TNF- and hyperglycemia-mediated superoxide (O2-) formation, DNA degeneration, and upregulation of caspase, but increased the expression of pAkt and Bcl-xL, proteins responsible for endothelial dysfunction in diabetes.	Superoxides	83-85	heme oxygenase 1	Homo sapiens	24-28
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Iron	192-196	heme oxygenase 1	Homo sapiens	39-55
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Iron	192-196	heme oxygenase 1	Homo sapiens	57-61
17979524-6	2007	Prior exposure of cells to N-acetyl-L -cysteine blocked not only the ROS production but also the nuclear translocation of Nrf2 and its ARE binding, as well as HO-1 induction by capsaicin.	Acetylcysteine	27-47	heme oxygenase 1	Homo sapiens	159-163
17979524-6	2007	Prior exposure of cells to N-acetyl-L -cysteine blocked not only the ROS production but also the nuclear translocation of Nrf2 and its ARE binding, as well as HO-1 induction by capsaicin.	Capsaicin	177-186	heme oxygenase 1	Homo sapiens	159-163
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Heme	12-16	heme oxygenase 1	Homo sapiens	88-104
17979524-7	2007	Immunoblot analysis showed that whereas the level of HO-1 protein was elevated, that of NAD(P)H:quinone oxidoreductase (NQO1) was decreased after the treatment with capsaicin or the inhibitor of NQO1, dicumarol.	Capsaicin	165-174	heme oxygenase 1	Homo sapiens	53-57
17979524-7	2007	Immunoblot analysis showed that whereas the level of HO-1 protein was elevated, that of NAD(P)H:quinone oxidoreductase (NQO1) was decreased after the treatment with capsaicin or the inhibitor of NQO1, dicumarol.	Dicumarol	201-210	heme oxygenase 1	Homo sapiens	53-57
17919067-7	2007	Accumulating evidence indicates that biliverdin/bilirubin can mediate the protective effects of HO-1 in many disease models, such as IRI and organ transplantation, via its antiinflammatory, antiapoptotic, antiproliferative, and antioxidant properties, as well as its effects on the immune response.	Biliverdine	37-47	heme oxygenase 1	Homo sapiens	96-100
17919067-7	2007	Accumulating evidence indicates that biliverdin/bilirubin can mediate the protective effects of HO-1 in many disease models, such as IRI and organ transplantation, via its antiinflammatory, antiapoptotic, antiproliferative, and antioxidant properties, as well as its effects on the immune response.	Bilirubin	48-57	heme oxygenase 1	Homo sapiens	96-100
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Heme	12-16	heme oxygenase 1	Homo sapiens	106-110
17979524-0	2007	Capsaicin induces heme oxygenase-1 expression in HepG2 cells via activation of PI3K-Nrf2 signaling: NAD(P)H:quinone oxidoreductase as a potential target.	Capsaicin	0-9	heme oxygenase 1	Homo sapiens	18-34
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	88-104
17979524-0	2007	Capsaicin induces heme oxygenase-1 expression in HepG2 cells via activation of PI3K-Nrf2 signaling: NAD(P)H:quinone oxidoreductase as a potential target.	nad(p)h	100-107	heme oxygenase 1	Homo sapiens	18-34
17979524-3	2007	In the present study, we found that capsaicin induced expression of heme oxygenase-1 (HO-1) in HepG2 cells.	Capsaicin	36-45	heme oxygenase 1	Homo sapiens	68-84
17979524-3	2007	In the present study, we found that capsaicin induced expression of heme oxygenase-1 (HO-1) in HepG2 cells.	Capsaicin	36-45	heme oxygenase 1	Homo sapiens	86-90
18077580-5	2007	Furthermore, NAC inhibited arsenite-induced elevation in the expression of stress proteins, such as heat shock protein 70 and heme oxygenase 1, as well as arsenite-induced phosphorylation of p38 mitogen-activated protein kinase.	Acetylcysteine	13-16	heme oxygenase 1	Homo sapiens	126-142
18077580-5	2007	Furthermore, NAC inhibited arsenite-induced elevation in the expression of stress proteins, such as heat shock protein 70 and heme oxygenase 1, as well as arsenite-induced phosphorylation of p38 mitogen-activated protein kinase.	arsenite	27-35	heme oxygenase 1	Homo sapiens	126-142
17887916-3	2007	Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	106-110
17919067-2	2007	The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	166-168	heme oxygenase 1	Homo sapiens	39-55
17982681-0	2007	Inhibition of heme oxygenase-1 increases responsiveness of melanoma cells to ALA-based photodynamic therapy.	5-amino levulinic acid	77-80	heme oxygenase 1	Homo sapiens	14-30
17924972-9	2007	The inductive effects of SP on HO-1 and CCL20 were enhanced by HO-1 inducer hemin and the membrane-permeable guanosine 3",5"-monophosphate (cGMP) analogue 8-bromo-cGMP.	Cyclic GMP	109-138	heme oxygenase 1	Homo sapiens	31-35
17924972-9	2007	The inductive effects of SP on HO-1 and CCL20 were enhanced by HO-1 inducer hemin and the membrane-permeable guanosine 3",5"-monophosphate (cGMP) analogue 8-bromo-cGMP.	Cyclic GMP	140-144	heme oxygenase 1	Homo sapiens	31-35
17924972-9	2007	The inductive effects of SP on HO-1 and CCL20 were enhanced by HO-1 inducer hemin and the membrane-permeable guanosine 3",5"-monophosphate (cGMP) analogue 8-bromo-cGMP.	8-bromocyclic GMP	155-167	heme oxygenase 1	Homo sapiens	31-35
17924972-10	2007	Conversely, this pathway was inhibited by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) and the selective inhibitor of guanylate cyclase, 1H-(1,2,4)oxadiazole(4,3-a)quinoxalin-1-one (ODQ).	zinc protoporphyrin	61-83	heme oxygenase 1	Homo sapiens	46-50
17924972-10	2007	Conversely, this pathway was inhibited by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) and the selective inhibitor of guanylate cyclase, 1H-(1,2,4)oxadiazole(4,3-a)quinoxalin-1-one (ODQ).	zinc protoporphyrin	85-89	heme oxygenase 1	Homo sapiens	46-50
17924972-10	2007	Conversely, this pathway was inhibited by the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) and the selective inhibitor of guanylate cyclase, 1H-(1,2,4)oxadiazole(4,3-a)quinoxalin-1-one (ODQ).	1H-(1,2,3)oxadiazolo(4,4-a)quinoxalin-1-one	189-192	heme oxygenase 1	Homo sapiens	46-50
18210237-0	2007	Costunolide inhibits production of tumor necrosis factor-alpha and interleukin-6 by inducing heme oxygenase-1 in RAW264.7 macrophages.	costunolide	0-11	heme oxygenase 1	Homo sapiens	93-109
17982681-5	2007	Thus, the production and degradation of PPIX (via heme by HO-1) were simultaneously enhanced, leading to a reduced intracellular concentration of the photodynamically active substance PPIX.	Heme	50-54	heme oxygenase 1	Homo sapiens	58-62
17982681-5	2007	Thus, the production and degradation of PPIX (via heme by HO-1) were simultaneously enhanced, leading to a reduced intracellular concentration of the photodynamically active substance PPIX.	protoporphyrin IX	184-188	heme oxygenase 1	Homo sapiens	58-62
17982681-6	2007	Diminishing HO-1 activity by the HO-1 inhibitor tin protoporphyrin IX (SnPPIX) significantly enhanced the formation of PPIX up to 1.8 fold.	tin protoporphyrin IX	48-69	heme oxygenase 1	Homo sapiens	12-16
17973866-2	2007	Heme compounds, like hemin, a heme oxygenase-1 inducer, are used in the treatment of acute porphyria treatment.	Heme	0-4	heme oxygenase 1	Homo sapiens	30-46
17973866-2	2007	Heme compounds, like hemin, a heme oxygenase-1 inducer, are used in the treatment of acute porphyria treatment.	Hemin	21-26	heme oxygenase 1	Homo sapiens	30-46
17982681-6	2007	Diminishing HO-1 activity by the HO-1 inhibitor tin protoporphyrin IX (SnPPIX) significantly enhanced the formation of PPIX up to 1.8 fold.	tin protoporphyrin IX	48-69	heme oxygenase 1	Homo sapiens	33-37
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	30-51	heme oxygenase 1	Homo sapiens	84-100
17982681-6	2007	Diminishing HO-1 activity by the HO-1 inhibitor tin protoporphyrin IX (SnPPIX) significantly enhanced the formation of PPIX up to 1.8 fold.	tin protoporphyrin IX	71-77	heme oxygenase 1	Homo sapiens	12-16
17982681-6	2007	Diminishing HO-1 activity by the HO-1 inhibitor tin protoporphyrin IX (SnPPIX) significantly enhanced the formation of PPIX up to 1.8 fold.	tin protoporphyrin IX	71-77	heme oxygenase 1	Homo sapiens	33-37
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	30-51	heme oxygenase 1	Homo sapiens	102-106
17982681-6	2007	Diminishing HO-1 activity by the HO-1 inhibitor tin protoporphyrin IX (SnPPIX) significantly enhanced the formation of PPIX up to 1.8 fold.	protoporphyrin IX	73-77	heme oxygenase 1	Homo sapiens	12-16
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	53-56	heme oxygenase 1	Homo sapiens	84-100
17982681-6	2007	Diminishing HO-1 activity by the HO-1 inhibitor tin protoporphyrin IX (SnPPIX) significantly enhanced the formation of PPIX up to 1.8 fold.	protoporphyrin IX	73-77	heme oxygenase 1	Homo sapiens	33-37
17982681-9	2007	The pharmacological inhibition of HO-1 activity by SnPPIX leads to a considerable increase in the sensitivity of tumor cells to ALA-PDT treatment.	tin protoporphyrin IX	51-57	heme oxygenase 1	Homo sapiens	34-38
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	53-56	heme oxygenase 1	Homo sapiens	102-106
17982681-9	2007	The pharmacological inhibition of HO-1 activity by SnPPIX leads to a considerable increase in the sensitivity of tumor cells to ALA-PDT treatment.	5-amino levulinic acid	128-131	heme oxygenase 1	Homo sapiens	34-38
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	53-56	heme oxygenase 1	Homo sapiens	148-152
17982681-13	2007	The results presented indicate that HO-1 can play a protective role against ALA-PDT mediated cytotoxicity so that a specific inhibition of HO-1 activity and/or expression might be used to increase the efficacy of ALA-based photodynamic therapy.	5-amino levulinic acid	76-79	heme oxygenase 1	Homo sapiens	36-40
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	177-198	heme oxygenase 1	Homo sapiens	84-100
17982681-13	2007	The results presented indicate that HO-1 can play a protective role against ALA-PDT mediated cytotoxicity so that a specific inhibition of HO-1 activity and/or expression might be used to increase the efficacy of ALA-based photodynamic therapy.	5-amino levulinic acid	76-79	heme oxygenase 1	Homo sapiens	139-143
17982681-13	2007	The results presented indicate that HO-1 can play a protective role against ALA-PDT mediated cytotoxicity so that a specific inhibition of HO-1 activity and/or expression might be used to increase the efficacy of ALA-based photodynamic therapy.	5-amino levulinic acid	213-216	heme oxygenase 1	Homo sapiens	36-40
17982681-13	2007	The results presented indicate that HO-1 can play a protective role against ALA-PDT mediated cytotoxicity so that a specific inhibition of HO-1 activity and/or expression might be used to increase the efficacy of ALA-based photodynamic therapy.	5-amino levulinic acid	213-216	heme oxygenase 1	Homo sapiens	139-143
17982681-1	2007	Based on the observation that 5-aminolevulinic acid (ALA) induces the expression of heme oxygenase-1 (HO-1) in cultured melanoma cells, the role of HO-1 on the effectiveness of 5-aminolevulinic acid-based photodynamic therapy (ALA-PDT) was examined.	5-amino levulinic acid	177-198	heme oxygenase 1	Homo sapiens	148-152
17982681-2	2007	Transcriptional activation of the HO-1 gene is considered to be an adaptive response to oxidative and cellular stress and confers a protective capacity against cell and tissue injury, which could affect the responsiveness to ALA-PDT.	5-amino levulinic acid	225-228	heme oxygenase 1	Homo sapiens	34-38
17982681-5	2007	Thus, the production and degradation of PPIX (via heme by HO-1) were simultaneously enhanced, leading to a reduced intracellular concentration of the photodynamically active substance PPIX.	protoporphyrin IX	40-44	heme oxygenase 1	Homo sapiens	58-62
17761847-1	2007	To enhance our understanding of the physiological roles of heme oxygenase (HO) isozymes, HO-1 (inducible) and HO-2 (constitutive), we developed novel imidazole-based HO inhibitors.	imidazole	150-159	heme oxygenase 1	Homo sapiens	89-93
17881360-1	2007	Heme oxygenase-1 (HO-1), an inducible enzyme that metabolizes the heme group, is highly expressed in human Kaposi sarcoma lesions.	Heme	66-70	heme oxygenase 1	Homo sapiens	0-16
17927807-7	2007	HO-1 inhibition, with small interfering RNA (siRNA) or zinc protoporphyrin IX, abrogated atorvastatin-mediated cytoprotection.	protoporphyrin IX	60-77	heme oxygenase 1	Homo sapiens	0-4
17927807-7	2007	HO-1 inhibition, with small interfering RNA (siRNA) or zinc protoporphyrin IX, abrogated atorvastatin-mediated cytoprotection.	Atorvastatin	89-101	heme oxygenase 1	Homo sapiens	0-4
17927807-9	2007	Iron chelation, adenoviral-mediated overexpression of ferritin or supplementation of culture media with biliverdin reversed the inhibitory effects of HO-1 and KLF2 siRNA, suggesting that bile pigments and ferritin mediate the antioxidant actions of statin-induced HO-1.	Biliverdine	104-114	heme oxygenase 1	Homo sapiens	150-154
17927807-9	2007	Iron chelation, adenoviral-mediated overexpression of ferritin or supplementation of culture media with biliverdin reversed the inhibitory effects of HO-1 and KLF2 siRNA, suggesting that bile pigments and ferritin mediate the antioxidant actions of statin-induced HO-1.	Biliverdine	104-114	heme oxygenase 1	Homo sapiens	264-268
17927807-10	2007	CONCLUSIONS: We have identified a novel link between KLF2 and HO-1 in human vascular ECs, demonstrating that atorvastatin-mediated HO-1 upregulation, and its associated antioxidant effect, is KLF2-dependent.	Atorvastatin	109-121	heme oxygenase 1	Homo sapiens	62-66
17927807-10	2007	CONCLUSIONS: We have identified a novel link between KLF2 and HO-1 in human vascular ECs, demonstrating that atorvastatin-mediated HO-1 upregulation, and its associated antioxidant effect, is KLF2-dependent.	Atorvastatin	109-121	heme oxygenase 1	Homo sapiens	131-135
18089404-1	2007	PURPOSE: The heme oxygenase-1 (HO-1) system is associated with the rate-limiting step of conversion of heme, one of the most critical roles in cytoprotective mechanisms.	Heme	13-17	heme oxygenase 1	Homo sapiens	31-35
18089404-10	2007	After using ZnPP, an inhibitor of HO-1, the rate of Jurkat T-cell adhesion recovered to 29.08%.	zinc protoporphyrin	12-16	heme oxygenase 1	Homo sapiens	34-38
17885094-0	2007	Chondroitin sulfate protects SH-SY5Y cells from oxidative stress by inducing heme oxygenase-1 via phosphatidylinositol 3-kinase/Akt.	Chondroitin Sulfates	0-19	heme oxygenase 1	Homo sapiens	77-93
17885094-7	2007	CS also increased the expression of phosphorylated Akt and heme oxygenase-1 by 2-fold.	Chondroitin Sulfates	0-2	heme oxygenase 1	Homo sapiens	59-75
17885094-9	2007	Taken together, these results show that CS can protect SH-SY5Y cells under oxidative stress conditions by activating protein kinase C, which phosphorylates Akt that, via the phosphatidylinositol 3-kinase/Akt pathway, induces the synthesis of the antioxidant protein heme oxygenase-1.	Chondroitin Sulfates	40-42	heme oxygenase 1	Homo sapiens	266-282
17927807-4	2007	METHODS/RESULTS: Treatment of human umbilical vein and aortic ECs with atorvastatin significantly upregulated HO-1 promoter activity, mRNA expression and protein expression, increasing HO-1 enzymatic activity as shown by raised intracellular bilirubin IXalpha.	Atorvastatin	71-83	heme oxygenase 1	Homo sapiens	110-114
17927807-4	2007	METHODS/RESULTS: Treatment of human umbilical vein and aortic ECs with atorvastatin significantly upregulated HO-1 promoter activity, mRNA expression and protein expression, increasing HO-1 enzymatic activity as shown by raised intracellular bilirubin IXalpha.	Atorvastatin	71-83	heme oxygenase 1	Homo sapiens	185-189
17976119-8	2007	However, the anti-apoptotic action of HO-1 was reversed by SnPP.	S-Nitroso-N-propionyl-D,L-penicillamine	59-63	heme oxygenase 1	Homo sapiens	38-42
17881360-1	2007	Heme oxygenase-1 (HO-1), an inducible enzyme that metabolizes the heme group, is highly expressed in human Kaposi sarcoma lesions.	Heme	66-70	heme oxygenase 1	Homo sapiens	18-22
17881360-9	2007	Likewise, inhibition of HO-1 activity by chronic administration of the HO-1 inhibitor tin protoporphyrin IX to mice reduces RhoAQL-induced tumor growth by 70%.	tin protoporphyrin IX	86-107	heme oxygenase 1	Homo sapiens	71-75
17881360-9	2007	Likewise, inhibition of HO-1 activity by chronic administration of the HO-1 inhibitor tin protoporphyrin IX to mice reduces RhoAQL-induced tumor growth by 70%.	rhoaql	124-130	heme oxygenase 1	Homo sapiens	71-75
17600318-8	2007	In functional studies, the HO-1 inhibitor, ZnPP-IX, partly reversed the growth-inhibitory effects of BMP4, and overexpression of HO-1 in PASMCs inhibited serum-stimulated [3H]-thymidine incorporation.	zinc protoporphyrin	43-50	heme oxygenase 1	Homo sapiens	27-31
17991645-0	2007	Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with iron status in persons with type 2 diabetes mellitus.	Iron	85-89	heme oxygenase 1	Homo sapiens	35-51
17991645-3	2007	Heme oxygenase (HO) 1 expression is increased when intracellular iron increases.	Iron	65-69	heme oxygenase 1	Homo sapiens	0-21
17600318-8	2007	In functional studies, the HO-1 inhibitor, ZnPP-IX, partly reversed the growth-inhibitory effects of BMP4, and overexpression of HO-1 in PASMCs inhibited serum-stimulated [3H]-thymidine incorporation.	pasmcs	137-143	heme oxygenase 1	Homo sapiens	129-133
17600318-8	2007	In functional studies, the HO-1 inhibitor, ZnPP-IX, partly reversed the growth-inhibitory effects of BMP4, and overexpression of HO-1 in PASMCs inhibited serum-stimulated [3H]-thymidine incorporation.	Tritium	172-174	heme oxygenase 1	Homo sapiens	27-31
17600318-8	2007	In functional studies, the HO-1 inhibitor, ZnPP-IX, partly reversed the growth-inhibitory effects of BMP4, and overexpression of HO-1 in PASMCs inhibited serum-stimulated [3H]-thymidine incorporation.	Tritium	172-174	heme oxygenase 1	Homo sapiens	129-133
17600318-8	2007	In functional studies, the HO-1 inhibitor, ZnPP-IX, partly reversed the growth-inhibitory effects of BMP4, and overexpression of HO-1 in PASMCs inhibited serum-stimulated [3H]-thymidine incorporation.	Thymidine	176-185	heme oxygenase 1	Homo sapiens	129-133
17868064-10	2007	Diannexin increased expression of HO-1/Bcl-2/Bcl-xl, and reduced Caspase-3/TUNEL+ apoptotic cells.	diannexin	0-9	heme oxygenase 1	Homo sapiens	34-38
17600318-10	2007	Inhibition of HO-1 function or expression will further increase the proproliferative capacity of BMPR-II-deficient PASMCs and may thus represent a potential "second hit" necessary for disease manifestation.	pasmcs	115-121	heme oxygenase 1	Homo sapiens	14-18
18087801-2	2007	One synthetic derivative of butein, 2",4",6"-tris(methoxymethoxy)chalcone (TMMC), has potent anti-inflammatory activity via an HO-1 (heme oxygenase 1) dependent pathway.	butein, 2",4",6"-tris(methoxymethoxy)chalcone	28-73	heme oxygenase 1	Homo sapiens	127-131
17963960-0	2007	The induction of heme oxygenase-1 modulates bismuth oxide-induced cytotoxicity in human dental pulp cells.	bismuth oxide	44-57	heme oxygenase 1	Homo sapiens	17-33
17963960-2	2007	We also assessed whether heme oxygenase-1 (HO-1) is involved in BPC-induced cytotoxicity in dental pulp cells.	S-(4-bromophenyl)cysteine sulfoxide	64-67	heme oxygenase 1	Homo sapiens	25-41
17963960-2	2007	We also assessed whether heme oxygenase-1 (HO-1) is involved in BPC-induced cytotoxicity in dental pulp cells.	S-(4-bromophenyl)cysteine sulfoxide	64-67	heme oxygenase 1	Homo sapiens	43-47
17963960-7	2007	Moreover, BPC-induced HO-1 expression in dental pulp cells plays a protective role against the cytotoxic effects of BPC.	S-(4-bromophenyl)cysteine sulfoxide	10-13	heme oxygenase 1	Homo sapiens	22-26
17822364-5	2007	CDDO-Im treatment significantly induced Nrf2-dependent antioxidative genes (HO-1, GCLC, GCLM, and NQO1) in PBMCs isolated from six normal subjects.	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	0-7	heme oxygenase 1	Homo sapiens	76-80
17956297-1	2007	The well-known adverse effects of CO (carbon monoxide) intoxication are counterbalanced by its positive actions when small amounts are produced intracellularly by the cytoprotective enzyme HO-1 (haem oxygenase-1).	Carbon Monoxide	34-54	heme oxygenase 1	Homo sapiens	189-211
18087801-2	2007	One synthetic derivative of butein, 2",4",6"-tris(methoxymethoxy)chalcone (TMMC), has potent anti-inflammatory activity via an HO-1 (heme oxygenase 1) dependent pathway.	butein, 2",4",6"-tris(methoxymethoxy)chalcone	28-73	heme oxygenase 1	Homo sapiens	133-149
18087801-2	2007	One synthetic derivative of butein, 2",4",6"-tris(methoxymethoxy)chalcone (TMMC), has potent anti-inflammatory activity via an HO-1 (heme oxygenase 1) dependent pathway.	2',4',6'-tris(methoxymethoxy) chalcone	75-79	heme oxygenase 1	Homo sapiens	127-131
18087801-2	2007	One synthetic derivative of butein, 2",4",6"-tris(methoxymethoxy)chalcone (TMMC), has potent anti-inflammatory activity via an HO-1 (heme oxygenase 1) dependent pathway.	2',4',6'-tris(methoxymethoxy) chalcone	75-79	heme oxygenase 1	Homo sapiens	133-149
17889572-8	2007	The level of iNOS and HO-1 mRNA expression were increased by CLP, which was prevented by both AG and L-NAME.	NG-Nitroarginine Methyl Ester	101-107	heme oxygenase 1	Homo sapiens	22-26
17823375-0	2007	Carbon monoxide induces heme oxygenase-1 via activation of protein kinase R-like endoplasmic reticulum kinase and inhibits endothelial cell apoptosis triggered by endoplasmic reticulum stress.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	24-40
17996129-9	2007	iNOS, COX-2 and HO-1 mRNA expression were fluctuated in the normal range following oligomycin administration (all P&gt;0.05).	Oligomycins	83-93	heme oxygenase 1	Homo sapiens	16-20
17915953-1	2007	Heme oxygenase-1 (HO-1) is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin.	Heme	87-91	heme oxygenase 1	Homo sapiens	0-16
17915953-1	2007	Heme oxygenase-1 (HO-1) is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin.	Heme	87-91	heme oxygenase 1	Homo sapiens	18-22
17915953-1	2007	Heme oxygenase-1 (HO-1) is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin.	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	0-16
17915953-1	2007	Heme oxygenase-1 (HO-1) is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin.	Biliverdine	95-105	heme oxygenase 1	Homo sapiens	18-22
17915953-2	2007	In the process of heme degradation, HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free iron and carbon monoxide.	Iron	164-168	heme oxygenase 1	Homo sapiens	36-40
17915953-2	2007	In the process of heme degradation, HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free iron and carbon monoxide.	Carbon Monoxide	173-188	heme oxygenase 1	Homo sapiens	36-40
17915953-10	2007	The R254K full-length form had a specific activity of approximately 200-225 nmol of bilirubin h-1 nmol-1 HO-1 as compared to approximately 140-150 nmol of bilirubin h-1 nmol-1 for the WT form, which contains the 30 kDa contaminant.	Bilirubin	84-93	heme oxygenase 1	Homo sapiens	105-109
17915953-10	2007	The R254K full-length form had a specific activity of approximately 200-225 nmol of bilirubin h-1 nmol-1 HO-1 as compared to approximately 140-150 nmol of bilirubin h-1 nmol-1 for the WT form, which contains the 30 kDa contaminant.	bilirubin h	84-95	heme oxygenase 1	Homo sapiens	105-109
17915953-12	2007	Because the membrane-spanning domain is present, the full-length hHO-1 has the potential to incorporate into phospholipid membranes, which can be reconstituted at known concentrations, in combination with other endoplasmic reticulum resident enzymes.	Phospholipids	109-121	heme oxygenase 1	Homo sapiens	65-70
17823375-1	2007	Carbon monoxide (CO), a reaction product of the cytoprotective heme oxygenase (HO)-1, is antiapoptotic in a variety of models of cellular injury, but the precise mechanisms remain to be established.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	63-84
17823375-1	2007	Carbon monoxide (CO), a reaction product of the cytoprotective heme oxygenase (HO)-1, is antiapoptotic in a variety of models of cellular injury, but the precise mechanisms remain to be established.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	63-84
17895889-6	2007	Cobalt protoporphyrin induced HMOX-1, instead of HIF-1 alpha expression and increased bortezomib-induced apoptosis in the presence of pharmacologically effective doses of bortezomib.	cobaltiprotoporphyrin	0-21	heme oxygenase 1	Homo sapiens	30-36
17967796-0	2007	A new road to induce heme oxygenase-1 expression by carbon monoxide.	Carbon Monoxide	52-67	heme oxygenase 1	Homo sapiens	21-37
17895889-7	2007	In contrast, zinc protoporphyrin downregulated HMOX-1 expression, thereby partially inhibiting bortezomib-induced cell death.	zinc protoporphyrin	13-32	heme oxygenase 1	Homo sapiens	47-53
17895889-0	2007	Induction of heme oxygenase-1 by cobalt protoporphyrin enhances the antitumour effect of bortezomib in adult T-cell leukaemia cells.	cobaltiprotoporphyrin	33-54	heme oxygenase 1	Homo sapiens	13-29
17895889-7	2007	In contrast, zinc protoporphyrin downregulated HMOX-1 expression, thereby partially inhibiting bortezomib-induced cell death.	Bortezomib	95-105	heme oxygenase 1	Homo sapiens	47-53
17895889-0	2007	Induction of heme oxygenase-1 by cobalt protoporphyrin enhances the antitumour effect of bortezomib in adult T-cell leukaemia cells.	Bortezomib	89-99	heme oxygenase 1	Homo sapiens	13-29
17895889-8	2007	This indicates that HMOX-1 may modulate anticancer effects of bortezomib in ATL cells, and could be a molecular target in treating ATL patients.	Bortezomib	62-72	heme oxygenase 1	Homo sapiens	20-26
17895889-5	2007	An oligonucleotide DNA microarray analysis of TaY cells revealed upregulation of genes encoding heat shock proteins (HSPA1A, STIP1, HSPA1B, and HSPCA), genes related to protein folding (CDC37 and ANAPC5), Fas-associated factor 1(FAF1) and an oxidative stress-related gene, heme oxygenase-1(HMOX-1), known to be a target gene of hypoxia-inducible gene-1 alpha (HIF-1 alpha).	Oligonucleotides	3-18	heme oxygenase 1	Homo sapiens	273-289
17895889-5	2007	An oligonucleotide DNA microarray analysis of TaY cells revealed upregulation of genes encoding heat shock proteins (HSPA1A, STIP1, HSPA1B, and HSPCA), genes related to protein folding (CDC37 and ANAPC5), Fas-associated factor 1(FAF1) and an oxidative stress-related gene, heme oxygenase-1(HMOX-1), known to be a target gene of hypoxia-inducible gene-1 alpha (HIF-1 alpha).	Oligonucleotides	3-18	heme oxygenase 1	Homo sapiens	290-296
17896171-8	2007	RESULTS: HO-1-overexpression reduced proliferative rates and DNA-synthesis of HUVEC, but provided potent protection from oxidative stress induced by heme and H(2)O(2).	Heme	149-153	heme oxygenase 1	Homo sapiens	9-13
17919491-1	2007	BACKGROUND &amp; AIMS: Induction of heme oxygenase-1 (HO-1) has been shown to be beneficial in immune-mediated liver damage.	Adenosine Monophosphate	12-15	heme oxygenase 1	Homo sapiens	36-52
17919491-1	2007	BACKGROUND &amp; AIMS: Induction of heme oxygenase-1 (HO-1) has been shown to be beneficial in immune-mediated liver damage.	Adenosine Monophosphate	12-15	heme oxygenase 1	Homo sapiens	54-58
17919491-7	2007	HO-1 was induced by either cobalt-protoporphyrin-IX or over expressed by adenoviral gene transfer.	cobaltiprotoporphyrin	27-51	heme oxygenase 1	Homo sapiens	0-4
17919492-1	2007	BACKGROUND &amp; AIMS: Heme oxygenase-1 (HO-1) is an antioxidant defense and key cytoprotective enzyme, which is repressed by Bach1.	Adenosine Monophosphate	12-15	heme oxygenase 1	Homo sapiens	23-39
17919492-1	2007	BACKGROUND &amp; AIMS: Heme oxygenase-1 (HO-1) is an antioxidant defense and key cytoprotective enzyme, which is repressed by Bach1.	Adenosine Monophosphate	12-15	heme oxygenase 1	Homo sapiens	41-45
17919492-3	2007	This study was to assess whether a specific miR-122 antagomir down-regulates HCV protein replication and up-regulates HO-1.	mir-122	44-51	heme oxygenase 1	Homo sapiens	118-122
17919492-7	2007	Antagomir of miR-122 also decreased Bach1 and increased HO-1 mRNA levels in CNS3, 9-13, and WT Huh-7 cells.	mir-122	13-20	heme oxygenase 1	Homo sapiens	56-60
17919492-8	2007	Increasing HO-1 by silencing Bach1 with 50 nmol/L Bach1-short interfering RNA or by treatment with 5 mumol/L cobalt protoporphyrin or heme (known inducers of HO-1) decreased HCV RNA and protein by 50% in HCV replicon cells.	cobaltiprotoporphyrin	109-130	heme oxygenase 1	Homo sapiens	11-15
17919492-8	2007	Increasing HO-1 by silencing Bach1 with 50 nmol/L Bach1-short interfering RNA or by treatment with 5 mumol/L cobalt protoporphyrin or heme (known inducers of HO-1) decreased HCV RNA and protein by 50% in HCV replicon cells.	cobaltiprotoporphyrin	109-130	heme oxygenase 1	Homo sapiens	158-162
17919492-8	2007	Increasing HO-1 by silencing Bach1 with 50 nmol/L Bach1-short interfering RNA or by treatment with 5 mumol/L cobalt protoporphyrin or heme (known inducers of HO-1) decreased HCV RNA and protein by 50% in HCV replicon cells.	Heme	134-138	heme oxygenase 1	Homo sapiens	11-15
17919492-8	2007	Increasing HO-1 by silencing Bach1 with 50 nmol/L Bach1-short interfering RNA or by treatment with 5 mumol/L cobalt protoporphyrin or heme (known inducers of HO-1) decreased HCV RNA and protein by 50% in HCV replicon cells.	Heme	134-138	heme oxygenase 1	Homo sapiens	158-162
17919492-10	2007	Increasing HO-1, by silencing the Bach1 gene or by treatment with cobalt protoporphyrin or heme, decreases HCV replication.	cobaltiprotoporphyrin	66-87	heme oxygenase 1	Homo sapiens	11-15
17679649-1	2007	Our previous studies suggest that heme oxygenase (HO)-1 induction and/or subsequent bilirubin generation in endothelial cells may suppress superoxide generation of from reduced nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase.	Superoxides	139-149	heme oxygenase 1	Homo sapiens	34-55
17919492-10	2007	Increasing HO-1, by silencing the Bach1 gene or by treatment with cobalt protoporphyrin or heme, decreases HCV replication.	Heme	91-95	heme oxygenase 1	Homo sapiens	11-15
17679649-5	2007	The increase in HO-1 activity and inhibition of NADPH oxidase activity by hemin were reversed by tin protoporphyrin-IX and were not associated with changes in Nox2 or Nox4 protein levels.	tin protoporphyrin IX	97-118	heme oxygenase 1	Homo sapiens	16-20
17919492-11	2007	Thus, miR-122 plays an important role in the regulation of HCV replication and HO-1/Bach1 expression in hepatocytes.	mir-122	6-13	heme oxygenase 1	Homo sapiens	79-83
17679649-10	2007	Thus, systemic expression of HO-1 suppresses NADPH oxidase activity by mechanisms at least partly mediated by the bile pigment bilirubin, thereby reducing oxidative stress.	Bilirubin	127-136	heme oxygenase 1	Homo sapiens	29-33
18044280-1	2007	INTRODUCTION: Heme-Oxygenase-1 catalyzes hemoglobin into bilirubin, iron, and carbon monoxide, a well known vasodilator.	Bilirubin	57-66	heme oxygenase 1	Homo sapiens	14-30
18044280-1	2007	INTRODUCTION: Heme-Oxygenase-1 catalyzes hemoglobin into bilirubin, iron, and carbon monoxide, a well known vasodilator.	Iron	68-72	heme oxygenase 1	Homo sapiens	14-30
18044280-1	2007	INTRODUCTION: Heme-Oxygenase-1 catalyzes hemoglobin into bilirubin, iron, and carbon monoxide, a well known vasodilator.	Carbon Monoxide	78-93	heme oxygenase 1	Homo sapiens	14-30
17678632-0	2007	2",4",6"-tris(methoxymethoxy) chalcone protects against trinitrobenzene sulfonic acid-induced colitis and blocks tumor necrosis factor-alpha-induced intestinal epithelial inflammation via heme oxygenase 1-dependent and independent pathways.	2',4',6'-tris(methoxymethoxy) chalcone	0-38	heme oxygenase 1	Homo sapiens	188-204
17678632-6	2007	TMMC induced the expression of heme oxygenase 1 (HO-1) in HT-29 cells.	2',4',6'-tris(methoxymethoxy) chalcone	0-4	heme oxygenase 1	Homo sapiens	31-47
17678632-6	2007	TMMC induced the expression of heme oxygenase 1 (HO-1) in HT-29 cells.	2',4',6'-tris(methoxymethoxy) chalcone	0-4	heme oxygenase 1	Homo sapiens	49-53
17678632-7	2007	TMMC increased extracellular signal-regulated kinase1/2 and p38 kinase phosphorylation levels, which led to the nuclear translocation of nuclear factor-erythroid 2-related factor 2 (Nrf2) and consequently to HO-1 expression.	2',4',6'-tris(methoxymethoxy) chalcone	0-4	heme oxygenase 1	Homo sapiens	208-212
17678632-10	2007	Moreover, we found that the different products of HO-1, carbon monoxide and bilirubin, exerted anti-inflammatory effects that were additive or synergistic in HT-29 cells stimulated with TNF-alpha.	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	50-54
17678632-10	2007	Moreover, we found that the different products of HO-1, carbon monoxide and bilirubin, exerted anti-inflammatory effects that were additive or synergistic in HT-29 cells stimulated with TNF-alpha.	Bilirubin	76-85	heme oxygenase 1	Homo sapiens	50-54
17726138-0	2007	Genetic variability in iron-related oxidative stress pathways (Nrf2, NQ01, NOS3, and HO-1), iron intake, and risk of postmenopausal breast cancer.	Iron	23-27	heme oxygenase 1	Homo sapiens	85-89
17567933-3	2007	HO-1 catabolizes pro-oxidant heme into substances with anti-oxidant, anti-apoptotic, anti-fibrogenic, vasodilatory and immune modulatory properties.	Heme	29-33	heme oxygenase 1	Homo sapiens	0-4
17567933-7	2007	Actinomycin D and nuclear run-on studies demonstrate that TGF-beta1 augments HO-1 expression by increased gene transcription and does not involve increased mRNA stability.	Dactinomycin	0-13	heme oxygenase 1	Homo sapiens	77-81
17569621-7	2007	Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1).	Heme	139-143	heme oxygenase 1	Homo sapiens	28-32
17569621-7	2007	Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1).	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	28-32
17569621-7	2007	Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1).	Carbon Monoxide	166-168	heme oxygenase 1	Homo sapiens	28-32
17569621-7	2007	Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1).	Iron	171-175	heme oxygenase 1	Homo sapiens	28-32
17729116-0	2007	Hemin-induced Erk1/2 activation and heme oxygenase-1 expression in human umbilical vein endothelial cells.	Hemin	0-5	heme oxygenase 1	Homo sapiens	36-52
17569621-7	2007	Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1).	Iron	177-179	heme oxygenase 1	Homo sapiens	28-32
17569621-7	2007	Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1).	Biliverdine	185-195	heme oxygenase 1	Homo sapiens	28-32
17418561-0	2007	Piperine protects cisplatin-induced apoptosis via heme oxygenase-1 induction in auditory cells.	piperine	0-8	heme oxygenase 1	Homo sapiens	50-66
17917164-1	2007	In this study, we evaluated the effect of lipoic acid (LA) and N-acetyl cysteine (NAC) on oxidative [4-hydroxy-2-nonenal, N(epsilon)-(carboxymethyl)lysine and heme oxygenase-1] and apoptotic (caspase 9 and Bax) markers in fibroblasts from patients with Alzheimer disease (AD) and age-matched and young controls.	Thioctic Acid	42-53	heme oxygenase 1	Homo sapiens	159-175
17917164-1	2007	In this study, we evaluated the effect of lipoic acid (LA) and N-acetyl cysteine (NAC) on oxidative [4-hydroxy-2-nonenal, N(epsilon)-(carboxymethyl)lysine and heme oxygenase-1] and apoptotic (caspase 9 and Bax) markers in fibroblasts from patients with Alzheimer disease (AD) and age-matched and young controls.	Acetylcysteine	82-85	heme oxygenase 1	Homo sapiens	159-175
17418561-0	2007	Piperine protects cisplatin-induced apoptosis via heme oxygenase-1 induction in auditory cells.	Cisplatin	18-27	heme oxygenase 1	Homo sapiens	50-66
17418561-2	2007	In this study, we examined whether piperine could protect House Ear Institute-Organ of Corti 1 (HEI-OC1) cells against cisplatin-induced apoptosis through the induction of heme oxygenase (HO)-1 expression.	piperine	35-43	heme oxygenase 1	Homo sapiens	172-193
17573819-9	2007	Stress-induced up-regulation of the heme-degrading enzyme, heme oxygenase-1 in AD-affected astroglia may impact central lipid homeostasis by promoting the oxidation of cholesterol to a host of oxysterol intermediates.	Heme	36-40	heme oxygenase 1	Homo sapiens	59-75
17418561-3	2007	Piperine (10-100 microM) induced the expression of HO-1 in dose- and time-dependent manners.	piperine	0-8	heme oxygenase 1	Homo sapiens	51-55
17573819-9	2007	Stress-induced up-regulation of the heme-degrading enzyme, heme oxygenase-1 in AD-affected astroglia may impact central lipid homeostasis by promoting the oxidation of cholesterol to a host of oxysterol intermediates.	Cholesterol	168-179	heme oxygenase 1	Homo sapiens	59-75
17418561-5	2007	Piperine activated the c-Jun N-terminal kinase (JNK), extracellular signal-regulated kinase and p38 mitogen-activated protein kinase (MAPK) pathways, and the JNK pathway played an important role in piperine-induced HO-1 expression.	piperine	0-8	heme oxygenase 1	Homo sapiens	215-219
17573819-9	2007	Stress-induced up-regulation of the heme-degrading enzyme, heme oxygenase-1 in AD-affected astroglia may impact central lipid homeostasis by promoting the oxidation of cholesterol to a host of oxysterol intermediates.	Oxysterols	193-202	heme oxygenase 1	Homo sapiens	59-75
17418561-5	2007	Piperine activated the c-Jun N-terminal kinase (JNK), extracellular signal-regulated kinase and p38 mitogen-activated protein kinase (MAPK) pathways, and the JNK pathway played an important role in piperine-induced HO-1 expression.	piperine	198-206	heme oxygenase 1	Homo sapiens	215-219
17418561-7	2007	The protective effect of piperine was abrogated by zinc protoporphyrin IX, an HO inhibitor, and antisense oligodeoxynucleotides against HO-1 gene.	piperine	25-33	heme oxygenase 1	Homo sapiens	136-140
17418561-8	2007	These results demonstrate that the expression of HO-1 by piperine is mediated by both JNK pathway and Nrf2, and the expression inhibits cisplatin-induced apoptosis in HEI-OC1 cells.	piperine	57-65	heme oxygenase 1	Homo sapiens	49-53
17418561-8	2007	These results demonstrate that the expression of HO-1 by piperine is mediated by both JNK pathway and Nrf2, and the expression inhibits cisplatin-induced apoptosis in HEI-OC1 cells.	Cisplatin	136-145	heme oxygenase 1	Homo sapiens	49-53
17785948-9	2007	Accordingly, under the heme-rich condition, heme binds to cysteine-proline (CP) motifs of ALAS1 and those of transcriptional repressor Bach1, thereby leading to repression of mitochondrial transport of ALAS1 and induction of HO-1 transcription, respectively.	Heme	44-48	heme oxygenase 1	Homo sapiens	225-229
17675106-1	2007	We investigated whether increased heme oxygenase (HO)-1 activity by NS-398 is responsible for protection against hypoxia-induced damage in C6 cells.	Nitrogen	68-70	heme oxygenase 1	Homo sapiens	34-55
17675106-3	2007	NS-398 increased HO-1 expression in a concentration- and time-dependent manner during both normoxia and hypoxia (95% N(2)/5% CO(2)), but the latter was much more sensitive.	Nitrogen	0-2	heme oxygenase 1	Homo sapiens	17-21
17675106-3	2007	NS-398 increased HO-1 expression in a concentration- and time-dependent manner during both normoxia and hypoxia (95% N(2)/5% CO(2)), but the latter was much more sensitive.	Nitrogen	117-121	heme oxygenase 1	Homo sapiens	17-21
17675106-3	2007	NS-398 increased HO-1 expression in a concentration- and time-dependent manner during both normoxia and hypoxia (95% N(2)/5% CO(2)), but the latter was much more sensitive.	co(2))	125-131	heme oxygenase 1	Homo sapiens	17-21
17675106-4	2007	Because induction of HO-1 occurred due to hypoxia itself, NS-398 seemed to potentiate the expression of HO-1.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	58-64	heme oxygenase 1	Homo sapiens	21-25
17675106-4	2007	Because induction of HO-1 occurred due to hypoxia itself, NS-398 seemed to potentiate the expression of HO-1.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	58-64	heme oxygenase 1	Homo sapiens	104-108
17675106-6	2007	Zinc protophorphrin (ZnPPIX), a HO-1 inhibitor, inhibited the protective effect of NS-398 against hypoxia.	zinc protophorphrin	0-19	heme oxygenase 1	Homo sapiens	32-36
17675106-6	2007	Zinc protophorphrin (ZnPPIX), a HO-1 inhibitor, inhibited the protective effect of NS-398 against hypoxia.	zinc protoporphyrin	21-27	heme oxygenase 1	Homo sapiens	32-36
17675106-6	2007	Zinc protophorphrin (ZnPPIX), a HO-1 inhibitor, inhibited the protective effect of NS-398 against hypoxia.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	83-89	heme oxygenase 1	Homo sapiens	32-36
17675106-10	2007	NS-398 increased phosphorylation of Akt, and LY-294002, a specific PI(3) kinase inhibitor, inhibited NS-398-induced HO-1 expression.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	0-6	heme oxygenase 1	Homo sapiens	116-120
17675106-10	2007	NS-398 increased phosphorylation of Akt, and LY-294002, a specific PI(3) kinase inhibitor, inhibited NS-398-induced HO-1 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	45-54	heme oxygenase 1	Homo sapiens	116-120
17675106-10	2007	NS-398 increased phosphorylation of Akt, and LY-294002, a specific PI(3) kinase inhibitor, inhibited NS-398-induced HO-1 expression.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	101-107	heme oxygenase 1	Homo sapiens	116-120
17675106-11	2007	Taken together, we conclude that therapeutic use of NS-398 in the treatment of oxidative stress-oriented neuronal disorders would be beneficial through dual actions: HO-1 induction and COX-2 inhibition.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	52-58	heme oxygenase 1	Homo sapiens	166-170
17785948-7	2007	Heme reduces heme synthesis by suppressing the expression of non-specific 5-aminolevulinate synthase (ALAS1) and stimulates heme breakdown by inducing heme oxygenase (HO)-1 expression.	Heme	0-4	heme oxygenase 1	Homo sapiens	151-172
17785948-8	2007	ALAS1 and HO-1 are the rate limiting enzymes in heme biosynthesis and catabolism, respectively.	Heme	48-52	heme oxygenase 1	Homo sapiens	10-14
17785948-9	2007	Accordingly, under the heme-rich condition, heme binds to cysteine-proline (CP) motifs of ALAS1 and those of transcriptional repressor Bach1, thereby leading to repression of mitochondrial transport of ALAS1 and induction of HO-1 transcription, respectively.	Heme	23-27	heme oxygenase 1	Homo sapiens	225-229
17785948-9	2007	Accordingly, under the heme-rich condition, heme binds to cysteine-proline (CP) motifs of ALAS1 and those of transcriptional repressor Bach1, thereby leading to repression of mitochondrial transport of ALAS1 and induction of HO-1 transcription, respectively.	cysteine-proline	58-74	heme oxygenase 1	Homo sapiens	225-229
17665394-2	2007	METHODS: In the K/BxN mouse serum transfer model, which mimics human inflammatory arthritis without lymphocyte influence, HO-1 was up-regulated by intraperitoneal injection of cobalt protoporphyrin IX (CoPP), a potent pharmacologic inducer, and was inhibited using a specific siRNA.	cobaltiprotoporphyrin	176-200	heme oxygenase 1	Homo sapiens	122-126
17520317-2	2007	A (GT)n dinucleotide repeat in HO-1 promoter is polymorphic and modulates the transcriptional activity of the gene.	Dinucleoside Phosphates	8-20	heme oxygenase 1	Homo sapiens	31-35
17665394-2	2007	METHODS: In the K/BxN mouse serum transfer model, which mimics human inflammatory arthritis without lymphocyte influence, HO-1 was up-regulated by intraperitoneal injection of cobalt protoporphyrin IX (CoPP), a potent pharmacologic inducer, and was inhibited using a specific siRNA.	cobaltiprotoporphyrin	202-206	heme oxygenase 1	Homo sapiens	122-126
17433488-0	2007	Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	87-103
17671894-14	2007	On the contrary, HO-1 is highly upregulated and it plays a very important role of antioxidation, because HO-1 generates biliverdin, which being converted to bilirubin exhibits a very potent antioxidative effect, and hence antiapoptosis in tumors.	Biliverdine	120-130	heme oxygenase 1	Homo sapiens	17-21
17671894-14	2007	On the contrary, HO-1 is highly upregulated and it plays a very important role of antioxidation, because HO-1 generates biliverdin, which being converted to bilirubin exhibits a very potent antioxidative effect, and hence antiapoptosis in tumors.	Biliverdine	120-130	heme oxygenase 1	Homo sapiens	105-109
17671894-14	2007	On the contrary, HO-1 is highly upregulated and it plays a very important role of antioxidation, because HO-1 generates biliverdin, which being converted to bilirubin exhibits a very potent antioxidative effect, and hence antiapoptosis in tumors.	Bilirubin	157-166	heme oxygenase 1	Homo sapiens	17-21
17671894-14	2007	On the contrary, HO-1 is highly upregulated and it plays a very important role of antioxidation, because HO-1 generates biliverdin, which being converted to bilirubin exhibits a very potent antioxidative effect, and hence antiapoptosis in tumors.	Bilirubin	157-166	heme oxygenase 1	Homo sapiens	105-109
17671894-15	2007	Thus this oxidation therapy, by inhibiting this HO-1 dependent antioxidant (bilirubin) formation by ZnPP, and by enhancing ROS generation, is expected to offer a powerful therapeutic modality for future anticancer therapy.	Bilirubin	76-85	heme oxygenase 1	Homo sapiens	48-52
17295091-0	2007	Heme oxygenase-1 and interleukin-11 are overexpressed in stress-induced premature senescence of human WI-38 fibroblasts induced by tert-butylhydroperoxide and ethanol.	tert-Butylhydroperoxide	131-154	heme oxygenase 1	Homo sapiens	0-16
17295091-0	2007	Heme oxygenase-1 and interleukin-11 are overexpressed in stress-induced premature senescence of human WI-38 fibroblasts induced by tert-butylhydroperoxide and ethanol.	Ethanol	159-166	heme oxygenase 1	Homo sapiens	0-16
17295091-2	2007	In the present work we found an increased mRNA and protein level of interleukin-11 and heme oxygenase-1 in premature senescence of WI-38 human diploid foetal lung fibroblasts induced by both tert-butylhydroperoxide and ethanol.	tert-Butylhydroperoxide	191-214	heme oxygenase 1	Homo sapiens	87-103
17295091-2	2007	In the present work we found an increased mRNA and protein level of interleukin-11 and heme oxygenase-1 in premature senescence of WI-38 human diploid foetal lung fibroblasts induced by both tert-butylhydroperoxide and ethanol.	Ethanol	219-226	heme oxygenase 1	Homo sapiens	87-103
17295091-3	2007	We tested whether interleukin-11 and heme oxygenase-1 could protect against tert-butylhydroperoxide- or ethanol-induced premature senescence when stable overexpression was established using a retroviral vector-based transduction.	tert-Butylhydroperoxide	76-99	heme oxygenase 1	Homo sapiens	37-53
17295091-3	2007	We tested whether interleukin-11 and heme oxygenase-1 could protect against tert-butylhydroperoxide- or ethanol-induced premature senescence when stable overexpression was established using a retroviral vector-based transduction.	Ethanol	104-111	heme oxygenase 1	Homo sapiens	37-53
17701549-2	2007	The transcription of Hmox-1 is regulated by the substrate of HO-1, heme.	Heme	67-71	heme oxygenase 1	Homo sapiens	21-27
17701549-2	2007	The transcription of Hmox-1 is regulated by the substrate of HO-1, heme.	Heme	67-71	heme oxygenase 1	Homo sapiens	61-65
17701549-3	2007	Heme induces expression of Hmox-1 in part by inhibiting the binding of Bach1 to the enhancers and inducing the nuclear export of Bach1.	Heme	0-4	heme oxygenase 1	Homo sapiens	27-33
17671894-15	2007	Thus this oxidation therapy, by inhibiting this HO-1 dependent antioxidant (bilirubin) formation by ZnPP, and by enhancing ROS generation, is expected to offer a powerful therapeutic modality for future anticancer therapy.	zinc protoporphyrin	100-104	heme oxygenase 1	Homo sapiens	48-52
17671894-15	2007	Thus this oxidation therapy, by inhibiting this HO-1 dependent antioxidant (bilirubin) formation by ZnPP, and by enhancing ROS generation, is expected to offer a powerful therapeutic modality for future anticancer therapy.	Reactive Oxygen Species	123-126	heme oxygenase 1	Homo sapiens	48-52
17433488-0	2007	Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways.	Ethanol	42-49	heme oxygenase 1	Homo sapiens	87-103
17673168-0	2007	WITHDRAWN: Heme oxygenase-1 mediates the anti-inflammatory effect of propyl gallate in LPS-stimulated macrophages.	Propyl Gallate	69-83	heme oxygenase 1	Homo sapiens	11-27
17559630-6	2007	CONCLUSION: These data suggest that heme oxygenase-1 induction plays a protective role in periodontal ligament cells against the cytotoxic and RANKL-inducing effects of H2O2, through multiple signaling pathways.	Hydrogen Peroxide	169-173	heme oxygenase 1	Homo sapiens	36-52
17559630-0	2007	Defense mechanism of heme oxygenase-1 against cytotoxic and receptor activator of nuclear factor-kappaB ligand inducing effects of hydrogen peroxide in human periodontal ligament cells.	Hydrogen Peroxide	131-148	heme oxygenase 1	Homo sapiens	21-37
17559630-1	2007	BACKGROUND AND OBJECTIVE: Although induction of heme oxygenase-1 by H2O2 has been reported, the protective role of heme oxygenase-1 against the cytotoxic and osteoclastogenic effects of H2O2 have not been elucidated in human periodontal ligament cells.	Hydrogen Peroxide	68-72	heme oxygenase 1	Homo sapiens	48-64
17559630-1	2007	BACKGROUND AND OBJECTIVE: Although induction of heme oxygenase-1 by H2O2 has been reported, the protective role of heme oxygenase-1 against the cytotoxic and osteoclastogenic effects of H2O2 have not been elucidated in human periodontal ligament cells.	Hydrogen Peroxide	186-190	heme oxygenase 1	Homo sapiens	115-131
17559630-2	2007	The aim of this work was to investigate the defense mechanism of heme oxygenase-1 on H2O2-induced cytotoxicity and to analyze the expression of receptor activator of nuclear factor-kappaB ligand (RANKL) and osteoprotegerin as markers for osteoclast differentiation in periodontal ligament cells.	Hydrogen Peroxide	85-89	heme oxygenase 1	Homo sapiens	65-81
17559630-4	2007	RESULTS: H2O2 produced a cytotoxic effect by reducing the cell viability and enhancing the expression of heme oxygenase-1 and RANKL mRNAs in a concentration- and time-dependent manner.	Hydrogen Peroxide	9-13	heme oxygenase 1	Homo sapiens	105-121
17526500-9	2007	The endogenous expression of HO-1 through ER stress-initiated ROS is believed to be as a protection signal.	Reactive Oxygen Species	62-65	heme oxygenase 1	Homo sapiens	29-33
17430897-1	2007	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is an integral membrane protein of the smooth endoplasmic reticulum.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
17420286-8	2007	Moreover, 2 Hsp32-targeting drugs, pegylated zinc protoporphyrin (PEG-ZnPP) and styrene maleic acid copolymer micelle-encapsulated ZnPP (SMA-ZnPP), were found to inhibit proliferation and to induce apoptosis in neoplastic MCs.	styrene maleic acid copolymer	80-109	heme oxygenase 1	Homo sapiens	12-17
17420286-8	2007	Moreover, 2 Hsp32-targeting drugs, pegylated zinc protoporphyrin (PEG-ZnPP) and styrene maleic acid copolymer micelle-encapsulated ZnPP (SMA-ZnPP), were found to inhibit proliferation and to induce apoptosis in neoplastic MCs.	copoly(styrene-maleic acid)-zinc protoporphyrin	137-145	heme oxygenase 1	Homo sapiens	12-17
17502383-9	2007	Finally, heme induced oxidative burst, neutrophil recruitment, and heme oxygenase-1 expression independently of TLR4.	Heme	9-13	heme oxygenase 1	Homo sapiens	67-83
17430897-1	2007	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is an integral membrane protein of the smooth endoplasmic reticulum.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
17430897-2	2007	However, we detected an HO-1 immunoreactive signal in the nucleus of cultured cells after exposure to hypoxia and heme or heme/hemopexin.	Heme	114-118	heme oxygenase 1	Homo sapiens	24-28
17430897-2	2007	However, we detected an HO-1 immunoreactive signal in the nucleus of cultured cells after exposure to hypoxia and heme or heme/hemopexin.	Heme	122-126	heme oxygenase 1	Homo sapiens	24-28
17430897-5	2007	Incubation with leptomycin B prior to hypoxia abolished nuclear HO-1 and the faster migrating band on Western analysis, suggesting that this process was facilitated by CRM1.	leptomycin B	16-28	heme oxygenase 1	Homo sapiens	64-68
17430897-9	2007	Nevertheless, nuclear HO-1 protected cells against hydrogen peroxide-mediated injury equally as well as cytoplasmic HO-1.	Hydrogen Peroxide	51-68	heme oxygenase 1	Homo sapiens	22-26
17508911-7	2007	These novel findings provide a link between the increase in HO-1 activity, with its concurrent enhanced production of carbon monoxide (CO) and bilirubin, a decrease in infiltrated CD11c(+) dendritic cells and an increase in anti-apoptotic proteins, including RSK and BcL-xL, in the interdiction of the diabetic state.	Carbon Monoxide	118-133	heme oxygenase 1	Homo sapiens	60-64
17508911-7	2007	These novel findings provide a link between the increase in HO-1 activity, with its concurrent enhanced production of carbon monoxide (CO) and bilirubin, a decrease in infiltrated CD11c(+) dendritic cells and an increase in anti-apoptotic proteins, including RSK and BcL-xL, in the interdiction of the diabetic state.	Carbon Monoxide	135-137	heme oxygenase 1	Homo sapiens	60-64
17508911-7	2007	These novel findings provide a link between the increase in HO-1 activity, with its concurrent enhanced production of carbon monoxide (CO) and bilirubin, a decrease in infiltrated CD11c(+) dendritic cells and an increase in anti-apoptotic proteins, including RSK and BcL-xL, in the interdiction of the diabetic state.	Bilirubin	143-152	heme oxygenase 1	Homo sapiens	60-64
17639610-5	2007	The levels of HO-1 showed a significant positive correlated with parameters of renal function, creatinine clearance, and renal blood flow and urine output (AUC; r = 0.8042, P = 0.03; r = 0.6028, P = 0.04; r = 0.6055, P = 0.04), demonstrating a possible protective role of this gene in this model of renal transplantation.	Creatinine	95-105	heme oxygenase 1	Homo sapiens	14-18
17627585-2	2007	When free heme concentration is increased, it results in the induction of heme oxygenase-1 (HO-1), which then breaks free heme down.	Heme	10-14	heme oxygenase 1	Homo sapiens	74-90
17627585-2	2007	When free heme concentration is increased, it results in the induction of heme oxygenase-1 (HO-1), which then breaks free heme down.	Heme	10-14	heme oxygenase 1	Homo sapiens	92-96
17627585-2	2007	When free heme concentration is increased, it results in the induction of heme oxygenase-1 (HO-1), which then breaks free heme down.	Heme	74-78	heme oxygenase 1	Homo sapiens	92-96
17349619-5	2007	The mechanisms by which salidroside protected neuron cells from oxidative stress included the induction of several antioxidant enzymes, thioredoxin, heme oxygenase-1, and peroxiredoxin-I; the downregulation of pro-apoptotic gene Bax and the upregulation of anti-apoptotic genes Bcl-2 and Bcl-X(L).	rhodioloside	24-35	heme oxygenase 1	Homo sapiens	149-165
17391667-0	2007	The alpha-methylene-gamma-butyrolactone moiety in dehydrocostus lactone is responsible for cytoprotective heme oxygenase-1 expression through activation of the nuclear factor E2-related factor 2 in HepG2 cells.	Lactones	32-39	heme oxygenase 1	Homo sapiens	106-122
17603281-7	2007	In human aortic smooth muscle cells (HASMCs), curcumin also inhibited growth triggered by TNF-alpha and increased p21(WAF1/CIP1) expression via HO-1-dependent manner.	Curcumin	46-54	heme oxygenase 1	Homo sapiens	144-148
17490617-6	2007	Binding of hemoglobin-haptoglobin complex (Hb/Hp) to CD163 resulted in significant induction of HO-1 by peripheral blood mononuclear cells after exposure to dexamethasone prior to culture.	Dexamethasone	157-170	heme oxygenase 1	Homo sapiens	96-100
17490617-9	2007	Steroid treatment was suggested to facilitate CD163-mediated endocytosis of hemoglobin to monocytes/macrophages and thereby induce acceleration of HO-1 synthesis.	Steroids	0-7	heme oxygenase 1	Homo sapiens	147-151
17416426-2	2007	Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	0-16
17449870-0	2007	Photooxidation generates biologically active phospholipids that induce heme oxygenase-1 in skin cells.	Phospholipids	45-58	heme oxygenase 1	Homo sapiens	71-87
17449870-2	2007	HO-1 enzymatic activity results in the formation of the cytoprotective metabolites CO and biliverdin.	Carbon Monoxide	83-85	heme oxygenase 1	Homo sapiens	0-4
17449870-2	2007	HO-1 enzymatic activity results in the formation of the cytoprotective metabolites CO and biliverdin.	Biliverdine	90-100	heme oxygenase 1	Homo sapiens	0-4
17449870-4	2007	Here we show that UVA-1 irradiation generates oxidized phospholipids derived from 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (PAPC) that mediate the expression of HO-1 in skin cells.	Phospholipids	55-68	heme oxygenase 1	Homo sapiens	178-182
17449870-4	2007	Here we show that UVA-1 irradiation generates oxidized phospholipids derived from 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (PAPC) that mediate the expression of HO-1 in skin cells.	1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine	82-139	heme oxygenase 1	Homo sapiens	178-182
17449870-4	2007	Here we show that UVA-1 irradiation generates oxidized phospholipids derived from 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (PAPC) that mediate the expression of HO-1 in skin cells.	PAPC	141-145	heme oxygenase 1	Homo sapiens	178-182
17449870-6	2007	Irradiation of arachidonate-containing phospholipids with UVA-1 led to formation of defined lipid oxidation products including epoxyisoprostane-phosphatidylcholine that induced HO-1 expression in dermal fibroblasts, in keratinocytes, and in a three-dimensional epidermal equivalent model.	Arachidonic Acid	15-27	heme oxygenase 1	Homo sapiens	177-181
17449870-6	2007	Irradiation of arachidonate-containing phospholipids with UVA-1 led to formation of defined lipid oxidation products including epoxyisoprostane-phosphatidylcholine that induced HO-1 expression in dermal fibroblasts, in keratinocytes, and in a three-dimensional epidermal equivalent model.	Phospholipids	39-52	heme oxygenase 1	Homo sapiens	177-181
17449870-6	2007	Irradiation of arachidonate-containing phospholipids with UVA-1 led to formation of defined lipid oxidation products including epoxyisoprostane-phosphatidylcholine that induced HO-1 expression in dermal fibroblasts, in keratinocytes, and in a three-dimensional epidermal equivalent model.	epoxyisoprostane-phosphatidylcholine	127-163	heme oxygenase 1	Homo sapiens	177-181
17449870-8	2007	Together, we present a novel mechanism of UVA-1-induced HO-1 expression that is mediated by the generation of biologically active phospholipid oxidation products.	Phospholipids	130-142	heme oxygenase 1	Homo sapiens	56-60
17511582-6	2007	After sleep in OSA patients, changes were noted in several genes involved in modulation of reactive oxygen species (ROS), including heme oxygenase 1, superoxide dismutase 1 and 2, and catalase.	Reactive Oxygen Species	91-114	heme oxygenase 1	Homo sapiens	132-148
17511582-6	2007	After sleep in OSA patients, changes were noted in several genes involved in modulation of reactive oxygen species (ROS), including heme oxygenase 1, superoxide dismutase 1 and 2, and catalase.	Reactive Oxygen Species	116-119	heme oxygenase 1	Homo sapiens	132-148
17095152-0	2007	Functional interaction between nitric oxide-induced iron homeostasis and heme oxygenase-1 in immortalized and malignant oral keratinocytes.	Nitric Oxide	31-43	heme oxygenase 1	Homo sapiens	73-89
17095152-10	2007	NO-induced cytotoxicity was also inhibited by hemin (an HO-1 agonist) and was enhanced by zinc protoporphyrin IX (an HO-1 inhibitor).	zinc protoporphyrin	90-112	heme oxygenase 1	Homo sapiens	117-121
17095152-11	2007	Based on these results, we conclude that HO-1 plays a major role in mediating cytoprotection and iron homeostasis against NO toxicity in immortalized and malignant oral keratinocytes.	Iron	97-101	heme oxygenase 1	Homo sapiens	41-45
17339115-3	2007	The imidazole-dioxolanes were all selective for the HO-1 isozyme (inducible) and exhibited substantially lower activity toward the HO-2 isozyme (constitutive).	imidazole-dioxolanes	4-24	heme oxygenase 1	Homo sapiens	52-56
17339115-4	2007	The corresponding imidazole-ketones and imidazole-alcohols showed selectivity toward HO-1 to a lesser degree than the similarly substituted imidazole-dioxolanes.	imidazole-ketones	18-35	heme oxygenase 1	Homo sapiens	85-89
17339115-4	2007	The corresponding imidazole-ketones and imidazole-alcohols showed selectivity toward HO-1 to a lesser degree than the similarly substituted imidazole-dioxolanes.	imidazole-alcohols	40-58	heme oxygenase 1	Homo sapiens	85-89
17339115-4	2007	The corresponding imidazole-ketones and imidazole-alcohols showed selectivity toward HO-1 to a lesser degree than the similarly substituted imidazole-dioxolanes.	imidazole-dioxolanes	140-160	heme oxygenase 1	Homo sapiens	85-89
17275847-0	2007	Inhibition of heme oxygenase-1 protects against tissue injury in carbon tetrachloride exposed livers.	Carbon Tetrachloride	65-85	heme oxygenase 1	Homo sapiens	14-30
17275847-2	2007	Heme oxygenase (HO-1) is an enzyme that is induced by heme as well as oxidative stress and has been reported to be involved in mediating protection against toxic liver injury.	Heme	54-58	heme oxygenase 1	Homo sapiens	16-20
17275847-3	2007	The purpose of the present study was to specify the role of HO-1 in CCl(4)-hepatotoxicity.	Carbon Tetrachloride	68-74	heme oxygenase 1	Homo sapiens	60-64
17275847-4	2007	METHODS AND RESULTS: We could demonstrate an up-regulation of HO-1 protein in CCl(4)-exposed liver tissue that reaches its maximum after 6 to 12 h, along with intrahepatic leukocyte accumulation and tissue injury.	Cefaclor	78-81	heme oxygenase 1	Homo sapiens	62-66
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	Cefaclor	77-80	heme oxygenase 1	Homo sapiens	60-64
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	Cefaclor	77-80	heme oxygenase 1	Homo sapiens	200-204
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	Cefaclor	185-188	heme oxygenase 1	Homo sapiens	60-64
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	Cefaclor	185-188	heme oxygenase 1	Homo sapiens	200-204
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	tin protoporphyrin IX	219-240	heme oxygenase 1	Homo sapiens	60-64
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	tin protoporphyrin IX	219-240	heme oxygenase 1	Homo sapiens	200-204
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	tin protoporphyrin IX	242-249	heme oxygenase 1	Homo sapiens	60-64
17275847-5	2007	When animals were pretreated with hemin for augmentation of HO-1 expression, CCl(4)-exposure was associated with a reduction of intrahepatic leukocyte accumulation, while inhibition of CCl(4)-induced HO-1 expression by tin protoporphyrin-IX (SnPP-IX) enhanced leukocytic response.	tin protoporphyrin IX	242-249	heme oxygenase 1	Homo sapiens	200-204
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Cefaclor	51-54	heme oxygenase 1	Homo sapiens	43-47
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Cefaclor	201-204	heme oxygenase 1	Homo sapiens	43-47
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Cefaclor	201-204	heme oxygenase 1	Homo sapiens	107-111
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Cefaclor	201-204	heme oxygenase 1	Homo sapiens	107-111
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Heme	253-257	heme oxygenase 1	Homo sapiens	43-47
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Heme	253-257	heme oxygenase 1	Homo sapiens	107-111
17275847-8	2007	CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity.	Heme	253-257	heme oxygenase 1	Homo sapiens	107-111
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Glutathione	30-33	heme oxygenase 1	Homo sapiens	92-108
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Glutathione	30-33	heme oxygenase 1	Homo sapiens	110-114
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Glutathione	30-33	heme oxygenase 1	Homo sapiens	268-272
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	gme	43-46	heme oxygenase 1	Homo sapiens	92-108
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	gme	43-46	heme oxygenase 1	Homo sapiens	110-114
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	gme	43-46	heme oxygenase 1	Homo sapiens	268-272
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Dopamine	56-58	heme oxygenase 1	Homo sapiens	268-272
17464197-4	2007	The inhibition was due to the induction of heme oxygenase (HO)-1 in LPS-activated macrophages, since blocking HO-1 activity with ZnPP, an HO-1 specific inhibitor, abolished hydroquinone"s NO inhibitory activity.	zinc protoporphyrin	129-133	heme oxygenase 1	Homo sapiens	43-64
17466351-9	2007	Both 3,6-BPQ and 1,6-BPQ induced oxidative stress-associated genes (HMOX1, GCLC, GCLM, and SLC7A11), phase 2 enzyme genes (NQO1, NQO2, ALDH3A1), PAH metabolizing genes (CYP1B1, EPHX1, AKR1C1), and certain EGF receptor-associated genes (EGFR, IER3, ING1, SQSTM1 and TRIM16).	benzo(a)pyrene-3,6-quinone	5-12	heme oxygenase 1	Homo sapiens	68-73
17466351-9	2007	Both 3,6-BPQ and 1,6-BPQ induced oxidative stress-associated genes (HMOX1, GCLC, GCLM, and SLC7A11), phase 2 enzyme genes (NQO1, NQO2, ALDH3A1), PAH metabolizing genes (CYP1B1, EPHX1, AKR1C1), and certain EGF receptor-associated genes (EGFR, IER3, ING1, SQSTM1 and TRIM16).	1,6-bpq	17-24	heme oxygenase 1	Homo sapiens	68-73
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Glutathione	17-28	heme oxygenase 1	Homo sapiens	92-108
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Glutathione	17-28	heme oxygenase 1	Homo sapiens	110-114
17400258-7	2007	In addition, the glutathione (GSH) analog (GME), blocks DA-induced superoxide accumulation, heme-oxygenase-1 (HO-1) expression and caspase-3 activation, and reduces cell death, while the glutathione synthetase inhibitor, buthionine sulfoximine, potentiates DA-induced HO-1 expression and cell death.	Glutathione	17-28	heme oxygenase 1	Homo sapiens	268-272
17464175-1	2007	Curcumin is a polyphenolic compound possessing interesting anti-inflammatory and antioxidant properties and has the ability to induce the defensive protein heme oxygenase-1 (HO-1).	Curcumin	0-8	heme oxygenase 1	Homo sapiens	156-172
17464175-1	2007	Curcumin is a polyphenolic compound possessing interesting anti-inflammatory and antioxidant properties and has the ability to induce the defensive protein heme oxygenase-1 (HO-1).	Curcumin	0-8	heme oxygenase 1	Homo sapiens	174-178
17464175-1	2007	Curcumin is a polyphenolic compound possessing interesting anti-inflammatory and antioxidant properties and has the ability to induce the defensive protein heme oxygenase-1 (HO-1).	polyphenolic compound	14-35	heme oxygenase 1	Homo sapiens	156-172
17464175-1	2007	Curcumin is a polyphenolic compound possessing interesting anti-inflammatory and antioxidant properties and has the ability to induce the defensive protein heme oxygenase-1 (HO-1).	polyphenolic compound	14-35	heme oxygenase 1	Homo sapiens	174-178
17464175-5	2007	In additional experiments, an inhibitor of heme oxygenase activity (tin protoporphyrin IX, 10 microM) or siRNA for HO-1 were used to investigate the participation of HO-1 as a mediator of curcumin-induced effects.	Curcumin	188-196	heme oxygenase 1	Homo sapiens	166-170
17464175-6	2007	Treatment with curcumin produced a marked induction of cardiac HO-1 in normothermic condition but cells were less responsive to the polyphenolic compound at low temperature.	Curcumin	15-23	heme oxygenase 1	Homo sapiens	63-67
17464175-8	2007	Thus, curcumin added to Celsior preservation solution effectively prevents the damage caused by cold-storage; this effect involves the protective enzyme HO-1 but also other not yet identified mechanisms.	Curcumin	6-14	heme oxygenase 1	Homo sapiens	153-157
17416426-2	2007	Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	18-22
17416426-2	2007	Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life.	Carbon Monoxide	166-168	heme oxygenase 1	Homo sapiens	0-16
17416426-2	2007	Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life.	Carbon Monoxide	166-168	heme oxygenase 1	Homo sapiens	18-22
17416426-2	2007	Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life.	Bilirubin	174-183	heme oxygenase 1	Homo sapiens	0-16
17416426-2	2007	Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life.	Bilirubin	174-183	heme oxygenase 1	Homo sapiens	18-22
17079780-4	2007	Heme oxygenase-1 expression increased dramatically in cytosolic and mitochondrial fractions of human alveolar (A549), or bronchial epithelial cells (Beas-2b) exposed to either hemin, lipopolysaccharide, or CSE.	Hemin	176-181	heme oxygenase 1	Homo sapiens	0-16
17307160-4	2007	Treatment of A549 cells with LY 294002 (2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one, a PI3K inhibitor), an Akt inhibitor, and the dominant negative mutant of Akt (Akt DN) inhibited TGF-beta1-induced HO-1 expression and HO-1-luciferase activity.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	40-88	heme oxygenase 1	Homo sapiens	204-208
17079780-10	2007	Overexpression of heme oxygenase-1 inhibited CSE-induced Beas-2b cell death and preserved cellular ATP levels.	Adenosine Triphosphate	99-102	heme oxygenase 1	Homo sapiens	18-34
17391133-2	2007	A functional dinucleotide repeat (GT)(n) polymorphism, within the HO-1 promoter, regulates gene expression; a short number of repeats (S-allele &lt;25) increases transcription.	Dinucleoside Phosphates	13-25	heme oxygenase 1	Homo sapiens	66-70
17392485-0	2007	Reduction of bilirubin by targeting human heme oxygenase-1 through siRNA.	Bilirubin	13-22	heme oxygenase 1	Homo sapiens	42-58
17219054-0	2007	Induction of heme-oxygenase 1 requires the p38MAPK and PI3K pathways and suppresses apoptotic cell death following hypericin-mediated photodynamic therapy.	hypericin	115-124	heme oxygenase 1	Homo sapiens	13-29
17219054-6	2007	Conversely, increasing HO-1 protein level by hemin prior to irradiation is cytoprotective.	Hemin	45-50	heme oxygenase 1	Homo sapiens	23-27
17219054-8	2007	Altogether these results indicate that stimulation of HO-1 expression by hypericin-PDT is a cytoprotective mechanism governed by the p38(MAPK) and PI3K pathways, likely through the control of the nuclear availability of the Nrf2 pool.	hypericin	73-82	heme oxygenase 1	Homo sapiens	54-58
17450221-7	2007	Additionally, the water-soluble fractions of UFPs were sufficient to induce the expression of F3, F2RL2, and heme oxygenase 1 (HMOX1).	Water	18-23	heme oxygenase 1	Homo sapiens	109-125
17450221-7	2007	Additionally, the water-soluble fractions of UFPs were sufficient to induce the expression of F3, F2RL2, and heme oxygenase 1 (HMOX1).	Water	18-23	heme oxygenase 1	Homo sapiens	127-132
17392485-3	2007	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme that generates bilirubin.	Bilirubin	65-74	heme oxygenase 1	Homo sapiens	0-16
17392485-3	2007	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme that generates bilirubin.	Bilirubin	65-74	heme oxygenase 1	Homo sapiens	18-22
17244614-0	2007	Cadmium-responsive element of the human heme oxygenase-1 gene mediates heat shock factor 1-dependent transcriptional activation.	Cadmium	0-7	heme oxygenase 1	Homo sapiens	40-56
17235328-0	2007	Dimethylfumarate induces immunosuppression via glutathione depletion and subsequent induction of heme oxygenase 1.	Dimethyl Fumarate	0-16	heme oxygenase 1	Homo sapiens	97-113
17235328-7	2007	Supplementation with exogenous glutathione (GSH), which is known to bind DMF, prevented both HO-1 induction as well as the anti-inflammatory effects of DMF.	Glutathione	31-42	heme oxygenase 1	Homo sapiens	93-97
17235328-7	2007	Supplementation with exogenous glutathione (GSH), which is known to bind DMF, prevented both HO-1 induction as well as the anti-inflammatory effects of DMF.	Glutathione	44-47	heme oxygenase 1	Homo sapiens	93-97
17235328-7	2007	Supplementation with exogenous glutathione (GSH), which is known to bind DMF, prevented both HO-1 induction as well as the anti-inflammatory effects of DMF.	Dimethyl Fumarate	73-76	heme oxygenase 1	Homo sapiens	93-97
17235328-9	2007	These results suggest that DMF acts as active compound within the FAE mixture and at least partially mediates its immunomodulatory activity by the induction of the anti-inflammatory stress protein HO-1 ascribed to the functional depletion of reduced GSH.	Dimethyl Fumarate	27-30	heme oxygenase 1	Homo sapiens	197-201
17235328-9	2007	These results suggest that DMF acts as active compound within the FAE mixture and at least partially mediates its immunomodulatory activity by the induction of the anti-inflammatory stress protein HO-1 ascribed to the functional depletion of reduced GSH.	Glutathione	250-253	heme oxygenase 1	Homo sapiens	197-201
17408452-8	2007	HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide.	Biliverdine	130-140	heme oxygenase 1	Homo sapiens	14-18
17408452-8	2007	HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide.	Iron	142-146	heme oxygenase 1	Homo sapiens	14-18
17408452-8	2007	HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide.	Carbon Monoxide	152-167	heme oxygenase 1	Homo sapiens	14-18
17244614-2	2007	From a comparison of heavy metal responses of several human genes, it was noted that the heme oxygenase-1 (HO-1) gene is quite similar in the spectrum of metal response and induction kinetics to the heat shock protein 70 (HSP70) gene, suggesting a common regulatory mechanism shared by these genes.	Metals	27-32	heme oxygenase 1	Homo sapiens	89-105
17244614-2	2007	From a comparison of heavy metal responses of several human genes, it was noted that the heme oxygenase-1 (HO-1) gene is quite similar in the spectrum of metal response and induction kinetics to the heat shock protein 70 (HSP70) gene, suggesting a common regulatory mechanism shared by these genes.	Metals	27-32	heme oxygenase 1	Homo sapiens	107-111
17244614-2	2007	From a comparison of heavy metal responses of several human genes, it was noted that the heme oxygenase-1 (HO-1) gene is quite similar in the spectrum of metal response and induction kinetics to the heat shock protein 70 (HSP70) gene, suggesting a common regulatory mechanism shared by these genes.	Metals	154-159	heme oxygenase 1	Homo sapiens	89-105
17244614-2	2007	From a comparison of heavy metal responses of several human genes, it was noted that the heme oxygenase-1 (HO-1) gene is quite similar in the spectrum of metal response and induction kinetics to the heat shock protein 70 (HSP70) gene, suggesting a common regulatory mechanism shared by these genes.	Metals	154-159	heme oxygenase 1	Homo sapiens	107-111
17244614-3	2007	The cadmium-responsive element (CdRE) known to be responsible for the metal regulation of ho-1 formed complexes with proteins from heavy metal-treated HeLa cells in an electrophoretic mobility shift assay (EMSA).	Cadmium	4-11	heme oxygenase 1	Homo sapiens	90-94
17244614-3	2007	The cadmium-responsive element (CdRE) known to be responsible for the metal regulation of ho-1 formed complexes with proteins from heavy metal-treated HeLa cells in an electrophoretic mobility shift assay (EMSA).	cdre	32-36	heme oxygenase 1	Homo sapiens	90-94
17244614-3	2007	The cadmium-responsive element (CdRE) known to be responsible for the metal regulation of ho-1 formed complexes with proteins from heavy metal-treated HeLa cells in an electrophoretic mobility shift assay (EMSA).	Metals	70-75	heme oxygenase 1	Homo sapiens	90-94
17244614-3	2007	The cadmium-responsive element (CdRE) known to be responsible for the metal regulation of ho-1 formed complexes with proteins from heavy metal-treated HeLa cells in an electrophoretic mobility shift assay (EMSA).	Metals	137-142	heme oxygenase 1	Homo sapiens	90-94
17320768-3	2007	In the current study, we demonstrated that transient transfection of rat astroglia with human (h)ho-1 cDNA for 3 days significantly decreased intracellular cholesterol concentrations and increased levels of four oxysterol species (measured by GC/MS) compared to untreated control cultures and HO-1-transfected cells exposed to the HO inhibitor, tin mesoporphyrin (SnMP).	Cholesterol	156-167	heme oxygenase 1	Homo sapiens	97-101
17257585-1	2007	Tin mesoporphyrin (SnMP), a competitive heme oxygenase (HO) inhibitor, also induces HO-1 mRNA and protein expression by a mechanism that is not fully understood.	tin mesoporphyrin	0-17	heme oxygenase 1	Homo sapiens	84-88
17257585-1	2007	Tin mesoporphyrin (SnMP), a competitive heme oxygenase (HO) inhibitor, also induces HO-1 mRNA and protein expression by a mechanism that is not fully understood.	tin mesoporphyrin	19-23	heme oxygenase 1	Homo sapiens	84-88
17257585-5	2007	Transfection of Bach1 shRNA in Hepa cells raised basal HO-1 expression significantly, and SnMP treatment further increased HO-1 mRNA.	tin mesoporphyrin	90-94	heme oxygenase 1	Homo sapiens	123-127
17257585-6	2007	In conclusion, SnMP induces HO-1 expression not only by de-repressing the HO-1 promoter by binding Bach1, but also by accelerating Bach1 degradation.	tin mesoporphyrin	15-19	heme oxygenase 1	Homo sapiens	28-32
17257585-6	2007	In conclusion, SnMP induces HO-1 expression not only by de-repressing the HO-1 promoter by binding Bach1, but also by accelerating Bach1 degradation.	tin mesoporphyrin	15-19	heme oxygenase 1	Homo sapiens	74-78
17339489-8	2007	The same low H(2)O(2) concentration also induced the anti-inflammatory gene coding for heme oxygenase-1 (HO-1) and IL-6.	Hydrogen Peroxide	13-21	heme oxygenase 1	Homo sapiens	87-103
17339489-8	2007	The same low H(2)O(2) concentration also induced the anti-inflammatory gene coding for heme oxygenase-1 (HO-1) and IL-6.	Hydrogen Peroxide	13-21	heme oxygenase 1	Homo sapiens	105-109
17320768-3	2007	In the current study, we demonstrated that transient transfection of rat astroglia with human (h)ho-1 cDNA for 3 days significantly decreased intracellular cholesterol concentrations and increased levels of four oxysterol species (measured by GC/MS) compared to untreated control cultures and HO-1-transfected cells exposed to the HO inhibitor, tin mesoporphyrin (SnMP).	Oxysterols	212-221	heme oxygenase 1	Homo sapiens	97-101
17320768-3	2007	In the current study, we demonstrated that transient transfection of rat astroglia with human (h)ho-1 cDNA for 3 days significantly decreased intracellular cholesterol concentrations and increased levels of four oxysterol species (measured by GC/MS) compared to untreated control cultures and HO-1-transfected cells exposed to the HO inhibitor, tin mesoporphyrin (SnMP).	tin mesoporphyrin	345-362	heme oxygenase 1	Homo sapiens	97-101
17320768-3	2007	In the current study, we demonstrated that transient transfection of rat astroglia with human (h)ho-1 cDNA for 3 days significantly decreased intracellular cholesterol concentrations and increased levels of four oxysterol species (measured by GC/MS) compared to untreated control cultures and HO-1-transfected cells exposed to the HO inhibitor, tin mesoporphyrin (SnMP).	tin mesoporphyrin	364-368	heme oxygenase 1	Homo sapiens	97-101
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	linoleoyl tyrosine	253-271	heme oxygenase 1	Homo sapiens	152-156
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	Leu-Thr	273-275	heme oxygenase 1	Homo sapiens	152-156
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	linoleoyl tyrosine cholesterol ester	278-314	heme oxygenase 1	Homo sapiens	152-156
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	ltc	316-319	heme oxygenase 1	Homo sapiens	152-156
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	linoleoyl tyrosine	278-296	heme oxygenase 1	Homo sapiens	152-156
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	deoxyguanosyl ester	344-363	heme oxygenase 1	Homo sapiens	152-156
17320768-4	2007	Relative to control preparations, oxidative stress was augmented in mitochondria (isolated by subcellular fractionation) and culture media derived from HO-1-transfected astrocytes, as evidenced by enhanced oxidation of the synthetic reporter molecules, linoleoyl tyrosine (LT), linoleoyl tyrosine cholesterol ester (LTC), or linoleoyl tyrosine deoxyguanosyl ester (LTG; measured by GC/MS and LC/MS/MS).	Lamotrigine	365-368	heme oxygenase 1	Homo sapiens	152-156
17320768-6	2007	In AD and other pathological states, glial HO-1 induction may transduce ambient noxious stimuli (e.g., beta-amyloid) into altered patterns of glial sterol metabolism which, in turn, may affect neuronal membrane turnover, survival, and adaptability.	Sterols	148-154	heme oxygenase 1	Homo sapiens	43-47
17204476-1	2007	Heme oxygenase-1 is a highly inducible gene, the product of which catalyzes breakdown of the prooxidant heme.	Heme	104-108	heme oxygenase 1	Homo sapiens	0-16
17204476-5	2007	Two mutations within HS-2 combined with a third mutation of the proximal E box abolished hemin- and cadmium-driven heme oxygenase-1 promoter activation, suggesting that these three sites synergized for maximal heme oxygenase-1 induction.	Hemin	89-94	heme oxygenase 1	Homo sapiens	115-131
17204476-5	2007	Two mutations within HS-2 combined with a third mutation of the proximal E box abolished hemin- and cadmium-driven heme oxygenase-1 promoter activation, suggesting that these three sites synergized for maximal heme oxygenase-1 induction.	Hemin	89-94	heme oxygenase 1	Homo sapiens	210-226
17204476-5	2007	Two mutations within HS-2 combined with a third mutation of the proximal E box abolished hemin- and cadmium-driven heme oxygenase-1 promoter activation, suggesting that these three sites synergized for maximal heme oxygenase-1 induction.	Cadmium	100-107	heme oxygenase 1	Homo sapiens	115-131
17204476-5	2007	Two mutations within HS-2 combined with a third mutation of the proximal E box abolished hemin- and cadmium-driven heme oxygenase-1 promoter activation, suggesting that these three sites synergized for maximal heme oxygenase-1 induction.	Cadmium	100-107	heme oxygenase 1	Homo sapiens	210-226
17160582-1	2007	Recombinant truncated human heme oxygenase-1 (hHO-1) expressed in Escherichia coli was efficiently separated and purified from feedstock by DEAE-ion exchange expanded bed adsorption.	2-diethylaminoethanol	140-144	heme oxygenase 1	Homo sapiens	28-44
17160582-1	2007	Recombinant truncated human heme oxygenase-1 (hHO-1) expressed in Escherichia coli was efficiently separated and purified from feedstock by DEAE-ion exchange expanded bed adsorption.	2-diethylaminoethanol	140-144	heme oxygenase 1	Homo sapiens	46-51
17279724-2	2007	It is known to inhibit heme-oxygenase-1 (HO-1), resulting in suppressed biliverdin/bilirubin production accompanying lowered antioxidative capacity.	Biliverdine	72-82	heme oxygenase 1	Homo sapiens	23-39
17279724-2	2007	It is known to inhibit heme-oxygenase-1 (HO-1), resulting in suppressed biliverdin/bilirubin production accompanying lowered antioxidative capacity.	Bilirubin	83-92	heme oxygenase 1	Homo sapiens	23-39
17160582-2	2007	Protocol optimization of hHO-1 on DEAE adsorbent resulted in adsorption in 0 M NaCl and elution in 150 mM NaCl at a pH of 8.5.	2-diethylaminoethanol	34-38	heme oxygenase 1	Homo sapiens	25-30
17160582-2	2007	Protocol optimization of hHO-1 on DEAE adsorbent resulted in adsorption in 0 M NaCl and elution in 150 mM NaCl at a pH of 8.5.	Sodium Chloride	79-83	heme oxygenase 1	Homo sapiens	25-30
17160582-2	2007	Protocol optimization of hHO-1 on DEAE adsorbent resulted in adsorption in 0 M NaCl and elution in 150 mM NaCl at a pH of 8.5.	Sodium Chloride	106-110	heme oxygenase 1	Homo sapiens	25-30
16924499-9	2007	After the initial increase in intracellular peroxides, the heat shock protein and antioxidant heme oxygenase-1 (HO-1) was upregulated.	Peroxides	44-53	heme oxygenase 1	Homo sapiens	94-110
16924499-9	2007	After the initial increase in intracellular peroxides, the heat shock protein and antioxidant heme oxygenase-1 (HO-1) was upregulated.	Peroxides	44-53	heme oxygenase 1	Homo sapiens	112-116
16924499-11	2007	NAC attenuated HO-1 upregulation, confirming the time course analysis.	Acetylcysteine	0-3	heme oxygenase 1	Homo sapiens	15-19
17291539-0	2007	Preconditioning with hyperbaric oxygen induces tolerance against oxidative injury via increased expression of heme oxygenase-1 in primary cultured spinal cord neurons.	Oxygen	32-38	heme oxygenase 1	Homo sapiens	110-126
17225922-9	2007	Micelle formulations prepared with ethanol/Tween40 resulted in the lowest LDH release, the highest carotenoid uptake and the lowest stress response (changes in HO-1 mRNA expression).	Ethanol	35-42	heme oxygenase 1	Homo sapiens	160-164
17225922-9	2007	Micelle formulations prepared with ethanol/Tween40 resulted in the lowest LDH release, the highest carotenoid uptake and the lowest stress response (changes in HO-1 mRNA expression).	polysorbate 40	43-50	heme oxygenase 1	Homo sapiens	160-164
17325212-3	2007	The boy was a homozygous carrier of short alleles of the heme oxygenase-1 (HO-1) gene GT dinucleotide-repeat promoter polymorphism, which is associated with increased activity and inducibility of the heme-degrading enzyme HO-1, which catalyzes the production of bilirubin.	Heme	57-61	heme oxygenase 1	Homo sapiens	75-79
17325212-3	2007	The boy was a homozygous carrier of short alleles of the heme oxygenase-1 (HO-1) gene GT dinucleotide-repeat promoter polymorphism, which is associated with increased activity and inducibility of the heme-degrading enzyme HO-1, which catalyzes the production of bilirubin.	Heme	57-61	heme oxygenase 1	Homo sapiens	222-226
17325212-3	2007	The boy was a homozygous carrier of short alleles of the heme oxygenase-1 (HO-1) gene GT dinucleotide-repeat promoter polymorphism, which is associated with increased activity and inducibility of the heme-degrading enzyme HO-1, which catalyzes the production of bilirubin.	Bilirubin	262-271	heme oxygenase 1	Homo sapiens	57-73
17325212-3	2007	The boy was a homozygous carrier of short alleles of the heme oxygenase-1 (HO-1) gene GT dinucleotide-repeat promoter polymorphism, which is associated with increased activity and inducibility of the heme-degrading enzyme HO-1, which catalyzes the production of bilirubin.	Bilirubin	262-271	heme oxygenase 1	Homo sapiens	75-79
17325212-5	2007	Because bilirubin production plays a critical role during the neonatal period, the HO-1 promoter polymorphism may be an important genetic factor for the clinical outcome of neonatal hyperbilirubinemia.	Bilirubin	8-17	heme oxygenase 1	Homo sapiens	83-87
17291539-7	2007	Treatment with tin-mesoporphyrin IX (SnMP), a specific HO-1 inhibitor, before HBO pretreatment abolished the HBO-induced adaptive protection noted in the cultured spinal neurons.	tin-mesoporphyrin ix	15-35	heme oxygenase 1	Homo sapiens	55-59
17291539-7	2007	Treatment with tin-mesoporphyrin IX (SnMP), a specific HO-1 inhibitor, before HBO pretreatment abolished the HBO-induced adaptive protection noted in the cultured spinal neurons.	tin mesoporphyrin	37-41	heme oxygenase 1	Homo sapiens	55-59
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Heme	54-58	heme oxygenase 1	Homo sapiens	72-76
16517059-0	2007	Ascorbic acid differentially modulates the induction of heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1 and glutathione S-transferase Ya by As(3+), Cd(2+) and Cr(6+).	Ascorbic Acid	0-13	heme oxygenase 1	Homo sapiens	56-72
16517059-0	2007	Ascorbic acid differentially modulates the induction of heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1 and glutathione S-transferase Ya by As(3+), Cd(2+) and Cr(6+).	Cadmium	151-153	heme oxygenase 1	Homo sapiens	56-72
16517059-0	2007	Ascorbic acid differentially modulates the induction of heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1 and glutathione S-transferase Ya by As(3+), Cd(2+) and Cr(6+).	Chromium	162-164	heme oxygenase 1	Homo sapiens	56-72
16517059-7	2007	Hence, it is tempting to speculate that AA may potentiate the therapeutic efficacy of As(3+) by enhancing the expression of HO-1, Nqo1, and Gst ya while acting as a potent antioxidant.	Arsenic(3+) ion	86-92	heme oxygenase 1	Homo sapiens	124-128
16980551-2	2007	HO-1 catalyzes the degradation of heme, a potent oxidant, into biliverdin, iron, and carbon monoxide (CO).	Biliverdine	63-73	heme oxygenase 1	Homo sapiens	0-4
16980551-2	2007	HO-1 catalyzes the degradation of heme, a potent oxidant, into biliverdin, iron, and carbon monoxide (CO).	Iron	75-79	heme oxygenase 1	Homo sapiens	0-4
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Heme	134-138	heme oxygenase 1	Homo sapiens	54-70
16980551-2	2007	HO-1 catalyzes the degradation of heme, a potent oxidant, into biliverdin, iron, and carbon monoxide (CO).	Carbon Monoxide	85-100	heme oxygenase 1	Homo sapiens	0-4
16980551-2	2007	HO-1 catalyzes the degradation of heme, a potent oxidant, into biliverdin, iron, and carbon monoxide (CO).	Carbon Monoxide	102-104	heme oxygenase 1	Homo sapiens	0-4
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Heme	134-138	heme oxygenase 1	Homo sapiens	72-76
16980551-3	2007	These downstream products of heme catabolism have recently been found to mediate the antioxidant, antiapoptotic, antiproliferative, vasodilatory, and anti-inflammatory properties of HO-1.	Heme	29-33	heme oxygenase 1	Homo sapiens	182-186
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Biliverdine	238-256	heme oxygenase 1	Homo sapiens	54-70
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Biliverdine	238-256	heme oxygenase 1	Homo sapiens	72-76
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Carbon Monoxide	258-273	heme oxygenase 1	Homo sapiens	54-70
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Carbon Monoxide	258-273	heme oxygenase 1	Homo sapiens	72-76
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Iron	279-283	heme oxygenase 1	Homo sapiens	54-70
16990612-3	2007	One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron).	Iron	279-283	heme oxygenase 1	Homo sapiens	72-76
16838348-4	2007	The aim of this study was to investigate the effects of zinc oxide-eugenol-based root canal sealer N2 and epoxy resin-based root canal sealer Topseal on the expression of HO-1 protein in cultured human gingival fibroblasts (HGFs).	Zinc Oxide	56-66	heme oxygenase 1	Homo sapiens	171-175
17018862-7	2007	Because CML cells are known to produce high levels of intracellular reactive oxygen species, overexpression of heme oxygenase-1 resulting from inhibition of Bach2 activity may contribute to their genomic instability and leukemic phenotype.	Reactive Oxygen Species	68-91	heme oxygenase 1	Homo sapiens	111-127
17258074-9	2007	CONCLUSIONS: Arsenic trioxide-induced renal toxicity is strongly associated with the increased expression of HMOX1, and the cytotoxic mechanisms of arsenic trioxide involves reactive oxygen species production as well as another pathway.	Arsenic Trioxide	13-29	heme oxygenase 1	Homo sapiens	109-114
17169865-6	2007	Interestingly, an increased expression of HO-1, a redox-sensitive stress protein, was observed in NO2-exposed NHBE cells at 24 h. Since neutrophils (PMNs) play an active role in acute lung inflammation and resultant oxidative injury, we also investigated changes in human PMN-NHBE cell interactions.	Nitrogen Dioxide	98-101	heme oxygenase 1	Homo sapiens	42-46
17229906-4	2007	Finally, current views regarding the molecular basis for heme-induced upregulation of HO-1 are discussed.	Heme	57-61	heme oxygenase 1	Homo sapiens	86-90
16838348-4	2007	The aim of this study was to investigate the effects of zinc oxide-eugenol-based root canal sealer N2 and epoxy resin-based root canal sealer Topseal on the expression of HO-1 protein in cultured human gingival fibroblasts (HGFs).	Eugenol	67-74	heme oxygenase 1	Homo sapiens	171-175
16838348-8	2007	However, BSO enhanced the N2-induced HO-1 protein level by up to twofold (p &lt; 0.05).	Nitrogen	26-28	heme oxygenase 1	Homo sapiens	37-41
17277740-15	2007	Both vitreous and TGF-beta signals increased HO-1 expression via ROS but the latter were not involved in vitreous-mediated MT expression.	Reactive Oxygen Species	65-68	heme oxygenase 1	Homo sapiens	45-49
17277740-0	2007	Vitreous induces heme oxygenase-1 expression mediated by transforming growth factor-beta and reactive oxygen species generation in human retinal pigment epithelial cells.	Reactive Oxygen Species	93-116	heme oxygenase 1	Homo sapiens	17-33
17184579-5	2007	The expression of HO-1 mRNA in PASMC was analyzed by fluorescent real-time quantitative PCR, and the proliferating cell nuclear antigen and caspase-3 were examined by immunocytochemical analysis.	pasmc	31-36	heme oxygenase 1	Homo sapiens	18-22
17277740-10	2007	Addition of inhibitors of TGF-beta signaling (SB431542 or TGF-beta-neutralizing antibodies) decreased the vitreous induction of HO-1.	4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide	46-54	heme oxygenase 1	Homo sapiens	128-132
17277740-11	2007	Several reactive oxygen species (ROS) quenchers inhibited the TGF-beta-induced or vitreous-induced elevation of HO-1 mRNA but had no effect on vitreous-mediated induction of MT expression.	Reactive Oxygen Species	8-31	heme oxygenase 1	Homo sapiens	112-116
17277740-11	2007	Several reactive oxygen species (ROS) quenchers inhibited the TGF-beta-induced or vitreous-induced elevation of HO-1 mRNA but had no effect on vitreous-mediated induction of MT expression.	Reactive Oxygen Species	33-36	heme oxygenase 1	Homo sapiens	112-116
17277740-12	2007	Inhibitors of the mitogen-activated protein kinase (p38MAPK; SB203580) and Jun N-terminal kinase (JNK; SP600125) pathways inhibited vitreous-induction of HO-1.	SB 203580	61-69	heme oxygenase 1	Homo sapiens	154-158
17277740-12	2007	Inhibitors of the mitogen-activated protein kinase (p38MAPK; SB203580) and Jun N-terminal kinase (JNK; SP600125) pathways inhibited vitreous-induction of HO-1.	pyrazolanthrone	103-111	heme oxygenase 1	Homo sapiens	154-158
17189831-6	2007	Incubation with the thiol antioxidant N-acetylcysteine strongly inhibited both the Nrf2 accumulation and the expression of Nrf2-regulated genes such as HO-1, GCLM, and SQSTM1.	Sulfhydryl Compounds	20-25	heme oxygenase 1	Homo sapiens	152-156
17189831-6	2007	Incubation with the thiol antioxidant N-acetylcysteine strongly inhibited both the Nrf2 accumulation and the expression of Nrf2-regulated genes such as HO-1, GCLM, and SQSTM1.	Acetylcysteine	38-54	heme oxygenase 1	Homo sapiens	152-156
17569214-1	2007	Curcumin possesses anti-inflammatory activity and is a potent inhibitor of reactive-oxygen-generating enzymes such as lipoxygenase/cyclooxygenase, xanthine dehydrogenase/oxidase, and inducible nitric oxide synthase (iNOS); it is an effective inducer of heme oxygenase-1.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	253-269
17196236-0	2007	Contributions of reactive oxygen species and mitogen-activated protein kinase signaling in arsenite-stimulated hemeoxygenase-1 production.	Reactive Oxygen Species	17-40	heme oxygenase 1	Homo sapiens	111-126
17184579-7	2007	Meanwhile, hypoxia induced HO-1 expression in PASMC and promoted CO production from PASMC, which inhibited PASMC proliferation and regulated PASMC apoptosis.	pasmc	46-51	heme oxygenase 1	Homo sapiens	27-31
17184579-8	2007	NO upregulated the expression of HO-1 mRNA in hypoxic PASMC; NO also inhibited proliferation and promoted apoptosis of hypoxic PASMC, possibly by regulating the production of CO.	pasmc	54-59	heme oxygenase 1	Homo sapiens	33-37
17569214-1	2007	Curcumin possesses anti-inflammatory activity and is a potent inhibitor of reactive-oxygen-generating enzymes such as lipoxygenase/cyclooxygenase, xanthine dehydrogenase/oxidase, and inducible nitric oxide synthase (iNOS); it is an effective inducer of heme oxygenase-1.	reactive-oxygen	75-90	heme oxygenase 1	Homo sapiens	253-269
17184579-8	2007	NO upregulated the expression of HO-1 mRNA in hypoxic PASMC; NO also inhibited proliferation and promoted apoptosis of hypoxic PASMC, possibly by regulating the production of CO.	pasmc	127-132	heme oxygenase 1	Homo sapiens	33-37
17264037-10	2007	This oxygen species may induce redox-sensitive gene transcription such as HO-1.	Oxygen	5-11	heme oxygenase 1	Homo sapiens	74-78
17265967-6	2007	Vanadium oxide leads to an induction of heme oxygenase 1 (HO-1) in a dose dependent manner in ECV304 cells whereas a reduction in protein levels can be observed for the epithelial cells (A549).	vanadium pentoxide	0-14	heme oxygenase 1	Homo sapiens	40-56
17245120-5	2007	This combined with experimental data showing anti-atherosclerotic properties of the enzyme heme oxygenase-1 encouraged us to hypothesize that bilirubin and its precursor biliverdin, would act to ameliorate components of atherosclerosis, in a manner similar to what has been shown with HO-1.	Bilirubin	142-151	heme oxygenase 1	Homo sapiens	91-107
17245120-5	2007	This combined with experimental data showing anti-atherosclerotic properties of the enzyme heme oxygenase-1 encouraged us to hypothesize that bilirubin and its precursor biliverdin, would act to ameliorate components of atherosclerosis, in a manner similar to what has been shown with HO-1.	Biliverdine	170-180	heme oxygenase 1	Homo sapiens	91-107
17115887-9	2007	Among these, the heme oxygenase-1/carbon monoxide system has emerged as a major intracellular antiapoptotic mechanism.	Carbon Monoxide	34-49	heme oxygenase 1	Homo sapiens	17-33
17095719-4	2007	Three genes involved in iron-heme homeostasis, CD163, HO-1, and transferrin receptor, were further analyzed in 40 independent plaques.	Iron	24-28	heme oxygenase 1	Homo sapiens	54-84
17095719-6	2007	The expression of HO-1 and CD163 correlated with tissue iron content but iron itself was not associated with the symptom status.	Iron	56-60	heme oxygenase 1	Homo sapiens	18-22
17265967-6	2007	Vanadium oxide leads to an induction of heme oxygenase 1 (HO-1) in a dose dependent manner in ECV304 cells whereas a reduction in protein levels can be observed for the epithelial cells (A549).	vanadium pentoxide	0-14	heme oxygenase 1	Homo sapiens	58-62
17143561-0	2007	Curcumin induces heme oxygenase 1 through generation of reactive oxygen species, p38 activation and phosphatase inhibition.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	17-33
17141778-8	2007	The nitric oxide (NO) donor-SNP ameliorates LPS-induced ALI, which may be related to the induction of HO-1 and the subsequent inhibition of iNOS.	Nitric Oxide	4-16	heme oxygenase 1	Homo sapiens	102-106
17143561-0	2007	Curcumin induces heme oxygenase 1 through generation of reactive oxygen species, p38 activation and phosphatase inhibition.	Reactive Oxygen Species	56-79	heme oxygenase 1	Homo sapiens	17-33
17143561-1	2007	Curcumin is a naturally occurring compound which is known to induce heme oxygenase 1 (HO-1), although the underlying mechanism has not been fully elucidated.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	68-84
17143561-1	2007	Curcumin is a naturally occurring compound which is known to induce heme oxygenase 1 (HO-1), although the underlying mechanism has not been fully elucidated.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	86-90
17143561-2	2007	This study investigates in detail the mechanism of HO-1 induction by curcumin in human hepatoma cells.	Curcumin	69-77	heme oxygenase 1	Homo sapiens	51-55
17143561-4	2007	Curcumin was found to induce HO-1 at doses of 10 to 25 microM.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	29-33
17143561-5	2007	At both non-toxic and toxic doses, HO-1 induction was found to correlate with production of reactive oxygen species (ROS), suggesting a causative relationship.	Reactive Oxygen Species	92-115	heme oxygenase 1	Homo sapiens	35-39
17143561-5	2007	At both non-toxic and toxic doses, HO-1 induction was found to correlate with production of reactive oxygen species (ROS), suggesting a causative relationship.	Reactive Oxygen Species	117-120	heme oxygenase 1	Homo sapiens	35-39
17143561-6	2007	This was reinforced by the finding that pretreatment with the antioxidants N-acetylcysteine, vitamin E and catalase prevented HO-1 induction by curcumin.	Acetylcysteine	75-91	heme oxygenase 1	Homo sapiens	126-130
17143561-6	2007	This was reinforced by the finding that pretreatment with the antioxidants N-acetylcysteine, vitamin E and catalase prevented HO-1 induction by curcumin.	Vitamin E	93-102	heme oxygenase 1	Homo sapiens	126-130
17143561-6	2007	This was reinforced by the finding that pretreatment with the antioxidants N-acetylcysteine, vitamin E and catalase prevented HO-1 induction by curcumin.	Curcumin	144-152	heme oxygenase 1	Homo sapiens	126-130
17143561-10	2007	A panel of kinase inhibitors was used to examine the contribution of MAP kinases to the induction of HO-1 by curcumin.	Curcumin	109-117	heme oxygenase 1	Homo sapiens	101-105
17143561-13	2007	In conclusion, curcumin treatment results in ROS generation, activation of Nrf2 and MAP kinases and the inhibition of phosphatase activity in hepatocytes, and when curcumin is not administered in toxic doses, these multiple pathways converge to induce HO-1.	Curcumin	15-23	heme oxygenase 1	Homo sapiens	252-256
17191021-9	2007	Moreover, while hemoxygenase-1 (HO-1) expression was induced by resveratrol in human umbilical vein endothelial cells, neither treatment with the HO-1 inhibitor tin-protoporphyrin IX nor siRNA-directed knockdown of HO-1 had any effect on the inhibition of MCP-1 mRNA or protein secretion by resveratrol.	Resveratrol	64-75	heme oxygenase 1	Homo sapiens	16-36
17825497-2	2007	One form of this of this enzyme, heme oxygenase-1, is inducible by numerous agents which promote oxidative stress, and is now known to provide important antioxidant protection, as demonstrated in many rodent models of free radical-mediated pathogenesis, and suggested by epidemiology observing favorable health outcomes in individuals carrying high-expression alleles of the HO-1 gene.	Free Radicals	218-230	heme oxygenase 1	Homo sapiens	33-49
17018578-0	2007	Motexafin gadolinium-induced cell death correlates with heme oxygenase-1 expression and inhibition of P450 reductase-dependent activities.	Motexafin	0-9	heme oxygenase 1	Homo sapiens	56-72
18274635-5	2007	The results show that production of both NO and HO-1 is fairly dose dependent but is particularly elevated using human plasma after transient exposure to a medium ozone concentration.	Ozone	163-168	heme oxygenase 1	Homo sapiens	48-52
17018578-0	2007	Motexafin gadolinium-induced cell death correlates with heme oxygenase-1 expression and inhibition of P450 reductase-dependent activities.	Gadolinium	10-20	heme oxygenase 1	Homo sapiens	56-72
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Heme	39-43	heme oxygenase 1	Homo sapiens	0-16
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Heme	39-43	heme oxygenase 1	Homo sapiens	18-21
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Biliverdine	47-57	heme oxygenase 1	Homo sapiens	0-16
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Biliverdine	47-57	heme oxygenase 1	Homo sapiens	18-21
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Carbon Monoxide	59-61	heme oxygenase 1	Homo sapiens	0-16
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Carbon Monoxide	59-61	heme oxygenase 1	Homo sapiens	18-21
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Iron	72-76	heme oxygenase 1	Homo sapiens	0-16
17018578-1	2007	Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic.	Iron	72-76	heme oxygenase 1	Homo sapiens	18-21
17018578-5	2007	MGd used in combination with tin protoporphyrin IX, an inhibitor of HO1, resulted in synergistic cell killing.	tin protoporphyrin IX	29-50	heme oxygenase 1	Homo sapiens	68-71
17018578-7	2007	We demonstrate that inhibition of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, that results in diversion of reducing equivalents from heme oxidation to oxygen reduction.	Heme	190-194	heme oxygenase 1	Homo sapiens	34-37
17018578-7	2007	We demonstrate that inhibition of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, that results in diversion of reducing equivalents from heme oxidation to oxygen reduction.	Heme	190-194	heme oxygenase 1	Homo sapiens	130-133
17018578-7	2007	We demonstrate that inhibition of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, that results in diversion of reducing equivalents from heme oxidation to oxygen reduction.	Oxygen	208-214	heme oxygenase 1	Homo sapiens	34-37
17108707-6	2007	Interestingly, pre-induction of heme oxygenase (HO)-1 by hemin prevented dialysis membrane-induced monocyte apoptosis, whereas inhibition of HO-1 activity (treatment with tin protoporphyrin, SN-P) enhanced dialysis membrane-induced monocyte apoptosis.	protoporphyrin IX	175-189	heme oxygenase 1	Homo sapiens	141-145
17018578-7	2007	We demonstrate that inhibition of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, that results in diversion of reducing equivalents from heme oxidation to oxygen reduction.	Oxygen	208-214	heme oxygenase 1	Homo sapiens	130-133
17942419-4	2007	HMOX1 induction, elicited by arsenite-mediated oxidative stress, follows inactivation of BACH1 and precedes activation of NRF2.	arsenite	29-37	heme oxygenase 1	Homo sapiens	0-5
17122584-1	2006	BACKGROUND: The volatile anesthetic isoflurane induces hypoxia inducible factor (HIF)-1-responsive genes heme oxygenase 1, inducible nitric oxide synthase, and vascular endothelial growth factor (VEGF) expression.	Isoflurane	36-46	heme oxygenase 1	Homo sapiens	105-154
17122584-10	2006	Isoflurane stimulated heme oxygenase 1, inducible nitric oxide synthase, and VEGF mRNA expression in a concentration-dependent manner, and inactivation of HIF-1alpha attenuated the induction of VEGF mRNA by isoflurane.	Isoflurane	0-10	heme oxygenase 1	Homo sapiens	22-71
17122584-11	2006	CONCLUSION: Isoflurane can up-regulate HIF-1alpha and enhance HIF-1-responsive genes heme oxygenase 1, inducible nitric oxide synthase, and VEGF mRNA expression in Hep3B cells.	Isoflurane	12-22	heme oxygenase 1	Homo sapiens	85-134
17156779-9	2006	Treatment with CdCl(2) (to induce haem oxygenase, HO-1) enhanced HCP1 expression and increased haem uptake into the cells.	Cadmium Chloride	15-22	heme oxygenase 1	Homo sapiens	50-54
16881871-2	2006	We have previously shown that PDTC (pyrrolidine dithiocarbamate), an HO-1 (haem oxygenase-1) donor, improves intestinal microvascular perfusion.	pyrrolidine dithiocarbamic acid	30-34	heme oxygenase 1	Homo sapiens	69-73
17384282-2	2006	15-Deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2), an endogenous ligand of peroxisome proliferator-activated receptor (PPAR) gamma, has been reported to upregulate VEGF synthesis through the induction of heme oxygenase (HO)-1.	14-prostaglandin j2	17-36	heme oxygenase 1	Homo sapiens	202-223
17384282-2	2006	15-Deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2), an endogenous ligand of peroxisome proliferator-activated receptor (PPAR) gamma, has been reported to upregulate VEGF synthesis through the induction of heme oxygenase (HO)-1.	15-deoxy-delta(12,14)-prostaglandin J2	38-46	heme oxygenase 1	Homo sapiens	202-223
17384282-3	2006	In this work, we found that treatment of human breast cancer (MCF-7) cells with 15d-PGJ2 led to time-dependent increases in the expression of HO-1.	15-deoxy-delta(12,14)-prostaglandin J2	80-88	heme oxygenase 1	Homo sapiens	142-146
17384282-6	2006	The induction of HO-1 expression preceded the upregulation of VEGF in MCF-7 cells stimulated with 15d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	98-106	heme oxygenase 1	Homo sapiens	17-21
17384282-8	2006	To determine whether the induction of HO-1 is responsible for ERK1/2 activation, the HO-1 inhibitor, zinc protoporphyrin (ZnPP) was used.	zinc protoporphyrin	101-120	heme oxygenase 1	Homo sapiens	38-42
17384282-10	2006	These results suggest that 15d-PGJ2 upregulates VEGF expression via induction of HO-1 and ERK-1 and -2 phosphorylation, which may contribute to increased angiogenesis of the tumor cells.	15-deoxy-delta(12,14)-prostaglandin J2	27-35	heme oxygenase 1	Homo sapiens	81-85
16881871-2	2006	We have previously shown that PDTC (pyrrolidine dithiocarbamate), an HO-1 (haem oxygenase-1) donor, improves intestinal microvascular perfusion.	pyrrolidine dithiocarbamic acid	30-34	heme oxygenase 1	Homo sapiens	75-91
16881871-2	2006	We have previously shown that PDTC (pyrrolidine dithiocarbamate), an HO-1 (haem oxygenase-1) donor, improves intestinal microvascular perfusion.	pyrrolidine dithiocarbamic acid	36-63	heme oxygenase 1	Homo sapiens	69-73
16881871-2	2006	We have previously shown that PDTC (pyrrolidine dithiocarbamate), an HO-1 (haem oxygenase-1) donor, improves intestinal microvascular perfusion.	pyrrolidine dithiocarbamic acid	36-63	heme oxygenase 1	Homo sapiens	75-91
17020887-0	2006	Resistance to nitric oxide-induced necrosis in heme oxygenase-1 overexpressing pulmonary epithelial cells associated with decreased lipid peroxidation.	Nitric Oxide	14-26	heme oxygenase 1	Homo sapiens	47-63
17065227-0	2006	Role of Bach1 and Nrf2 in up-regulation of the heme oxygenase-1 gene by cobalt protoporphyrin.	cobaltiprotoporphyrin	72-93	heme oxygenase 1	Homo sapiens	47-63
17168739-5	2006	Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1).	Iron	115-119	heme oxygenase 1	Homo sapiens	240-256
17168739-5	2006	Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1).	Iron	115-119	heme oxygenase 1	Homo sapiens	258-262
17168739-5	2006	Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1).	Iron	202-206	heme oxygenase 1	Homo sapiens	240-256
17168739-5	2006	Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1).	Iron	202-206	heme oxygenase 1	Homo sapiens	258-262
17020887-4	2006	Compared with the Neo control, the HO-1-overexpressing cells also showed significantly less lipid peroxide formation and decreased perturbation of transition metal oxidation and coordination states following a cytotoxic NO exposure.	neo	18-21	heme oxygenase 1	Homo sapiens	35-39
17020887-4	2006	Compared with the Neo control, the HO-1-overexpressing cells also showed significantly less lipid peroxide formation and decreased perturbation of transition metal oxidation and coordination states following a cytotoxic NO exposure.	Lipid Peroxides	92-106	heme oxygenase 1	Homo sapiens	35-39
17020887-4	2006	Compared with the Neo control, the HO-1-overexpressing cells also showed significantly less lipid peroxide formation and decreased perturbation of transition metal oxidation and coordination states following a cytotoxic NO exposure.	Metals	158-163	heme oxygenase 1	Homo sapiens	35-39
17020887-5	2006	These effects were blocked by the HO-1 inhibitors Zn- and Sn-protoporphyrin IX.	Zinc	50-52	heme oxygenase 1	Homo sapiens	34-38
16972258-0	2006	N-(4-hydroxyphenyl)retinamide induces apoptosis in human retinal pigment epithelial cells: retinoic acid receptors regulate apoptosis, reactive oxygen species generation, and the expression of heme oxygenase-1 and Gadd153.	Fenretinide	0-29	heme oxygenase 1	Homo sapiens	193-209
17020887-5	2006	These effects were blocked by the HO-1 inhibitors Zn- and Sn-protoporphyrin IX.	Tin complex of Protoporphyrin-IX	58-78	heme oxygenase 1	Homo sapiens	34-38
16972258-7	2006	In addition, the increase in the expression of heme oxygenase-1 (HO-1), a stress response protein, and the growth arrest and DNA damage-inducible transcription factor 153 (Gadd153) in response to the ROS generation were also blocked by these receptor antagonists.	Reactive Oxygen Species	200-203	heme oxygenase 1	Homo sapiens	47-63
17020887-7	2006	While increased HO-1 activity prevented NO-induced fluctuations in transition metal homeostasis, addition of an iron chelator decreased NO toxicity only slightly.	Metals	78-83	heme oxygenase 1	Homo sapiens	16-20
17020887-8	2006	Our results indicate that lipid peroxidation is a significant cause of NO-induced necrosis in human lung epithelial cells, and that the increased NO survival of L1 cells is due at least in part to decreased lipid peroxidation mediated by HO-1-generated biliverdin or bilirubin.	Biliverdine	253-263	heme oxygenase 1	Homo sapiens	238-242
17020887-8	2006	Our results indicate that lipid peroxidation is a significant cause of NO-induced necrosis in human lung epithelial cells, and that the increased NO survival of L1 cells is due at least in part to decreased lipid peroxidation mediated by HO-1-generated biliverdin or bilirubin.	Bilirubin	267-276	heme oxygenase 1	Homo sapiens	238-242
17027882-6	2006	According to our data, sodium nitroprusside (SNP) increased HO-1 expression in a concentration dependent manner.	Nitroprusside	23-43	heme oxygenase 1	Homo sapiens	60-64
17199800-0	2006	Carnitine"S protective effect on oxidative stress is mediated by heme oxygenase-1.	Carnitine	0-9	heme oxygenase 1	Homo sapiens	65-81
17138185-0	2006	Heme oxygenase-1 mediates cytoprotection against nitric oxide-induced cytotoxicity via the cGMP pathway in human pulp cells.	Nitric Oxide	49-61	heme oxygenase 1	Homo sapiens	0-16
17138185-0	2006	Heme oxygenase-1 mediates cytoprotection against nitric oxide-induced cytotoxicity via the cGMP pathway in human pulp cells.	Cyclic GMP	91-95	heme oxygenase 1	Homo sapiens	0-16
17138185-1	2006	OBJECTIVE: This study examined the effects of exogenous nitric oxide (NO) on human pulp cells and the involvement of cyclic 3",5"-monophosphate (cGMP) in pulpal protection induced by heme oxygenase-1 (HO-1) against NO-induced cytotoxicity.	cyclic 3",5"-monophosphate	117-143	heme oxygenase 1	Homo sapiens	183-199
17138185-1	2006	OBJECTIVE: This study examined the effects of exogenous nitric oxide (NO) on human pulp cells and the involvement of cyclic 3",5"-monophosphate (cGMP) in pulpal protection induced by heme oxygenase-1 (HO-1) against NO-induced cytotoxicity.	cyclic 3",5"-monophosphate	117-143	heme oxygenase 1	Homo sapiens	201-205
17138185-1	2006	OBJECTIVE: This study examined the effects of exogenous nitric oxide (NO) on human pulp cells and the involvement of cyclic 3",5"-monophosphate (cGMP) in pulpal protection induced by heme oxygenase-1 (HO-1) against NO-induced cytotoxicity.	Cyclic GMP	145-149	heme oxygenase 1	Homo sapiens	183-199
17138185-2	2006	STUDY DESIGN: This study investigated cytotoxicity and HO-1 induction in pulp cells induced by the NO donor S-nitroso-N-acetyl-D,L-penicillamine (SNAP), by using Western blotting and a cell viability assay.	snap	108-144	heme oxygenase 1	Homo sapiens	55-59
17138185-4	2006	RESULTS: S-nitroso-N-acetyl-D,L-penicillamine decreased cell viability, but increased HO-1 expression in a concentration- and time-dependent manner in human pulp cells.	snap	9-45	heme oxygenase 1	Homo sapiens	86-90
17138185-5	2006	NO-induced cytotoxicity was inhibited in the presence of hemin (inducer of HO-1), whereas it was enhanced in the presence of zinc protoporphyrin IX (ZnPP IX, HO-1 inhibitor); therefore, the NO-induced cytotoxicity was correlated with HO-1 expression.	zinc protoporphyrin	125-147	heme oxygenase 1	Homo sapiens	158-162
17138185-5	2006	NO-induced cytotoxicity was inhibited in the presence of hemin (inducer of HO-1), whereas it was enhanced in the presence of zinc protoporphyrin IX (ZnPP IX, HO-1 inhibitor); therefore, the NO-induced cytotoxicity was correlated with HO-1 expression.	zinc protoporphyrin	125-147	heme oxygenase 1	Homo sapiens	158-162
17138185-6	2006	Pretreatment with a membrane-permeable cGMP analog, 8-bromo-cGMP, restored cell death and enhanced the HO-1 protein expression induced by SNAP.	Cyclic GMP	39-43	heme oxygenase 1	Homo sapiens	103-107
17138185-6	2006	Pretreatment with a membrane-permeable cGMP analog, 8-bromo-cGMP, restored cell death and enhanced the HO-1 protein expression induced by SNAP.	8-bromocyclic GMP	52-64	heme oxygenase 1	Homo sapiens	103-107
17138185-8	2006	CONCLUSION: These findings of a link between HO-1, regulated via the cGMP system and NO-induced cytotoxicity in human pulp cells, suggest a protective role for HO-1 in pulpal inflammation.	Cyclic GMP	69-73	heme oxygenase 1	Homo sapiens	45-49
17138185-8	2006	CONCLUSION: These findings of a link between HO-1, regulated via the cGMP system and NO-induced cytotoxicity in human pulp cells, suggest a protective role for HO-1 in pulpal inflammation.	Cyclic GMP	69-73	heme oxygenase 1	Homo sapiens	160-164
17027882-7	2006	Preconditioning with low concentration SNP (0.3mM) inhibited subsequent high concentration SNP (1.5mM)-induced apoptosis, and this effect was reversed by the HO-1 inhibitor SnPP.	S-Nitroso-N-propionyl-D,L-penicillamine	173-177	heme oxygenase 1	Homo sapiens	158-162
16950787-7	2006	Because we observed notably high levels of phosphorylated protein kinase C alpha and its suppression by EGCG and deferoxamine (an iron chelator), a possible mechanism involving phosphorylated protein kinase C alpha and iron in Nrf2-HO-1 activation was further investigated.	Iron	219-223	heme oxygenase 1	Homo sapiens	232-236
16950787-8	2006	Collectively, our findings suggest that Nrf2-mediated HO-1 overexpression confers resistance to apoptosis induction by EGCG; therefore, its inactivation may be a target for overcoming the resistance to chemoprevention and chemotherapy.	epigallocatechin gallate	119-123	heme oxygenase 1	Homo sapiens	54-58
17049479-6	2006	Oxidised LDL treatment also increased the expression of the antioxidant stress protein heme oxygenase-1 in macrophages; however, this increase was markedly attenuated by ascorbate pretreatment.	Ascorbic Acid	170-179	heme oxygenase 1	Homo sapiens	87-103
16950787-0	2006	Constitutive overexpression of Nrf2-dependent heme oxygenase-1 in A549 cells contributes to resistance to apoptosis induced by epigallocatechin 3-gallate.	epigallocatechin gallate	127-153	heme oxygenase 1	Homo sapiens	46-62
16950787-4	2006	Because we found that A549 cells constitutively overexpress HO-1 and its associated transcription factor Nrf2, we tested an hypothesis that EGCG resistance in these cells may be linked with Nrf2-mediated HO-1 overexpression.	epigallocatechin gallate	140-144	heme oxygenase 1	Homo sapiens	60-64
16950787-4	2006	Because we found that A549 cells constitutively overexpress HO-1 and its associated transcription factor Nrf2, we tested an hypothesis that EGCG resistance in these cells may be linked with Nrf2-mediated HO-1 overexpression.	epigallocatechin gallate	140-144	heme oxygenase 1	Homo sapiens	204-208
16950787-5	2006	HO-1 inhibition with tin-protoporphyrin IX and silencing with RNA interference rendered cells more sensitive to apoptosis induction by EGCG and classical prooxidants.	tin protoporphyrin IX	21-42	heme oxygenase 1	Homo sapiens	0-4
16950787-5	2006	HO-1 inhibition with tin-protoporphyrin IX and silencing with RNA interference rendered cells more sensitive to apoptosis induction by EGCG and classical prooxidants.	epigallocatechin gallate	135-139	heme oxygenase 1	Homo sapiens	0-4
16950787-6	2006	Interestingly, EGCG at high concentration (&gt;200 microm) induced apoptosis by suppressing expression of HO-1 protein and mRNA, and this effect correlated with a decrease in both Nrf2-ARE binding and HO-1-ARE-luciferase activity, suggesting Nrf2-driven transcriptional activation of ho-1.	epigallocatechin gallate	15-19	heme oxygenase 1	Homo sapiens	106-110
16950787-6	2006	Interestingly, EGCG at high concentration (&gt;200 microm) induced apoptosis by suppressing expression of HO-1 protein and mRNA, and this effect correlated with a decrease in both Nrf2-ARE binding and HO-1-ARE-luciferase activity, suggesting Nrf2-driven transcriptional activation of ho-1.	epigallocatechin gallate	15-19	heme oxygenase 1	Homo sapiens	201-205
16950787-6	2006	Interestingly, EGCG at high concentration (&gt;200 microm) induced apoptosis by suppressing expression of HO-1 protein and mRNA, and this effect correlated with a decrease in both Nrf2-ARE binding and HO-1-ARE-luciferase activity, suggesting Nrf2-driven transcriptional activation of ho-1.	epigallocatechin gallate	15-19	heme oxygenase 1	Homo sapiens	284-288
16950787-7	2006	Because we observed notably high levels of phosphorylated protein kinase C alpha and its suppression by EGCG and deferoxamine (an iron chelator), a possible mechanism involving phosphorylated protein kinase C alpha and iron in Nrf2-HO-1 activation was further investigated.	epigallocatechin gallate	104-108	heme oxygenase 1	Homo sapiens	232-236
16950787-7	2006	Because we observed notably high levels of phosphorylated protein kinase C alpha and its suppression by EGCG and deferoxamine (an iron chelator), a possible mechanism involving phosphorylated protein kinase C alpha and iron in Nrf2-HO-1 activation was further investigated.	Deferoxamine	113-125	heme oxygenase 1	Homo sapiens	232-236
16950787-7	2006	Because we observed notably high levels of phosphorylated protein kinase C alpha and its suppression by EGCG and deferoxamine (an iron chelator), a possible mechanism involving phosphorylated protein kinase C alpha and iron in Nrf2-HO-1 activation was further investigated.	Iron	130-134	heme oxygenase 1	Homo sapiens	232-236
16982957-3	2006	In human microvascular endothelial cells, the NO donor DETA-NONOate (0.1 to 1 mmol/L) strongly induced expression of heme oxygenase-1 but not Cu/Zn superoxide dismutase.	2,2'-(hydroxynitrosohydrazono)bis-ethanamine	55-67	heme oxygenase 1	Homo sapiens	117-133
17140381-0	2006	Changes in expression of genes encoding antioxidant enzymes, heme oxygenase-1, Bcl-2, and Bcl-xl and in level of reactive oxygen species in tumor cells resistant to doxorubicin.	Doxorubicin	165-176	heme oxygenase 1	Homo sapiens	61-77
17140381-1	2006	The relationship between expression of genes encoding key antioxidant enzymes, heme oxygenase-1, Bcl-2, and Bcl-xl and change in production of reactive oxygen species (ROS) resulting from development of resistance of cancer cells K562, MCF-7, and SKOV-3 to the prooxidant chemotherapeutic agent doxorubicin (DOX) has been studied.	Reactive Oxygen Species	143-166	heme oxygenase 1	Homo sapiens	79-95
17140381-1	2006	The relationship between expression of genes encoding key antioxidant enzymes, heme oxygenase-1, Bcl-2, and Bcl-xl and change in production of reactive oxygen species (ROS) resulting from development of resistance of cancer cells K562, MCF-7, and SKOV-3 to the prooxidant chemotherapeutic agent doxorubicin (DOX) has been studied.	Reactive Oxygen Species	168-171	heme oxygenase 1	Homo sapiens	79-95
16999951-6	2006	RESULTS: HO-1 expression and activity (5.3+/-2.1 nmol bilirubin/mg protein/h) were only present in ECs from advanced atherosclerotic lesions.	Bilirubin	54-63	heme oxygenase 1	Homo sapiens	9-13
16982957-4	2006	This was associated with a reduction of the superoxide-generating capacity of NADPH oxidase, an effect that depended on de novo gene transcription and heme oxygenase-1 activity.	Superoxides	44-54	heme oxygenase 1	Homo sapiens	151-167
16982957-6	2006	DETA-NONOate alone had little effect on TNF-stimulated reactive oxygen species, but it enhanced the TNF response when: (1) heme oxygenase-1 expression was blocked with specific small-interfering RNA; (2) heme oxygenase-1 activity was blocked by zinc-protoporphyrin; or (3) NADPH oxidase activity was blocked by diphenyleneiodonium.	2,2'-(hydroxynitrosohydrazono)bis-ethanamine	0-12	heme oxygenase 1	Homo sapiens	123-139
16982957-6	2006	DETA-NONOate alone had little effect on TNF-stimulated reactive oxygen species, but it enhanced the TNF response when: (1) heme oxygenase-1 expression was blocked with specific small-interfering RNA; (2) heme oxygenase-1 activity was blocked by zinc-protoporphyrin; or (3) NADPH oxidase activity was blocked by diphenyleneiodonium.	2,2'-(hydroxynitrosohydrazono)bis-ethanamine	0-12	heme oxygenase 1	Homo sapiens	204-220
16982957-6	2006	DETA-NONOate alone had little effect on TNF-stimulated reactive oxygen species, but it enhanced the TNF response when: (1) heme oxygenase-1 expression was blocked with specific small-interfering RNA; (2) heme oxygenase-1 activity was blocked by zinc-protoporphyrin; or (3) NADPH oxidase activity was blocked by diphenyleneiodonium.	zinc protoporphyrin	245-264	heme oxygenase 1	Homo sapiens	204-220
16982957-6	2006	DETA-NONOate alone had little effect on TNF-stimulated reactive oxygen species, but it enhanced the TNF response when: (1) heme oxygenase-1 expression was blocked with specific small-interfering RNA; (2) heme oxygenase-1 activity was blocked by zinc-protoporphyrin; or (3) NADPH oxidase activity was blocked by diphenyleneiodonium.	diphenyleneiodonium	311-330	heme oxygenase 1	Homo sapiens	204-220
16982957-7	2006	Moreover, the heme oxygenase-1 end product bilirubin directly inhibited fully functional NADPH oxidase and seemed to interrupt the assembly and activation of the oxidase.	Bilirubin	43-52	heme oxygenase 1	Homo sapiens	14-30
16982957-8	2006	In conclusion, NO may modulate superoxide production by NADPH oxidase in human vascular endothelial cells, at least partly by inducing heme oxygenase-1.	Superoxides	31-41	heme oxygenase 1	Homo sapiens	135-151
16982957-9	2006	Our results indicate that suppression of NADPH oxidase-dependent reactive oxygen species formation may represent a novel mechanism underlying the cardiovascular protective actions of heme oxygenase-1 and bilirubin.	Reactive Oxygen Species	65-88	heme oxygenase 1	Homo sapiens	183-199
17048120-5	2006	Whereas BHA failed to induce HO-1 in wild-type and Nrf2 knock-out MFs, tBHQ strongly induced HO-1 in wild-type, but not in Nrf2 knock-out MFs.	2-tert-butylhydroquinone	71-75	heme oxygenase 1	Homo sapiens	93-97
17099512-9	2006	Inhibition of HO-1 activity by Zn-PP administration abolished the beneficial effect of hemin-pretreatment.	zinc protoporphyrin	31-36	heme oxygenase 1	Homo sapiens	14-18
16739127-4	2006	In this study, we investigated the potential roles of extracellular signal-regulated kinase (ERK) and c-jun N-terminal kinase (JNK) in the regulation of butylated hydroxyanisole (BHA)-induced and Nrf2-dependent ARE transcriptional activity and ARE-mediated endogenous heme oxygenase-1 (HO-1) protein expression in HepG2 cells.	Butylated Hydroxyanisole	179-182	heme oxygenase 1	Homo sapiens	268-284
16739127-4	2006	In this study, we investigated the potential roles of extracellular signal-regulated kinase (ERK) and c-jun N-terminal kinase (JNK) in the regulation of butylated hydroxyanisole (BHA)-induced and Nrf2-dependent ARE transcriptional activity and ARE-mediated endogenous heme oxygenase-1 (HO-1) protein expression in HepG2 cells.	Butylated Hydroxyanisole	179-182	heme oxygenase 1	Homo sapiens	286-290
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	Butylated Hydroxyanisole	109-133	heme oxygenase 1	Homo sapiens	13-29
17048120-6	2006	CONCLUSIONS: Our data demonstrate that both BHA and tBHQ are strong chemical inducers of HO-1, NQO1 and Nrf2 proteins in primary-cultured human and rat hepatocytes with the activation of MAPK ERK1/2 and JNK1/2.	Butylated Hydroxyanisole	44-47	heme oxygenase 1	Homo sapiens	89-93
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	Butylated Hydroxyanisole	109-133	heme oxygenase 1	Homo sapiens	31-35
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	Butylated Hydroxyanisole	135-138	heme oxygenase 1	Homo sapiens	13-29
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	Butylated Hydroxyanisole	135-138	heme oxygenase 1	Homo sapiens	31-35
17048120-6	2006	CONCLUSIONS: Our data demonstrate that both BHA and tBHQ are strong chemical inducers of HO-1, NQO1 and Nrf2 proteins in primary-cultured human and rat hepatocytes with the activation of MAPK ERK1/2 and JNK1/2.	2-tert-butylhydroquinone	52-56	heme oxygenase 1	Homo sapiens	89-93
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	2-tert-butylhydroquinone	160-182	heme oxygenase 1	Homo sapiens	13-29
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	2-tert-butylhydroquinone	160-182	heme oxygenase 1	Homo sapiens	31-35
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	2-tert-butylhydroquinone	184-188	heme oxygenase 1	Homo sapiens	13-29
17048120-0	2006	Induction of heme oxygenase-1 (HO-1) and NAD[P]H: quinone oxidoreductase 1 (NQO1) by a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) in primary-cultured human and rat hepatocytes.	2-tert-butylhydroquinone	184-188	heme oxygenase 1	Homo sapiens	31-35
17048120-1	2006	PURPOSE: This study was aimed to investigate the effects of a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) on the induction of HO-1, NQO1 and Nrf2 proteins and their regulatory mechanisms in primary-cultured hepatocytes.	Butylated Hydroxyanisole	84-108	heme oxygenase 1	Homo sapiens	185-189
17048120-1	2006	PURPOSE: This study was aimed to investigate the effects of a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) on the induction of HO-1, NQO1 and Nrf2 proteins and their regulatory mechanisms in primary-cultured hepatocytes.	Butylated Hydroxyanisole	110-113	heme oxygenase 1	Homo sapiens	185-189
17048120-1	2006	PURPOSE: This study was aimed to investigate the effects of a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) on the induction of HO-1, NQO1 and Nrf2 proteins and their regulatory mechanisms in primary-cultured hepatocytes.	2-tert-butylhydroquinone	135-157	heme oxygenase 1	Homo sapiens	185-189
17048120-1	2006	PURPOSE: This study was aimed to investigate the effects of a phenolic antioxidant, butylated hydroxyanisole (BHA) and its metabolite, tert-butylhydroquinone (tBHQ) on the induction of HO-1, NQO1 and Nrf2 proteins and their regulatory mechanisms in primary-cultured hepatocytes.	2-tert-butylhydroquinone	159-163	heme oxygenase 1	Homo sapiens	185-189
17048120-7	2006	However, in MFs, BHA failed to induce HO-1, whereas tBHQ strongly induced HO-1 in Nrf2 wild-type but not in Nrf2 knock-out, suggesting that Nrf2 is indispensable for tBHQ-induced HO-1 in MF.	2-tert-butylhydroquinone	52-56	heme oxygenase 1	Homo sapiens	74-78
17048120-7	2006	However, in MFs, BHA failed to induce HO-1, whereas tBHQ strongly induced HO-1 in Nrf2 wild-type but not in Nrf2 knock-out, suggesting that Nrf2 is indispensable for tBHQ-induced HO-1 in MF.	2-tert-butylhydroquinone	52-56	heme oxygenase 1	Homo sapiens	74-78
16858012-0	2006	Heme oxygenase-1, a potential biomarker of chronic silicosis, attenuates silica-induced lung injury.	Silicon Dioxide	73-79	heme oxygenase 1	Homo sapiens	0-16
16858012-8	2006	Serum HO-1 levels also correlated inversely with serum 8-hydroxydeoxyguanosine levels and positively with vital capacity and forced expiratory volume in one second in patients with silicosis.	8-ohdg	55-78	heme oxygenase 1	Homo sapiens	6-10
16858012-9	2006	HO-1 was present in the lungs of humans and mice with silicosis, especially at sites of silica particle deposition.	Silicon Dioxide	88-94	heme oxygenase 1	Homo sapiens	0-4
16858012-11	2006	The inflammation was suppressed by treatment with hemin, an inducer of HO-1, and enhanced by zinc protoporphyrin, an inhibitor of HO-1.	Hemin	50-55	heme oxygenase 1	Homo sapiens	71-75
16858012-11	2006	The inflammation was suppressed by treatment with hemin, an inducer of HO-1, and enhanced by zinc protoporphyrin, an inhibitor of HO-1.	zinc protoporphyrin	93-112	heme oxygenase 1	Homo sapiens	130-134
16858012-13	2006	HO-1 suppresses reactive oxygen species activity, and subsequent pathologic changes, thereby attenuating disease progression.	Reactive Oxygen Species	16-39	heme oxygenase 1	Homo sapiens	0-4
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Heme	73-77	heme oxygenase 1	Homo sapiens	0-16
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Heme	73-77	heme oxygenase 1	Homo sapiens	18-22
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Biliverdine	83-93	heme oxygenase 1	Homo sapiens	0-16
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Biliverdine	83-93	heme oxygenase 1	Homo sapiens	18-22
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Iron	110-114	heme oxygenase 1	Homo sapiens	0-16
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Iron	110-114	heme oxygenase 1	Homo sapiens	18-22
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Carbon Monoxide	119-134	heme oxygenase 1	Homo sapiens	0-16
17042977-2	2006	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide.	Carbon Monoxide	119-134	heme oxygenase 1	Homo sapiens	18-22
17042977-9	2006	Flow cytometry was used to detect apoptotic cells in the HO-1 group and in the control group after induction by recombinant human tumor necrosis factor-alpha (rTNFalpha) and cycloheximide (CHX) for 48 hours.	Cycloheximide	174-187	heme oxygenase 1	Homo sapiens	57-61
16485034-0	2006	Flunarizine induces Nrf2-mediated transcriptional activation of heme oxygenase-1 in protection of auditory cells from cisplatin.	Flunarizine	0-11	heme oxygenase 1	Homo sapiens	64-80
16375908-4	2006	We found that, in vascular endothelial cells, simvastatin increased the steady-state levels of heat shock proteins 90 and 70, and heme oxygenase-1 and caused the nuclear translocation of heat shock factor 1.	Simvastatin	46-57	heme oxygenase 1	Homo sapiens	130-146
16953189-5	2006	KEY RESULTS: Intraperitoneal challenge with carrageenan enhanced HO-1 protein expression in mesentery and bilirubin concentration in peritoneal exudates.	Carrageenan	44-55	heme oxygenase 1	Homo sapiens	65-69
16953189-6	2006	Pretreatment of mice with a non-specific inhibitor of HO (ZnDPBG) or with a HO-1 specific inhibitor (ZnPP IX) enhanced neutrophil migration, rolling and adhesion on endothelium induced by carrageenan.	zinc protoporphyrin	101-108	heme oxygenase 1	Homo sapiens	76-80
16953189-6	2006	Pretreatment of mice with a non-specific inhibitor of HO (ZnDPBG) or with a HO-1 specific inhibitor (ZnPP IX) enhanced neutrophil migration, rolling and adhesion on endothelium induced by carrageenan.	Carrageenan	188-199	heme oxygenase 1	Homo sapiens	76-80
16485034-5	2006	Furthermore, both pharmacological inhibition and siRNA transfection of HO-1 completely abolished the flunarizine-mediated protection of HEI-OC1 cells and the primary rat (P2) organ of Corti explants from cisplatin.	Cisplatin	204-213	heme oxygenase 1	Homo sapiens	71-75
16485034-0	2006	Flunarizine induces Nrf2-mediated transcriptional activation of heme oxygenase-1 in protection of auditory cells from cisplatin.	Cisplatin	118-127	heme oxygenase 1	Homo sapiens	64-80
16485034-6	2006	These results suggest that Nrf2-driven transcriptional activation of ARE through PI3K-Akt signaling augments the generation of HO-1, which may be a critically important determinant in cellular response toward cisplatin and the cytoprotective effect of flunarizine against cisplatin.	Cisplatin	209-218	heme oxygenase 1	Homo sapiens	127-131
16485034-6	2006	These results suggest that Nrf2-driven transcriptional activation of ARE through PI3K-Akt signaling augments the generation of HO-1, which may be a critically important determinant in cellular response toward cisplatin and the cytoprotective effect of flunarizine against cisplatin.	Flunarizine	252-263	heme oxygenase 1	Homo sapiens	127-131
16485034-6	2006	These results suggest that Nrf2-driven transcriptional activation of ARE through PI3K-Akt signaling augments the generation of HO-1, which may be a critically important determinant in cellular response toward cisplatin and the cytoprotective effect of flunarizine against cisplatin.	Cisplatin	272-281	heme oxygenase 1	Homo sapiens	127-131
16485034-4	2006	Pretreatment with flunarizine predominantly increased the transcriptional activity of HO-1 among Nrf2-driven transcripts, including HO-1, NQO1, GCLC, GCLM, GST micro-1, and GSTA4.	Flunarizine	18-29	heme oxygenase 1	Homo sapiens	86-90
16485034-4	2006	Pretreatment with flunarizine predominantly increased the transcriptional activity of HO-1 among Nrf2-driven transcripts, including HO-1, NQO1, GCLC, GCLM, GST micro-1, and GSTA4.	Flunarizine	18-29	heme oxygenase 1	Homo sapiens	132-136
16485034-5	2006	Furthermore, both pharmacological inhibition and siRNA transfection of HO-1 completely abolished the flunarizine-mediated protection of HEI-OC1 cells and the primary rat (P2) organ of Corti explants from cisplatin.	Flunarizine	101-112	heme oxygenase 1	Homo sapiens	71-75
16775837-3	2006	To investigate the mechanisms for this inhibition, Cr(VI) effects on basal and arsenic (As(III))-induced HO-1 expression were examined in cultured human bronchial epithelial (BEAS-2B) cells.	Chromium	51-53	heme oxygenase 1	Homo sapiens	105-109
16775837-3	2006	To investigate the mechanisms for this inhibition, Cr(VI) effects on basal and arsenic (As(III))-induced HO-1 expression were examined in cultured human bronchial epithelial (BEAS-2B) cells.	Arsenic	79-86	heme oxygenase 1	Homo sapiens	105-109
16775837-3	2006	To investigate the mechanisms for this inhibition, Cr(VI) effects on basal and arsenic (As(III))-induced HO-1 expression were examined in cultured human bronchial epithelial (BEAS-2B) cells.	as(iii)	88-95	heme oxygenase 1	Homo sapiens	105-109
16775837-4	2006	An effect of Cr(VI) on the low basal HO-1 mRNA and protein levels in BEAS-2B cells was not detectible.	chromium hexavalent ion	13-19	heme oxygenase 1	Homo sapiens	37-41
16951197-2	2006	Using human HO-1 promoter reporter plasmids and ChIP assay, we have identified that sulforaphane transcriptionally activated the upstream ARE-rich enhancer region, located at -9.0 kb upstream human HO-1 promoter.	sulforaphane	84-96	heme oxygenase 1	Homo sapiens	198-202
16596642-2	2006	Recently, a (GT)n dinucleotide repeat polymorphism in the HO-1 promoter was shown to modulate HO-1 gene expression.	(gt)n dinucleotide	12-30	heme oxygenase 1	Homo sapiens	58-62
16596642-2	2006	Recently, a (GT)n dinucleotide repeat polymorphism in the HO-1 promoter was shown to modulate HO-1 gene expression.	(gt)n dinucleotide	12-30	heme oxygenase 1	Homo sapiens	94-98
16840713-0	2006	Protection of human vascular smooth muscle cells from H2O2-induced apoptosis through functional codependence between HO-1 and AKT.	Hydrogen Peroxide	54-58	heme oxygenase 1	Homo sapiens	117-129
16840713-9	2006	HO-1 reduced H2O2-induced OS and apoptosis.	Hydrogen Peroxide	13-17	heme oxygenase 1	Homo sapiens	0-4
16840713-10	2006	Akt knockdown removed the protective effect of HO-1 on delta psi(m) during exposure to H2O2.	Hydrogen Peroxide	87-91	heme oxygenase 1	Homo sapiens	47-51
16840713-12	2006	Inhibition of PI3K-Akt reduced induction of HO-1 protein expression by H2O2 and blocked its anti-apoptotic effects.	Hydrogen Peroxide	71-75	heme oxygenase 1	Homo sapiens	44-48
16840713-14	2006	CONCLUSIONS: HO-1 and Akt exert codependent cytoprotective effects against OS-induced apoptosis in HASMCs.	hasmcs	99-105	heme oxygenase 1	Homo sapiens	13-17
16951197-0	2006	Mechanism of action of sulforaphane: inhibition of p38 mitogen-activated protein kinase isoforms contributing to the induction of antioxidant response element-mediated heme oxygenase-1 in human hepatoma HepG2 cells.	sulforaphane	23-35	heme oxygenase 1	Homo sapiens	168-184
16951197-1	2006	Exposure of sulforaphane to HepG2 cells increased heme oxygenase-1 (HO-1) expression by activating antioxidant response element (ARE) through induction of Nrf2 and suppression of Kelch-like ECH-associated protein 1 (Keap1).	sulforaphane	12-24	heme oxygenase 1	Homo sapiens	50-66
16951197-1	2006	Exposure of sulforaphane to HepG2 cells increased heme oxygenase-1 (HO-1) expression by activating antioxidant response element (ARE) through induction of Nrf2 and suppression of Kelch-like ECH-associated protein 1 (Keap1).	sulforaphane	12-24	heme oxygenase 1	Homo sapiens	68-72
16959797-0	2006	The antioxidant role of a reagent, 2",7"-dichlorodihydrofluorescin diacetate, detecting reactive-oxygen species and blocking the induction of heme oxygenase-1 and preventing cytotoxicity.	2",7"-dichlorodihydrofluorescin diacetate	35-76	heme oxygenase 1	Homo sapiens	142-158
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-16
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Biliverdine	43-53	heme oxygenase 1	Homo sapiens	0-16
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Biliverdine	43-53	heme oxygenase 1	Homo sapiens	18-22
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Iron	55-59	heme oxygenase 1	Homo sapiens	0-16
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Iron	55-59	heme oxygenase 1	Homo sapiens	18-22
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Carbon Monoxide	64-66	heme oxygenase 1	Homo sapiens	0-16
16959797-1	2006	Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO.	Carbon Monoxide	64-66	heme oxygenase 1	Homo sapiens	18-22
16959797-6	2006	511, 21-27], and then examined the effect of DCFH-DA on the induction of HO-1 expression by arsenite, cadmium and hemin, which induce oxidative stress and cytotoxicity.	diacetyldichlorofluorescein	45-52	heme oxygenase 1	Homo sapiens	73-77
16959797-6	2006	511, 21-27], and then examined the effect of DCFH-DA on the induction of HO-1 expression by arsenite, cadmium and hemin, which induce oxidative stress and cytotoxicity.	arsenite	92-100	heme oxygenase 1	Homo sapiens	73-77
16959797-6	2006	511, 21-27], and then examined the effect of DCFH-DA on the induction of HO-1 expression by arsenite, cadmium and hemin, which induce oxidative stress and cytotoxicity.	Cadmium	102-109	heme oxygenase 1	Homo sapiens	73-77
16959797-6	2006	511, 21-27], and then examined the effect of DCFH-DA on the induction of HO-1 expression by arsenite, cadmium and hemin, which induce oxidative stress and cytotoxicity.	Hemin	114-119	heme oxygenase 1	Homo sapiens	73-77
16959797-7	2006	We found suppression of the arsenite-, cadmium- and hemin-dependent induction of HO-1 with DCFH-DA.	arsenite	28-36	heme oxygenase 1	Homo sapiens	81-85
16959797-7	2006	We found suppression of the arsenite-, cadmium- and hemin-dependent induction of HO-1 with DCFH-DA.	Cadmium	39-46	heme oxygenase 1	Homo sapiens	81-85
16959797-7	2006	We found suppression of the arsenite-, cadmium- and hemin-dependent induction of HO-1 with DCFH-DA.	diacetyldichlorofluorescein	91-98	heme oxygenase 1	Homo sapiens	81-85
16959797-8	2006	The suppression occurred at the transcriptional level since the promoter activity of the Maf-recognition site of the HO-1 gene decreased with the DCFH-DA treatment.	diacetyldichlorofluorescein	146-153	heme oxygenase 1	Homo sapiens	117-121
16951197-2	2006	Using human HO-1 promoter reporter plasmids and ChIP assay, we have identified that sulforaphane transcriptionally activated the upstream ARE-rich enhancer region, located at -9.0 kb upstream human HO-1 promoter.	sulforaphane	84-96	heme oxygenase 1	Homo sapiens	12-16
16951197-3	2006	Induction of HO-1 by sulforaphane was attenuated by overexpression of mutant Nrf2 plasmid in HepG2 cells and totally abolished in Nrf2 knockout mouse embryonic keratinocytes and fibroblasts.	sulforaphane	21-33	heme oxygenase 1	Homo sapiens	13-17
16951197-8	2006	Collectively, our results indicate that transcriptional activation of Nrf2/ARE is critical in sulforaphane-mediated induction of HO-1, which can be modulated in part by the blockade of p38 MAPK signaling pathway.	sulforaphane	94-106	heme oxygenase 1	Homo sapiens	129-133
16927154-0	2006	Ketamine-induced gastroprotection during endotoxemia: role of heme-oxygenase-1.	Ketamine	0-8	heme oxygenase 1	Homo sapiens	62-78
16927154-4	2006	We hypothesized that ketamine would diminish gastric injury from lipopolysacharide via down-regulation of nuclear factor-kappass, activator protein-1, and inducible nitric oxide synthase, as well as up-regulation of heme-oxygenase-1.	Ketamine	21-29	heme oxygenase 1	Homo sapiens	216-232
16927154-5	2006	Ketamine up-regulated heme-oxygenase-1 and attenuated lipopolysacharide-induced changes in gastric nuclear factor-kappass, activator protein-1, and inducible nitric oxide synthase.	Ketamine	0-8	heme oxygenase 1	Homo sapiens	22-38
16816389-0	2006	Pescadillo interacts with the cadmium response element of the human heme oxygenase-1 promoter in renal epithelial cells.	pescadillo	0-10	heme oxygenase 1	Homo sapiens	68-84
16953118-1	2006	Recently, it has been reported that curcumin, which is known as a potent antioxidant, acts as a non- stressful and non-cytotoxic inducer of the cytoprotective heme oxygenase (HO)-1.	Curcumin	36-44	heme oxygenase 1	Homo sapiens	159-180
16802348-10	2006	Moreover, we found that the activation of the ARE and the induction of HO-1 mRNA caused by Apo were suppressed in the presence of the antioxidant N-acetylcysteine and also that Apo produced intracellular reactive oxygen species (ROS), indicating that the low level of ROS produced by Apo may play a critical role in this phenomenon.	Acetylcysteine	146-162	heme oxygenase 1	Homo sapiens	71-75
16802348-10	2006	Moreover, we found that the activation of the ARE and the induction of HO-1 mRNA caused by Apo were suppressed in the presence of the antioxidant N-acetylcysteine and also that Apo produced intracellular reactive oxygen species (ROS), indicating that the low level of ROS produced by Apo may play a critical role in this phenomenon.	Reactive Oxygen Species	204-227	heme oxygenase 1	Homo sapiens	71-75
16802348-10	2006	Moreover, we found that the activation of the ARE and the induction of HO-1 mRNA caused by Apo were suppressed in the presence of the antioxidant N-acetylcysteine and also that Apo produced intracellular reactive oxygen species (ROS), indicating that the low level of ROS produced by Apo may play a critical role in this phenomenon.	Reactive Oxygen Species	229-232	heme oxygenase 1	Homo sapiens	71-75
16802348-10	2006	Moreover, we found that the activation of the ARE and the induction of HO-1 mRNA caused by Apo were suppressed in the presence of the antioxidant N-acetylcysteine and also that Apo produced intracellular reactive oxygen species (ROS), indicating that the low level of ROS produced by Apo may play a critical role in this phenomenon.	Reactive Oxygen Species	268-271	heme oxygenase 1	Homo sapiens	71-75
16816389-0	2006	Pescadillo interacts with the cadmium response element of the human heme oxygenase-1 promoter in renal epithelial cells.	Cadmium	30-37	heme oxygenase 1	Homo sapiens	68-84
16816389-3	2006	Exposure of renal proximal tubular epithelial cells to 10 mum cadmium demonstrated induction ( approximately 20-fold) of heme oxygenase-1 mRNA and protein.	Cadmium	62-69	heme oxygenase 1	Homo sapiens	121-137
16816389-4	2006	Using a 4.5-kb human heme oxygenase-1 promoter construct, the importance of a previously identified cadmium response element (TGCTAGAT) in HeLa cells was verified in renal epithelial cells.	Cadmium	100-107	heme oxygenase 1	Homo sapiens	21-37
16816389-10	2006	The findings demonstrate the important and previously unrecognized role of pescadillo as a DNA-binding protein interacting specifically with the cadmium response element of the human heme oxygenase-1 gene.	Cadmium	145-152	heme oxygenase 1	Homo sapiens	183-199
16857833-0	2006	The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothelial cells via induction of heme oxygenase-1 and ferritin.	Dipeptides	19-28	heme oxygenase 1	Homo sapiens	115-131
16867247-9	2006	After the treatment with NaHS for 11 weeks, H(2)S donor ameliorated PVSR and downregulated PCNA expression and ERK activation with an increase in lung tissue CO production and HO-1 protein expression but a decrease in NO production, NOS activity and eNOS protein expression in shunted rats.	sodium bisulfide	25-29	heme oxygenase 1	Homo sapiens	176-180
16867247-9	2006	After the treatment with NaHS for 11 weeks, H(2)S donor ameliorated PVSR and downregulated PCNA expression and ERK activation with an increase in lung tissue CO production and HO-1 protein expression but a decrease in NO production, NOS activity and eNOS protein expression in shunted rats.	Hydrogen Sulfide	44-49	heme oxygenase 1	Homo sapiens	176-180
16780547-4	2006	Under this scheme, the viability of PEGylated islets was improved; that is, PEG molecules could block cellular immunity and HO-1 could exert its cytoprotective property against inflammation.	Polyethylene Glycols	36-39	heme oxygenase 1	Homo sapiens	124-128
16780547-5	2006	Interestingly, when employed with a low dose of CsA (1 mg/kg/day), a cooperative action of PEG molecules and HO-1 in immune reactions could result in the complete survival of transplanted islets for 100 days without islet function impairment.	Cyclosporine	48-51	heme oxygenase 1	Homo sapiens	109-113
16246346-0	2006	3-Hydroxyanthranilic acid, one of L-tryptophan metabolites, inhibits monocyte chemoattractant protein-1 secretion and vascular cell adhesion molecule-1 expression via heme oxygenase-1 induction in human umbilical vein endothelial cells.	3-Hydroxyanthranilic Acid	0-25	heme oxygenase 1	Homo sapiens	167-183
16849502-2	2006	This effect is mimicked by CO, generated via the catabolism of heme by HO-1.	Carbon Monoxide	27-29	heme oxygenase 1	Homo sapiens	71-75
16849502-2	2006	This effect is mimicked by CO, generated via the catabolism of heme by HO-1.	Heme	63-67	heme oxygenase 1	Homo sapiens	71-75
16849502-5	2006	When overexpressed in EC, HO-1 targeted specifically the p38alpha but not the p38beta MAPK isoform for degradation by the 26S proteasome, an effect reversed by the 26S proteasome inhibitors MG-132 or lactacystin.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	190-196	heme oxygenase 1	Homo sapiens	26-30
16849502-5	2006	When overexpressed in EC, HO-1 targeted specifically the p38alpha but not the p38beta MAPK isoform for degradation by the 26S proteasome, an effect reversed by the 26S proteasome inhibitors MG-132 or lactacystin.	lactacystin	200-211	heme oxygenase 1	Homo sapiens	26-30
16849502-6	2006	Inhibition of p38alpha expression was also observed when HO-1 was induced physiologically by iron protoporphyrin IX (hemin).	iron protoporphyrin IX	93-115	heme oxygenase 1	Homo sapiens	57-61
16849502-9	2006	The antiapoptotic effect of HO-1 was impaired when p38alpha expression was restored ectopically or when its degradation by the 26S proteasome was inhibited by MG-132.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	159-165	heme oxygenase 1	Homo sapiens	28-32
16857833-0	2006	The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothelial cells via induction of heme oxygenase-1 and ferritin.	H-MET-TYR-OH	29-36	heme oxygenase 1	Homo sapiens	115-131
16857833-3	2006	The present study investigates the effect of Met-Tyr on the expression of the antioxidant stress proteins, heme oxygenase-1 (HO-1) and ferritin, in endothelial cells derived from the human umbilical vein and their contribution to the decrease in radical formation that occurs under the influence of this dipeptide.	H-MET-TYR-OH	45-52	heme oxygenase 1	Homo sapiens	107-123
16857833-3	2006	The present study investigates the effect of Met-Tyr on the expression of the antioxidant stress proteins, heme oxygenase-1 (HO-1) and ferritin, in endothelial cells derived from the human umbilical vein and their contribution to the decrease in radical formation that occurs under the influence of this dipeptide.	H-MET-TYR-OH	45-52	heme oxygenase 1	Homo sapiens	125-129
16857833-3	2006	The present study investigates the effect of Met-Tyr on the expression of the antioxidant stress proteins, heme oxygenase-1 (HO-1) and ferritin, in endothelial cells derived from the human umbilical vein and their contribution to the decrease in radical formation that occurs under the influence of this dipeptide.	Dipeptides	304-313	heme oxygenase 1	Homo sapiens	107-123
16857833-5	2006	This indirect protection was associated with a significant increase in protein expression of HO-1 and ferritin and abolished by the HO inhibitor zinc deuteroporphyrin IX 2,4-bis-ethylene glycol (ZnBG).	znbg	195-199	heme oxygenase 1	Homo sapiens	93-97
16857833-7	2006	Met-Tyr raised HO-1 mRNA levels by enhancing mRNA stability.	H-MET-TYR-OH	0-7	heme oxygenase 1	Homo sapiens	15-19
16857833-9	2006	Our results demonstrate that Met-Tyr protects endothelial cells from oxidative stress via induction of HO-1 and ferritin but independently of its ACE inhibitory properties.	H-MET-TYR-OH	29-36	heme oxygenase 1	Homo sapiens	103-107
16480751-0	2006	Upregulation of endothelial heme oxygenase-1 expression through the activation of the JNK pathway by sublethal concentrations of acrolein.	Acrolein	129-137	heme oxygenase 1	Homo sapiens	28-44
16866988-9	2006	In addition, FeSO(4) reversed the protective effect of DFO on DA-induced cytotoxicity, HO-1 expression and caspase-3 activation.	ferrous sulfate	13-20	heme oxygenase 1	Homo sapiens	87-91
16866988-9	2006	In addition, FeSO(4) reversed the protective effect of DFO on DA-induced cytotoxicity, HO-1 expression and caspase-3 activation.	Deferoxamine	55-58	heme oxygenase 1	Homo sapiens	87-91
16928811-3	2006	In the present study, we investigated the roles of extracellular signal-regulated kinase (ERK) and c-Jun-NH(2)-kinase (JNK) in the regulation of phenethyl isothiocyanate (PEITC)-induced and Nrf2-dependent ARE activity and ARE-driven heme oxygenase-1 (HO-1) gene expression in PC-3 cells.	phenethyl isothiocyanate	145-169	heme oxygenase 1	Homo sapiens	233-249
16928811-3	2006	In the present study, we investigated the roles of extracellular signal-regulated kinase (ERK) and c-Jun-NH(2)-kinase (JNK) in the regulation of phenethyl isothiocyanate (PEITC)-induced and Nrf2-dependent ARE activity and ARE-driven heme oxygenase-1 (HO-1) gene expression in PC-3 cells.	phenethyl isothiocyanate	145-169	heme oxygenase 1	Homo sapiens	251-255
16928811-4	2006	ARE activity and HO-1 expression were strongly increased after treatment with PEITC.	phenethyl isothiocyanate	78-83	heme oxygenase 1	Homo sapiens	17-21
16480751-3	2006	In this study, the regulatory effects of acrolein upon the expression of HO-1 were investigated in endothelial cells (ECs).	Acrolein	41-49	heme oxygenase 1	Homo sapiens	73-77
16480751-4	2006	We demonstrate that acrolein induces the elevation of HO-1 protein levels, and subsequent enzyme activity, at non-cytotoxic concentrations.	Acrolein	20-28	heme oxygenase 1	Homo sapiens	54-58
16480751-5	2006	An additional alpha,beta-unsaturated aldehyde, cinnamaldehyde, was also found to increase HO-1 expression and have less cytotoxicity than acrolein.	alpha,beta-unsaturated aldehyde	14-45	heme oxygenase 1	Homo sapiens	90-94
16480751-5	2006	An additional alpha,beta-unsaturated aldehyde, cinnamaldehyde, was also found to increase HO-1 expression and have less cytotoxicity than acrolein.	cinnamaldehyde	47-61	heme oxygenase 1	Homo sapiens	90-94
16829200-2	2006	Carbon monoxide is one of the products of the degradation of heme by heme oxygenase 1.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	69-85
16480751-6	2006	Moreover, acrolein-mediated HO-1 induction is abrogated in the presence of actinomycin D and cycloheximide.	Dactinomycin	75-88	heme oxygenase 1	Homo sapiens	28-32
16480751-6	2006	Moreover, acrolein-mediated HO-1 induction is abrogated in the presence of actinomycin D and cycloheximide.	Cycloheximide	93-106	heme oxygenase 1	Homo sapiens	28-32
16480751-15	2006	In addition, only the JNK inhibitor SP600125 and tyrosine kinase inhibitor genistein had any significant inhibitory impact upon the upregulation of HO-1 by acrolein.	pyrazolanthrone	36-44	heme oxygenase 1	Homo sapiens	148-152
16480751-15	2006	In addition, only the JNK inhibitor SP600125 and tyrosine kinase inhibitor genistein had any significant inhibitory impact upon the upregulation of HO-1 by acrolein.	Genistein	75-84	heme oxygenase 1	Homo sapiens	148-152
16480751-15	2006	In addition, only the JNK inhibitor SP600125 and tyrosine kinase inhibitor genistein had any significant inhibitory impact upon the upregulation of HO-1 by acrolein.	Acrolein	156-164	heme oxygenase 1	Homo sapiens	148-152
16480751-17	2006	Hence, we show in our current experiments that a sublethal concentration of acrolein is in fact a novel HO-1 inducer, and we further identify the principal underlying mechanisms involved in this process.	Acrolein	76-84	heme oxygenase 1	Homo sapiens	104-108
16814105-8	2006	Inhibition of HO-1 with Sn protoporphyrin IX and blockage of Sp-1-mediatied upregulation of HO-1 with mithramycin attenuated antioxidant and cytoprotective functions of NGF against hydrogen peroxide.	sn protoporphyrin ix	24-44	heme oxygenase 1	Homo sapiens	14-18
16627864-0	2006	Dobutamine improves liver function after hemorrhagic shock through induction of heme oxygenase-1.	Dobutamine	0-10	heme oxygenase 1	Homo sapiens	80-96
16814105-8	2006	Inhibition of HO-1 with Sn protoporphyrin IX and blockage of Sp-1-mediatied upregulation of HO-1 with mithramycin attenuated antioxidant and cytoprotective functions of NGF against hydrogen peroxide.	Plicamycin	102-113	heme oxygenase 1	Homo sapiens	92-96
16814105-8	2006	Inhibition of HO-1 with Sn protoporphyrin IX and blockage of Sp-1-mediatied upregulation of HO-1 with mithramycin attenuated antioxidant and cytoprotective functions of NGF against hydrogen peroxide.	Hydrogen Peroxide	181-198	heme oxygenase 1	Homo sapiens	92-96
16804400-8	2006	Interestingly, gliotoxin induced HO-1 in HT-29 cells and, in turn, inhibition of HO-1 activity by a zinc protoporphyrin IX reversed the effects of gliotoxin in terms of I-kappaB degradation, intercellular adhesion molecule-1 expression, and IL-8 production.	Gliotoxin	15-24	heme oxygenase 1	Homo sapiens	33-37
16712795-3	2006	This effect was abrogated in the presence of the heme oxygenase-1 (HO-1) inhibitor ZnBG.	zinc deuteroporphyrin IX 2,4-bis(glycol)	83-87	heme oxygenase 1	Homo sapiens	49-65
16712795-3	2006	This effect was abrogated in the presence of the heme oxygenase-1 (HO-1) inhibitor ZnBG.	zinc deuteroporphyrin IX 2,4-bis(glycol)	83-87	heme oxygenase 1	Homo sapiens	67-71
16713997-7	2006	Furthermore, l-arginine-induced NO formation was accompanied by a reduction in oxidative stress and an increase in protein expression and enzyme activity of heme oxygenase (HO)-1.	Arginine	13-23	heme oxygenase 1	Homo sapiens	157-178
16787441-2	2006	Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide.	Carbon Monoxide	161-176	heme oxygenase 1	Homo sapiens	62-78
16787441-2	2006	Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide.	Biliverdine	140-150	heme oxygenase 1	Homo sapiens	62-78
16787441-2	2006	Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide.	Iron	152-156	heme oxygenase 1	Homo sapiens	62-78
16804400-8	2006	Interestingly, gliotoxin induced HO-1 in HT-29 cells and, in turn, inhibition of HO-1 activity by a zinc protoporphyrin IX reversed the effects of gliotoxin in terms of I-kappaB degradation, intercellular adhesion molecule-1 expression, and IL-8 production.	Gliotoxin	15-24	heme oxygenase 1	Homo sapiens	81-85
16804400-8	2006	Interestingly, gliotoxin induced HO-1 in HT-29 cells and, in turn, inhibition of HO-1 activity by a zinc protoporphyrin IX reversed the effects of gliotoxin in terms of I-kappaB degradation, intercellular adhesion molecule-1 expression, and IL-8 production.	zinc protoporphyrin	100-122	heme oxygenase 1	Homo sapiens	81-85
16804400-8	2006	Interestingly, gliotoxin induced HO-1 in HT-29 cells and, in turn, inhibition of HO-1 activity by a zinc protoporphyrin IX reversed the effects of gliotoxin in terms of I-kappaB degradation, intercellular adhesion molecule-1 expression, and IL-8 production.	Gliotoxin	147-156	heme oxygenase 1	Homo sapiens	33-37
16799064-7	2006	Finally, the ability of flavonoids to induce phase-2 detoxifying enzymes was tested by immunoblot analysis for the transcription factor Nrf2 and the phase-2 gene product heme-oxygenase 1.	Flavonoids	24-34	heme oxygenase 1	Homo sapiens	170-186
16799064-13	2006	Many of these flavonoids induced the expression of Nrf2 and the phase-2 gene product heme-oxygenase 1 in human RPE cells.	Flavonoids	14-24	heme oxygenase 1	Homo sapiens	85-101
16804400-8	2006	Interestingly, gliotoxin induced HO-1 in HT-29 cells and, in turn, inhibition of HO-1 activity by a zinc protoporphyrin IX reversed the effects of gliotoxin in terms of I-kappaB degradation, intercellular adhesion molecule-1 expression, and IL-8 production.	Gliotoxin	147-156	heme oxygenase 1	Homo sapiens	81-85
16624973-0	2006	Nuclear factor-kappa B-independent anti-inflammatory action of salicylate in human endothelial cells: induction of heme oxygenase-1 by the c-jun N-terminal kinase/activator protein-1 pathway.	Salicylates	63-73	heme oxygenase 1	Homo sapiens	115-131
16530877-6	2006	Addition of increasing concentrations of N-acetylcysteine (NAC) led to down-regulation of HO-1 in cells expressing HCV proteins.	Acetylcysteine	41-57	heme oxygenase 1	Homo sapiens	90-94
16530877-6	2006	Addition of increasing concentrations of N-acetylcysteine (NAC) led to down-regulation of HO-1 in cells expressing HCV proteins.	Acetylcysteine	59-62	heme oxygenase 1	Homo sapiens	90-94
16530877-8	2006	Sodium arsenite, a strong inducer of oxidative stress and HO-1, reduced Bach1 expression in wild type Huh-7 cells, and NAC partially abrogated this decrease.	sodium arsenite	0-15	heme oxygenase 1	Homo sapiens	58-62
16624973-11	2006	In summary, our study introduces HO-1 as novel NF-kappaB-independent anti-inflammatory target of salicylate in human endothelial cells.	Salicylates	97-107	heme oxygenase 1	Homo sapiens	33-37
16624973-6	2006	As judged by Western blot analysis, salicylate increased endothelial heme oxygenase-1 (HO-1) protein levels.	Salicylates	36-46	heme oxygenase 1	Homo sapiens	69-85
16624973-12	2006	Moreover, we elucidated the JNK/AP-1 pathway as crucial for the induction of HO-1 by salicylate.	Salicylates	85-95	heme oxygenase 1	Homo sapiens	77-81
16624973-6	2006	As judged by Western blot analysis, salicylate increased endothelial heme oxygenase-1 (HO-1) protein levels.	Salicylates	36-46	heme oxygenase 1	Homo sapiens	87-91
16624973-7	2006	Using both the HO-1 inhibitor tin(II) protoporphyrin IX and HO-1 antisense oligonucleotides, we causally linked the induction of HO-1 to the decrease of P-selectin.	Oligonucleotides	75-91	heme oxygenase 1	Homo sapiens	60-64
16624973-7	2006	Using both the HO-1 inhibitor tin(II) protoporphyrin IX and HO-1 antisense oligonucleotides, we causally linked the induction of HO-1 to the decrease of P-selectin.	Oligonucleotides	75-91	heme oxygenase 1	Homo sapiens	60-64
16624973-8	2006	Moreover, we were interested in the signaling mechanisms leading to the up-regulation of HO-1 by salicylate.	Salicylates	97-107	heme oxygenase 1	Homo sapiens	89-93
16624973-9	2006	c-Jun NH2-terminal kinase (JNK) was found to be activated by salicylate, and we could causally link this activation to the induction of HO-1 by using the JNK inhibitor 1,9-pyrazoloanthrone.	Salicylates	61-71	heme oxygenase 1	Homo sapiens	136-140
16624973-9	2006	c-Jun NH2-terminal kinase (JNK) was found to be activated by salicylate, and we could causally link this activation to the induction of HO-1 by using the JNK inhibitor 1,9-pyrazoloanthrone.	pyrazolanthrone	168-188	heme oxygenase 1	Homo sapiens	136-140
16759310-11	2006	In contrast, HO-1 gene expression was correlated negatively with p22phox, TBARS, PCO, HbA(1c) and diabetes duration.	tbars	74-79	heme oxygenase 1	Homo sapiens	13-17
16462769-7	2006	On the other hand, zinc (II) protoporphyrin IX, an HO-1 inhibitor, markedly augmented PDT-mediated cytotoxicity towards C-26 and human ovarian carcinoma MDAH2774 cells.	zinc;3-[7,12-bis(ethenyl)-18-(3-hydroperoxyprop-1-en-2-yl)-3,8,13,17-tetramethylporphyrin-21,23-diid-2-yl]propanoic acid	19-46	heme oxygenase 1	Homo sapiens	51-55
16462769-7	2006	On the other hand, zinc (II) protoporphyrin IX, an HO-1 inhibitor, markedly augmented PDT-mediated cytotoxicity towards C-26 and human ovarian carcinoma MDAH2774 cells.	C-26	120-124	heme oxygenase 1	Homo sapiens	51-55
16462769-8	2006	Neither bilirubin, biliverdin nor carbon monoxide, direct products of HO-1 catalysed heme degradation, was responsible for cytoprotection.	Heme	85-89	heme oxygenase 1	Homo sapiens	70-74
16271489-0	2006	Expression of heme oxygenase-1 due to intracellular reactive oxygen species induced by ultrasound.	Reactive Oxygen Species	52-75	heme oxygenase 1	Homo sapiens	14-30
16271489-8	2006	These results indicate that superoxide secondarily generated from damaged mitochondria, not hydroxyl radicals generated in medium directly by sonication, give rise to intracellular oxidative stress inducing HO-1 expression.	Superoxides	28-38	heme oxygenase 1	Homo sapiens	207-211
16595661-1	2006	Up-regulation of heme oxygenase (HO-1) by either cobalt protoporphyrin (CoPP) or human gene transfer improves vascular and renal function by several mechanisms, including increases in antioxidant levels and decreases in reactive oxygen species (ROS) in vascular and renal tissue.	cobaltiprotoporphyrin	49-70	heme oxygenase 1	Homo sapiens	33-37
16595661-1	2006	Up-regulation of heme oxygenase (HO-1) by either cobalt protoporphyrin (CoPP) or human gene transfer improves vascular and renal function by several mechanisms, including increases in antioxidant levels and decreases in reactive oxygen species (ROS) in vascular and renal tissue.	cobaltiprotoporphyrin	72-76	heme oxygenase 1	Homo sapiens	33-37
16595661-1	2006	Up-regulation of heme oxygenase (HO-1) by either cobalt protoporphyrin (CoPP) or human gene transfer improves vascular and renal function by several mechanisms, including increases in antioxidant levels and decreases in reactive oxygen species (ROS) in vascular and renal tissue.	Reactive Oxygen Species	220-243	heme oxygenase 1	Homo sapiens	33-37
16595661-1	2006	Up-regulation of heme oxygenase (HO-1) by either cobalt protoporphyrin (CoPP) or human gene transfer improves vascular and renal function by several mechanisms, including increases in antioxidant levels and decreases in reactive oxygen species (ROS) in vascular and renal tissue.	Reactive Oxygen Species	245-248	heme oxygenase 1	Homo sapiens	33-37
16595661-8	2006	Human HO-1 cDNA transfer into diabetic rats increased both HO-1 protein and activity, and restored mitochondrial ADP/ATP and deoxynucleotide carriers.	Adenosine Diphosphate	113-116	heme oxygenase 1	Homo sapiens	6-10
16595661-8	2006	Human HO-1 cDNA transfer into diabetic rats increased both HO-1 protein and activity, and restored mitochondrial ADP/ATP and deoxynucleotide carriers.	Adenosine Triphosphate	117-120	heme oxygenase 1	Homo sapiens	6-10
16678019-0	2006	Heme oxygenase-1 attenuates the cisplatin-induced apoptosis of auditory cells via down-regulation of reactive oxygen species generation.	Cisplatin	32-41	heme oxygenase 1	Homo sapiens	0-16
16528678-1	2006	Heme oxygenase (HO)-1 is the inducible isoform of the first and rate-controlling enzyme of heme degradation.	Heme	91-95	heme oxygenase 1	Homo sapiens	0-21
16728265-2	2006	In honor of my dear friend and colleague, Prof. Dr. Jon van Rood, I summarize here our work in this area making use of heme oxygenase-1 (HO-1) and the products that degradation of heme by HO-1 generates.	Heme	119-123	heme oxygenase 1	Homo sapiens	137-141
16728265-2	2006	In honor of my dear friend and colleague, Prof. Dr. Jon van Rood, I summarize here our work in this area making use of heme oxygenase-1 (HO-1) and the products that degradation of heme by HO-1 generates.	Heme	119-123	heme oxygenase 1	Homo sapiens	188-192
16378625-0	2006	Upregulation of heme oxygenase-1 by Epigallocatechin-3-gallate via the phosphatidylinositol 3-kinase/Akt and ERK pathways.	epigallocatechin gallate	36-62	heme oxygenase 1	Homo sapiens	16-32
16378625-1	2006	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by various phytochemicals and we examined the ability of Epigallocatechin-3-gallate (EGCG), the major constituent of green tea, to upregulate HO-1 expression in endothelial cells (ECs).	epigallocatechin gallate	118-144	heme oxygenase 1	Homo sapiens	0-16
16378625-1	2006	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by various phytochemicals and we examined the ability of Epigallocatechin-3-gallate (EGCG), the major constituent of green tea, to upregulate HO-1 expression in endothelial cells (ECs).	epigallocatechin gallate	118-144	heme oxygenase 1	Homo sapiens	18-22
16678019-0	2006	Heme oxygenase-1 attenuates the cisplatin-induced apoptosis of auditory cells via down-regulation of reactive oxygen species generation.	Reactive Oxygen Species	101-124	heme oxygenase 1	Homo sapiens	0-16
16678019-3	2006	Herein, we demonstrate that pharmacologic induction of HO-1 along with catalytic activation significantly suppressed apoptosis of HEI-OC1 cells induced by cisplatin.	Cisplatin	155-164	heme oxygenase 1	Homo sapiens	55-59
16678019-4	2006	Studies of ectopic expression of pcDNA3-HO-1 and siRNA of HO-1 further revealed the protective role of HO-1 against cisplatin in HEI-OC1 cells.	Cisplatin	116-125	heme oxygenase 1	Homo sapiens	58-62
16678019-4	2006	Studies of ectopic expression of pcDNA3-HO-1 and siRNA of HO-1 further revealed the protective role of HO-1 against cisplatin in HEI-OC1 cells.	Cisplatin	116-125	heme oxygenase 1	Homo sapiens	58-62
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Carbon Monoxide	46-61	heme oxygenase 1	Homo sapiens	35-39
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Carbon Monoxide	46-61	heme oxygenase 1	Homo sapiens	130-134
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Carbon Monoxide	63-65	heme oxygenase 1	Homo sapiens	35-39
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Carbon Monoxide	63-65	heme oxygenase 1	Homo sapiens	130-134
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Bilirubin	71-80	heme oxygenase 1	Homo sapiens	35-39
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Bilirubin	71-80	heme oxygenase 1	Homo sapiens	130-134
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Cisplatin	143-152	heme oxygenase 1	Homo sapiens	35-39
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Cisplatin	143-152	heme oxygenase 1	Homo sapiens	130-134
16495208-0	2006	The interaction of nitric oxide with distinct hemoglobins differentially amplifies endothelial heme uptake and heme oxygenase-1 expression.	Nitric Oxide	19-31	heme oxygenase 1	Homo sapiens	111-127
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Heme	0-4	heme oxygenase 1	Homo sapiens	61-77
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Heme	0-4	heme oxygenase 1	Homo sapiens	79-83
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Carbon Monoxide	101-116	heme oxygenase 1	Homo sapiens	61-77
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Carbon Monoxide	101-116	heme oxygenase 1	Homo sapiens	79-83
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Iron	118-122	heme oxygenase 1	Homo sapiens	61-77
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Iron	118-122	heme oxygenase 1	Homo sapiens	79-83
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Bilirubin	128-137	heme oxygenase 1	Homo sapiens	61-77
16495208-1	2006	Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin.	Bilirubin	128-137	heme oxygenase 1	Homo sapiens	79-83
16495208-2	2006	We have reported recently that nitric oxide (NO) augments the incorporation of free hemin in endothelial cells, resulting in amplified HO-1 expression and production of bilirubin.	Nitric Oxide	31-43	heme oxygenase 1	Homo sapiens	135-139
16495208-2	2006	We have reported recently that nitric oxide (NO) augments the incorporation of free hemin in endothelial cells, resulting in amplified HO-1 expression and production of bilirubin.	Hemin	84-89	heme oxygenase 1	Homo sapiens	135-139
16495208-7	2006	In conclusion, our data indicate a novel role for NO in the modulation of heme transport and HO-1 induction in endothelial cells, which may be relevant for hematological disorders characterized by disruption of the heme-NO equilibrium.	Heme	215-219	heme oxygenase 1	Homo sapiens	93-97
16378625-1	2006	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by various phytochemicals and we examined the ability of Epigallocatechin-3-gallate (EGCG), the major constituent of green tea, to upregulate HO-1 expression in endothelial cells (ECs).	epigallocatechin gallate	118-144	heme oxygenase 1	Homo sapiens	203-207
16378625-1	2006	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by various phytochemicals and we examined the ability of Epigallocatechin-3-gallate (EGCG), the major constituent of green tea, to upregulate HO-1 expression in endothelial cells (ECs).	epigallocatechin gallate	146-150	heme oxygenase 1	Homo sapiens	0-16
16378625-1	2006	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by various phytochemicals and we examined the ability of Epigallocatechin-3-gallate (EGCG), the major constituent of green tea, to upregulate HO-1 expression in endothelial cells (ECs).	epigallocatechin gallate	146-150	heme oxygenase 1	Homo sapiens	18-22
16378625-2	2006	We demonstrate that EGCG induces HO-1 expression in a concentration- and time-dependent manner.	epigallocatechin gallate	20-24	heme oxygenase 1	Homo sapiens	33-37
16378625-3	2006	Furthermore, EGCG-mediated HO-1 induction was abrogated in the presence of actinomycin D and cycloheximide, indicating that this upregulation of HO-1 occurred at the transcriptional level.	epigallocatechin gallate	13-17	heme oxygenase 1	Homo sapiens	27-31
16378625-3	2006	Furthermore, EGCG-mediated HO-1 induction was abrogated in the presence of actinomycin D and cycloheximide, indicating that this upregulation of HO-1 occurred at the transcriptional level.	epigallocatechin gallate	13-17	heme oxygenase 1	Homo sapiens	145-149
16378625-3	2006	Furthermore, EGCG-mediated HO-1 induction was abrogated in the presence of actinomycin D and cycloheximide, indicating that this upregulation of HO-1 occurred at the transcriptional level.	Dactinomycin	75-88	heme oxygenase 1	Homo sapiens	27-31
16378625-3	2006	Furthermore, EGCG-mediated HO-1 induction was abrogated in the presence of actinomycin D and cycloheximide, indicating that this upregulation of HO-1 occurred at the transcriptional level.	Dactinomycin	75-88	heme oxygenase 1	Homo sapiens	145-149
16378625-3	2006	Furthermore, EGCG-mediated HO-1 induction was abrogated in the presence of actinomycin D and cycloheximide, indicating that this upregulation of HO-1 occurred at the transcriptional level.	Cycloheximide	93-106	heme oxygenase 1	Homo sapiens	27-31
16378625-3	2006	Furthermore, EGCG-mediated HO-1 induction was abrogated in the presence of actinomycin D and cycloheximide, indicating that this upregulation of HO-1 occurred at the transcriptional level.	Cycloheximide	93-106	heme oxygenase 1	Homo sapiens	145-149
16378625-5	2006	Furthermore, EGCG is the most potent inducer of HO-1 expression of the different green tea constituents that we analyzed, but had no detectable cytotoxic effects over the 25-100 microM dosage range.	epigallocatechin gallate	13-17	heme oxygenase 1	Homo sapiens	48-52
16378625-7	2006	In addition, we determined that tyrosine kinase is involved in EGCG induction of HO-1 as this is abrogated by genistein.	epigallocatechin gallate	63-67	heme oxygenase 1	Homo sapiens	81-85
16378625-7	2006	In addition, we determined that tyrosine kinase is involved in EGCG induction of HO-1 as this is abrogated by genistein.	Genistein	110-119	heme oxygenase 1	Homo sapiens	81-85
16378625-9	2006	In addition, pharmacological inhibitors of phosphatidylinositol 3-kinase and MEK1/2, which are upstream of Akt and ERK1/2, respectively, attenuate EGCG-induced HO-1 expression.	epigallocatechin gallate	147-151	heme oxygenase 1	Homo sapiens	160-164
16378625-10	2006	On the other hand, pretreatment of these cells with EGCG exerts significant cytoprotective effects against H2O2, suggesting that the induction of HO-1 is an important component in the protection against oxidative stress.	epigallocatechin gallate	52-56	heme oxygenase 1	Homo sapiens	146-150
16378625-10	2006	On the other hand, pretreatment of these cells with EGCG exerts significant cytoprotective effects against H2O2, suggesting that the induction of HO-1 is an important component in the protection against oxidative stress.	Hydrogen Peroxide	107-111	heme oxygenase 1	Homo sapiens	146-150
16378625-11	2006	Hence, EGCG is a novel phytochemical inducer of HO-1 expression and we further identify the principal underlying mechanisms involved in this process.	epigallocatechin gallate	7-11	heme oxygenase 1	Homo sapiens	48-52
16574070-0	2006	Carbon monoxide mediates heme oxygenase 1 induction via Nrf2 activation in hepatoma cells.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	25-41
16574070-7	2006	Taken together, we suggest that CO induces Nrf2 activation via MAPKs signaling pathways, thereby resulting in HO1 expression in HepG2 cells.	Carbon Monoxide	32-34	heme oxygenase 1	Homo sapiens	110-113
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Reactive Oxygen Species	175-198	heme oxygenase 1	Homo sapiens	35-39
16678019-5	2006	Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation.	Reactive Oxygen Species	175-198	heme oxygenase 1	Homo sapiens	130-134
16651638-5	2006	Inhibition of ERK activation with MEK inhibitors (PD98059 or U0126) diminished induction of the antioxidant enzyme heme oxygenase-1.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	50-57	heme oxygenase 1	Homo sapiens	115-131
16651615-7	2006	In steatotic livers, preconditioning and geranylgeranylacetone treatment (which are responsible for HO-1 induction) increased protein kinase C activity.	geranylgeranylacetone	41-62	heme oxygenase 1	Homo sapiens	100-104
16651638-5	2006	Inhibition of ERK activation with MEK inhibitors (PD98059 or U0126) diminished induction of the antioxidant enzyme heme oxygenase-1.	U 0126	61-66	heme oxygenase 1	Homo sapiens	115-131
16651615-8	2006	HO-1 activators (cobalt(III) protoporphyrin IX) protected both liver types.	cobaltiprotoporphyrin	17-46	heme oxygenase 1	Homo sapiens	0-4
16607117-5	2006	RECENT FINDINGS: Recent studies indicate glutamine induces heat shock protein-70, HO-1 (heat shock protein-32), and heat shock protein-27 in models of illness/injury.	Glutamine	41-50	heme oxygenase 1	Homo sapiens	82-86
16476737-1	2006	Heme oxygenase-1 (HO-1), the inducible enzyme responsible for the rate-limiting step in the heme catabolism, is expressed in AIDS-Kaposi sarcoma (KS) lesions.	Heme	92-96	heme oxygenase 1	Homo sapiens	0-16
16737592-0	2006	[Experimental research on antagonistic effect of heme oxygenase-1 on acute mercury chloride induced renal impairment].	calomel	75-91	heme oxygenase 1	Homo sapiens	49-65
16476785-1	2006	Nitric oxide (NO) and NO donors were among the first reported inducers of the tissue-protective protein heme oxygenase-1 (HO-1) with a potential for eventual use in humans.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	104-120
16476785-1	2006	Nitric oxide (NO) and NO donors were among the first reported inducers of the tissue-protective protein heme oxygenase-1 (HO-1) with a potential for eventual use in humans.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	122-126
16476785-2	2006	Besides other clinically established NO releasing drugs, sodium nitroprusside (SNP) has frequently been employed as an experimental tool to explore effects of NO on HO-1 and other biological targets.	Nitroprusside	57-77	heme oxygenase 1	Homo sapiens	165-169
16476785-4	2006	(p. 1633) demonstrate that the effects of SNP on expression of HO-1 are mainly due to free iron released from SNP in aqueous solution, whereas NO plays a negligible role, if any, as the mediator of response to SNP.	Iron	91-95	heme oxygenase 1	Homo sapiens	63-67
16476785-5	2006	Downstream effects of iron, after being dissociated from SNP, include increases in intracellular cAMP that are causally linked to subsequent phosphorylation of specific MAPK targets and enhanced HO-1 protein levels.	Iron	22-26	heme oxygenase 1	Homo sapiens	195-199
16476785-5	2006	Downstream effects of iron, after being dissociated from SNP, include increases in intracellular cAMP that are causally linked to subsequent phosphorylation of specific MAPK targets and enhanced HO-1 protein levels.	Cyclic AMP	97-101	heme oxygenase 1	Homo sapiens	195-199
16476737-1	2006	Heme oxygenase-1 (HO-1), the inducible enzyme responsible for the rate-limiting step in the heme catabolism, is expressed in AIDS-Kaposi sarcoma (KS) lesions.	Heme	92-96	heme oxygenase 1	Homo sapiens	18-22
16476737-3	2006	In this study we investigated whether the oncogenic G protein-coupled receptor (KSHV-GPCR or vGPCR), one of the key KSHV genes involved in KS development, activated HO-1 expression.	ks	80-82	heme oxygenase 1	Homo sapiens	165-169
16476737-5	2006	Moreover, targeted knock-down gene expression of HO-1 by small hairpin RNA and chemical inhibition of HO-1 enzymatic activity by tin protoporphyrin IX (SnPP), impaired vGPCR-induced survival, proliferation, transformation, and vascular endothelial growth factor (VEGF)-A expression.	tin protoporphyrin IX	129-150	heme oxygenase 1	Homo sapiens	102-106
16476737-5	2006	Moreover, targeted knock-down gene expression of HO-1 by small hairpin RNA and chemical inhibition of HO-1 enzymatic activity by tin protoporphyrin IX (SnPP), impaired vGPCR-induced survival, proliferation, transformation, and vascular endothelial growth factor (VEGF)-A expression.	S-Nitroso-N-propionyl-D,L-penicillamine	152-156	heme oxygenase 1	Homo sapiens	102-106
16476737-8	2006	On the contrary, administration of the HO-1 inducer cobalt protoporphyrin (CoPP) further enhanced vGPCR-induced tumor growth.	cobaltiprotoporphyrin	52-73	heme oxygenase 1	Homo sapiens	39-43
16476737-8	2006	On the contrary, administration of the HO-1 inducer cobalt protoporphyrin (CoPP) further enhanced vGPCR-induced tumor growth.	cobaltiprotoporphyrin	75-79	heme oxygenase 1	Homo sapiens	39-43
16631521-0	2006	Heme oxygenase-1 contributes to the cytoprotection of alpha-lipoic acid via activation of p44/42 mitogen-activated protein kinase in vascular smooth muscle cells.	Thioctic Acid	54-71	heme oxygenase 1	Homo sapiens	0-16
16636651-7	2006	In addition, expression levels of three other important antioxidant genes, heme oxygenase-1, thioredoxin reductase-1, and manganese superoxide dismutase were monitored by real-time RT-PCR following exposure to TBHP.	tert-Butylhydroperoxide	210-214	heme oxygenase 1	Homo sapiens	75-91
16636651-12	2006	In addition, TBHP induced the expression of MTIIa, heme oxygenase-1, thioredoxin reductase-1, and MnSOD in both normal and MTIIa over-expressed cell lines.	tert-Butylhydroperoxide	13-17	heme oxygenase 1	Homo sapiens	51-67
16631521-4	2006	ALA significantly induced HO-1 expression accompanied by an increase in HO activity in A10 cells.	Thioctic Acid	0-3	heme oxygenase 1	Homo sapiens	26-30
16631525-2	2006	We have earlier shown that a novel antioxidant from the bamboo leaves constituent 3-O-caffeoyl-1-methylquinic acid (MCGA3) induces heme oxygenase-1 (HO-1) and protects endothelial cells from ROS-induced endothelial injury.	3-O-caffeoyl-1-methylquinic acid	82-114	heme oxygenase 1	Homo sapiens	131-147
16631525-2	2006	We have earlier shown that a novel antioxidant from the bamboo leaves constituent 3-O-caffeoyl-1-methylquinic acid (MCGA3) induces heme oxygenase-1 (HO-1) and protects endothelial cells from ROS-induced endothelial injury.	3-O-caffeoyl-1-methylquinic acid	82-114	heme oxygenase 1	Homo sapiens	149-153
16631521-7	2006	ALA significantly increased ROS, and this effect was blocked by N-acetyl-cysteine, which also inhibited ALA-induced activation of p44/42 mitogen-activated protein kinase (MAPK) and AP-1, HO-1 expression, and HO activity.	Thioctic Acid	0-3	heme oxygenase 1	Homo sapiens	187-191
16631525-7	2006	By employing N-acetylcysteine and GSH biosynthetic enzyme inhibitors as well as prooxidants, hemin and H(2)O(2), we show that a decreased intracellular GSH/GSSG homeostasis, at least in part, may be involved in the MCGA3-mediated phase II gene induction and Nrf2 translocation, although the attenuation of HO-1 expression with SP 600125 supports a partial involvement of JNK signaling.	Glutathione	152-155	heme oxygenase 1	Homo sapiens	306-310
16631521-7	2006	ALA significantly increased ROS, and this effect was blocked by N-acetyl-cysteine, which also inhibited ALA-induced activation of p44/42 mitogen-activated protein kinase (MAPK) and AP-1, HO-1 expression, and HO activity.	Acetylcysteine	64-81	heme oxygenase 1	Homo sapiens	187-191
16631525-7	2006	By employing N-acetylcysteine and GSH biosynthetic enzyme inhibitors as well as prooxidants, hemin and H(2)O(2), we show that a decreased intracellular GSH/GSSG homeostasis, at least in part, may be involved in the MCGA3-mediated phase II gene induction and Nrf2 translocation, although the attenuation of HO-1 expression with SP 600125 supports a partial involvement of JNK signaling.	Glutathione Disulfide	156-160	heme oxygenase 1	Homo sapiens	306-310
16631521-7	2006	ALA significantly increased ROS, and this effect was blocked by N-acetyl-cysteine, which also inhibited ALA-induced activation of p44/42 mitogen-activated protein kinase (MAPK) and AP-1, HO-1 expression, and HO activity.	Thioctic Acid	104-107	heme oxygenase 1	Homo sapiens	187-191
16631521-8	2006	These results suggest that ALA induces HO-1 expression through the production of ROS and subsequent activation of the p44/42 MAPK pathway and AP-1 in vascular smooth muscle cells.	Thioctic Acid	27-30	heme oxygenase 1	Homo sapiens	39-43
16631521-8	2006	These results suggest that ALA induces HO-1 expression through the production of ROS and subsequent activation of the p44/42 MAPK pathway and AP-1 in vascular smooth muscle cells.	Reactive Oxygen Species	81-84	heme oxygenase 1	Homo sapiens	39-43
16631521-9	2006	This study demonstrated that ALA increases the expression of HO-1, a critical cytoprotective molecule, and identified a novel pleiotropic effect of ALA on cardiovascular protection.	Thioctic Acid	29-32	heme oxygenase 1	Homo sapiens	61-65
16631522-7	2006	Intracellular free iron determined with the fluorescent probe calcein rose to approximately 160% of the control level 6 h after SPNO, but declined to approximately 70% after 24 h. Immunoblot analyses revealed a rapid early (approximately 2 h post-NO) increase in heme oxygenase-1 level, followed by a gradual (4-20 h post-NO) increase in ferritin.	Iron	19-23	heme oxygenase 1	Homo sapiens	263-279
16759519-9	2006	RESULTS: After stimulation of glucose the insulin concentration in the supernatant of the Ad-HO-1 group was 270 mIU/L +/- 89 mIU/L, significantly higher than those of the Ad-EGFP group (189 mIU/L +/- 88 mIU/L) and control group (182 mIU/L +/- 59 mIU/L, both P &lt; 0.05).	Glucose	30-37	heme oxygenase 1	Homo sapiens	93-97
16572448-1	2006	OBJECTIVE: To examine the expression and pathogenetic roles of heme oxygenase 1 (HO-1), an inducible heme-degrading enzyme with antiinflammatory properties, in rheumatoid arthritis (RA).	Heme	63-67	heme oxygenase 1	Homo sapiens	81-85
16531144-0	2006	The effect of heme oxygenase-1 induction by glutamine on radiation-induced intestinal damage: the effect of heme oxygenase-1 on radiation enteritis.	Glutamine	44-53	heme oxygenase 1	Homo sapiens	14-30
16531144-5	2006	The present study was undertaken to investigate the effect of glutamine administration on heme oxygenase-1 (HO-1) expression of the radiation enteritis model.	Glutamine	62-71	heme oxygenase 1	Homo sapiens	90-106
16531144-5	2006	The present study was undertaken to investigate the effect of glutamine administration on heme oxygenase-1 (HO-1) expression of the radiation enteritis model.	Glutamine	62-71	heme oxygenase 1	Homo sapiens	108-112
16531144-12	2006	Glutamine treatment was associated with increased HO-1 expression, decreased MPO activity, caspase-3 activity, and MDA levels.	Glutamine	0-9	heme oxygenase 1	Homo sapiens	50-54
16531144-13	2006	Inhibition of HO-1 activity by Zn-PP completely eliminated the protective effects of glutamine.	zn-pp	31-36	heme oxygenase 1	Homo sapiens	14-18
16531144-13	2006	Inhibition of HO-1 activity by Zn-PP completely eliminated the protective effects of glutamine.	Glutamine	85-94	heme oxygenase 1	Homo sapiens	14-18
16531144-18	2006	This protective effect is mediated in part by the induction of HO-1 activity because inhibition of Zn-PP resulted in the complete abolishment of the protective effect of glutamine.	zn-pp	99-104	heme oxygenase 1	Homo sapiens	63-67
16531144-18	2006	This protective effect is mediated in part by the induction of HO-1 activity because inhibition of Zn-PP resulted in the complete abolishment of the protective effect of glutamine.	Glutamine	170-179	heme oxygenase 1	Homo sapiens	63-67
16572448-6	2006	Hemin, auranofin, and HO-1 expression vector induced HO-1 and reduced expression of tumor necrosis factor alpha (TNFalpha) messenger RNA, lipopolysaccharide (LPS)-induced secretion of interleukin-6 (IL-6) and IL-8, and expression of cyclooxygenase 2 in the synovial cell lines.	Auranofin	7-16	heme oxygenase 1	Homo sapiens	53-57
16572448-7	2006	Treatment with HO-1-specific siRNA augmented the synthesis of TNFalpha, IL-6, and IL-8 and canceled the suppressive effects of auranofin on TNFalpha secretion.	Auranofin	127-136	heme oxygenase 1	Homo sapiens	15-19
16572448-10	2006	The pharmacologic effects of auranofin depend, in part, on the levels of HO-1, suggesting that HO-1 induction is a novel therapeutic strategy for RA.	Auranofin	29-38	heme oxygenase 1	Homo sapiens	73-77
16572448-10	2006	The pharmacologic effects of auranofin depend, in part, on the levels of HO-1, suggesting that HO-1 induction is a novel therapeutic strategy for RA.	Auranofin	29-38	heme oxygenase 1	Homo sapiens	95-99
16601269-1	2006	The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO).	Carbon Monoxide	271-286	heme oxygenase 1	Homo sapiens	75-79
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Heme	48-52	heme oxygenase 1	Homo sapiens	95-111
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Heme	48-52	heme oxygenase 1	Homo sapiens	113-117
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Carbon Monoxide	122-137	heme oxygenase 1	Homo sapiens	95-111
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Carbon Monoxide	122-137	heme oxygenase 1	Homo sapiens	113-117
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Iron	139-143	heme oxygenase 1	Homo sapiens	95-111
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Iron	139-143	heme oxygenase 1	Homo sapiens	113-117
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Biliverdine	149-159	heme oxygenase 1	Homo sapiens	95-111
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Biliverdine	149-159	heme oxygenase 1	Homo sapiens	113-117
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Bilirubin	185-194	heme oxygenase 1	Homo sapiens	95-111
16545694-1	2006	BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin.	Bilirubin	185-194	heme oxygenase 1	Homo sapiens	113-117
16545694-3	2006	RESULTS: Treatment of HaCaT keratinocytes with hemin (heme chloride) induced HO-1 expression and activity.	Hemin	47-52	heme oxygenase 1	Homo sapiens	77-81
16545694-3	2006	RESULTS: Treatment of HaCaT keratinocytes with hemin (heme chloride) induced HO-1 expression and activity.	heme chloride	54-67	heme oxygenase 1	Homo sapiens	77-81
16545694-5	2006	The involvement of HO-1 in VEGF synthesis was confirmed by inhibition of VEGF expression by SnPPIX, a blocker of HO activity and by attenuation of HO-1 mRNA expression with specific siRNA.	tin protoporphyrin IX	92-98	heme oxygenase 1	Homo sapiens	19-23
16545694-6	2006	Importantly, induction of HO-1 by hemin was able to overcome the inhibitory effect of high glucose on VEGF synthesis.	Glucose	91-98	heme oxygenase 1	Homo sapiens	26-30
16545694-7	2006	Moreover, HO-1 expression was also induced in keratinocytes cultured in hypoxia, with concomitant augmentation of VEGF production, which was further potentiated by hemin stimulation.	Hemin	164-169	heme oxygenase 1	Homo sapiens	10-14
16545694-9	2006	CONCLUSIONS: HO-1 is involved in hemin-induced VEGF expression in HaCaT and may play a role in hypoxic regulation of this protein.	Hemin	33-38	heme oxygenase 1	Homo sapiens	13-17
16547262-7	2006	Suppression of HIV replication in hemin-activated cells correlated with the induction of HO-1 and was attenuated by tin protoporphyrin (SnPP) IX, an inhibitor of HO-1 activity, suggesting a pivotal role of this endogenous enzyme in the regulation of HIV infection.	tin protoporphyrin IX	116-134	heme oxygenase 1	Homo sapiens	162-166
16547262-7	2006	Suppression of HIV replication in hemin-activated cells correlated with the induction of HO-1 and was attenuated by tin protoporphyrin (SnPP) IX, an inhibitor of HO-1 activity, suggesting a pivotal role of this endogenous enzyme in the regulation of HIV infection.	S-Nitroso-N-propionyl-D,L-penicillamine	136-140	heme oxygenase 1	Homo sapiens	162-166
16601269-1	2006	The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO).	Heme	4-8	heme oxygenase 1	Homo sapiens	75-79
16601269-1	2006	The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO).	Biliverdine	184-194	heme oxygenase 1	Homo sapiens	75-79
16601269-1	2006	The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO).	Bilirubin	199-208	heme oxygenase 1	Homo sapiens	75-79
16601269-1	2006	The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO).	Iron	262-266	heme oxygenase 1	Homo sapiens	75-79
16473885-4	2006	Similarly, long-term survival induced by DST was ablated when HO-1 activity was blocked by zinc protoporphyrin IX (ZnPPIX).	zinc protoporphyrin	91-113	heme oxygenase 1	Homo sapiens	62-66
16473885-4	2006	Similarly, long-term survival induced by DST was ablated when HO-1 activity was blocked by zinc protoporphyrin IX (ZnPPIX).	zinc protoporphyrin	115-121	heme oxygenase 1	Homo sapiens	62-66
16473885-7	2006	However, long-term survival and (dominant peripheral) tolerance were readily induced when DST was combined with induction of HO-1 expression by cobalt protoporphyrin IX (CoPPIX).	cobaltiprotoporphyrin	144-168	heme oxygenase 1	Homo sapiens	125-129
16473885-7	2006	However, long-term survival and (dominant peripheral) tolerance were readily induced when DST was combined with induction of HO-1 expression by cobalt protoporphyrin IX (CoPPIX).	cobaltiprotoporphyrin	170-176	heme oxygenase 1	Homo sapiens	125-129
16704082-3	2006	The expression of HO-1 in dental pulp was detected by means of SABC immunohistochemical technology.	sabc	63-67	heme oxygenase 1	Homo sapiens	18-22
16601269-1	2006	The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO).	Carbon Monoxide	288-290	heme oxygenase 1	Homo sapiens	75-79
16537525-5	2006	This induction of HO-1 occurred within clinical LNO(2) concentration ranges, far exceeded responses to equimolar amounts of linoleic acid and oxidized linoleic acid, and rivaled that induced by hemin.	Linoleic Acid	124-137	heme oxygenase 1	Homo sapiens	18-22
16582079-3	2006	A (GT)(n) dinucleotide repeat in the human HO-1 promoter modulates HO-1 gene expression and shows length polymorphism, which is grouped into three classes: class S (&lt;27 repeats), class M (&gt; or = 27, &lt;33 repeats), and class L (&gt; or = 33 repeats) alleles.	(n) dinucleotide	6-22	heme oxygenase 1	Homo sapiens	43-47
16582079-3	2006	A (GT)(n) dinucleotide repeat in the human HO-1 promoter modulates HO-1 gene expression and shows length polymorphism, which is grouped into three classes: class S (&lt;27 repeats), class M (&gt; or = 27, &lt;33 repeats), and class L (&gt; or = 33 repeats) alleles.	(n) dinucleotide	6-22	heme oxygenase 1	Homo sapiens	67-71
16460683-4	2006	Curcumin increased HO-1 and glutamyl cysteine ligase modulator (GCLM) expression and stimulated Nrf2 binding to the ARE.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	19-23
16460683-5	2006	Curcumin also rapidly stimulated PKC phosphorylation and Ro-31-8220, a pan-PKC inhibitor, decreased curcumin-induced GCLM and HO-1 mRNA expression and ARE binding.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	126-130
16460683-5	2006	Curcumin also rapidly stimulated PKC phosphorylation and Ro-31-8220, a pan-PKC inhibitor, decreased curcumin-induced GCLM and HO-1 mRNA expression and ARE binding.	Curcumin	100-108	heme oxygenase 1	Homo sapiens	126-130
16460683-6	2006	Rottlerin (a PKC delta inhibitor) and PKC delta antisense oligonucleotides significantly inhibited curcumin-induced GCLM and HO-1 mRNA expression and ARE binding.	rottlerin	0-9	heme oxygenase 1	Homo sapiens	125-129
16460683-6	2006	Rottlerin (a PKC delta inhibitor) and PKC delta antisense oligonucleotides significantly inhibited curcumin-induced GCLM and HO-1 mRNA expression and ARE binding.	Oligonucleotides	58-74	heme oxygenase 1	Homo sapiens	125-129
16460683-6	2006	Rottlerin (a PKC delta inhibitor) and PKC delta antisense oligonucleotides significantly inhibited curcumin-induced GCLM and HO-1 mRNA expression and ARE binding.	Curcumin	99-107	heme oxygenase 1	Homo sapiens	125-129
16537525-0	2006	Fatty acid transduction of nitric oxide signaling: nitrolinoleic acid potently activates endothelial heme oxygenase 1 expression.	Fatty Acids	0-10	heme oxygenase 1	Homo sapiens	101-117
16537525-0	2006	Fatty acid transduction of nitric oxide signaling: nitrolinoleic acid potently activates endothelial heme oxygenase 1 expression.	Nitric Oxide	27-39	heme oxygenase 1	Homo sapiens	101-117
16537525-0	2006	Fatty acid transduction of nitric oxide signaling: nitrolinoleic acid potently activates endothelial heme oxygenase 1 expression.	10-nitro-9,12-octadecadienoic acid	51-69	heme oxygenase 1	Homo sapiens	101-117
16537525-5	2006	This induction of HO-1 occurred within clinical LNO(2) concentration ranges, far exceeded responses to equimolar amounts of linoleic acid and oxidized linoleic acid, and rivaled that induced by hemin.	L-Leucyl-Hydroxylamine	48-51	heme oxygenase 1	Homo sapiens	18-22
16537525-5	2006	This induction of HO-1 occurred within clinical LNO(2) concentration ranges, far exceeded responses to equimolar amounts of linoleic acid and oxidized linoleic acid, and rivaled that induced by hemin.	Linoleic Acid	151-164	heme oxygenase 1	Homo sapiens	18-22
16537525-7	2006	Actinomycin D inhibited LNO(2) induction of HO-1 in human aortic endothelial cells, and LNO(2) activated a 4.5-kb human HO-1 promoter construct, indicating transcriptional regulation of the HO-1 gene.	Dactinomycin	0-13	heme oxygenase 1	Homo sapiens	44-48
16537525-7	2006	Actinomycin D inhibited LNO(2) induction of HO-1 in human aortic endothelial cells, and LNO(2) activated a 4.5-kb human HO-1 promoter construct, indicating transcriptional regulation of the HO-1 gene.	L-Leucyl-Hydroxylamine	24-27	heme oxygenase 1	Homo sapiens	44-48
16537525-9	2006	The NO scavengers 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide and oxymyoglobin partially reversed induction of HO-1 by LNO(2), revealing that LNO(2) regulates HO-1 expression by predominantly NO-independent mechanisms.	1,3-dihydroxy-4,4,5,5-tetramethyl-2-(4-carboxyphenyl)tetrahydroimidazole	18-83	heme oxygenase 1	Homo sapiens	133-137
16537525-9	2006	The NO scavengers 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide and oxymyoglobin partially reversed induction of HO-1 by LNO(2), revealing that LNO(2) regulates HO-1 expression by predominantly NO-independent mechanisms.	L-Leucyl-Hydroxylamine	141-144	heme oxygenase 1	Homo sapiens	133-137
16537525-9	2006	The NO scavengers 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide and oxymyoglobin partially reversed induction of HO-1 by LNO(2), revealing that LNO(2) regulates HO-1 expression by predominantly NO-independent mechanisms.	L-Leucyl-Hydroxylamine	141-144	heme oxygenase 1	Homo sapiens	181-185
16537525-10	2006	In summary, the metabolic and inflammatory signaling actions of nitroalkenes can be transduced by robust HO-1 induction.	nitroalkenes	64-76	heme oxygenase 1	Homo sapiens	105-109
16468956-5	2006	Therefore, we examined the impact of donor treatment with the selective inducer of HO-1, cobalt protoporphyrin (CoPP), on organ quality and transplant outcome in a standardized BD model in a F344--&gt;LEW kidney transplant rat model.	cobaltiprotoporphyrin	89-110	heme oxygenase 1	Homo sapiens	83-87
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Heme	115-119	heme oxygenase 1	Homo sapiens	0-16
16468956-5	2006	Therefore, we examined the impact of donor treatment with the selective inducer of HO-1, cobalt protoporphyrin (CoPP), on organ quality and transplant outcome in a standardized BD model in a F344--&gt;LEW kidney transplant rat model.	cobaltiprotoporphyrin	112-116	heme oxygenase 1	Homo sapiens	83-87
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Heme	115-119	heme oxygenase 1	Homo sapiens	18-22
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Biliverdine	158-168	heme oxygenase 1	Homo sapiens	0-16
16468956-6	2006	Immediately after BD induction, donor animals were administered a single dose of CoPP (5 mg/kg) and in control groups, HO-1 activity was blocked with zinc protoporphyrin (ZnPP, 20 mg/kg).	zinc protoporphyrin	150-169	heme oxygenase 1	Homo sapiens	119-123
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Biliverdine	158-168	heme oxygenase 1	Homo sapiens	18-22
16468956-6	2006	Immediately after BD induction, donor animals were administered a single dose of CoPP (5 mg/kg) and in control groups, HO-1 activity was blocked with zinc protoporphyrin (ZnPP, 20 mg/kg).	zinc protoporphyrin	171-175	heme oxygenase 1	Homo sapiens	119-123
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Biliverdine	170-172	heme oxygenase 1	Homo sapiens	0-16
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Biliverdine	170-172	heme oxygenase 1	Homo sapiens	18-22
16468956-8	2006	Blockade of HO-1 with ZnPP decreased the survival rates (p &lt; 0.05) comparable to untreated brain-dead donors.	zinc protoporphyrin	22-26	heme oxygenase 1	Homo sapiens	12-16
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Carbon Monoxide	175-190	heme oxygenase 1	Homo sapiens	0-16
16677090-5	2006	Of the various HSPs, heme oxygenase-I (HO-1), by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	84-99	heme oxygenase 1	Homo sapiens	39-43
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Carbon Monoxide	175-190	heme oxygenase 1	Homo sapiens	18-22
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Carbon Monoxide	192-194	heme oxygenase 1	Homo sapiens	0-16
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Carbon Monoxide	192-194	heme oxygenase 1	Homo sapiens	18-22
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Iron	201-205	heme oxygenase 1	Homo sapiens	0-16
16461755-1	2006	Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron.	Iron	201-205	heme oxygenase 1	Homo sapiens	18-22
16385084-4	2006	Cortical 15d-PGJ2 in Adv-COX-1-treated rats was increased by 3-fold over control, which was correlated with reduced infarct volume and activated caspase 3, and increased peroxisome proliferator activated receptor-gamma (PPARgamma) and heme oxygenase-1 (HO-1).	15-deoxy-delta(12,14)-prostaglandin J2	9-17	heme oxygenase 1	Homo sapiens	253-257
16385084-7	2006	15d-PGJ2 and rosiglitazone at low concentrations suppressed H2O2-induced rat or human neuronal apoptosis and necrosis and induced PPARgamma and HO-1 expression.	15-deoxy-delta(12,14)-prostaglandin J2	0-8	heme oxygenase 1	Homo sapiens	144-148
16557439-4	2006	The isoform hemeoxygenase-1 is inducible by oxidative stress and may mediate cytoprotection mainly attributable to endogenously produced carbon monoxide.	Carbon Monoxide	137-152	heme oxygenase 1	Homo sapiens	12-27
16385084-7	2006	15d-PGJ2 and rosiglitazone at low concentrations suppressed H2O2-induced rat or human neuronal apoptosis and necrosis and induced PPARgamma and HO-1 expression.	Rosiglitazone	13-26	heme oxygenase 1	Homo sapiens	144-148
16677090-5	2006	Of the various HSPs, heme oxygenase-I (HO-1), by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	127-136	heme oxygenase 1	Homo sapiens	39-43
27277612-6	2006	When a potent antioxidant, N-acetyl-L-cysteine, was added to the culture medium before or after sonication, the induction was attenuated, indicating that reactive oxygen species are involved in HO-1 induction.	Acetylcysteine	27-46	heme oxygenase 1	Homo sapiens	194-198
16222706-2	2006	Up-regulation of HO-1 in rat astroglia has been shown to facilitate iron sequestration by the mitochondrial compartment.	Iron	68-72	heme oxygenase 1	Homo sapiens	17-21
16222706-9	2006	Glial HO-1 hyperactivity may contribute to cellular oxidative stress, pathological iron deposition, and bioenergetic failure characteristic of degenerating and inflamed neural tissues and may constitute a rational target for therapeutic intervention in these conditions.	Iron	83-87	heme oxygenase 1	Homo sapiens	6-10
27277612-6	2006	When a potent antioxidant, N-acetyl-L-cysteine, was added to the culture medium before or after sonication, the induction was attenuated, indicating that reactive oxygen species are involved in HO-1 induction.	Reactive Oxygen Species	154-177	heme oxygenase 1	Homo sapiens	194-198
16480975-0	2006	Heme oxygenase 1 mediates anti-inflammatory effects of 2",4",6"-tris(methoxymethoxy) chalcone.	2',4',6'-tris(methoxymethoxy) chalcone	55-93	heme oxygenase 1	Homo sapiens	0-16
16386335-10	2006	The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels.	ethyl ferulate	56-60	heme oxygenase 1	Homo sapiens	151-155
16386335-10	2006	The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels.	2,2'-azobis(2-amidinopropane)	91-95	heme oxygenase 1	Homo sapiens	151-155
16386335-10	2006	The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels.	Iron	99-101	heme oxygenase 1	Homo sapiens	151-155
16386335-10	2006	The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels.	h(2)o	106-111	heme oxygenase 1	Homo sapiens	151-155
16498227-6	2006	We note the ability of Cd to elicit "oxidative stress" and to alter metal homeostasis notably of zinc which may lead to augmentation of the defense mechanisms involving induction of the antioxidant enzyme heme oxygenase-1 (HO-1) and the metal binding protein metallothionein (MT) in the kidney.	Cadmium	23-25	heme oxygenase 1	Homo sapiens	205-221
16498227-6	2006	We note the ability of Cd to elicit "oxidative stress" and to alter metal homeostasis notably of zinc which may lead to augmentation of the defense mechanisms involving induction of the antioxidant enzyme heme oxygenase-1 (HO-1) and the metal binding protein metallothionein (MT) in the kidney.	Cadmium	23-25	heme oxygenase 1	Homo sapiens	223-227
16498227-6	2006	We note the ability of Cd to elicit "oxidative stress" and to alter metal homeostasis notably of zinc which may lead to augmentation of the defense mechanisms involving induction of the antioxidant enzyme heme oxygenase-1 (HO-1) and the metal binding protein metallothionein (MT) in the kidney.	Metals	68-73	heme oxygenase 1	Homo sapiens	205-221
16498227-6	2006	We note the ability of Cd to elicit "oxidative stress" and to alter metal homeostasis notably of zinc which may lead to augmentation of the defense mechanisms involving induction of the antioxidant enzyme heme oxygenase-1 (HO-1) and the metal binding protein metallothionein (MT) in the kidney.	Metals	68-73	heme oxygenase 1	Homo sapiens	223-227
16498227-7	2006	We hypothesize that renal Cd accumulation triggers the host responses mediated by HO-1 and MT in an attempt to protect the kidney against injurious oxidative stress and to resist a rise in blood pressure levels.	Cadmium	26-28	heme oxygenase 1	Homo sapiens	82-93
16498227-8	2006	This hypothesis predicts that individuals with less active HO-1 (caused by the HO-1 genetic polymorphisms) are more likely to have renal injury and express a hypertensive phenotype following chronic ingestion of low-level Cd, compared with those having more active HO-1.	Cadmium	222-224	heme oxygenase 1	Homo sapiens	59-63
16498227-8	2006	This hypothesis predicts that individuals with less active HO-1 (caused by the HO-1 genetic polymorphisms) are more likely to have renal injury and express a hypertensive phenotype following chronic ingestion of low-level Cd, compared with those having more active HO-1.	Cadmium	222-224	heme oxygenase 1	Homo sapiens	79-83
16498227-8	2006	This hypothesis predicts that individuals with less active HO-1 (caused by the HO-1 genetic polymorphisms) are more likely to have renal injury and express a hypertensive phenotype following chronic ingestion of low-level Cd, compared with those having more active HO-1.	Cadmium	222-224	heme oxygenase 1	Homo sapiens	79-83
16495813-5	2006	Pretreatment with curcumin protected hepatocytes in a model of oxidative injury and this protection was mediated through HO-1.	Curcumin	18-26	heme oxygenase 1	Homo sapiens	121-125
16495813-6	2006	In a model of cold preservation injury, curcumin pretreatment resulted in elevation of HO-1 throughout the cold storage and rewarming period, and was cytoprotective against oxidative injury.	Curcumin	40-48	heme oxygenase 1	Homo sapiens	87-91
16495813-7	2006	This is the first study to demonstrate that curcumin induces HO-1 in human hepatocytes, and that the protective effects of curcumin pretreatment may have clinical potential in hepatic transplantation.	Curcumin	44-52	heme oxygenase 1	Homo sapiens	61-65
16480975-2	2006	We also demonstrate that TMMC by itself is a potent inducer of heme oxygenase 1 (HO-1).	2',4',6'-tris(methoxymethoxy) chalcone	25-29	heme oxygenase 1	Homo sapiens	63-79
16480975-2	2006	We also demonstrate that TMMC by itself is a potent inducer of heme oxygenase 1 (HO-1).	2',4',6'-tris(methoxymethoxy) chalcone	25-29	heme oxygenase 1	Homo sapiens	81-85
16480975-4	2006	Treating cells with the specific p42/44 MAPK inhibitor, PD98059, blocked the TMMC-mediated induction of HO-1 and the inhibition of LPS-stimulated expression of iNOS.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	56-63	heme oxygenase 1	Homo sapiens	104-108
16480975-4	2006	Treating cells with the specific p42/44 MAPK inhibitor, PD98059, blocked the TMMC-mediated induction of HO-1 and the inhibition of LPS-stimulated expression of iNOS.	2',4',6'-tris(methoxymethoxy) chalcone	77-81	heme oxygenase 1	Homo sapiens	104-108
16480975-6	2006	Our data suggest that TMMC exerts an anti-inflammatory effect in macrophages through a mechanism that involves the induction of HO-1, which is mediated by activation of p42/44 MAPK and GSH depletion.	2',4',6'-tris(methoxymethoxy) chalcone	22-26	heme oxygenase 1	Homo sapiens	128-132
16480975-6	2006	Our data suggest that TMMC exerts an anti-inflammatory effect in macrophages through a mechanism that involves the induction of HO-1, which is mediated by activation of p42/44 MAPK and GSH depletion.	Glutathione	185-188	heme oxygenase 1	Homo sapiens	128-132
16495813-4	2006	This study investigates in detail the effect of curcumin on the stress-response in human hepatocytes, in particular its effect on heme oxygenase 1 (HO-1) and its cytoprotective effect.	Curcumin	48-56	heme oxygenase 1	Homo sapiens	130-146
16495813-4	2006	This study investigates in detail the effect of curcumin on the stress-response in human hepatocytes, in particular its effect on heme oxygenase 1 (HO-1) and its cytoprotective effect.	Curcumin	48-56	heme oxygenase 1	Homo sapiens	148-152
16337498-4	2006	RESULTS: HO-1 as well as ecNOS gene and protein expression significantly increased upon Carnitines incubation.	Carnitine	88-98	heme oxygenase 1	Homo sapiens	9-13
16337498-7	2006	Coincubation of C (0.5-1.0-2.0 mM), AC (0.1-0.2-0.4 mM) and PC (0.05-0.1-0.2 mM) with H2O2 further increased HO-1 gene expression and not only normalized vs. H2O2 but even increased vs. basal ecNOS mRNA.	Hydrogen Peroxide	86-90	heme oxygenase 1	Homo sapiens	109-113
16337498-9	2006	CONCLUSION: This is the first report that has utilized a molecular biological approach to demonstrate a direct stimulatory effect of Carnitines on gene and protein expression of the oxidative stress related markers HO-1 and ecNOS.	Carnitine	133-143	heme oxygenase 1	Homo sapiens	215-219
16337498-10	2006	As HO-1 and NO are known as antioxidant, antiproliferative and anti-inflammatory, their increased expression would be expected to protect from oxidative stress related cardiovascular risk factors and myocardial damage, therefore adding this effect to the multiple pathways involved in the effects of carnitines.	Carnitine	300-310	heme oxygenase 1	Homo sapiens	3-7
16329999-0	2006	CO from enhanced HO activity or from CORM-2 inhibits both O2- and NO production and downregulates HO-1 expression in LPS-stimulated macrophages.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	98-102
16243536-0	2006	Piceatannol upregulates endothelial heme oxygenase-1 expression via novel protein kinase C and tyrosine kinase pathways.	3,3',4,5'-tetrahydroxystilbene	0-11	heme oxygenase 1	Homo sapiens	36-52
16243536-3	2006	In this study, we examined the ability of piceatannol to upregulate HO-1 expression in endothelial cells.	3,3',4,5'-tetrahydroxystilbene	42-53	heme oxygenase 1	Homo sapiens	68-72
16243536-4	2006	We found piceatannol at micromolar (10-50 microM) concentrations dramatically increased HO-1 protein levels in a time-dependent manner.	3,3',4,5'-tetrahydroxystilbene	9-20	heme oxygenase 1	Homo sapiens	88-92
16243536-5	2006	Piceatannol was similarly potent in the induction of HO-1 as hemin, arsenate, and 15d-PGJ2, and was more potent than some other phytochemicals including curcumin, EGCG, baicalein, and quercetin.	3,3',4,5'-tetrahydroxystilbene	0-11	heme oxygenase 1	Homo sapiens	53-57
16482620-5	2006	Moreover, PGG induced Nrf2 nuclear translocation, which was found to be an upstream step of PGG-induced HO-1 expression, and ERK activation, of which pathway was involved in PGG-induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	beta-penta-O-galloyl-glucose	92-95	heme oxygenase 1	Homo sapiens	214-218
16482620-6	2006	CONCLUSION: PGG up-regulates HO-1 expression by stimulating Nrf2 nuclear translocation in an ERK-dependent manner, and HO-1 expression by PGG may serve as one of the important mechanisms for its hepatoprotective effects.	beta-penta-O-galloyl-glucose	12-15	heme oxygenase 1	Homo sapiens	29-33
16482620-6	2006	CONCLUSION: PGG up-regulates HO-1 expression by stimulating Nrf2 nuclear translocation in an ERK-dependent manner, and HO-1 expression by PGG may serve as one of the important mechanisms for its hepatoprotective effects.	beta-penta-O-galloyl-glucose	138-141	heme oxygenase 1	Homo sapiens	119-123
16329999-1	2006	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS).	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	117-121
16329999-1	2006	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS).	Heme	34-38	heme oxygenase 1	Homo sapiens	99-115
16254033-5	2006	Donor treatment with bilirubin up-regulated mRNA expression of protective genes such as HO-1 and bcl-2 and suppressed proinflammatory and proapoptotic genes including monocyte chemoattractant protein-1 and caspase-3 and -8 in the islet grafts before transplantation.	Bilirubin	21-30	heme oxygenase 1	Homo sapiens	88-92
16137675-3	2006	Biodegradation of extravasated hemoglobin (exvHb) and deposition of iron in alveoli occurred at 3-56 h post-exposure and was preceded by LKC degranulation and accumulation of MPO, HO-1, and SOD-1 in HLs.	Iron	68-72	heme oxygenase 1	Homo sapiens	180-184
16474202-4	2006	Increased HO-1 induction by hemin resulted in a significant decrease in the Lyso-PC-mediated induction of MCP-1 mRNA expression.	Hemin	28-33	heme oxygenase 1	Homo sapiens	10-14
16474202-4	2006	Increased HO-1 induction by hemin resulted in a significant decrease in the Lyso-PC-mediated induction of MCP-1 mRNA expression.	Lysophosphatidylcholines	76-83	heme oxygenase 1	Homo sapiens	10-14
16474202-5	2006	SnPP (IX), the specific inhibitor of HO-1 enzymatic activity, prevented the hemin-mediated attenuation of MCP-1 mRNA expression.	S-Nitroso-N-propionyl-D,L-penicillamine	0-4	heme oxygenase 1	Homo sapiens	37-41
16474202-5	2006	SnPP (IX), the specific inhibitor of HO-1 enzymatic activity, prevented the hemin-mediated attenuation of MCP-1 mRNA expression.	Hemin	76-81	heme oxygenase 1	Homo sapiens	37-41
16243536-8	2006	Piceatannol-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine and glutathione, but not by other antioxidants.	3,3',4,5'-tetrahydroxystilbene	0-11	heme oxygenase 1	Homo sapiens	21-25
16243536-8	2006	Piceatannol-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine and glutathione, but not by other antioxidants.	Acetylcysteine	69-85	heme oxygenase 1	Homo sapiens	21-25
16243536-8	2006	Piceatannol-mediated HO-1 induction was abrogated in the presence of N-acetylcysteine and glutathione, but not by other antioxidants.	Glutathione	90-101	heme oxygenase 1	Homo sapiens	21-25
16243536-9	2006	Induction of HO-1 by piceatannol was further enhanced by using buthionine sulfoximine.	3,3',4,5'-tetrahydroxystilbene	21-32	heme oxygenase 1	Homo sapiens	13-17
16243536-9	2006	Induction of HO-1 by piceatannol was further enhanced by using buthionine sulfoximine.	Buthionine Sulfoximine	63-85	heme oxygenase 1	Homo sapiens	13-17
16243536-10	2006	In addition, we determined that tyrosine kinase was involved in the induction of HO-1 by using tyrosine kinase inhibitors, herbimycin A, erbstatin, and genistein; in contrast, no significant changes in the pretreatment of PI3 kinase or MAP kinase inhibitors was determined.	herbimycin	123-135	heme oxygenase 1	Homo sapiens	81-85
16243536-10	2006	In addition, we determined that tyrosine kinase was involved in the induction of HO-1 by using tyrosine kinase inhibitors, herbimycin A, erbstatin, and genistein; in contrast, no significant changes in the pretreatment of PI3 kinase or MAP kinase inhibitors was determined.	erbstatin	137-146	heme oxygenase 1	Homo sapiens	81-85
16243536-10	2006	In addition, we determined that tyrosine kinase was involved in the induction of HO-1 by using tyrosine kinase inhibitors, herbimycin A, erbstatin, and genistein; in contrast, no significant changes in the pretreatment of PI3 kinase or MAP kinase inhibitors was determined.	Genistein	152-161	heme oxygenase 1	Homo sapiens	81-85
16243536-11	2006	HO-1 induction was blocked by the protein kinase C inhibitors calphostin C, rottlerin, and long PMA pretreatment, whereas conventional PKC inhibitors, Go6976, and Ca2+ chelator BAPTA/AM, had no effect.	rottlerin	76-85	heme oxygenase 1	Homo sapiens	0-4
16243536-11	2006	HO-1 induction was blocked by the protein kinase C inhibitors calphostin C, rottlerin, and long PMA pretreatment, whereas conventional PKC inhibitors, Go6976, and Ca2+ chelator BAPTA/AM, had no effect.	Tetradecanoylphorbol Acetate	96-99	heme oxygenase 1	Homo sapiens	0-4
16243536-11	2006	HO-1 induction was blocked by the protein kinase C inhibitors calphostin C, rottlerin, and long PMA pretreatment, whereas conventional PKC inhibitors, Go6976, and Ca2+ chelator BAPTA/AM, had no effect.	Go 6976	151-157	heme oxygenase 1	Homo sapiens	0-4
16243536-11	2006	HO-1 induction was blocked by the protein kinase C inhibitors calphostin C, rottlerin, and long PMA pretreatment, whereas conventional PKC inhibitors, Go6976, and Ca2+ chelator BAPTA/AM, had no effect.	1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid	177-182	heme oxygenase 1	Homo sapiens	0-4
16243536-13	2006	Treating ECs with zinc protoporphyrin, an HO-1 inhibito blocked the anti-inflammatory effect of piceatannol.	zinc protoporphyrin	18-37	heme oxygenase 1	Homo sapiens	42-46
16243536-13	2006	Treating ECs with zinc protoporphyrin, an HO-1 inhibito blocked the anti-inflammatory effect of piceatannol.	3,3',4,5'-tetrahydroxystilbene	96-107	heme oxygenase 1	Homo sapiens	42-46
16243536-14	2006	In summary, this study identified piceatannol as a novel phytochemical inducer of HO-1 expression and identified the mechanisms involved in this process.	3,3',4,5'-tetrahydroxystilbene	34-45	heme oxygenase 1	Homo sapiens	82-86
16233958-4	2006	In the present study, we demonstrate that systemically administered SUL can enter the brain as determined by increased mRNA and protein levels of the Nrf2-responsive gene heme oxygenase 1 (HO-1).	sulforaphane	68-71	heme oxygenase 1	Homo sapiens	171-187
16482620-0	2006	1,2,3,4,6-penta-O-galloyl-beta-D-glucose up-regulates heme oxygenase-1 expression by stimulating Nrf2 nuclear translocation in an extracellular signal-regulated kinase-dependent manner in HepG2 cells.	beta-penta-O-galloyl-glucose	0-40	heme oxygenase 1	Homo sapiens	54-70
16482620-1	2006	AIM: To examine the potency of 1,2,3,4,6-penta-O-galloyl-beta-D-glucose (PGG) as a hepatic heme oxygenase-1 (HO-1) inducer and its regulation in HepG2 cells.	beta-penta-O-galloyl-glucose	31-71	heme oxygenase 1	Homo sapiens	91-107
16482620-1	2006	AIM: To examine the potency of 1,2,3,4,6-penta-O-galloyl-beta-D-glucose (PGG) as a hepatic heme oxygenase-1 (HO-1) inducer and its regulation in HepG2 cells.	beta-penta-O-galloyl-glucose	31-71	heme oxygenase 1	Homo sapiens	109-113
16482620-1	2006	AIM: To examine the potency of 1,2,3,4,6-penta-O-galloyl-beta-D-glucose (PGG) as a hepatic heme oxygenase-1 (HO-1) inducer and its regulation in HepG2 cells.	beta-penta-O-galloyl-glucose	73-76	heme oxygenase 1	Homo sapiens	91-107
16482620-1	2006	AIM: To examine the potency of 1,2,3,4,6-penta-O-galloyl-beta-D-glucose (PGG) as a hepatic heme oxygenase-1 (HO-1) inducer and its regulation in HepG2 cells.	beta-penta-O-galloyl-glucose	73-76	heme oxygenase 1	Homo sapiens	109-113
16482620-4	2006	RESULTS: PGG up-regulated HO-1 expression and this expression conferred cytoprotection against oxidative injury induced by t-butyl hydroperoxide.	beta-penta-O-galloyl-glucose	9-12	heme oxygenase 1	Homo sapiens	26-30
16482620-4	2006	RESULTS: PGG up-regulated HO-1 expression and this expression conferred cytoprotection against oxidative injury induced by t-butyl hydroperoxide.	tert-Butylhydroperoxide	123-144	heme oxygenase 1	Homo sapiens	26-30
16482620-5	2006	Moreover, PGG induced Nrf2 nuclear translocation, which was found to be an upstream step of PGG-induced HO-1 expression, and ERK activation, of which pathway was involved in PGG-induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	beta-penta-O-galloyl-glucose	10-13	heme oxygenase 1	Homo sapiens	104-108
16482620-5	2006	Moreover, PGG induced Nrf2 nuclear translocation, which was found to be an upstream step of PGG-induced HO-1 expression, and ERK activation, of which pathway was involved in PGG-induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	beta-penta-O-galloyl-glucose	10-13	heme oxygenase 1	Homo sapiens	214-218
16482620-5	2006	Moreover, PGG induced Nrf2 nuclear translocation, which was found to be an upstream step of PGG-induced HO-1 expression, and ERK activation, of which pathway was involved in PGG-induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	beta-penta-O-galloyl-glucose	92-95	heme oxygenase 1	Homo sapiens	104-108
16482620-5	2006	Moreover, PGG induced Nrf2 nuclear translocation, which was found to be an upstream step of PGG-induced HO-1 expression, and ERK activation, of which pathway was involved in PGG-induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	beta-penta-O-galloyl-glucose	92-95	heme oxygenase 1	Homo sapiens	214-218
16482620-5	2006	Moreover, PGG induced Nrf2 nuclear translocation, which was found to be an upstream step of PGG-induced HO-1 expression, and ERK activation, of which pathway was involved in PGG-induced Nrf2 nuclear translocation, HO-1 expression and cytoprotection.	beta-penta-O-galloyl-glucose	92-95	heme oxygenase 1	Homo sapiens	104-108
16388581-2	2006	The heme orientation within the active site, which is thought to determine the oxidation regiospecificity, is shown here for the human enzyme (hHO1) to be largely determined by interactions between the heme carboxylic acid groups and residues Arg183 and Lys18 but not Tyr134.	Heme	4-8	heme oxygenase 1	Homo sapiens	143-147
16388581-2	2006	The heme orientation within the active site, which is thought to determine the oxidation regiospecificity, is shown here for the human enzyme (hHO1) to be largely determined by interactions between the heme carboxylic acid groups and residues Arg183 and Lys18 but not Tyr134.	heme carboxylic acid	202-222	heme oxygenase 1	Homo sapiens	143-147
16388581-2	2006	The heme orientation within the active site, which is thought to determine the oxidation regiospecificity, is shown here for the human enzyme (hHO1) to be largely determined by interactions between the heme carboxylic acid groups and residues Arg183 and Lys18 but not Tyr134.	octadeca(lysine)	254-259	heme oxygenase 1	Homo sapiens	143-147
16388581-6	2006	Kinetic studies demonstrate that mutations of Arg183 greatly impair the rate of the P450 reductase-dependent reaction, in accord with the earlier finding that Arg183 is involved in binding of the reductase to hHO1, but have little effect on the ascorbate reaction.	Ascorbic Acid	245-254	heme oxygenase 1	Homo sapiens	209-213
16329999-1	2006	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS).	Heme	34-38	heme oxygenase 1	Homo sapiens	117-121
16329999-11	2006	However, endogenous overproduction of CO by super-induction of HO-1 (obtained by pretreatment of macrophages with either buthionine sulfoximine or hemin) decreased the LPS-derived iNOS expression without affecting cell survival.	Carbon Monoxide	38-40	heme oxygenase 1	Homo sapiens	63-67
16329999-11	2006	However, endogenous overproduction of CO by super-induction of HO-1 (obtained by pretreatment of macrophages with either buthionine sulfoximine or hemin) decreased the LPS-derived iNOS expression without affecting cell survival.	Buthionine Sulfoximine	121-143	heme oxygenase 1	Homo sapiens	63-67
16329999-11	2006	However, endogenous overproduction of CO by super-induction of HO-1 (obtained by pretreatment of macrophages with either buthionine sulfoximine or hemin) decreased the LPS-derived iNOS expression without affecting cell survival.	Hemin	147-152	heme oxygenase 1	Homo sapiens	63-67
16329999-13	2006	Thus, upregulation of HO-1 and overproduction of CO may allow the survival of LPS-stimulated macrophages; first, by eliminating the free heme to prevent Fenton reaction, second, by limiting the availability of free heme required for induction of NO-producing heme enzyme (i.e., iNOS), third, by limiting additional production of O(2)(-) and NO via CO-derived inhibition on the activities of heme enzymes like NADPH oxidase and iNOS, respectively.	Heme	137-141	heme oxygenase 1	Homo sapiens	22-26
16329999-13	2006	Thus, upregulation of HO-1 and overproduction of CO may allow the survival of LPS-stimulated macrophages; first, by eliminating the free heme to prevent Fenton reaction, second, by limiting the availability of free heme required for induction of NO-producing heme enzyme (i.e., iNOS), third, by limiting additional production of O(2)(-) and NO via CO-derived inhibition on the activities of heme enzymes like NADPH oxidase and iNOS, respectively.	Heme	215-219	heme oxygenase 1	Homo sapiens	22-26
16329999-13	2006	Thus, upregulation of HO-1 and overproduction of CO may allow the survival of LPS-stimulated macrophages; first, by eliminating the free heme to prevent Fenton reaction, second, by limiting the availability of free heme required for induction of NO-producing heme enzyme (i.e., iNOS), third, by limiting additional production of O(2)(-) and NO via CO-derived inhibition on the activities of heme enzymes like NADPH oxidase and iNOS, respectively.	Superoxides	329-333	heme oxygenase 1	Homo sapiens	22-26
16329999-1	2006	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS).	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	99-115
16329999-1	2006	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS).	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	117-121
16329999-1	2006	Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS).	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	99-115
16629181-7	2006	These results suggested that heme oxygenase-1 mediates heme iron influx and efflux in intestinal cells.	Iron	60-64	heme oxygenase 1	Homo sapiens	29-45
17302375-5	2006	Enhancing cellular thiols with N-acetylcystein prevented the NFV-induced drop in reduced thiols and partially protected against the induction in HO-1, but failed to prevent insulin resistance or cleavage of poly ADP ribose polymerase (PARP), a process indicative of activation of pro-apoptotic caspases.	Sulfhydryl Compounds	19-25	heme oxygenase 1	Homo sapiens	145-149
16629181-0	2006	Heme oxygenase 1 overexpression increases iron fluxes in caco-2 cells.	Iron	42-46	heme oxygenase 1	Homo sapiens	0-16
16487037-8	2006	Expression of the enzyme heme oxygenase-1 (HO-1), a known Nrf2 target gene, was upregulated by exposure of JAR cells to arsenic.	Arsenic	120-127	heme oxygenase 1	Homo sapiens	25-41
16633995-5	2006	EPO cellular mechanisms are not completely known, and the identification of close biochemical and molecular relationships between EPO and heme oxygenase-1 (HO-1), which has potent antioxidant and anti-apoptotic properties, could provide the rationale for the beneficial effect of carnitine having been shown to possess antioxidant, anti-apoptotic and erythropoietic activities and to induce HO-1 expression, not only in dialysis patients who fail to respond adequately to EPO, but also in patients with heart failure.	Carnitine	280-289	heme oxygenase 1	Homo sapiens	138-154
16629181-2	2006	Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous Fe.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
16629181-2	2006	Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous Fe.	Biliverdine	73-83	heme oxygenase 1	Homo sapiens	0-16
16629181-2	2006	Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous Fe.	Carbon Monoxide	85-87	heme oxygenase 1	Homo sapiens	0-16
16629181-2	2006	Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous Fe.	Iron	100-102	heme oxygenase 1	Homo sapiens	0-16
16943657-1	2006	Heme oxygenase 1 (HO-1) is an enzyme important in the catabolism of heme that is induced under conditions of oxidative stress.	Heme	68-72	heme oxygenase 1	Homo sapiens	0-16
16943657-1	2006	Heme oxygenase 1 (HO-1) is an enzyme important in the catabolism of heme that is induced under conditions of oxidative stress.	Heme	68-72	heme oxygenase 1	Homo sapiens	18-22
16943657-2	2006	HO-1 degradation of heme yields biliverdin, bilirubin, carbon monoxide and iron.	Biliverdine	32-42	heme oxygenase 1	Homo sapiens	0-4
16943657-2	2006	HO-1 degradation of heme yields biliverdin, bilirubin, carbon monoxide and iron.	Bilirubin	44-53	heme oxygenase 1	Homo sapiens	0-4
16943657-2	2006	HO-1 degradation of heme yields biliverdin, bilirubin, carbon monoxide and iron.	Carbon Monoxide	55-70	heme oxygenase 1	Homo sapiens	0-4
16943657-2	2006	HO-1 degradation of heme yields biliverdin, bilirubin, carbon monoxide and iron.	Iron	75-79	heme oxygenase 1	Homo sapiens	0-4
16633995-5	2006	EPO cellular mechanisms are not completely known, and the identification of close biochemical and molecular relationships between EPO and heme oxygenase-1 (HO-1), which has potent antioxidant and anti-apoptotic properties, could provide the rationale for the beneficial effect of carnitine having been shown to possess antioxidant, anti-apoptotic and erythropoietic activities and to induce HO-1 expression, not only in dialysis patients who fail to respond adequately to EPO, but also in patients with heart failure.	Carnitine	280-289	heme oxygenase 1	Homo sapiens	156-160
16337271-1	2006	Solution proton NMR has been used here to show that, as either the high-spin ferric, protohemin (PH) substrate complex at neutral pH, or the low-spin ferric, cyanide-inhibited PH substrate complex, the active site electronic and molecular structure of the 233- and 265-residue recombinant constructs of human heme oxygenase-1, hHO, are essentially indistinguishable.	Cyanides	158-165	heme oxygenase 1	Homo sapiens	309-325
16697692-5	2006	Heme oxygenase-1 induction by treatment with cobalt protoporphyrin IX resulted in resistance to apoptosis, activation of Akt, reduction in p21(Cip/WAF1) levels and modification of bcl2/bax ratio towards survival.	cobaltiprotoporphyrin	45-69	heme oxygenase 1	Homo sapiens	0-16
16697692-8	2006	Protection against apoptosis in cells treated with cobalt protoporphyrin IX was reverted by incubation with heme oxygenase-1 small interfering RNA.	cobaltiprotoporphyrin	51-75	heme oxygenase 1	Homo sapiens	108-124
16697692-9	2006	This study shows an antiapoptotic effect of heme oxygenase-1 in colon cancer cells which could be mediated by the formation of bilirubin and biliverdin.	Bilirubin	127-136	heme oxygenase 1	Homo sapiens	44-60
16697692-9	2006	This study shows an antiapoptotic effect of heme oxygenase-1 in colon cancer cells which could be mediated by the formation of bilirubin and biliverdin.	Biliverdine	141-151	heme oxygenase 1	Homo sapiens	44-60
16600087-0	2006	[Heme oxygenase-1 expression and apoptosis induced by cadmium in human embryon kidney cells].	Cadmium	54-61	heme oxygenase 1	Homo sapiens	1-17
16288501-7	2006	In particular, we examined the effect of anthocyanidins on endothelial heme oxygenase-1 (HO-1), an inducible stress protein.	Anthocyanins	41-55	heme oxygenase 1	Homo sapiens	71-87
16401919-8	2006	Doxazosin concentration dependently reduced HO-1 gene and protein expression (0.57 +/- 0.07 vs. 0.49 +/- 0.06 d.u.	Doxazosin	0-9	heme oxygenase 1	Homo sapiens	44-48
16401919-13	2006	Surprisingly, HO-1, which is induced and protected by oxidative stress, is also reduced by doxazosin.	Doxazosin	91-100	heme oxygenase 1	Homo sapiens	14-18
16401919-15	2006	From the results of this preliminary study it could be proposed that the proapoptotic effect of doxazosin could be mediated, at least in part, through the contemporary inhibition of HO-1.	Doxazosin	96-105	heme oxygenase 1	Homo sapiens	182-186
18958680-7	2006	Indirubin-3"-monoxime treatment also enhanced cyclo-oxygenase 2 expression in PMA-differentiated cells, but reduced the expression of macrophage inflammatory protein, catalase, heme oxygenase-1, glutathione peroxidase, and manganese superoxide dismutase; a scenario consistent with oxidative stress.	indirubin-3'-monoxime	0-21	heme oxygenase 1	Homo sapiens	177-193
16374435-10	2006	Intradialytic removal of L-ascorbic acid, uric acid, bilirubin, 3-indoxyl sulfate, indoxyl-beta-D-glucuronide, p-cresol, and phenol increases the risk of LDL oxidation and subsequent endothelial cell damage, which underlines the importance of activation of cytoprotective HO-1 and ferritin in endothelium.	Phenol	125-131	heme oxygenase 1	Homo sapiens	272-276
16374439-1	2006	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, producing carbon monoxide (CO), which carries potent antiproliferative and anti-inflammatory effects in the vascular walls.	Carbon Monoxide	81-96	heme oxygenase 1	Homo sapiens	0-16
16374439-1	2006	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, producing carbon monoxide (CO), which carries potent antiproliferative and anti-inflammatory effects in the vascular walls.	Carbon Monoxide	81-96	heme oxygenase 1	Homo sapiens	18-22
16374439-1	2006	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, producing carbon monoxide (CO), which carries potent antiproliferative and anti-inflammatory effects in the vascular walls.	Carbon Monoxide	98-100	heme oxygenase 1	Homo sapiens	0-16
16374439-1	2006	Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, producing carbon monoxide (CO), which carries potent antiproliferative and anti-inflammatory effects in the vascular walls.	Carbon Monoxide	98-100	heme oxygenase 1	Homo sapiens	18-22
16600087-1	2006	OBJECTIVE: To investigate apoptosis and expression of heme oxygenase-1 (HO-1) induced by cadmium in human embryonic kidney cells (HEK239T).	Cadmium	89-96	heme oxygenase 1	Homo sapiens	54-70
16600087-1	2006	OBJECTIVE: To investigate apoptosis and expression of heme oxygenase-1 (HO-1) induced by cadmium in human embryonic kidney cells (HEK239T).	Cadmium	89-96	heme oxygenase 1	Homo sapiens	72-76
16600087-6	2006	The CdCl(2) of between 10 and 40 micromol/L could highly induce the expression of HO-1 of the human embryonic kidney cells.	cdcl	4-8	heme oxygenase 1	Homo sapiens	82-86
16600087-8	2006	CONCLUSION: The cadmium can induce the apoptosis of the human embryonic kidney cells and up-regulate the expression of HO-1.	Cadmium	16-23	heme oxygenase 1	Homo sapiens	119-123
16183036-1	2005	In the beginning, the microsomal HO system was presumed to be made of one isozymes, now known as HO-1, which was cytP450-dependent; and, was thought to be of physiological significance solely in the context of catalysis of hemoglobin heme to bile pigments and CO. A succession of discoveries including characterization of the system as an independent mono-oxygenase, identification of a second form, called HO-2, free radical quenching activity of bile pigments, analogous function of CO in cell signaling to NO, and characterization of the system as HSP32 cognates has led to such an impressive expansion in the number of reports dealing with the HO system that surpass anyone"s expectation.	Heme	234-238	heme oxygenase 1	Homo sapiens	97-101
16298686-4	2005	In neuron-glia cultures, we found that H2O2, a product of dopamine metabolism, or l-3,4-dihydroxyphenylalanine (L-DOPA), the dopamine precursor used in the therapy of PD, induced a fast up-regulation of HO-1 mRNA and protein levels, followed by a secondary down-regulation.	Hydrogen Peroxide	39-43	heme oxygenase 1	Homo sapiens	203-207
16298686-4	2005	In neuron-glia cultures, we found that H2O2, a product of dopamine metabolism, or l-3,4-dihydroxyphenylalanine (L-DOPA), the dopamine precursor used in the therapy of PD, induced a fast up-regulation of HO-1 mRNA and protein levels, followed by a secondary down-regulation.	Levodopa	82-110	heme oxygenase 1	Homo sapiens	203-207
16298686-4	2005	In neuron-glia cultures, we found that H2O2, a product of dopamine metabolism, or l-3,4-dihydroxyphenylalanine (L-DOPA), the dopamine precursor used in the therapy of PD, induced a fast up-regulation of HO-1 mRNA and protein levels, followed by a secondary down-regulation.	Levodopa	112-118	heme oxygenase 1	Homo sapiens	203-207
16298686-5	2005	H2O2 and L-DOPA also increased HO-1 expression in astrocyte cultures, but with a delayed time course in H2O2-treated cultures.	Hydrogen Peroxide	0-4	heme oxygenase 1	Homo sapiens	31-35
16298686-5	2005	H2O2 and L-DOPA also increased HO-1 expression in astrocyte cultures, but with a delayed time course in H2O2-treated cultures.	Levodopa	9-15	heme oxygenase 1	Homo sapiens	31-35
16298686-7	2005	Because exogenously applied GDNF prevented HO-1 up-regulation in cultures treated with H2O2 or l-DOPA, and antibody neutralization of GDNF prevented the secondary HO-1 down-regulation observed in neuron-glia cultures, we propose that GDNF negatively modulates HO-1 expression induced by oxidative stress.	Hydrogen Peroxide	87-91	heme oxygenase 1	Homo sapiens	43-47
16298686-7	2005	Because exogenously applied GDNF prevented HO-1 up-regulation in cultures treated with H2O2 or l-DOPA, and antibody neutralization of GDNF prevented the secondary HO-1 down-regulation observed in neuron-glia cultures, we propose that GDNF negatively modulates HO-1 expression induced by oxidative stress.	Levodopa	95-101	heme oxygenase 1	Homo sapiens	43-47
16154530-7	2005	Ortiz de Montellano, Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1, J. Biol.	Heme	100-104	heme oxygenase 1	Homo sapiens	114-130
16198234-2	2005	Heme oxygenase-1 (HO-1), implicated in a role in NO resistance, might confer its protective effect through the direct products biliverdin and CO or the secondary product bilirubin.	Biliverdine	127-137	heme oxygenase 1	Homo sapiens	0-16
16382109-3	2005	Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear.	Heme	105-109	heme oxygenase 1	Homo sapiens	14-18
16382109-3	2005	Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear.	Carbon Monoxide	128-130	heme oxygenase 1	Homo sapiens	14-18
16382109-3	2005	Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear.	Biliverdine	135-145	heme oxygenase 1	Homo sapiens	14-18
16356130-1	2005	Heme oxygenase (HO)-1, involved in the heme degradation process, is an important antioxidant enzyme.	Heme	39-43	heme oxygenase 1	Homo sapiens	0-21
16323392-4	2005	Other mediators such as endothelin-1 and the heme oxygenase-1/carbon monoxide system have recently been found to be important contributors.	Carbon Monoxide	62-77	heme oxygenase 1	Homo sapiens	45-61
16198371-4	2005	Human coronary arteriolar endothelial cells exposed to resveratrol or Trx-1 on Matrigel demonstrated significantly accelerated tubular morphogenesis with induction of HO-1 and VEGF expression.	Resveratrol	55-66	heme oxygenase 1	Homo sapiens	167-171
16208635-8	2005	Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron.	Heme	22-26	heme oxygenase 1	Homo sapiens	0-16
16208635-8	2005	Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron.	Porphyrins	59-68	heme oxygenase 1	Homo sapiens	0-16
16208635-8	2005	Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron.	Biliverdine	85-95	heme oxygenase 1	Homo sapiens	0-16
16208635-8	2005	Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron.	Carbon Monoxide	97-112	heme oxygenase 1	Homo sapiens	0-16
16208635-8	2005	Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron.	Iron	165-169	heme oxygenase 1	Homo sapiens	0-16
16154535-0	2005	Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
16154535-0	2005	Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte.	Adenosine Triphosphate	52-74	heme oxygenase 1	Homo sapiens	0-16
16373841-0	2005	Mechanisms of heme oxygenase-1-mediated cardiac and pulmonary vascular protection in chronic hypoxia: roles of carbon monoxide and bilirubin.	Carbon Monoxide	111-126	heme oxygenase 1	Homo sapiens	14-30
16373841-0	2005	Mechanisms of heme oxygenase-1-mediated cardiac and pulmonary vascular protection in chronic hypoxia: roles of carbon monoxide and bilirubin.	Bilirubin	131-140	heme oxygenase 1	Homo sapiens	14-30
16313248-1	2005	BACKGROUND: A functional GT dinucleotide length polymorphism in the haem oxygenase-1 (HO-1) gene promoter is thought to be involved in the pathogenesis of cardiovascular disease.	Dinucleoside Phosphates	28-40	heme oxygenase 1	Homo sapiens	68-90
16234431-6	2005	When HO-1 was induced by hemin in vitro, a significant dose-dependent inhibition of osteoclastogenesis was observed.	Hemin	25-30	heme oxygenase 1	Homo sapiens	5-9
16234431-12	2005	Moreover, serum levels of bilirubin, a metabolite of HO-1, were elevated in rheumatoid arthritis patients without bone damage, suggesting HO-1 affects bone loss in humans.	Bilirubin	26-35	heme oxygenase 1	Homo sapiens	53-57
16234431-12	2005	Moreover, serum levels of bilirubin, a metabolite of HO-1, were elevated in rheumatoid arthritis patients without bone damage, suggesting HO-1 affects bone loss in humans.	Bilirubin	26-35	heme oxygenase 1	Homo sapiens	138-142
16308001-4	2005	The aim of our study was to induce heme oxygenase 1 by using hemin in human internal thoracic and radial arteries and to evaluate the effect of this induction on the contractility of these arterial grafts.	Hemin	61-66	heme oxygenase 1	Homo sapiens	35-51
16308001-11	2005	Immunohistochemical staining revealed a large expression of heme oxygenase 1 in all vascular layers of hemin-treated internal thoracic artery and radial artery rings.	Hemin	103-108	heme oxygenase 1	Homo sapiens	60-76
16308001-12	2005	Enzyme-linked immunosorbent assay studies showed a significant increase in heme oxygenase 1 levels in hemin-treated internal thoracic artery and radial artery rings.	Hemin	102-107	heme oxygenase 1	Homo sapiens	75-91
16308001-13	2005	CONCLUSION: Hemin caused in vitro induction of heme oxygenase 1 in human internal thoracic artery and radial artery grafts.	Hemin	12-17	heme oxygenase 1	Homo sapiens	47-63
16283523-6	2005	Real-time RT-PCR confirmed the effect of copper on the levels of MT2A, HSPA1A, CYP1A1 and HMOX1 expression.	Copper	41-47	heme oxygenase 1	Homo sapiens	90-95
16198234-2	2005	Heme oxygenase-1 (HO-1), implicated in a role in NO resistance, might confer its protective effect through the direct products biliverdin and CO or the secondary product bilirubin.	Biliverdine	127-137	heme oxygenase 1	Homo sapiens	18-22
16198234-2	2005	Heme oxygenase-1 (HO-1), implicated in a role in NO resistance, might confer its protective effect through the direct products biliverdin and CO or the secondary product bilirubin.	Bilirubin	170-179	heme oxygenase 1	Homo sapiens	0-16
16198234-2	2005	Heme oxygenase-1 (HO-1), implicated in a role in NO resistance, might confer its protective effect through the direct products biliverdin and CO or the secondary product bilirubin.	Bilirubin	170-179	heme oxygenase 1	Homo sapiens	18-22
16123320-10	2005	Pretreatment with SB203580, a p38 mitogen-activated protein kinase inhibitor, reduced ALA-induced HO-1 mRNA expression by 75% and inhibited ALA-induced Nrf2 binding to the HO-1 ARE.	Thioctic Acid	86-89	heme oxygenase 1	Homo sapiens	98-102
16123320-10	2005	Pretreatment with SB203580, a p38 mitogen-activated protein kinase inhibitor, reduced ALA-induced HO-1 mRNA expression by 75% and inhibited ALA-induced Nrf2 binding to the HO-1 ARE.	Thioctic Acid	86-89	heme oxygenase 1	Homo sapiens	172-176
16123320-0	2005	Alpha-lipoic acid-induced heme oxygenase-1 expression is mediated by nuclear factor erythroid 2-related factor 2 and p38 mitogen-activated protein kinase in human monocytic cells.	Thioctic Acid	0-17	heme oxygenase 1	Homo sapiens	26-42
16123320-10	2005	Pretreatment with SB203580, a p38 mitogen-activated protein kinase inhibitor, reduced ALA-induced HO-1 mRNA expression by 75% and inhibited ALA-induced Nrf2 binding to the HO-1 ARE.	Thioctic Acid	140-143	heme oxygenase 1	Homo sapiens	172-176
16123320-5	2005	This study examined the effects of ALA on HO-1 expression in human monocytic cells.	Thioctic Acid	35-38	heme oxygenase 1	Homo sapiens	42-46
16123320-6	2005	METHODS AND RESULTS: ALA time and dose-dependently induced HO-1 mRNA expression in THP-1 cells, with peak expression at 4 hours and returning to baseline by 24 hours.	Thioctic Acid	21-24	heme oxygenase 1	Homo sapiens	59-63
16123320-11	2005	CONCLUSIONS: These results demonstrate that ALA induces HO-1 expression in THP-1 monocytic cells via Nrf2 and p38.	Thioctic Acid	44-47	heme oxygenase 1	Homo sapiens	56-60
16123320-8	2005	ALA stimulated translocation of the transcription factor nuclear factor-erythroid 2-related factor 2 (Nrf2) into the nucleus and binding to a human HO-1 antioxidant response element (ARE) by 30 minutes.	Thioctic Acid	0-3	heme oxygenase 1	Homo sapiens	148-152
16123320-12	2005	Further studies are required to investigate whether the protective effects of ALA in monocytes are mediated by HO-1.	Thioctic Acid	78-81	heme oxygenase 1	Homo sapiens	111-115
16123320-9	2005	A dominant-negative Nrf2 inhibitor reduced ALA-induced HO-1 mRNA expression by 66%.	Thioctic Acid	43-46	heme oxygenase 1	Homo sapiens	55-59
16177082-8	2005	Ro-31-8220, a pan-protein kinase C (PKC) inhibitor, and Go6976, a classical PKC inhibitor, blunted LPS-induced HO-1 mRNA expression in monocytes and THP-1 cells.	Ro 31-8220	0-10	heme oxygenase 1	Homo sapiens	111-115
16123320-10	2005	Pretreatment with SB203580, a p38 mitogen-activated protein kinase inhibitor, reduced ALA-induced HO-1 mRNA expression by 75% and inhibited ALA-induced Nrf2 binding to the HO-1 ARE.	SB 203580	18-26	heme oxygenase 1	Homo sapiens	98-102
16123320-10	2005	Pretreatment with SB203580, a p38 mitogen-activated protein kinase inhibitor, reduced ALA-induced HO-1 mRNA expression by 75% and inhibited ALA-induced Nrf2 binding to the HO-1 ARE.	SB 203580	18-26	heme oxygenase 1	Homo sapiens	172-176
16183497-2	2005	Heme oxygenase-1 (HO-1) has recently been shown to be cytoprotective, and is known to be induced by heme moieties.	Heme	100-104	heme oxygenase 1	Homo sapiens	0-16
16183497-2	2005	Heme oxygenase-1 (HO-1) has recently been shown to be cytoprotective, and is known to be induced by heme moieties.	Heme	100-104	heme oxygenase 1	Homo sapiens	18-22
16183497-3	2005	We investigated the effects of this hemoglobin-based oxygen carrier on HO-1 induction and proinflammatory activation of pulmonary endothelium.	Oxygen	53-59	heme oxygenase 1	Homo sapiens	71-75
16210136-2	2005	Inducibility of this enzyme is modulated by a (GT)n dinucleotide length polymorphism in the HO-1 gene promoter.	Dinucleoside Phosphates	52-64	heme oxygenase 1	Homo sapiens	92-96
16210136-6	2005	The HO-1 genotype was assessed using genomic DNA isolated from paraffin-embedded allograft biopsy specimens.	Paraffin	63-71	heme oxygenase 1	Homo sapiens	4-8
16177082-8	2005	Ro-31-8220, a pan-protein kinase C (PKC) inhibitor, and Go6976, a classical PKC inhibitor, blunted LPS-induced HO-1 mRNA expression in monocytes and THP-1 cells.	Go 6976	56-62	heme oxygenase 1	Homo sapiens	111-115
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Heme	34-38	heme oxygenase 1	Homo sapiens	0-16
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Heme	34-38	heme oxygenase 1	Homo sapiens	18-22
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Bilirubin	72-81	heme oxygenase 1	Homo sapiens	0-16
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Bilirubin	72-81	heme oxygenase 1	Homo sapiens	18-22
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Iron	83-87	heme oxygenase 1	Homo sapiens	0-16
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Iron	83-87	heme oxygenase 1	Homo sapiens	18-22
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	0-16
16249618-2	2005	Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	18-22
16408059-4	2005	We further find that nitrite readily affects cyclic GMP production, cytochrome P450 activities, and heat shock protein 70 and heme oxygenase-1 expression in a variety of tissues.	Nitrites	21-28	heme oxygenase 1	Homo sapiens	126-142
16309584-0	2005	Heme oxygenase-1-dependent and -independent regulation of angiogenic genes expression: effect of cobalt protoporphyrin and cobalt chloride on VEGF and IL-8 synthesis in human microvascular endothelial cells.	cobaltiprotoporphyrin	97-118	heme oxygenase 1	Homo sapiens	0-16
16309584-0	2005	Heme oxygenase-1-dependent and -independent regulation of angiogenic genes expression: effect of cobalt protoporphyrin and cobalt chloride on VEGF and IL-8 synthesis in human microvascular endothelial cells.	cobaltous chloride	123-138	heme oxygenase 1	Homo sapiens	0-16
16309585-2	2005	HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-4
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	cobaltiprotoporphyrin	84-105	heme oxygenase 1	Homo sapiens	13-29
16309585-2	2005	HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	43-58	heme oxygenase 1	Homo sapiens	0-4
16309588-2	2005	We previously revealed a substantial oxidation of plasma hemoglobin to methemoglobin and a subsequent heme-catalyzed LDL oxidation generating moieties toxic to endothelium in heme oxygenase-1 (HO-1)-deficiency in human.	Heme	102-106	heme oxygenase 1	Homo sapiens	175-191
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	cobaltiprotoporphyrin	84-105	heme oxygenase 1	Homo sapiens	31-35
16309588-6	2005	Both cytotoxicity and HO-1 inducing ability of the oxidized LDL were strongly dependent on its lipid hydroperoxide content.	Lipid Peroxides	95-114	heme oxygenase 1	Homo sapiens	22-26
16309585-2	2005	HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Carbon Monoxide	60-62	heme oxygenase 1	Homo sapiens	0-4
16309585-2	2005	HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Iron	65-69	heme oxygenase 1	Homo sapiens	0-4
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	coppix	107-113	heme oxygenase 1	Homo sapiens	13-29
16309585-2	2005	HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Biliverdine	75-85	heme oxygenase 1	Homo sapiens	0-4
16309585-2	2005	HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin.	Bilirubin	122-131	heme oxygenase 1	Homo sapiens	0-4
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	coppix	107-113	heme oxygenase 1	Homo sapiens	31-35
16309585-3	2005	The beneficial effects of HO-1 induction include decreasing pro-oxidants (heme), increasing anti-oxidants (biliverdin and bilirubin), and producing a vasodilator with anti-apoptotic and anti-inflammatory properties (CO).	Biliverdine	107-117	heme oxygenase 1	Homo sapiens	26-30
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	cobaltous chloride	118-133	heme oxygenase 1	Homo sapiens	13-29
16309585-3	2005	The beneficial effects of HO-1 induction include decreasing pro-oxidants (heme), increasing anti-oxidants (biliverdin and bilirubin), and producing a vasodilator with anti-apoptotic and anti-inflammatory properties (CO).	Bilirubin	122-131	heme oxygenase 1	Homo sapiens	26-30
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	cobaltous chloride	118-133	heme oxygenase 1	Homo sapiens	31-35
16309586-5	2005	Overexpression of HO-1 decreased both 8-epi-PGF2alpha and MCP-1.	8-epi-prostaglandin F2alpha	38-53	heme oxygenase 1	Homo sapiens	18-22
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	cobaltous chloride	135-140	heme oxygenase 1	Homo sapiens	13-29
16309584-1	2005	Induction of heme oxygenase-1 (HO-1) expression can be achieved by stimulation with cobalt protoporphyrin (CoPPIX) or cobalt chloride (CoCl2).	cobaltous chloride	135-140	heme oxygenase 1	Homo sapiens	31-35
16309584-2	2005	HO-1 has been recently implicated in regulation of angiogenesis and CoCl2 is known to potently activate hypoxia inducible factor-1 (HIF-1) transcription factor, a key regulator of angiogenic response in hypoxia.	cobaltous chloride	68-73	heme oxygenase 1	Homo sapiens	0-4
16309584-4	2005	CoPPIX induced HO-1 expression and strongly enhanced VEGF and IL-8 synthesis, through the activation of VEGF and IL-8 promoters.	coppix	0-6	heme oxygenase 1	Homo sapiens	15-19
16309584-8	2005	Our data show that although both CoCl2 and CoPPIX induce HO-1, the influence of CoCl2 on VEGF does not involve HO-1 and is HIF-1-dependent, while the effect of CoPPIX does not involve HIF-1 but relies on HO-1.	cobaltous chloride	33-38	heme oxygenase 1	Homo sapiens	57-61
16309584-8	2005	Our data show that although both CoCl2 and CoPPIX induce HO-1, the influence of CoCl2 on VEGF does not involve HO-1 and is HIF-1-dependent, while the effect of CoPPIX does not involve HIF-1 but relies on HO-1.	coppix	43-49	heme oxygenase 1	Homo sapiens	57-61
15901614-4	2005	The protective effects of heme oxygenase-1 and products of its enzymatic activity, including carbon monoxide, biliverdin and bilirubin, and ferritin, have opened the door to potential therapeutic and disease-monitoring possibilities that one day may be applicable to pulmonary medicine.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	26-42
15901614-4	2005	The protective effects of heme oxygenase-1 and products of its enzymatic activity, including carbon monoxide, biliverdin and bilirubin, and ferritin, have opened the door to potential therapeutic and disease-monitoring possibilities that one day may be applicable to pulmonary medicine.	Biliverdine	110-120	heme oxygenase 1	Homo sapiens	26-42
15901614-4	2005	The protective effects of heme oxygenase-1 and products of its enzymatic activity, including carbon monoxide, biliverdin and bilirubin, and ferritin, have opened the door to potential therapeutic and disease-monitoring possibilities that one day may be applicable to pulmonary medicine.	Bilirubin	125-134	heme oxygenase 1	Homo sapiens	26-42
15901601-0	2005	Novel lipid mediator aspirin-triggered lipoxin A4 induces heme oxygenase-1 in endothelial cells.	Aspirin	21-28	heme oxygenase 1	Homo sapiens	58-74
15985429-5	2005	Both IAB and tBHQ induced antioxidant response element (ARE)-directed green fluorescent protein (GFP) expression in ARE/thymidine kinase GFP HepG2 cells, and both initiated nuclear Nrf2 accumulation and induction of heme oxygenase 1 in HEK293 cells.	2-tert-butylhydroquinone	13-17	heme oxygenase 1	Homo sapiens	216-232
16020746-6	2005	The proposed mechanisms by which HO-1 exerts its cytoprotective effects include its abilities to degrade the pro-oxidative heme, to release biliverdin and subsequently convert it bilirubin, both of which have antioxidant properties, and to generate carbon monoxide, which has antiproliferative and antiinflammatory as well as vasodilatory properties.	Heme	123-127	heme oxygenase 1	Homo sapiens	33-37
16020746-6	2005	The proposed mechanisms by which HO-1 exerts its cytoprotective effects include its abilities to degrade the pro-oxidative heme, to release biliverdin and subsequently convert it bilirubin, both of which have antioxidant properties, and to generate carbon monoxide, which has antiproliferative and antiinflammatory as well as vasodilatory properties.	Biliverdine	140-150	heme oxygenase 1	Homo sapiens	33-37
16020746-6	2005	The proposed mechanisms by which HO-1 exerts its cytoprotective effects include its abilities to degrade the pro-oxidative heme, to release biliverdin and subsequently convert it bilirubin, both of which have antioxidant properties, and to generate carbon monoxide, which has antiproliferative and antiinflammatory as well as vasodilatory properties.	Bilirubin	179-188	heme oxygenase 1	Homo sapiens	33-37
16020746-6	2005	The proposed mechanisms by which HO-1 exerts its cytoprotective effects include its abilities to degrade the pro-oxidative heme, to release biliverdin and subsequently convert it bilirubin, both of which have antioxidant properties, and to generate carbon monoxide, which has antiproliferative and antiinflammatory as well as vasodilatory properties.	Carbon Monoxide	249-264	heme oxygenase 1	Homo sapiens	33-37
15920011-1	2005	Heme oxygenase-1 (HO-1) is an intracellular enzyme that degrades heme and inhibits immune responses and inflammation in vivo.	Heme	65-69	heme oxygenase 1	Homo sapiens	0-16
15920011-1	2005	Heme oxygenase-1 (HO-1) is an intracellular enzyme that degrades heme and inhibits immune responses and inflammation in vivo.	Heme	65-69	heme oxygenase 1	Homo sapiens	18-22
15920011-6	2005	Induction of HO-1 expression with cobalt protoporphyrin (CoPP) in human and rat DCs inhibits lipopolysaccharide (LPS)-induced phenotypic maturation and secretion of proinflammatory cytokines, resulting in the inhibition of alloreactive T-cell proliferation.	cobaltiprotoporphyrin	34-55	heme oxygenase 1	Homo sapiens	13-17
15920011-6	2005	Induction of HO-1 expression with cobalt protoporphyrin (CoPP) in human and rat DCs inhibits lipopolysaccharide (LPS)-induced phenotypic maturation and secretion of proinflammatory cytokines, resulting in the inhibition of alloreactive T-cell proliferation.	cobaltiprotoporphyrin	57-61	heme oxygenase 1	Homo sapiens	13-17
15920011-8	2005	Reactive oxygen species induced by LPS in DCs were inhibited by induction of HO-1.	Reactive Oxygen Species	0-23	heme oxygenase 1	Homo sapiens	77-81
16020495-2	2005	Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous antioxidant bilirubin and carbon monoxide, both of which exert antiinflammatory and antiproliferative effects.	Bilirubin	84-93	heme oxygenase 1	Homo sapiens	0-16
16020495-2	2005	Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous antioxidant bilirubin and carbon monoxide, both of which exert antiinflammatory and antiproliferative effects.	Bilirubin	84-93	heme oxygenase 1	Homo sapiens	18-22
16020495-2	2005	Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous antioxidant bilirubin and carbon monoxide, both of which exert antiinflammatory and antiproliferative effects.	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	0-16
16020495-2	2005	Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous antioxidant bilirubin and carbon monoxide, both of which exert antiinflammatory and antiproliferative effects.	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	18-22
15901601-0	2005	Novel lipid mediator aspirin-triggered lipoxin A4 induces heme oxygenase-1 in endothelial cells.	lipoxin A4	39-49	heme oxygenase 1	Homo sapiens	58-74
15901601-2	2005	Recently, it was reported that aspirin induces heme oxygenase-1 (HO-1) expression on endothelial cells (EC) in a COX-independent manner, what confers protection against prooxidant insults.	Aspirin	31-38	heme oxygenase 1	Homo sapiens	47-63
15901601-2	2005	Recently, it was reported that aspirin induces heme oxygenase-1 (HO-1) expression on endothelial cells (EC) in a COX-independent manner, what confers protection against prooxidant insults.	Aspirin	31-38	heme oxygenase 1	Homo sapiens	65-69
15901601-4	2005	In this study, we investigated whether an aspirin-triggered lipoxin A(4) stable analog, 15-epi-16-(para-fluoro)-phenoxy-lipoxin A(4) (ATL-1) was able to induce endothelial HO-1.	Aspirin	42-49	heme oxygenase 1	Homo sapiens	172-176
15901601-4	2005	In this study, we investigated whether an aspirin-triggered lipoxin A(4) stable analog, 15-epi-16-(para-fluoro)-phenoxy-lipoxin A(4) (ATL-1) was able to induce endothelial HO-1.	15-epi-16-(para-fluoro)-phenoxy-lipoxin a	88-129	heme oxygenase 1	Homo sapiens	172-176
15901601-8	2005	This inhibitory effect of the analog is modulated by HO-1 because it was blocked by SnPPIX, a competitive inhibitor that blocks HO-1 activity.	tin protoporphyrin IX	84-90	heme oxygenase 1	Homo sapiens	53-57
15901601-8	2005	This inhibitory effect of the analog is modulated by HO-1 because it was blocked by SnPPIX, a competitive inhibitor that blocks HO-1 activity.	tin protoporphyrin IX	84-90	heme oxygenase 1	Homo sapiens	128-132
15996234-7	2005	Postoperatively, serum transaminases were significantly lower and the bile salt secretion was higher in the initial low HO-1 group, compared to the high expression group.	Bile Acids and Salts	70-79	heme oxygenase 1	Homo sapiens	120-124
16146339-0	2005	L-methionine reduces oxidant stress in endothelial cells: role of heme oxygenase-1, ferritin, and nitric oxide.	Methionine	0-12	heme oxygenase 1	Homo sapiens	66-82
16146339-2	2005	In the present study, L-methionine led to a concentration-dependent induction of the antioxidant proteins heme oxygenase-1 (HO-1) and ferritin in cultured endothelial cells (ECV 304).	Methionine	22-34	heme oxygenase 1	Homo sapiens	106-122
16146339-2	2005	In the present study, L-methionine led to a concentration-dependent induction of the antioxidant proteins heme oxygenase-1 (HO-1) and ferritin in cultured endothelial cells (ECV 304).	Methionine	22-34	heme oxygenase 1	Homo sapiens	124-128
16146339-5	2005	The antioxidant effect of L-methionine was mimicked by the HO-1 product bilirubin, which suppressed free radical formation almost completely.	Methionine	26-38	heme oxygenase 1	Homo sapiens	59-63
16146339-5	2005	The antioxidant effect of L-methionine was mimicked by the HO-1 product bilirubin, which suppressed free radical formation almost completely.	Bilirubin	72-81	heme oxygenase 1	Homo sapiens	59-63
16146339-7	2005	These findings demonstrate that L-methionine reduces free radical formation in endothelial cells, possibly through induction of heme oxygenase-1 and ferritin.	Methionine	32-44	heme oxygenase 1	Homo sapiens	128-144
15993853-0	2005	Sequential induction of heme oxygenase-1 and manganese superoxide dismutase protects cultured astrocytes against nitric oxide.	Nitric Oxide	113-125	heme oxygenase 1	Homo sapiens	24-40
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Heme	84-88	heme oxygenase 1	Homo sapiens	12-28
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Heme	84-88	heme oxygenase 1	Homo sapiens	30-34
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Bilirubin	92-101	heme oxygenase 1	Homo sapiens	12-28
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Bilirubin	92-101	heme oxygenase 1	Homo sapiens	30-34
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Carbon Monoxide	116-131	heme oxygenase 1	Homo sapiens	12-28
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Carbon Monoxide	116-131	heme oxygenase 1	Homo sapiens	30-34
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Carbon Monoxide	133-135	heme oxygenase 1	Homo sapiens	12-28
16117883-1	2005	BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function.	Carbon Monoxide	133-135	heme oxygenase 1	Homo sapiens	30-34
16455537-3	2005	A length polymorphic variant of the HO-1 gene promoter region, comprising (GT)n dinucleotide repeats, is associated with altered levels of gene transcription: long (= 36 GT) repeats are associated with decreased HO-1.	Dinucleoside Phosphates	80-92	heme oxygenase 1	Homo sapiens	36-40
16455537-3	2005	A length polymorphic variant of the HO-1 gene promoter region, comprising (GT)n dinucleotide repeats, is associated with altered levels of gene transcription: long (= 36 GT) repeats are associated with decreased HO-1.	Dinucleoside Phosphates	80-92	heme oxygenase 1	Homo sapiens	212-216
15880142-7	2005	CORM-2 or CORM-3 did not cause any evident cytotoxicity and produced an increase in HO-1 expression and heme oxygenase activity; this effect was completely prevented by the thiol donor N-acetylcysteine.	Sulfhydryl Compounds	173-178	heme oxygenase 1	Homo sapiens	84-88
15964514-2	2005	In the present study we investigated induction of HO-1 and adaptive increases in reduced glutathione (GSH) in human aortic smooth muscle cells (SMC) in response to moderately oxidized LDL (moxLDL, 100 microg protein/ml, 24 h), a species containing high levels of lipid hydroperoxides.	moxldl	189-195	heme oxygenase 1	Homo sapiens	50-54
15964514-3	2005	Expression and activity of HO-1 and GSH levels were elevated to a greater extent by moxLDL than highly oxidized LDL but unaffected by native or acetylated LDL.	moxldl	84-90	heme oxygenase 1	Homo sapiens	27-31
15964514-6	2005	Pretreatment of SMC with the antioxidant vitamin C (100 microM, 24 h) attenuated the induction of HO-1 by moxLDL.	Ascorbic Acid	41-50	heme oxygenase 1	Homo sapiens	98-102
15964514-6	2005	Pretreatment of SMC with the antioxidant vitamin C (100 microM, 24 h) attenuated the induction of HO-1 by moxLDL.	moxldl	106-112	heme oxygenase 1	Homo sapiens	98-102
15964514-8	2005	These findings demonstrate for the first time that activation of PKC, p38(MAPK), JNK, ERK1/2, and Nrf2 by oxidized LDL in human SMC leads to HO-1 induction, constituting an adaptive response against oxidative injury that can be ameliorated by vitamin C.	Ascorbic Acid	243-252	heme oxygenase 1	Homo sapiens	141-145
15993334-9	2005	Whereas inhibiting the ERK pathway with the MEK inhibitor PD98059 significantly decreased HNE-mediated ERK phosphorylation, c-Fos protein induction, AP-1 binding, and HO-1 protein induction, inhibition of the ERK pathway had no effect on HNE-induced HO-1 mRNA.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	58-65	heme oxygenase 1	Homo sapiens	167-171
15993334-9	2005	Whereas inhibiting the ERK pathway with the MEK inhibitor PD98059 significantly decreased HNE-mediated ERK phosphorylation, c-Fos protein induction, AP-1 binding, and HO-1 protein induction, inhibition of the ERK pathway had no effect on HNE-induced HO-1 mRNA.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	58-65	heme oxygenase 1	Homo sapiens	250-254
15880142-7	2005	CORM-2 or CORM-3 did not cause any evident cytotoxicity and produced an increase in HO-1 expression and heme oxygenase activity; this effect was completely prevented by the thiol donor N-acetylcysteine.	Acetylcysteine	185-201	heme oxygenase 1	Homo sapiens	84-88
15925276-3	2005	The upregulation of HO-1 can be achieved through the use of pharmaceutical agents, such as metalloporphyrins and some HMG-CoA reductase inhibitors.	Metalloporphyrins	91-108	heme oxygenase 1	Homo sapiens	20-24
16181113-3	2005	In a prior study, we reported that increasing HO-1 expression by adenoviral gene transfer prior to hemin exposure attenuated oxidative stress and cell death in astrocytes.	Hemin	99-104	heme oxygenase 1	Homo sapiens	46-50
16181113-7	2005	Treatment of cortical astrocyte cultures with 1 microM MG-132 resulted in a rapid increase in Nrf2, to a level that was five-fold that of vehicle-treated cultures by 2 h. This was followed by a three to six-fold increase in HO-1 expression that persisted through the 16 h observation period.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	55-61	heme oxygenase 1	Homo sapiens	224-228
16181113-12	2005	These results suggest that increasing HO-1 expression with a proteasome inhibitor protects astrocytes from heme-mediated oxidative injury.	Heme	107-111	heme oxygenase 1	Homo sapiens	38-42
15925276-4	2005	Among other agents, atrial natriretic peptide and donors of nitric oxide (NO) are important modulators of the heme-HO system, either through induction of HO-1 or the biological activity of its products.	Nitric Oxide	60-72	heme oxygenase 1	Homo sapiens	154-158
15925276-8	2005	In other cardiovascular situations, delivery of human HO-1 to hyperglycemic rats significantly lowers superoxide (O(2)(-)) levels and prevents EC damage and sloughing of vascular EC into the circulation.	Superoxides	102-112	heme oxygenase 1	Homo sapiens	54-58
15925276-8	2005	In other cardiovascular situations, delivery of human HO-1 to hyperglycemic rats significantly lowers superoxide (O(2)(-)) levels and prevents EC damage and sloughing of vascular EC into the circulation.	Superoxides	114-118	heme oxygenase 1	Homo sapiens	54-58
15920743-5	2005	The results showed that the treatment of differentiated NB cells with PGA1 for a period of 48 hr increased the expression of HO-1 and catalase, decreased the expression of GPx1 and Mn-SOD-2, and did not change the expression of Cu/Zn-SOD-1 as measured by gene array and confirmed by real-time PCR.	prostaglandin A1	70-74	heme oxygenase 1	Homo sapiens	125-142
16240585-1	2005	Heme oxygenase 1 (HO-1) catalyses the oxidation of heme to biliverdin, and its expression is induced by oxidative stress.	Heme	51-55	heme oxygenase 1	Homo sapiens	0-16
16240585-1	2005	Heme oxygenase 1 (HO-1) catalyses the oxidation of heme to biliverdin, and its expression is induced by oxidative stress.	Heme	51-55	heme oxygenase 1	Homo sapiens	18-22
16240585-1	2005	Heme oxygenase 1 (HO-1) catalyses the oxidation of heme to biliverdin, and its expression is induced by oxidative stress.	Biliverdine	59-69	heme oxygenase 1	Homo sapiens	0-16
16240585-1	2005	Heme oxygenase 1 (HO-1) catalyses the oxidation of heme to biliverdin, and its expression is induced by oxidative stress.	Biliverdine	59-69	heme oxygenase 1	Homo sapiens	18-22
16240585-9	2005	The present study demonstrates a correlation between PAH exposure, as assessed by urinary 1-OHP, and the induction of HO-1 expression.	p-Aminohippuric Acid	53-56	heme oxygenase 1	Homo sapiens	118-122
16240585-9	2005	The present study demonstrates a correlation between PAH exposure, as assessed by urinary 1-OHP, and the induction of HO-1 expression.	Oxaliplatin	90-95	heme oxygenase 1	Homo sapiens	118-122
15833736-0	2005	Heme oxygenase-1 gene activation by the NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride via a protein kinase B, p38-dependent signaling pathway in monocytes.	4-(2-aminoethyl)benzenesulfonylfluoride	66-107	heme oxygenase 1	Homo sapiens	0-16
15876423-11	2005	These data suggest that induction of HO-1 protein may participate in the protective mechanism of QE on oxidative stress (H(2)O(2))-induced apoptosis, and reduction of intracellular ROS production and mitochondria dysfunction with blocking apoptotic events were involved.	ros	181-184	heme oxygenase 1	Homo sapiens	37-41
15876423-12	2005	Differential anti-apoptotic effect between QE and its glycosides RUT and QI via distinct HO-1 protein induction was also delineated.	Glycosides	54-64	heme oxygenase 1	Homo sapiens	89-93
15896810-13	2005	Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	203-218	heme oxygenase 1	Homo sapiens	24-29
15896810-13	2005	Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	203-218	heme oxygenase 1	Homo sapiens	63-67
15896810-13	2005	Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	203-218	heme oxygenase 1	Homo sapiens	149-153
15896810-13	2005	Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	246-255	heme oxygenase 1	Homo sapiens	24-29
15896810-13	2005	Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	246-255	heme oxygenase 1	Homo sapiens	63-67
15896810-13	2005	Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	246-255	heme oxygenase 1	Homo sapiens	149-153
15876423-0	2005	Quercetin, but not rutin and quercitrin, prevention of H2O2-induced apoptosis via anti-oxidant activity and heme oxygenase 1 gene expression in macrophages.	Quercetin	0-9	heme oxygenase 1	Homo sapiens	108-124
15876423-2	2005	Results of Western blotting show that QE but not its glycoside rutin (RUT) and quicitrin-induced HO-1 protein expression in a time- and dose-dependent manner, and HO-1 protein induced by QE was blocked by an addition of cycloheximide or actinomycin D.	Cycloheximide	220-233	heme oxygenase 1	Homo sapiens	163-167
15876423-2	2005	Results of Western blotting show that QE but not its glycoside rutin (RUT) and quicitrin-induced HO-1 protein expression in a time- and dose-dependent manner, and HO-1 protein induced by QE was blocked by an addition of cycloheximide or actinomycin D.	Dactinomycin	237-250	heme oxygenase 1	Homo sapiens	163-167
15876423-4	2005	Addition of PD98059, but not SB203580 or SP600125, significantly attenuates QE-induced HO-1 protein and mRNA expression associated with blocking the expression of phosphorylated ERKs proteins.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	12-19	heme oxygenase 1	Homo sapiens	87-91
15876423-10	2005	Furthermore, HO-1 catalytic metabolites carbon monoxide (CO), but not Fe(2+), Fe(3+), biliverdin or bilirubin, performed protective effect on cells from H(2)O(2)-induced cell death with an increase in HO-1 protein expression and ERKs protein phosphorylation.	Carbon Monoxide	40-55	heme oxygenase 1	Homo sapiens	13-17
15876423-10	2005	Furthermore, HO-1 catalytic metabolites carbon monoxide (CO), but not Fe(2+), Fe(3+), biliverdin or bilirubin, performed protective effect on cells from H(2)O(2)-induced cell death with an increase in HO-1 protein expression and ERKs protein phosphorylation.	Carbon Monoxide	40-55	heme oxygenase 1	Homo sapiens	201-205
15876423-10	2005	Furthermore, HO-1 catalytic metabolites carbon monoxide (CO), but not Fe(2+), Fe(3+), biliverdin or bilirubin, performed protective effect on cells from H(2)O(2)-induced cell death with an increase in HO-1 protein expression and ERKs protein phosphorylation.	Carbon Monoxide	57-59	heme oxygenase 1	Homo sapiens	13-17
15876423-10	2005	Furthermore, HO-1 catalytic metabolites carbon monoxide (CO), but not Fe(2+), Fe(3+), biliverdin or bilirubin, performed protective effect on cells from H(2)O(2)-induced cell death with an increase in HO-1 protein expression and ERKs protein phosphorylation.	Carbon Monoxide	57-59	heme oxygenase 1	Homo sapiens	201-205
15833736-2	2005	Because HO-1 is up-regulated by NAD(P)H oxidase activators such as lipopolysaccharide and 12-O-tetradecanoylphorbol-13-acetate in monocytic cells, we investigated the gene regulation of HO-1 by the chemical NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride (AEBSF).	4-(2-aminoethyl)benzenesulfonylfluoride	233-274	heme oxygenase 1	Homo sapiens	8-12
15833736-2	2005	Because HO-1 is up-regulated by NAD(P)H oxidase activators such as lipopolysaccharide and 12-O-tetradecanoylphorbol-13-acetate in monocytic cells, we investigated the gene regulation of HO-1 by the chemical NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride (AEBSF).	4-(2-aminoethyl)benzenesulfonylfluoride	276-281	heme oxygenase 1	Homo sapiens	8-12
15833736-9	2005	Finally, AEBSF- and PKB-dependent induction of HO-1 promoter activity was reduced by simultaneous mutation of an E-box motif (-47/-42) and a cAMP response element/AP-1 element (-664/-657) of the proximal HO-1 gene promoter.	Cyclic AMP	141-145	heme oxygenase 1	Homo sapiens	47-51
15833736-1	2005	Heme oxygenase (HO)-1 is the inducible isoform of the rate-limiting enzyme of heme degradation and modulates the inflammatory immune response.	Heme	78-82	heme oxygenase 1	Homo sapiens	0-21
15833736-2	2005	Because HO-1 is up-regulated by NAD(P)H oxidase activators such as lipopolysaccharide and 12-O-tetradecanoylphorbol-13-acetate in monocytic cells, we investigated the gene regulation of HO-1 by the chemical NAD(P)H oxidase inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride (AEBSF).	Tetradecanoylphorbol Acetate	90-126	heme oxygenase 1	Homo sapiens	8-12
15930299-0	2005	The synthetic triterpenoids, CDDO and CDDO-imidazolide, are potent inducers of heme oxygenase-1 and Nrf2/ARE signaling.	triterpenoids	14-27	heme oxygenase 1	Homo sapiens	79-95
15930299-0	2005	The synthetic triterpenoids, CDDO and CDDO-imidazolide, are potent inducers of heme oxygenase-1 and Nrf2/ARE signaling.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	29-33	heme oxygenase 1	Homo sapiens	79-95
15930299-0	2005	The synthetic triterpenoids, CDDO and CDDO-imidazolide, are potent inducers of heme oxygenase-1 and Nrf2/ARE signaling.	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	38-54	heme oxygenase 1	Homo sapiens	79-95
15930299-3	2005	Transfection studies using a series of reporter constructs show that activation of the human HO-1 promoter by the triterpenoids requires an antioxidant response element (ARE), a cyclic AMP response element, and an E Box sequence.	triterpenoids	114-127	heme oxygenase 1	Homo sapiens	93-97
15930299-3	2005	Transfection studies using a series of reporter constructs show that activation of the human HO-1 promoter by the triterpenoids requires an antioxidant response element (ARE), a cyclic AMP response element, and an E Box sequence.	Cyclic AMP	178-188	heme oxygenase 1	Homo sapiens	93-97
15930299-7	2005	These studies are the first to investigate the induction of the HO-1 and Nrf2/ARE pathways by CDDO and CDDO-Im, and our results suggest that further in vivo studies are needed to explore the chemopreventive and chemotherapeutic potential of the triterpenoids.	2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid	94-98	heme oxygenase 1	Homo sapiens	64-68
15930299-7	2005	These studies are the first to investigate the induction of the HO-1 and Nrf2/ARE pathways by CDDO and CDDO-Im, and our results suggest that further in vivo studies are needed to explore the chemopreventive and chemotherapeutic potential of the triterpenoids.	1-(2-cyano-3,12-dioxooleana-1,9-dien-28-oyl) imidazole	103-110	heme oxygenase 1	Homo sapiens	64-68
15930299-7	2005	These studies are the first to investigate the induction of the HO-1 and Nrf2/ARE pathways by CDDO and CDDO-Im, and our results suggest that further in vivo studies are needed to explore the chemopreventive and chemotherapeutic potential of the triterpenoids.	triterpenoids	245-258	heme oxygenase 1	Homo sapiens	64-68
15932518-4	2005	In vitro induction of HO-1 by the HO-1 inducer cobalt protoporphyrin (CoPP) resulted in a dose-dependent down-regulation of caspase-3 activation in HT-29 cells, indicating an anti-apoptotic function of HO-1 in the intestine.	cobaltiprotoporphyrin	47-68	heme oxygenase 1	Homo sapiens	22-26
15681695-5	2005	Increased HO-1 expression in VSMCs leads to increased production of CO and its second messenger cGMP, which are important regulators of vascular tone and paracrine interactions in the vasculature.	Carbon Monoxide	68-70	heme oxygenase 1	Homo sapiens	10-14
15681695-5	2005	Increased HO-1 expression in VSMCs leads to increased production of CO and its second messenger cGMP, which are important regulators of vascular tone and paracrine interactions in the vasculature.	Cyclic GMP	96-100	heme oxygenase 1	Homo sapiens	10-14
15932518-4	2005	In vitro induction of HO-1 by the HO-1 inducer cobalt protoporphyrin (CoPP) resulted in a dose-dependent down-regulation of caspase-3 activation in HT-29 cells, indicating an anti-apoptotic function of HO-1 in the intestine.	cobaltiprotoporphyrin	47-68	heme oxygenase 1	Homo sapiens	34-38
15932518-5	2005	In vivo, preventive HO-1 induction by CoPP in acute dextran sodium sulphate (DSS)-induced colitis led to a significant down-regulation of colonic inflammation (P &lt; 0.01) with a concomitant reduction in interferon (IFN)-gamma - but unaffected interleukin (IL)-10-secretion by isolated mesenteric lymph nodes (P &lt; 0.01).	dss	77-80	heme oxygenase 1	Homo sapiens	20-24
15932518-4	2005	In vitro induction of HO-1 by the HO-1 inducer cobalt protoporphyrin (CoPP) resulted in a dose-dependent down-regulation of caspase-3 activation in HT-29 cells, indicating an anti-apoptotic function of HO-1 in the intestine.	cobaltiprotoporphyrin	47-68	heme oxygenase 1	Homo sapiens	34-38
15932518-4	2005	In vitro induction of HO-1 by the HO-1 inducer cobalt protoporphyrin (CoPP) resulted in a dose-dependent down-regulation of caspase-3 activation in HT-29 cells, indicating an anti-apoptotic function of HO-1 in the intestine.	cobaltiprotoporphyrin	70-74	heme oxygenase 1	Homo sapiens	22-26
15932518-4	2005	In vitro induction of HO-1 by the HO-1 inducer cobalt protoporphyrin (CoPP) resulted in a dose-dependent down-regulation of caspase-3 activation in HT-29 cells, indicating an anti-apoptotic function of HO-1 in the intestine.	cobaltiprotoporphyrin	70-74	heme oxygenase 1	Homo sapiens	34-38
15932518-4	2005	In vitro induction of HO-1 by the HO-1 inducer cobalt protoporphyrin (CoPP) resulted in a dose-dependent down-regulation of caspase-3 activation in HT-29 cells, indicating an anti-apoptotic function of HO-1 in the intestine.	cobaltiprotoporphyrin	70-74	heme oxygenase 1	Homo sapiens	34-38
15932518-5	2005	In vivo, preventive HO-1 induction by CoPP in acute dextran sodium sulphate (DSS)-induced colitis led to a significant down-regulation of colonic inflammation (P &lt; 0.01) with a concomitant reduction in interferon (IFN)-gamma - but unaffected interleukin (IL)-10-secretion by isolated mesenteric lymph nodes (P &lt; 0.01).	dextran sodium sulphate	52-75	heme oxygenase 1	Homo sapiens	20-24
15911218-0	2005	AZD3582 increases heme oxygenase-1 expression and antioxidant activity in vascular endothelial and gastric mucosal cells.	naproxen-n-butyl nitrate	0-7	heme oxygenase 1	Homo sapiens	18-34
15911218-2	2005	Incubation of human endothelial cells (derived from umbilical cord) with AZD3582 (10-100muM) led to increased expression of heme oxygenase (HO)-1 mRNA and protein.	naproxen-n-butyl nitrate	73-80	heme oxygenase 1	Homo sapiens	124-145
15911218-5	2005	Pre-treating endothelial cells with AZD3582 at concentrations that were effective at inducing HO-1 also reduced NADPH-dependent production of oxygen radicals.	naproxen-n-butyl nitrate	36-43	heme oxygenase 1	Homo sapiens	94-98
15911218-5	2005	Pre-treating endothelial cells with AZD3582 at concentrations that were effective at inducing HO-1 also reduced NADPH-dependent production of oxygen radicals.	NADP	112-117	heme oxygenase 1	Homo sapiens	94-98
15911218-5	2005	Pre-treating endothelial cells with AZD3582 at concentrations that were effective at inducing HO-1 also reduced NADPH-dependent production of oxygen radicals.	Reactive Oxygen Species	142-157	heme oxygenase 1	Homo sapiens	94-98
15911218-7	2005	When added exogenously to the cells at low micromolar concentrations, the HO-1 metabolite, bilirubin, virtually abolished NADPH-dependent oxidative stress.	Bilirubin	91-100	heme oxygenase 1	Homo sapiens	74-78
15911218-7	2005	When added exogenously to the cells at low micromolar concentrations, the HO-1 metabolite, bilirubin, virtually abolished NADPH-dependent oxidative stress.	NADP	122-127	heme oxygenase 1	Homo sapiens	74-78
15911218-8	2005	AZD3582-induced blockade of free-radical formation was reversed in the presence of the HO-1 inhibitor, tin protoporphyrin-IX (SnPP).	naproxen-n-butyl nitrate	0-7	heme oxygenase 1	Homo sapiens	87-91
15911218-8	2005	AZD3582-induced blockade of free-radical formation was reversed in the presence of the HO-1 inhibitor, tin protoporphyrin-IX (SnPP).	tin protoporphyrin IX	103-124	heme oxygenase 1	Homo sapiens	87-91
15911218-8	2005	AZD3582-induced blockade of free-radical formation was reversed in the presence of the HO-1 inhibitor, tin protoporphyrin-IX (SnPP).	S-Nitroso-N-propionyl-D,L-penicillamine	126-130	heme oxygenase 1	Homo sapiens	87-91
15911218-10	2005	Our results demonstrate that HO-1 is a novel target of AZD3582.	naproxen-n-butyl nitrate	55-62	heme oxygenase 1	Homo sapiens	29-33
15927501-4	2005	Heme is catabolised by heme oxygenase 1, anchored in the endoplasmic reticulum membrane.	Heme	0-4	heme oxygenase 1	Homo sapiens	23-39
16044631-5	2005	In particular, heme oxygenase-1 (HO-1), the enzyme involved in heme protein metabolism, can provide antioxidant protection through the production of the antioxidant bilirubin.	Heme	15-19	heme oxygenase 1	Homo sapiens	33-37
16044631-5	2005	In particular, heme oxygenase-1 (HO-1), the enzyme involved in heme protein metabolism, can provide antioxidant protection through the production of the antioxidant bilirubin.	Bilirubin	165-174	heme oxygenase 1	Homo sapiens	15-31
16044631-5	2005	In particular, heme oxygenase-1 (HO-1), the enzyme involved in heme protein metabolism, can provide antioxidant protection through the production of the antioxidant bilirubin.	Bilirubin	165-174	heme oxygenase 1	Homo sapiens	33-37
16044631-6	2005	Furthermore, polyamines have been shown to indirectly increase HO-1 content and antioxidant protection.	Polyamines	13-23	heme oxygenase 1	Homo sapiens	63-67
16044631-7	2005	The beta2-adrenoceptor agonist clenbuterol has been shown to stimulate polyamine synthesis and by extension, might provide a margin of antioxidant protection through increasing HO-1 content.	Clenbuterol	31-42	heme oxygenase 1	Homo sapiens	177-181
15853972-0	2005	The up-regulation of heme oxygenase-1 expression in human gingival fibroblasts stimulated with nicotine.	Nicotine	95-103	heme oxygenase 1	Homo sapiens	21-37
15853972-4	2005	OBJECTIVES: The aim of the present study was to investigate the effects of nicotine on the expression of HO-1 protein in cultured human gingival fibroblasts in vitro and further to compare HO-1 expression in gingival tissues obtained from cigarette smokers and non-smokers in vivo.	Nicotine	75-83	heme oxygenase 1	Homo sapiens	105-109
15853972-6	2005	In addition, antioxidants catalase, superoxide dismutase (SOD), and N-acetyl-l-cysteine (NAC) were added to test how they modulated the effects on nicotine-induced HO-1 expression.	Nicotine	147-155	heme oxygenase 1	Homo sapiens	164-168
15853972-8	2005	RESULTS: The exposure of quiescent human gingival fibroblasts to 10 mm nicotine resulted in the induction of HO-1 protein expression in a time-dependent manner (p &lt; 0.05).	Nicotine	71-79	heme oxygenase 1	Homo sapiens	109-113
15853972-9	2005	The addition of glutathione (GSH) precursor NAC inhibited the nicotine-induced HO-1 protein expression (p &lt; 0.05).	Glutathione	16-27	heme oxygenase 1	Homo sapiens	79-83
15853972-9	2005	The addition of glutathione (GSH) precursor NAC inhibited the nicotine-induced HO-1 protein expression (p &lt; 0.05).	Glutathione	29-32	heme oxygenase 1	Homo sapiens	79-83
15853972-9	2005	The addition of glutathione (GSH) precursor NAC inhibited the nicotine-induced HO-1 protein expression (p &lt; 0.05).	Nicotine	62-70	heme oxygenase 1	Homo sapiens	79-83
15853972-13	2005	CONCLUSIONS: Taken together, these results suggest that HO-1 expression is significantly up-regulated in gingival tissues from cigarette smokers, and nicotine may, among other constituents, be responsible for the enhanced HO-1 expression in vivo.	Nicotine	150-158	heme oxygenase 1	Homo sapiens	222-226
15853972-14	2005	The regulation of HO-1 expression induced by nicotine is critically dependent on the intracellular GSH concentration.	Nicotine	45-53	heme oxygenase 1	Homo sapiens	18-22
15853972-14	2005	The regulation of HO-1 expression induced by nicotine is critically dependent on the intracellular GSH concentration.	Glutathione	99-102	heme oxygenase 1	Homo sapiens	18-22
15855051-7	2005	DEM plus LPS caused synergistic induction of heme oxygenase-1 (HO-1), suggesting its role in the inhibitory effects of DEM.	diethyl maleate	0-3	heme oxygenase 1	Homo sapiens	45-61
15855051-7	2005	DEM plus LPS caused synergistic induction of heme oxygenase-1 (HO-1), suggesting its role in the inhibitory effects of DEM.	diethyl maleate	0-3	heme oxygenase 1	Homo sapiens	63-67
16020198-8	2005	Acute exposure to Cd was found to trigger the upregulation of genes encoding the chaperone proteins HSP90A, HSP27, HSP40, GRP78, HSP72, and HO-1 in S-cells.	Cadmium	18-20	heme oxygenase 1	Homo sapiens	140-144
15897578-9	2005	Treatment of the pancreatic cancer cell lines with gemcitabine or radiation strongly induced HO-1 expression.	gemcitabine	51-62	heme oxygenase 1	Homo sapiens	93-97
15890016-1	2005	Heme oxygenase isoforms (HO-1/HO-2) catalyze the conversion of heme to carbon monoxide (CO) and bilirubin.	Heme	63-67	heme oxygenase 1	Homo sapiens	0-34
15965068-4	2005	To investigate the molecular basis of the renal injury, we evaluated the expression of the stress marker, heme oxygenase-1 (HO-1), in celecoxib-stimulated mesangial cells.	Celecoxib	134-143	heme oxygenase 1	Homo sapiens	106-122
15965068-4	2005	To investigate the molecular basis of the renal injury, we evaluated the expression of the stress marker, heme oxygenase-1 (HO-1), in celecoxib-stimulated mesangial cells.	Celecoxib	134-143	heme oxygenase 1	Homo sapiens	124-128
15965068-5	2005	We report here that a COX-2 selective NSAID, celecoxib, induced a concentration- and time-dependent increase of HO-1 expression in glomerular mesangial cells.	Celecoxib	45-54	heme oxygenase 1	Homo sapiens	112-116
15965068-6	2005	Celecoxib-induced HO-1 protein expression was inhibited by actinomycin D and cycloheximide, suggesting that de novo transcription and translation are required in this process.	Celecoxib	0-9	heme oxygenase 1	Homo sapiens	18-22
15965068-6	2005	Celecoxib-induced HO-1 protein expression was inhibited by actinomycin D and cycloheximide, suggesting that de novo transcription and translation are required in this process.	Dactinomycin	59-72	heme oxygenase 1	Homo sapiens	18-22
15965068-6	2005	Celecoxib-induced HO-1 protein expression was inhibited by actinomycin D and cycloheximide, suggesting that de novo transcription and translation are required in this process.	Cycloheximide	77-90	heme oxygenase 1	Homo sapiens	18-22
15965068-7	2005	N-acetylcysteine, a free radical scavenger, strongly decreased HO-1 expression, suggesting the involvement of reactive oxygen species (ROS).	Acetylcysteine	0-16	heme oxygenase 1	Homo sapiens	63-67
15965068-7	2005	N-acetylcysteine, a free radical scavenger, strongly decreased HO-1 expression, suggesting the involvement of reactive oxygen species (ROS).	Reactive Oxygen Species	110-133	heme oxygenase 1	Homo sapiens	63-67
15890016-1	2005	Heme oxygenase isoforms (HO-1/HO-2) catalyze the conversion of heme to carbon monoxide (CO) and bilirubin.	Carbon Monoxide	71-86	heme oxygenase 1	Homo sapiens	0-34
15965068-7	2005	N-acetylcysteine, a free radical scavenger, strongly decreased HO-1 expression, suggesting the involvement of reactive oxygen species (ROS).	Reactive Oxygen Species	135-138	heme oxygenase 1	Homo sapiens	63-67
15890016-1	2005	Heme oxygenase isoforms (HO-1/HO-2) catalyze the conversion of heme to carbon monoxide (CO) and bilirubin.	Carbon Monoxide	88-90	heme oxygenase 1	Homo sapiens	0-34
15965068-8	2005	Celecoxib-induced HO-1 expression was attenuated by pretreatment of the cells with SP 600125 (a specific JNK inhibitor), but not SB 203580 (a specific p38 MAPK inhibitor), or PD 98059 (a specific MEK inhibitor).	Celecoxib	0-9	heme oxygenase 1	Homo sapiens	18-22
15890016-1	2005	Heme oxygenase isoforms (HO-1/HO-2) catalyze the conversion of heme to carbon monoxide (CO) and bilirubin.	Bilirubin	96-105	heme oxygenase 1	Homo sapiens	0-34
15965068-8	2005	Celecoxib-induced HO-1 expression was attenuated by pretreatment of the cells with SP 600125 (a specific JNK inhibitor), but not SB 203580 (a specific p38 MAPK inhibitor), or PD 98059 (a specific MEK inhibitor).	pyrazolanthrone	83-92	heme oxygenase 1	Homo sapiens	18-22
15689417-0	2005	Oxidative stress mediates sodium arsenite-induced expression of heme oxygenase-1, monocyte chemoattractant protein-1, and interleukin-6 in vascular smooth muscle cells.	sodium arsenite	26-41	heme oxygenase 1	Homo sapiens	64-80
15965068-10	2005	N-acetylcysteine reduced the stimulatory effect of celecoxib on stress kinase activities, suggesting an involvement of JNK in HO-1 expression.	Acetylcysteine	0-16	heme oxygenase 1	Homo sapiens	126-130
15965068-10	2005	N-acetylcysteine reduced the stimulatory effect of celecoxib on stress kinase activities, suggesting an involvement of JNK in HO-1 expression.	Celecoxib	51-60	heme oxygenase 1	Homo sapiens	126-130
15965068-11	2005	On the other hand, LY 294002, a phosphatidylinositol 3-kinase (PI-3K)-specific inhibitor, prevented the enhancement of HO-1 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	19-28	heme oxygenase 1	Homo sapiens	119-123
15965068-13	2005	In conclusion, our data suggest that celecoxib-induced HO-1 expression in glomerular mesangial cells may be mediated by ROS via the JNK-PI-3K cascade.	Celecoxib	37-46	heme oxygenase 1	Homo sapiens	55-59
15965068-13	2005	In conclusion, our data suggest that celecoxib-induced HO-1 expression in glomerular mesangial cells may be mediated by ROS via the JNK-PI-3K cascade.	Reactive Oxygen Species	120-123	heme oxygenase 1	Homo sapiens	55-59
15855326-1	2005	Treatment of animals or certain cells with carbon monoxide (CO), a product of heme degradation by heme oxygenase-1 (HO-1), has potent anti-inflammatory and antiapoptotic effects that contribute to the survival of transplanted organs.	Carbon Monoxide	43-58	heme oxygenase 1	Homo sapiens	98-114
15855326-1	2005	Treatment of animals or certain cells with carbon monoxide (CO), a product of heme degradation by heme oxygenase-1 (HO-1), has potent anti-inflammatory and antiapoptotic effects that contribute to the survival of transplanted organs.	Carbon Monoxide	43-58	heme oxygenase 1	Homo sapiens	116-120
15855326-1	2005	Treatment of animals or certain cells with carbon monoxide (CO), a product of heme degradation by heme oxygenase-1 (HO-1), has potent anti-inflammatory and antiapoptotic effects that contribute to the survival of transplanted organs.	Carbon Monoxide	60-62	heme oxygenase 1	Homo sapiens	98-114
15855326-1	2005	Treatment of animals or certain cells with carbon monoxide (CO), a product of heme degradation by heme oxygenase-1 (HO-1), has potent anti-inflammatory and antiapoptotic effects that contribute to the survival of transplanted organs.	Carbon Monoxide	60-62	heme oxygenase 1	Homo sapiens	116-120
15843512-4	2005	In this study, we present a model for Treg activity that implicates carbon monoxide, a by-product of heme oxygenase-1 activity, as an important and underappreciated facet in the suppressive capacity of Treg.	Carbon Monoxide	68-83	heme oxygenase 1	Homo sapiens	101-117
15689417-8	2005	Furthermore, using tin protoporphyrin IX (SnPP) and anti-MCP-1 antibody to abolish iAs-induced HO-1 and MCP-1 activity, respectively, shows that HO-1 has protective effect against iAs-induced injury in VSMCs and MCP-1 is chemoattractive to human monocytes, THP-1.	S-Nitroso-N-propionyl-D,L-penicillamine	42-46	heme oxygenase 1	Homo sapiens	95-99
15689417-8	2005	Furthermore, using tin protoporphyrin IX (SnPP) and anti-MCP-1 antibody to abolish iAs-induced HO-1 and MCP-1 activity, respectively, shows that HO-1 has protective effect against iAs-induced injury in VSMCs and MCP-1 is chemoattractive to human monocytes, THP-1.	S-Nitroso-N-propionyl-D,L-penicillamine	42-46	heme oxygenase 1	Homo sapiens	145-149
15661856-1	2005	Heme oxygenase (HO)-1 has been shown to be an important biological target of nitric oxide (NO).	Nitric Oxide	77-89	heme oxygenase 1	Homo sapiens	0-21
15834314-2	2005	The inducible form of heme oxygenase-1 (HO-1) can be induced by cytokines, lipopolysaccharide, and reactive oxygen species during sepsis.	Reactive Oxygen Species	99-122	heme oxygenase 1	Homo sapiens	22-38
15834314-2	2005	The inducible form of heme oxygenase-1 (HO-1) can be induced by cytokines, lipopolysaccharide, and reactive oxygen species during sepsis.	Reactive Oxygen Species	99-122	heme oxygenase 1	Homo sapiens	40-44
15689417-6	2005	In iAs-treated rVSMCs, catalase, dimethylsulfoxide, and L-omega-nitro-L-arginine significantly inhibited the increase in expression of all three genes, allopurinol inhibited the increase in MCP-1 and IL-6 expression, but had no effect on HO-1 expression, while superoxide dismutase had no significant effect on HO-1 expression, but had an inhibitory effect on IL-6 expression and a stimulatory effect on MCP-1 expression.	l-omega-nitro-l-arginine	56-80	heme oxygenase 1	Homo sapiens	238-242
15834587-0	2005	Heme oxygenase-1 accelerates protumoral effects of nitric oxide in cancer cells.	Nitric Oxide	51-63	heme oxygenase 1	Homo sapiens	0-16
15834587-1	2005	We examined the biological effects of nitric oxide (NO) and its mediator, heme oxygenase-1 (HO-1), in cancer.	Nitric Oxide	38-50	heme oxygenase 1	Homo sapiens	92-96
15834587-10	2005	HO-1 inhibition by HO-1 antisense S-oligodeoxynucleotide treatment increased NO-induced growth inhibition, and decreased Bcl-2 expression or VEGF secretion in the three cell lines.	Oligodeoxyribonucleotides	36-56	heme oxygenase 1	Homo sapiens	0-4
15689417-6	2005	In iAs-treated rVSMCs, catalase, dimethylsulfoxide, and L-omega-nitro-L-arginine significantly inhibited the increase in expression of all three genes, allopurinol inhibited the increase in MCP-1 and IL-6 expression, but had no effect on HO-1 expression, while superoxide dismutase had no significant effect on HO-1 expression, but had an inhibitory effect on IL-6 expression and a stimulatory effect on MCP-1 expression.	l-omega-nitro-l-arginine	56-80	heme oxygenase 1	Homo sapiens	311-315
15834587-10	2005	HO-1 inhibition by HO-1 antisense S-oligodeoxynucleotide treatment increased NO-induced growth inhibition, and decreased Bcl-2 expression or VEGF secretion in the three cell lines.	Oligodeoxyribonucleotides	36-56	heme oxygenase 1	Homo sapiens	19-23
15689417-7	2005	Therefore, iAs may enhance the expression of HO-1, MCP-1, and IL-6 in VSMCs via different reactive oxygen molecules.	4-Iodoacetamidosalicylic acid	11-14	heme oxygenase 1	Homo sapiens	45-49
15689417-8	2005	Furthermore, using tin protoporphyrin IX (SnPP) and anti-MCP-1 antibody to abolish iAs-induced HO-1 and MCP-1 activity, respectively, shows that HO-1 has protective effect against iAs-induced injury in VSMCs and MCP-1 is chemoattractive to human monocytes, THP-1.	tin protoporphyrin IX	19-40	heme oxygenase 1	Homo sapiens	95-99
15689417-8	2005	Furthermore, using tin protoporphyrin IX (SnPP) and anti-MCP-1 antibody to abolish iAs-induced HO-1 and MCP-1 activity, respectively, shows that HO-1 has protective effect against iAs-induced injury in VSMCs and MCP-1 is chemoattractive to human monocytes, THP-1.	tin protoporphyrin IX	19-40	heme oxygenase 1	Homo sapiens	145-149
15770161-0	2005	Heme oxygenase-1 induction by dieldrin in dopaminergic cells.	Dieldrin	30-38	heme oxygenase 1	Homo sapiens	0-16
15741166-4	2005	Presently, small interference (si) RNA constructs were used to investigate the role of human BVR in sodium arsenite (As)-mediated induction of HO-1 and in cytoprotection against apoptosis.	sodium arsenite	100-115	heme oxygenase 1	Homo sapiens	143-147
15741166-4	2005	Presently, small interference (si) RNA constructs were used to investigate the role of human BVR in sodium arsenite (As)-mediated induction of HO-1 and in cytoprotection against apoptosis.	arsenite	117-119	heme oxygenase 1	Homo sapiens	143-147
15770161-1	2005	We investigated the transcriptional events and signaling pathways involved in the induction of heme oxygenase-1 (HO-1) by dieldrin, an environmental risk factor of Parkinson"s disease, in a dopaminergic neuronal cells (SN4741).	Dieldrin	122-130	heme oxygenase 1	Homo sapiens	95-111
15770161-1	2005	We investigated the transcriptional events and signaling pathways involved in the induction of heme oxygenase-1 (HO-1) by dieldrin, an environmental risk factor of Parkinson"s disease, in a dopaminergic neuronal cells (SN4741).	Dieldrin	122-130	heme oxygenase 1	Homo sapiens	113-117
15770161-2	2005	Dieldrin exposure caused dose-dependent and time-dependent induction of heme oxygenase activity and HO-1 protein expression.	Dieldrin	0-8	heme oxygenase 1	Homo sapiens	100-104
15770161-3	2005	Deletional and mutational analyses showed that the 5" distal enhancers, E1 and E2, mediate dieldrin-induced HO-1 gene transcription, and the AP-1 DNA binding sites in the E2 enhancer are critical for E2-mediated HO-1 gene activation.	Dieldrin	91-99	heme oxygenase 1	Homo sapiens	108-112
15770161-3	2005	Deletional and mutational analyses showed that the 5" distal enhancers, E1 and E2, mediate dieldrin-induced HO-1 gene transcription, and the AP-1 DNA binding sites in the E2 enhancer are critical for E2-mediated HO-1 gene activation.	Dieldrin	91-99	heme oxygenase 1	Homo sapiens	212-216
15770161-4	2005	Furthermore, both the p38 and JNK mitogen-activated protein kinase pathways are utilized for HO-1 transcriptional activation by dieldrin.	Dieldrin	128-136	heme oxygenase 1	Homo sapiens	93-97
15770161-5	2005	HO-1 inhibitor, ZnPP IX reduced the expression of HO-1 but enhanced the cytotoxicity induced by dieldrin.	zinc protoporphyrin	16-20	heme oxygenase 1	Homo sapiens	50-54
15770161-5	2005	HO-1 inhibitor, ZnPP IX reduced the expression of HO-1 but enhanced the cytotoxicity induced by dieldrin.	Dieldrin	96-104	heme oxygenase 1	Homo sapiens	0-4
15763346-8	2005	Moreover, NASH patients with lower levels of GSH exhibited higher expression of HO-1.	Glutathione	45-48	heme oxygenase 1	Homo sapiens	80-84
15869055-2	2005	These products have important physiologic effects: bilirubin is a potent antioxidant that can act against ischemia/reperfusion injury; there is a negative correlation between the content of HO-1 and the incidence of coronary heart disease (CHD).	Bilirubin	51-60	heme oxygenase 1	Homo sapiens	190-194
16181106-0	2005	Propofol inhibits caspase-3 in astroglial cells: role of heme oxygenase-1.	Propofol	0-8	heme oxygenase 1	Homo sapiens	57-73
16181102-1	2005	Heme oxygenase (HO-1) is a stress protein, which has been suggested to participate in defense mechanisms against glucose induced oxidative injury.	Glucose	113-120	heme oxygenase 1	Homo sapiens	16-20
16181102-2	2005	The purpose of this study was to examine the role of human HO-1 in attenuating glucose-mediated oxidative stress.	Glucose	79-86	heme oxygenase 1	Homo sapiens	59-63
16181102-3	2005	We investigated the effect of high ambient glucose (15, 33 and 66 mM) on HO-1 gene expression in endothelial cells grown in a serum deprived media compared to the effect of glucose on exponentially grown cells (10% FBS).	Glucose	43-50	heme oxygenase 1	Homo sapiens	73-77
16181102-4	2005	High glucose at 15 and 33 mM caused significant inhibition of HO-1 protein and activity in G0/G1 and in cells exponentially grown.	Glucose	5-12	heme oxygenase 1	Homo sapiens	62-66
16181102-5	2005	Glucose concentration at 66 mM caused a significant increase in HO-1.	Glucose	0-7	heme oxygenase 1	Homo sapiens	64-68
16181102-6	2005	Addition of heme (10 microM) increased HO-1 protein and bilirubin formation in G0/G1, in a time dependent manner peaking at 16 h. Glucose attenuated heme mediated increase in HO-1 proteins.	Heme	12-16	heme oxygenase 1	Homo sapiens	39-43
16181102-6	2005	Addition of heme (10 microM) increased HO-1 protein and bilirubin formation in G0/G1, in a time dependent manner peaking at 16 h. Glucose attenuated heme mediated increase in HO-1 proteins.	Heme	12-16	heme oxygenase 1	Homo sapiens	175-179
16181102-7	2005	RT-PCR demonstrated that glucose decreased the levels of HO-1 mRNA in both G0/G1 or cells grown in 10% FBS.	Glucose	25-32	heme oxygenase 1	Homo sapiens	57-61
16181102-8	2005	The rate of HO-1 induction in response to heme was several fold higher in serum-starved cells compared to cells cultured in 10% FBS.	Heme	42-46	heme oxygenase 1	Homo sapiens	12-16
16181102-10	2005	HO-1 gene transduction prevented glucose-mediated elevation of 8-epi-isoprostane PGF(2alpha).	Glucose	33-40	heme oxygenase 1	Homo sapiens	0-4
16181102-10	2005	HO-1 gene transduction prevented glucose-mediated elevation of 8-epi-isoprostane PGF(2alpha).	8-epi-isoprostane	63-80	heme oxygenase 1	Homo sapiens	0-4
16181102-10	2005	HO-1 gene transduction prevented glucose-mediated elevation of 8-epi-isoprostane PGF(2alpha).	Prostaglandins F	81-84	heme oxygenase 1	Homo sapiens	0-4
16181102-11	2005	These results imply that expression of HO-1 in G0/G1 cells may be a key player in decreasing cellular heme, associated with increased generation of bilirubin, and in attenuating glucose mediated oxidative stress.	Heme	102-106	heme oxygenase 1	Homo sapiens	39-43
16181102-11	2005	These results imply that expression of HO-1 in G0/G1 cells may be a key player in decreasing cellular heme, associated with increased generation of bilirubin, and in attenuating glucose mediated oxidative stress.	Bilirubin	148-157	heme oxygenase 1	Homo sapiens	39-43
16181102-11	2005	These results imply that expression of HO-1 in G0/G1 cells may be a key player in decreasing cellular heme, associated with increased generation of bilirubin, and in attenuating glucose mediated oxidative stress.	Glucose	178-185	heme oxygenase 1	Homo sapiens	39-43
15688187-1	2005	Heme oxygenase-1 (HO-1) acts in cytoprotection against oxidants and aromatic hydrocarbons in cigarette smoke.	Hydrocarbons, Aromatic	68-89	heme oxygenase 1	Homo sapiens	0-16
15688187-1	2005	Heme oxygenase-1 (HO-1) acts in cytoprotection against oxidants and aromatic hydrocarbons in cigarette smoke.	Hydrocarbons, Aromatic	68-89	heme oxygenase 1	Homo sapiens	18-22
15618017-2	2005	Overexpression of HSF-1 and heat-shock experiments indicated that HSF-1 repressed the 15d-PGJ2-and arsenite-induced HO-1 gene expression through directly binding to the consensus heat shock element (HSE) of the HO-1 gene promoter.	15-deoxy-delta(12,14)-prostaglandin J2	86-94	heme oxygenase 1	Homo sapiens	116-120
15826493-3	2005	SUL strongly induced Nrf2 protein expression and ARE-mediated transcription activation, retarded degradation of Nrf2 through inhibiting Keap1, and thereby activating the transcriptional expression of HO-1.	sulforaphane	0-3	heme oxygenase 1	Homo sapiens	200-204
15786820-4	2005	METHODS: Real-time RT-PCR was performed for complement component C3 and heme oxygenase-1 (HO-1) genes compared to the housekeeping gene beta-actin using whole section RNA extracted from formalin-fixed and paraffin-embedded archival material of 16 explanted, rejected renal allografts.	Paraffin	205-213	heme oxygenase 1	Homo sapiens	90-94
15618017-2	2005	Overexpression of HSF-1 and heat-shock experiments indicated that HSF-1 repressed the 15d-PGJ2-and arsenite-induced HO-1 gene expression through directly binding to the consensus heat shock element (HSE) of the HO-1 gene promoter.	15-deoxy-delta(12,14)-prostaglandin J2	86-94	heme oxygenase 1	Homo sapiens	211-215
15618017-2	2005	Overexpression of HSF-1 and heat-shock experiments indicated that HSF-1 repressed the 15d-PGJ2-and arsenite-induced HO-1 gene expression through directly binding to the consensus heat shock element (HSE) of the HO-1 gene promoter.	arsenite	99-107	heme oxygenase 1	Homo sapiens	116-120
15618017-2	2005	Overexpression of HSF-1 and heat-shock experiments indicated that HSF-1 repressed the 15d-PGJ2-and arsenite-induced HO-1 gene expression through directly binding to the consensus heat shock element (HSE) of the HO-1 gene promoter.	arsenite	99-107	heme oxygenase 1	Homo sapiens	211-215
15740980-8	2005	When the GSH-depleted or BSO-pretreated macrophages were exposed to NO, delivered either exogenously from spermine NONOate or endogenously from LPS-derived elevation of iNOS, super-induction of HO-1 was observed.	Glutathione	9-12	heme oxygenase 1	Homo sapiens	194-198
15690204-2	2005	Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis.	Glycine	10-18	heme oxygenase 1	Homo sapiens	68-84
15690204-2	2005	Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis.	Glycine	10-18	heme oxygenase 1	Homo sapiens	86-90
15690204-2	2005	Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis.	Glycine	10-18	heme oxygenase 1	Homo sapiens	231-235
15690204-2	2005	Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis.	Heme	68-72	heme oxygenase 1	Homo sapiens	86-90
15690204-2	2005	Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis.	Heme	68-72	heme oxygenase 1	Homo sapiens	231-235
15740980-0	2005	Super-induction of HO-1 in macrophages stimulated with lipopolysaccharide by prior depletion of glutathione decreases iNOS expression and NO production.	Glutathione	96-107	heme oxygenase 1	Homo sapiens	19-23
15740980-2	2005	In response to the depletion of GSH, expression of HO-1 is induced and HO activity is elevated.	Glutathione	32-35	heme oxygenase 1	Homo sapiens	51-55
15740980-6	2005	In support of this, HO-1 is induced in macrophages treated only with buthionine sulfoximine (BSO), an inhibitor of GSH biosynthesis depleting the GSH level.	Buthionine Sulfoximine	69-91	heme oxygenase 1	Homo sapiens	20-24
15740980-6	2005	In support of this, HO-1 is induced in macrophages treated only with buthionine sulfoximine (BSO), an inhibitor of GSH biosynthesis depleting the GSH level.	Buthionine Sulfoximine	93-96	heme oxygenase 1	Homo sapiens	20-24
15740980-6	2005	In support of this, HO-1 is induced in macrophages treated only with buthionine sulfoximine (BSO), an inhibitor of GSH biosynthesis depleting the GSH level.	Glutathione	115-118	heme oxygenase 1	Homo sapiens	20-24
15740980-6	2005	In support of this, HO-1 is induced in macrophages treated only with buthionine sulfoximine (BSO), an inhibitor of GSH biosynthesis depleting the GSH level.	Glutathione	146-149	heme oxygenase 1	Homo sapiens	20-24
15740980-7	2005	Alternatively, when the macrophages were exposed to spermine NONOate, an exogenous NO-donor, HO-1, was induced also.	spermine nitric oxide complex	52-68	heme oxygenase 1	Homo sapiens	93-97
15740980-8	2005	When the GSH-depleted or BSO-pretreated macrophages were exposed to NO, delivered either exogenously from spermine NONOate or endogenously from LPS-derived elevation of iNOS, super-induction of HO-1 was observed.	spermine nitric oxide complex	106-122	heme oxygenase 1	Homo sapiens	194-198
15740980-10	2005	Thus, when the depletion of GSH is combined with NO delivery, expression of HO-1 is enhanced to a greater extent than that enhanced either by GSH depletion or by NO delivery.	Glutathione	28-31	heme oxygenase 1	Homo sapiens	76-80
15740980-10	2005	Thus, when the depletion of GSH is combined with NO delivery, expression of HO-1 is enhanced to a greater extent than that enhanced either by GSH depletion or by NO delivery.	Glutathione	142-145	heme oxygenase 1	Homo sapiens	76-80
15590657-8	2005	Promoter sequence analysis revealed two putative Ets binding sites (EBSs) in this region, and mutation of these sites showed that EBS -93, more than EBS -125, was critical for full HO-1 promoter activity.	ethylbenzene	130-133	heme oxygenase 1	Homo sapiens	181-185
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Heme	141-145	heme oxygenase 1	Homo sapiens	0-16
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Heme	141-145	heme oxygenase 1	Homo sapiens	18-22
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Iron	177-181	heme oxygenase 1	Homo sapiens	0-16
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Iron	177-181	heme oxygenase 1	Homo sapiens	18-22
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Iron	183-185	heme oxygenase 1	Homo sapiens	0-16
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Iron	183-185	heme oxygenase 1	Homo sapiens	18-22
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Biliverdine	188-198	heme oxygenase 1	Homo sapiens	0-16
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Biliverdine	188-198	heme oxygenase 1	Homo sapiens	18-22
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Carbon Monoxide	212-227	heme oxygenase 1	Homo sapiens	0-16
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Carbon Monoxide	212-227	heme oxygenase 1	Homo sapiens	18-22
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Carbon Monoxide	229-231	heme oxygenase 1	Homo sapiens	0-16
15649645-1	2005	Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO).	Carbon Monoxide	229-231	heme oxygenase 1	Homo sapiens	18-22
15649645-4	2005	We will argue that the protective effects exerted by HO-1 are mediated to a large extent by the end products that it generates via the catabolism of heme.	Heme	149-153	heme oxygenase 1	Homo sapiens	53-57
15590657-9	2005	Additional studies showed that EBS -93 binds Ets-2 and that mutation of the DNA binding domain of Ets-2 entirely prevented transactivation of HO-1.	ethylbenzene	31-34	heme oxygenase 1	Homo sapiens	142-146
15466933-4	2005	Treatment with As(2)O(3) and trolox increased intracellular oxidative stress, as evidenced by heme oxygenase-1 (HO-1) protein levels, c-Jun terminal kinase (JNK) activation, and protein and lipid oxidation.	Arsenic Trioxide	15-24	heme oxygenase 1	Homo sapiens	94-110
15466933-4	2005	Treatment with As(2)O(3) and trolox increased intracellular oxidative stress, as evidenced by heme oxygenase-1 (HO-1) protein levels, c-Jun terminal kinase (JNK) activation, and protein and lipid oxidation.	Arsenic Trioxide	15-24	heme oxygenase 1	Homo sapiens	112-116
15466933-4	2005	Treatment with As(2)O(3) and trolox increased intracellular oxidative stress, as evidenced by heme oxygenase-1 (HO-1) protein levels, c-Jun terminal kinase (JNK) activation, and protein and lipid oxidation.	6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid	29-35	heme oxygenase 1	Homo sapiens	94-110
15466933-4	2005	Treatment with As(2)O(3) and trolox increased intracellular oxidative stress, as evidenced by heme oxygenase-1 (HO-1) protein levels, c-Jun terminal kinase (JNK) activation, and protein and lipid oxidation.	6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid	29-35	heme oxygenase 1	Homo sapiens	112-116
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
15629867-7	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
15680334-0	2005	N-acetylcysteine attenuates early induction of heme oxygenase-1 following traumatic brain injury.	Acetylcysteine	0-16	heme oxygenase 1	Homo sapiens	47-63
15680334-3	2005	We have studied the temporal and spatial effects of the antioxidant N-acetylcysteine (NAC) on HO-1 levels following lateral fluid-percussion injury by immunoblotting and immunohistochemistry.	Acetylcysteine	68-84	heme oxygenase 1	Homo sapiens	94-98
15680334-3	2005	We have studied the temporal and spatial effects of the antioxidant N-acetylcysteine (NAC) on HO-1 levels following lateral fluid-percussion injury by immunoblotting and immunohistochemistry.	Acetylcysteine	86-89	heme oxygenase 1	Homo sapiens	94-98
15680334-7	2005	The administration of NAC 5 min following TBI resulted in a marked reduction in this widespread induction of HO-1, concomitant with a decrease in the volume of injury in all three brain regions.	Acetylcysteine	22-25	heme oxygenase 1	Homo sapiens	109-113
15686476-9	2005	Consistent with a cellular stress response to the Abeta(1-42)-induced oxidative stress, FAEE treatment increases the levels of heme oxygenase-1 and heat shock protein 72, which may be regulated by oxidative stresses in a coordinated manner and play a pivotal role in the cytoprotection of neuronal cells against Abeta(1-42)-induced toxicity.	faee	88-92	heme oxygenase 1	Homo sapiens	127-143
15611319-0	2005	Heme-induced heme oxygenase-1 (HO-1) in human monocytes inhibits apoptosis despite caspase-3 up-regulation.	Heme	0-4	heme oxygenase 1	Homo sapiens	13-29
15611319-0	2005	Heme-induced heme oxygenase-1 (HO-1) in human monocytes inhibits apoptosis despite caspase-3 up-regulation.	Heme	0-4	heme oxygenase 1	Homo sapiens	31-35
15611319-2	2005	We studied the effects of heme oxygenase-1 (HO-1) induced by its substrate hemin on apoptosis, caspase-3 expression and the differentiation of freshly isolated human monocytes.	Hemin	75-80	heme oxygenase 1	Homo sapiens	26-42
15611319-2	2005	We studied the effects of heme oxygenase-1 (HO-1) induced by its substrate hemin on apoptosis, caspase-3 expression and the differentiation of freshly isolated human monocytes.	Hemin	75-80	heme oxygenase 1	Homo sapiens	44-48
15611319-3	2005	Hemin induced HO-1 in a dose- and time-dependent fashion as measured by semi-quantitative RT-PCR and flow cytometry.	Hemin	0-5	heme oxygenase 1	Homo sapiens	14-18
15611319-5	2005	The specific HO-1 inhibitor zinc protoporphyrin (ZnPP) reversed the effects of hemin on monocyte apoptosis and diminished cell lifespan.	zinc protoporphyrin	28-47	heme oxygenase 1	Homo sapiens	13-17
15611319-5	2005	The specific HO-1 inhibitor zinc protoporphyrin (ZnPP) reversed the effects of hemin on monocyte apoptosis and diminished cell lifespan.	zinc protoporphyrin	49-53	heme oxygenase 1	Homo sapiens	13-17
15525643-1	2005	The ability of the human heme oxygenase-1 (hHO-1) R183E mutant to oxidize heme in reactions supported by either NADPH-cytochrome P450 reductase or ascorbic acid has been compared.	Heme	25-29	heme oxygenase 1	Homo sapiens	43-48
15708121-1	2005	Heme oxygenases (HO-1 and HO-2) are responsible for the production of carbon monoxide, a vasodilator.	Carbon Monoxide	70-85	heme oxygenase 1	Homo sapiens	0-30
15525643-2	2005	The NADPH-dependent reaction, like that of wild-type hHO-1, yields exclusively biliverdin IXalpha.	NADP	4-9	heme oxygenase 1	Homo sapiens	53-58
15525643-2	2005	The NADPH-dependent reaction, like that of wild-type hHO-1, yields exclusively biliverdin IXalpha.	Biliverdine	79-97	heme oxygenase 1	Homo sapiens	53-58
15525643-7	2005	The crystal structure of the R183E mutant, determined in the ferric and ferrous-NO bound forms, shows that the heme primarily adopts the same orientation as in wild-type hHO-1.	ferrous-no	72-82	heme oxygenase 1	Homo sapiens	170-175
15525643-7	2005	The crystal structure of the R183E mutant, determined in the ferric and ferrous-NO bound forms, shows that the heme primarily adopts the same orientation as in wild-type hHO-1.	Heme	111-115	heme oxygenase 1	Homo sapiens	170-175
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Heme	86-90	heme oxygenase 1	Homo sapiens	0-16
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Heme	86-90	heme oxygenase 1	Homo sapiens	18-22
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Biliverdine	94-104	heme oxygenase 1	Homo sapiens	0-16
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Biliverdine	94-104	heme oxygenase 1	Homo sapiens	18-22
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Iron	106-110	heme oxygenase 1	Homo sapiens	0-16
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Iron	106-110	heme oxygenase 1	Homo sapiens	18-22
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Carbon Monoxide	116-131	heme oxygenase 1	Homo sapiens	0-16
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Carbon Monoxide	116-131	heme oxygenase 1	Homo sapiens	18-22
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Carbon Monoxide	133-135	heme oxygenase 1	Homo sapiens	0-16
15546873-2	2005	Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO).	Carbon Monoxide	133-135	heme oxygenase 1	Homo sapiens	18-22
15546873-4	2005	The induction of HO-1 by ER stress was blocked by actinomycin D or cycloheximide and was independent of any changes in HO-1 mRNA stability.	Dactinomycin	50-63	heme oxygenase 1	Homo sapiens	17-21
15546873-4	2005	The induction of HO-1 by ER stress was blocked by actinomycin D or cycloheximide and was independent of any changes in HO-1 mRNA stability.	Cycloheximide	67-80	heme oxygenase 1	Homo sapiens	17-21
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	2"-phosphate	137-149	heme oxygenase 1	Homo sapiens	25-29
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	NADP	153-158	heme oxygenase 1	Homo sapiens	25-29
15516695-0	2005	Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase.	NADP	15-20	heme oxygenase 1	Homo sapiens	48-94
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	Arginine	176-179	heme oxygenase 1	Homo sapiens	25-29
15516695-1	2005	Heme oxygenase-1 (HO-1) catalyzes the physiological degradation of heme at the expense of molecular oxygen using electrons donated by NADPH-cytochrome P450 reductase (CPR).	Heme	67-71	heme oxygenase 1	Homo sapiens	0-16
15516695-1	2005	Heme oxygenase-1 (HO-1) catalyzes the physiological degradation of heme at the expense of molecular oxygen using electrons donated by NADPH-cytochrome P450 reductase (CPR).	Heme	67-71	heme oxygenase 1	Homo sapiens	18-22
15516695-1	2005	Heme oxygenase-1 (HO-1) catalyzes the physiological degradation of heme at the expense of molecular oxygen using electrons donated by NADPH-cytochrome P450 reductase (CPR).	Oxygen	5-11	heme oxygenase 1	Homo sapiens	18-22
15516695-2	2005	In this study, we investigated the effect of NADP(H) on the interaction of HO-1 with CPR by surface plasmon resonance.	NADP	45-52	heme oxygenase 1	Homo sapiens	75-79
15516695-3	2005	We found that HO-1 associated with CPR more tightly in the presence of NADP(+) (K(D) = 0.5 microm) than in its absence (K(D) = 2.4 microm).	NADP	71-78	heme oxygenase 1	Homo sapiens	14-18
15516695-4	2005	The HO-1 mutants, K149A, K149A/K153A, and R185A, showed almost no heme degradation activity with NADPH-CPR, whereas they exhibited activity comparable to that of the wild type when sodium ascorbate was used.	Heme	66-70	heme oxygenase 1	Homo sapiens	4-8
15516695-4	2005	The HO-1 mutants, K149A, K149A/K153A, and R185A, showed almost no heme degradation activity with NADPH-CPR, whereas they exhibited activity comparable to that of the wild type when sodium ascorbate was used.	Ascorbic Acid	181-197	heme oxygenase 1	Homo sapiens	4-8
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	guanidino	58-67	heme oxygenase 1	Homo sapiens	25-29
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	Arginine	77-80	heme oxygenase 1	Homo sapiens	25-29
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	Phosphates	140-149	heme oxygenase 1	Homo sapiens	25-29
15516695-8	2005	Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group.	Hydrogen	108-116	heme oxygenase 1	Homo sapiens	25-29
15516695-10	2005	Thus, Lys(149) and Lys(153) appear to interact with CPR in such a way as to orient the redox partners for optimal electron transfer from FMN of CPR to heme of HO-1.	Lysine	6-9	heme oxygenase 1	Homo sapiens	159-163
15516695-10	2005	Thus, Lys(149) and Lys(153) appear to interact with CPR in such a way as to orient the redox partners for optimal electron transfer from FMN of CPR to heme of HO-1.	Lysine	19-22	heme oxygenase 1	Homo sapiens	159-163
15516695-10	2005	Thus, Lys(149) and Lys(153) appear to interact with CPR in such a way as to orient the redox partners for optimal electron transfer from FMN of CPR to heme of HO-1.	Heme	151-155	heme oxygenase 1	Homo sapiens	159-163
15650398-6	2005	Expression of HO-1 responds to chemical and physical agents that directly or indirectly generate ROS.	Reactive Oxygen Species	97-100	heme oxygenase 1	Homo sapiens	14-18
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Bilirubin	199-208	heme oxygenase 1	Homo sapiens	18-22
15933765-4	2005	Induction of HO-1 occurs as an adaptive and beneficial response to several injurious stimuli including heme and this inducible nature of HO-1 signifies its importance in several pathophysiological disease states.	Heme	103-107	heme oxygenase 1	Homo sapiens	13-17
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Heme	79-83	heme oxygenase 1	Homo sapiens	0-16
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Heme	79-83	heme oxygenase 1	Homo sapiens	18-22
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Iron	126-130	heme oxygenase 1	Homo sapiens	0-16
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Iron	126-130	heme oxygenase 1	Homo sapiens	18-22
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Carbon Monoxide	132-147	heme oxygenase 1	Homo sapiens	0-16
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Carbon Monoxide	132-147	heme oxygenase 1	Homo sapiens	18-22
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Biliverdine	152-162	heme oxygenase 1	Homo sapiens	0-16
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Biliverdine	152-162	heme oxygenase 1	Homo sapiens	18-22
15933765-1	2005	Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase.	Bilirubin	199-208	heme oxygenase 1	Homo sapiens	0-16
15650398-10	2005	HO-1 protein expression can occur in the lung in response to oxidative stress associated with infection, altered oxygen tension, and inflammatory diseases.	Oxygen	113-119	heme oxygenase 1	Homo sapiens	0-4
15650398-7	2005	Depletion of cellular reduced glutathione may act as a signal for HO-1 transcriptional activation.	Glutathione	30-41	heme oxygenase 1	Homo sapiens	66-70
15650398-8	2005	Furthermore, antioxidants and metal-chelating compounds can modulate HO-1 expression.	Metals	30-35	heme oxygenase 1	Homo sapiens	69-73
15899048-1	2005	Heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, is expressed by macrophages and endothelial cells in response to various stresses.	Heme	38-42	heme oxygenase 1	Homo sapiens	0-16
15899048-1	2005	Heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, is expressed by macrophages and endothelial cells in response to various stresses.	Heme	38-42	heme oxygenase 1	Homo sapiens	18-22
15899048-2	2005	Because ferritin synthesis is stimulated by Fe2+, which is a product of heme degradation, we examined the relation between HO-1 and ferritin levels in the serum of patients with hemophagocytic syndrome (HPS), adult-onset Still"s disease (ASD), and other diseases that may cause hyperferritinemia.	ammonium ferrous sulfate	44-48	heme oxygenase 1	Homo sapiens	123-127
15899039-6	2005	Protection from chondrocyte death conferred by 0.1 mM SNP was mediated by heme oxygenase 1 (HO-1), as was revealed by the increased expression of HO-1 in 0.1 mM SNP pretreated chondrocytes and by the reversal of this protective effect by the HO-1 inhibitor, zinc protoporphyrin.	zinc protoporphyrin	258-277	heme oxygenase 1	Homo sapiens	74-90
15899039-6	2005	Protection from chondrocyte death conferred by 0.1 mM SNP was mediated by heme oxygenase 1 (HO-1), as was revealed by the increased expression of HO-1 in 0.1 mM SNP pretreated chondrocytes and by the reversal of this protective effect by the HO-1 inhibitor, zinc protoporphyrin.	zinc protoporphyrin	258-277	heme oxygenase 1	Homo sapiens	92-96
15899039-6	2005	Protection from chondrocyte death conferred by 0.1 mM SNP was mediated by heme oxygenase 1 (HO-1), as was revealed by the increased expression of HO-1 in 0.1 mM SNP pretreated chondrocytes and by the reversal of this protective effect by the HO-1 inhibitor, zinc protoporphyrin.	zinc protoporphyrin	258-277	heme oxygenase 1	Homo sapiens	146-150
15899039-6	2005	Protection from chondrocyte death conferred by 0.1 mM SNP was mediated by heme oxygenase 1 (HO-1), as was revealed by the increased expression of HO-1 in 0.1 mM SNP pretreated chondrocytes and by the reversal of this protective effect by the HO-1 inhibitor, zinc protoporphyrin.	zinc protoporphyrin	258-277	heme oxygenase 1	Homo sapiens	146-150
15589375-0	2005	Distinct protective mechanisms of HO-1 and HO-2 against hydroperoxide-induced cytotoxicity.	Hydrogen Peroxide	56-69	heme oxygenase 1	Homo sapiens	34-47
15589375-1	2005	Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin.	Iron	120-124	heme oxygenase 1	Homo sapiens	0-30
15588712-0	2005	Mechanism of concentration-dependent induction of heme oxygenase-1 by resveratrol in human aortic smooth muscle cells.	Resveratrol	70-81	heme oxygenase 1	Homo sapiens	50-66
15588712-1	2005	Resveratrol-mediated heme oxygenase-1 (HO-1) induction has been shown to occur in primary neuronal cultures and is thought to have potential neuroprotective action.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	21-37
15588712-1	2005	Resveratrol-mediated heme oxygenase-1 (HO-1) induction has been shown to occur in primary neuronal cultures and is thought to have potential neuroprotective action.	Resveratrol	0-11	heme oxygenase 1	Homo sapiens	39-43
15588712-3	2005	We attempted to examine resveratrol"s HO-1 inducing potency and its induction regulation in human aortic smooth muscle cells (HASMC).	Resveratrol	24-35	heme oxygenase 1	Homo sapiens	38-42
15588712-4	2005	We showed that resveratrol-mediated HO-1 induction occurred in concentration- and time-dependent manners, but only at low concentrations (1-10 microM), and that it was modulated at both the transcription and translation levels.	Resveratrol	15-26	heme oxygenase 1	Homo sapiens	36-40
15588712-5	2005	Additionally, the results of our study showed that nuclear factor-kappa B (NF-kappaB) inhibitors eliminated resveratrol-mediated HO-1 induction and promoter activity, and that deletion of NF-kappaB binding sites in the HO-1 promoter region strongly reduced promoter activity, suggesting involvement of the NF-kappaB pathway in HO-1 induction by resveratrol.	Resveratrol	108-119	heme oxygenase 1	Homo sapiens	129-133
15588712-5	2005	Additionally, the results of our study showed that nuclear factor-kappa B (NF-kappaB) inhibitors eliminated resveratrol-mediated HO-1 induction and promoter activity, and that deletion of NF-kappaB binding sites in the HO-1 promoter region strongly reduced promoter activity, suggesting involvement of the NF-kappaB pathway in HO-1 induction by resveratrol.	Resveratrol	108-119	heme oxygenase 1	Homo sapiens	219-223
15588712-5	2005	Additionally, the results of our study showed that nuclear factor-kappa B (NF-kappaB) inhibitors eliminated resveratrol-mediated HO-1 induction and promoter activity, and that deletion of NF-kappaB binding sites in the HO-1 promoter region strongly reduced promoter activity, suggesting involvement of the NF-kappaB pathway in HO-1 induction by resveratrol.	Resveratrol	108-119	heme oxygenase 1	Homo sapiens	219-223
15588712-5	2005	Additionally, the results of our study showed that nuclear factor-kappa B (NF-kappaB) inhibitors eliminated resveratrol-mediated HO-1 induction and promoter activity, and that deletion of NF-kappaB binding sites in the HO-1 promoter region strongly reduced promoter activity, suggesting involvement of the NF-kappaB pathway in HO-1 induction by resveratrol.	Resveratrol	345-356	heme oxygenase 1	Homo sapiens	219-223
15588712-5	2005	Additionally, the results of our study showed that nuclear factor-kappa B (NF-kappaB) inhibitors eliminated resveratrol-mediated HO-1 induction and promoter activity, and that deletion of NF-kappaB binding sites in the HO-1 promoter region strongly reduced promoter activity, suggesting involvement of the NF-kappaB pathway in HO-1 induction by resveratrol.	Resveratrol	345-356	heme oxygenase 1	Homo sapiens	219-223
15588712-7	2005	Likewise, we showed that resveratrol at concentrations of &gt; or =20 microM blocked the activity of NF-kappaB through suppression of I kappa-B alpha (IkappaBalpha) phosphorylation, which caused inhibition of HO-1 induction.	Resveratrol	25-36	heme oxygenase 1	Homo sapiens	209-213
15588712-8	2005	Conversely, resveratrol in a range of 1-10 microM enhanced the phosphorylation and degradation of IkappaBalpha, a key step in NF-kappaB activation, resulting in HO-1 induction.	Resveratrol	12-23	heme oxygenase 1	Homo sapiens	161-165
15588712-9	2005	Collectively, we suggest that resveratrol-mediated HO-1 expression occurs, at least in part, through the NF-kappaB pathway, which might contribute to resveratrol"s vascular-protective effect at physiological concentrations after moderate red wine consumption.	Resveratrol	30-41	heme oxygenase 1	Homo sapiens	51-55
15588712-9	2005	Collectively, we suggest that resveratrol-mediated HO-1 expression occurs, at least in part, through the NF-kappaB pathway, which might contribute to resveratrol"s vascular-protective effect at physiological concentrations after moderate red wine consumption.	Resveratrol	150-161	heme oxygenase 1	Homo sapiens	51-55
15881418-4	2005	We tested the effect of the use of protoporphyrins (CoPP and FePP), powerful inducers of the cytoprotective protein heme-oxygenase 1 (HO-1), on allogeneic islet graft survival.	Protoporphyrins	35-50	heme oxygenase 1	Homo sapiens	116-132
15881418-4	2005	We tested the effect of the use of protoporphyrins (CoPP and FePP), powerful inducers of the cytoprotective protein heme-oxygenase 1 (HO-1), on allogeneic islet graft survival.	Protoporphyrins	35-50	heme oxygenase 1	Homo sapiens	134-138
15881418-12	2005	Administration of protoporphyrins to the recipients of allogeneic islets also resulted in transient powerful immunosuppression with reduced lymphocyte proliferative responses, increased proportion of regulatory cells (CD4+CD25+), decreased mononuclear cell infiltrating the graft, paralleled by a systemic upregulation of HO-1 expression.	Protoporphyrins	18-33	heme oxygenase 1	Homo sapiens	322-326
15589375-1	2005	Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin.	Carbon Monoxide	126-141	heme oxygenase 1	Homo sapiens	0-30
15589375-1	2005	Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin.	Biliverdine	147-157	heme oxygenase 1	Homo sapiens	0-30
15589375-1	2005	Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin.	Bilirubin	181-190	heme oxygenase 1	Homo sapiens	0-30
15589375-8	2005	Results indicate that the HO-1 and HO-2 cells are more resistant than controls to hemin and to the organic tert-butyl hydroperoxide, t-BuOOH.	Hemin	82-87	heme oxygenase 1	Homo sapiens	26-39
15589375-8	2005	Results indicate that the HO-1 and HO-2 cells are more resistant than controls to hemin and to the organic tert-butyl hydroperoxide, t-BuOOH.	tert-Butylhydroperoxide	107-131	heme oxygenase 1	Homo sapiens	26-39
15589375-8	2005	Results indicate that the HO-1 and HO-2 cells are more resistant than controls to hemin and to the organic tert-butyl hydroperoxide, t-BuOOH.	di-tert-butyl peroxide	133-140	heme oxygenase 1	Homo sapiens	26-39
15589375-10	2005	The levels of oxidatively modified proteins of HO-1 and HO-2 cells in response to t-BuOOH toxicity are identical, but the level of oxidatively modified proteins of HO-2 cells is less than that of HO-1 cells in response to H(2)O(2) toxicity.	di-tert-butyl peroxide	82-89	heme oxygenase 1	Homo sapiens	47-60
15589375-1	2005	Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin.	Heme	110-114	heme oxygenase 1	Homo sapiens	0-30
16196283-6	2005	The relation analysis showed that PBMC HO-1 protein and mRNA levels had significantly negative relation with FEV1%, PEFR, MEFR50%, respectively (r = -0.51-0.89, P &lt; 0.05-0.001, respectively) and a positive relation with COHb and serum total IgE (r = 0.48-0.	cohb	223-227	heme oxygenase 1	Homo sapiens	39-43
16259722-13	2005	Induction of HSP32 with diacetylrhein appeared to be more effective and may hold greater promise.	diacerein	24-37	heme oxygenase 1	Homo sapiens	13-18
15797262-9	2005	Up-regulated HO-1 expression was accompanied by increase of the numbers of Hoechst-33342 positive MSCs, the reduction of infarct size, and the improvement of cardiac function.	bisbenzimide ethoxide trihydrochloride	75-88	heme oxygenase 1	Homo sapiens	13-17
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Heme	71-75	heme oxygenase 1	Homo sapiens	28-32
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Oxygen	219-225	heme oxygenase 1	Homo sapiens	28-32
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Oxygen	227-229	heme oxygenase 1	Homo sapiens	28-32
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Nitrogen	236-244	heme oxygenase 1	Homo sapiens	28-32
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Carbon Monoxide	291-306	heme oxygenase 1	Homo sapiens	28-32
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Carbon Monoxide	308-310	heme oxygenase 1	Homo sapiens	28-32
16291246-3	2005	The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively.	Oxygen	345-347	heme oxygenase 1	Homo sapiens	28-32
16291246-4	2005	Thus, the NO overproduced by the O2- -dependent induction of iNOS expression can scavenge O2- to produce ONOO-, first to kill the invading pathogens and second to enhance the HO-1 expression in macrophages.	Oxygen	33-35	heme oxygenase 1	Homo sapiens	175-179
16291246-4	2005	Thus, the NO overproduced by the O2- -dependent induction of iNOS expression can scavenge O2- to produce ONOO-, first to kill the invading pathogens and second to enhance the HO-1 expression in macrophages.	Oxygen	90-92	heme oxygenase 1	Homo sapiens	175-179
16291246-4	2005	Thus, the NO overproduced by the O2- -dependent induction of iNOS expression can scavenge O2- to produce ONOO-, first to kill the invading pathogens and second to enhance the HO-1 expression in macrophages.	oxido nitrite	105-110	heme oxygenase 1	Homo sapiens	175-179
15773552-1	2005	Previously it was shown that thiol antioxidants are potent inhibitors of the NO-dependent induction of heme oxygenase 1 (HOX-1) gene.	Sulfhydryl Compounds	29-34	heme oxygenase 1	Homo sapiens	103-119
15773552-1	2005	Previously it was shown that thiol antioxidants are potent inhibitors of the NO-dependent induction of heme oxygenase 1 (HOX-1) gene.	Sulfhydryl Compounds	29-34	heme oxygenase 1	Homo sapiens	121-126
15773552-2	2005	However, the mechanism of HOX-1 gene down-regulation by thiol antioxidants and underlying signaling pathway remain unclear.	Sulfhydryl Compounds	56-61	heme oxygenase 1	Homo sapiens	26-31
15773552-3	2005	In this study we have examined, whether the scavenging of reactive oxygen and reactive nitrogen species (ROS and RNS) is the major cause for thiol-mediated suppression of the HOX-1 induction by NO.	reactive oxygen and reactive nitrogen species	58-103	heme oxygenase 1	Homo sapiens	175-180
16291250-1	2005	Survival of macrophages, which serve as the first-line defense against invading pathogens by invoking the overproduction of highly toxic peroxynitrite (ONOO-), depends on their ability to maintain the intracellular GSH level and to induce the expression of heme oxygenase-1 (HO-1).	Peroxynitrous Acid	137-150	heme oxygenase 1	Homo sapiens	257-273
16291250-1	2005	Survival of macrophages, which serve as the first-line defense against invading pathogens by invoking the overproduction of highly toxic peroxynitrite (ONOO-), depends on their ability to maintain the intracellular GSH level and to induce the expression of heme oxygenase-1 (HO-1).	Peroxynitrous Acid	137-150	heme oxygenase 1	Homo sapiens	275-279
16291250-3	2005	However, macrophages can survive the toxicity of ONOO- by replenishing the depleted GSH level and by inducing HO-1 expression.	onoo	49-53	heme oxygenase 1	Homo sapiens	110-114
16291250-5	2005	However, in cells surviving the toxicity caused by lower doses of O2-, NO, or ONOO-, the depleted intracellular GSH level was replenished, and HO-1 expression was increased, but not when they were coexposed to an inhibitor of HO-1 activity.	Oxygen	66-68	heme oxygenase 1	Homo sapiens	143-147
16291250-5	2005	However, in cells surviving the toxicity caused by lower doses of O2-, NO, or ONOO-, the depleted intracellular GSH level was replenished, and HO-1 expression was increased, but not when they were coexposed to an inhibitor of HO-1 activity.	Oxygen	66-68	heme oxygenase 1	Homo sapiens	226-230
16291250-5	2005	However, in cells surviving the toxicity caused by lower doses of O2-, NO, or ONOO-, the depleted intracellular GSH level was replenished, and HO-1 expression was increased, but not when they were coexposed to an inhibitor of HO-1 activity.	onoo	78-82	heme oxygenase 1	Homo sapiens	143-147
16291250-5	2005	However, in cells surviving the toxicity caused by lower doses of O2-, NO, or ONOO-, the depleted intracellular GSH level was replenished, and HO-1 expression was increased, but not when they were coexposed to an inhibitor of HO-1 activity.	onoo	78-82	heme oxygenase 1	Homo sapiens	226-230
16291250-6	2005	Cells exposed to an inhibitor of GSH synthesis had greater induction of HO-1 expression and survived.	Glutathione	33-36	heme oxygenase 1	Homo sapiens	72-76
16291250-7	2005	However, cells exposed to an inhibitor of HO-1 activity died extensively and could not be revived by addition of N-acetylcysteine (NAC), a precursor of GSH synthesis.	Glutathione	152-155	heme oxygenase 1	Homo sapiens	42-46
16291250-8	2005	Thus, the dichotomous cytotoxic or cytoprotective effects of O2-, NO, or ONOO- in macrophages are determined both by cellular GSH level and by HO-1 activity.	Oxygen	61-63	heme oxygenase 1	Homo sapiens	143-147
16291250-8	2005	Thus, the dichotomous cytotoxic or cytoprotective effects of O2-, NO, or ONOO- in macrophages are determined both by cellular GSH level and by HO-1 activity.	onoo	73-77	heme oxygenase 1	Homo sapiens	143-147
15773552-4	2005	Further, to identify the ROS family members implicated in the HOX-1 induction, we also exposed cells to various non-thiol antioxidants: dimethyl sulfoxide, dimetylthiourea, sodium salicylate, sodium formate, uric acid, catalase, and superoxide dismutase.	ros	25-28	heme oxygenase 1	Homo sapiens	62-67
15773552-4	2005	Further, to identify the ROS family members implicated in the HOX-1 induction, we also exposed cells to various non-thiol antioxidants: dimethyl sulfoxide, dimetylthiourea, sodium salicylate, sodium formate, uric acid, catalase, and superoxide dismutase.	Dimethyl Sulfoxide	136-154	heme oxygenase 1	Homo sapiens	62-67
15773552-4	2005	Further, to identify the ROS family members implicated in the HOX-1 induction, we also exposed cells to various non-thiol antioxidants: dimethyl sulfoxide, dimetylthiourea, sodium salicylate, sodium formate, uric acid, catalase, and superoxide dismutase.	Sodium Salicylate	173-190	heme oxygenase 1	Homo sapiens	62-67
15773552-4	2005	Further, to identify the ROS family members implicated in the HOX-1 induction, we also exposed cells to various non-thiol antioxidants: dimethyl sulfoxide, dimetylthiourea, sodium salicylate, sodium formate, uric acid, catalase, and superoxide dismutase.	formic acid	192-206	heme oxygenase 1	Homo sapiens	62-67
15773552-4	2005	Further, to identify the ROS family members implicated in the HOX-1 induction, we also exposed cells to various non-thiol antioxidants: dimethyl sulfoxide, dimetylthiourea, sodium salicylate, sodium formate, uric acid, catalase, and superoxide dismutase.	Uric Acid	208-217	heme oxygenase 1	Homo sapiens	62-67
15773552-5	2005	A partial inhibition of HOX-1 induction occurred in the presence of non-polar hydroxyl radical scavengers, dimethyl sulfoxide and dimetylthiourea.	Hydroxyl Radical	78-94	heme oxygenase 1	Homo sapiens	24-29
15773552-5	2005	A partial inhibition of HOX-1 induction occurred in the presence of non-polar hydroxyl radical scavengers, dimethyl sulfoxide and dimetylthiourea.	Dimethyl Sulfoxide	107-125	heme oxygenase 1	Homo sapiens	24-29
15773552-5	2005	A partial inhibition of HOX-1 induction occurred in the presence of non-polar hydroxyl radical scavengers, dimethyl sulfoxide and dimetylthiourea.	dimetylthiourea	130-145	heme oxygenase 1	Homo sapiens	24-29
15773552-7	2005	Then, in order to determine, whether RNS scavenging is implicated in the HOX-1 down-regulation by thiol antioxidants, we took advantage of the capacity of suboptimal concentrations of the NO scavenger PTIO (2-phenyl-4,4,5,5-tetramethylimidazole-1-oxyl-3-oxide) to oxidize NO to nitrosating species.	Sulfhydryl Compounds	98-103	heme oxygenase 1	Homo sapiens	73-78
15773552-3	2005	In this study we have examined, whether the scavenging of reactive oxygen and reactive nitrogen species (ROS and RNS) is the major cause for thiol-mediated suppression of the HOX-1 induction by NO.	ros	105-108	heme oxygenase 1	Homo sapiens	175-180
15773552-3	2005	In this study we have examined, whether the scavenging of reactive oxygen and reactive nitrogen species (ROS and RNS) is the major cause for thiol-mediated suppression of the HOX-1 induction by NO.	Sulfhydryl Compounds	141-146	heme oxygenase 1	Homo sapiens	175-180
15541371-0	2004	Rosuvastatin upregulates the antioxidant defense protein heme oxygenase-1.	Rosuvastatin Calcium	0-12	heme oxygenase 1	Homo sapiens	57-73
15808651-5	2005	One of these genes that has been shown to mediate protective effects decodes the enzyme heme oxygenase-1 (HO-1), and an HO-1 downstream product, carbon monoxide (CO).	Carbon Monoxide	145-160	heme oxygenase 1	Homo sapiens	120-124
15808651-5	2005	One of these genes that has been shown to mediate protective effects decodes the enzyme heme oxygenase-1 (HO-1), and an HO-1 downstream product, carbon monoxide (CO).	Carbon Monoxide	162-164	heme oxygenase 1	Homo sapiens	106-110
15808651-5	2005	One of these genes that has been shown to mediate protective effects decodes the enzyme heme oxygenase-1 (HO-1), and an HO-1 downstream product, carbon monoxide (CO).	Carbon Monoxide	162-164	heme oxygenase 1	Homo sapiens	120-124
15808653-5	2005	Donor animals were treated with cobalt protoporphyrin (CoPP; 5 mg/kg IP) 24 hours prior to organ harvesting to induce HO-1.	cobaltiprotoporphyrin	32-53	heme oxygenase 1	Homo sapiens	118-122
15808653-5	2005	Donor animals were treated with cobalt protoporphyrin (CoPP; 5 mg/kg IP) 24 hours prior to organ harvesting to induce HO-1.	cobaltiprotoporphyrin	55-59	heme oxygenase 1	Homo sapiens	118-122
15808653-6	2005	Controls remained untreated or received zinc protoporphyrin (ZnPP; 20 mg/kg, IP) to block HO-1 induction.	zinc protoporphyrin	61-65	heme oxygenase 1	Homo sapiens	90-94
15541371-2	2004	This study explores the role of heme oxygenase-1 (HO-1) as target and potential mediator of rosuvastatin.	Rosuvastatin Calcium	92-104	heme oxygenase 1	Homo sapiens	32-48
15541371-2	2004	This study explores the role of heme oxygenase-1 (HO-1) as target and potential mediator of rosuvastatin.	Rosuvastatin Calcium	92-104	heme oxygenase 1	Homo sapiens	50-54
15541371-3	2004	In cultured human endothelial cells (ECV 304), rosuvastatin increased HO-1 mRNA and protein levels in a concentration-dependent fashion.	Rosuvastatin Calcium	47-59	heme oxygenase 1	Homo sapiens	70-74
15541371-4	2004	HO-1 induction by rosuvastatin remained unaffected by mevalonate and N-nitro-L-arginine-methylester, showing that isoprenoid- and NO-dependent pathways were not involved.	Rosuvastatin Calcium	18-30	heme oxygenase 1	Homo sapiens	0-4
15541371-6	2004	The HO-1 metabolite bilirubin, when added exogenously to the cells, virtually abolished NADPH-dependent oxidative stress.	Bilirubin	20-29	heme oxygenase 1	Homo sapiens	4-8
15541371-6	2004	The HO-1 metabolite bilirubin, when added exogenously to the cells, virtually abolished NADPH-dependent oxidative stress.	NADP	88-93	heme oxygenase 1	Homo sapiens	4-8
15541371-8	2004	Our results demonstrate that HO-1 is a target site and antioxidant mediator of rosuvastatin in endothelial cells.	Rosuvastatin Calcium	79-91	heme oxygenase 1	Homo sapiens	29-33
15577407-6	2004	Treatment of cells with this protease inhibitor led to a significant increase in expression of the heme oxygenase-1 gene that could be reduced by 100 microM of the antioxidant ascorbate.	Ascorbic Acid	176-185	heme oxygenase 1	Homo sapiens	99-115
15544924-3	2004	In cultured endothelial cells derived from human umbilical vein, simvastatin and lovastatin increased HO-1 mRNA levels in a concentration- and time-dependent fashion.	Simvastatin	65-76	heme oxygenase 1	Homo sapiens	102-106
15544924-3	2004	In cultured endothelial cells derived from human umbilical vein, simvastatin and lovastatin increased HO-1 mRNA levels in a concentration- and time-dependent fashion.	Lovastatin	81-91	heme oxygenase 1	Homo sapiens	102-106
15544924-5	2004	HO-1 mRNA induction was abrogated in the presence of actinomycin D and cycloheximide.	Dactinomycin	53-66	heme oxygenase 1	Homo sapiens	0-4
15544924-5	2004	HO-1 mRNA induction was abrogated in the presence of actinomycin D and cycloheximide.	Cycloheximide	71-84	heme oxygenase 1	Homo sapiens	0-4
15542064-0	2004	Diallyl sulfide induces heme oxygenase-1 through MAPK pathway.	allyl sulfide	0-15	heme oxygenase 1	Homo sapiens	24-40
15542064-3	2004	In this study, we found that DAS can induce the expression of heme oxygenase-1 (HO-1), which plays a critical role in the cell defense system against oxidative stress.	allyl sulfide	29-32	heme oxygenase 1	Homo sapiens	62-78
15542064-3	2004	In this study, we found that DAS can induce the expression of heme oxygenase-1 (HO-1), which plays a critical role in the cell defense system against oxidative stress.	allyl sulfide	29-32	heme oxygenase 1	Homo sapiens	80-84
15542064-10	2004	N-Acetyl-cysteine blocked this increase of ROS production as well as DAS-induced ERK activation, Nrf2 protein expression and nuclear translocation, and ho-1 gene activation.	Acetylcysteine	0-17	heme oxygenase 1	Homo sapiens	152-156
15542064-11	2004	The increase in HO-1 produced by DAS protected the HepG2 cells against toxicity by hydrogen peroxide or arachidonic acid.	Hydrogen Peroxide	83-100	heme oxygenase 1	Homo sapiens	16-20
15542064-11	2004	The increase in HO-1 produced by DAS protected the HepG2 cells against toxicity by hydrogen peroxide or arachidonic acid.	Arachidonic Acid	104-120	heme oxygenase 1	Homo sapiens	16-20
15542064-12	2004	These results suggest that DAS induces ho-1 through production of ROS, and Nrf2 and MAPK (ERK and p38) mediate this induction.	allyl sulfide	27-30	heme oxygenase 1	Homo sapiens	39-43
15542064-12	2004	These results suggest that DAS induces ho-1 through production of ROS, and Nrf2 and MAPK (ERK and p38) mediate this induction.	Reactive Oxygen Species	66-69	heme oxygenase 1	Homo sapiens	39-43
15542064-13	2004	Induction of ho-1 may play a role in the protective effects of DAS.	allyl sulfide	63-66	heme oxygenase 1	Homo sapiens	13-17
15659834-0	2004	Effects of cyclopentenone prostaglandins on the expression of heme oxygenase-1 in MCF-7 cells.	cyclopentenone	11-25	heme oxygenase 1	Homo sapiens	62-78
15465821-1	2004	Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide.	Heme	64-68	heme oxygenase 1	Homo sapiens	0-16
15465821-1	2004	Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide.	Biliverdine	72-82	heme oxygenase 1	Homo sapiens	0-16
15465821-1	2004	Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide.	Iron	84-88	heme oxygenase 1	Homo sapiens	0-16
15465821-1	2004	Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	0-16
15465821-7	2004	The effect of increasing concentrations of heme to up-regulate levels of heme oxygenase-1 was more pronounced when Bach-1 siRNA was present.	Heme	43-47	heme oxygenase 1	Homo sapiens	73-89
15581622-5	2004	Isotopic 32P-labeling of HEK293T cells confirmed that HO-1 is a phosphoprotein and that the basal HO-1 phosphorylation is increased by Akt1 activation.	Phosphorus-32	9-12	heme oxygenase 1	Homo sapiens	54-58
15581622-5	2004	Isotopic 32P-labeling of HEK293T cells confirmed that HO-1 is a phosphoprotein and that the basal HO-1 phosphorylation is increased by Akt1 activation.	Phosphorus-32	9-12	heme oxygenase 1	Homo sapiens	98-102
15308469-4	2004	After it enters the cell, heme is degraded by heme oxygenase-1 (HO-1), and iron is released.	Heme	26-30	heme oxygenase 1	Homo sapiens	46-62
15564944-2	2004	The authors hypothesized that propofol, because of its particular chemical structure, mitigates the effects of peroxynitrite-mediated oxidative stress and apoptosis by the induction of heme oxygenase (HO)-1 in primary cultured astroglial cells.	Propofol	30-38	heme oxygenase 1	Homo sapiens	185-206
15564944-2	2004	The authors hypothesized that propofol, because of its particular chemical structure, mitigates the effects of peroxynitrite-mediated oxidative stress and apoptosis by the induction of heme oxygenase (HO)-1 in primary cultured astroglial cells.	Peroxynitrous Acid	111-124	heme oxygenase 1	Homo sapiens	185-206
15659834-0	2004	Effects of cyclopentenone prostaglandins on the expression of heme oxygenase-1 in MCF-7 cells.	Prostaglandins	26-40	heme oxygenase 1	Homo sapiens	62-78
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Heme	72-76	heme oxygenase 1	Homo sapiens	90-94
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Iron	185-189	heme oxygenase 1	Homo sapiens	72-88
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Iron	185-189	heme oxygenase 1	Homo sapiens	90-94
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Carbon Monoxide	191-206	heme oxygenase 1	Homo sapiens	72-88
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Carbon Monoxide	191-206	heme oxygenase 1	Homo sapiens	90-94
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Biliverdine	212-222	heme oxygenase 1	Homo sapiens	72-88
15659834-5	2004	In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin.	Biliverdine	212-222	heme oxygenase 1	Homo sapiens	90-94
15659834-6	2004	Treatment of the human breast cancer cell line (MCF-7) with 15d-PGJ(2) resulted in a concentration- and time-dependent increase in the expression of HO-1, whereas prostaglandin A(2) (PGA(2)) and the non-PG derivative 2-cyclopenten-1-one failed to induce HO-1 expression at the protein level.	Prostaglandins	64-66	heme oxygenase 1	Homo sapiens	149-153
15659834-6	2004	Treatment of the human breast cancer cell line (MCF-7) with 15d-PGJ(2) resulted in a concentration- and time-dependent increase in the expression of HO-1, whereas prostaglandin A(2) (PGA(2)) and the non-PG derivative 2-cyclopenten-1-one failed to induce HO-1 expression at the protein level.	Prostaglandins	64-66	heme oxygenase 1	Homo sapiens	254-258
15659834-6	2004	Treatment of the human breast cancer cell line (MCF-7) with 15d-PGJ(2) resulted in a concentration- and time-dependent increase in the expression of HO-1, whereas prostaglandin A(2) (PGA(2)) and the non-PG derivative 2-cyclopenten-1-one failed to induce HO-1 expression at the protein level.	cyclopentenone	217-236	heme oxygenase 1	Homo sapiens	149-153
15659834-11	2004	Thus, the induction of HO-1 expression and the activation of Akt/PKB by 15d-PGJ(2) and PGA(2) are likely to confer cytoprotective or antiapoptotic effects exerted by these cyPGs.	15d-pgj	72-79	heme oxygenase 1	Homo sapiens	23-27
15659834-11	2004	Thus, the induction of HO-1 expression and the activation of Akt/PKB by 15d-PGJ(2) and PGA(2) are likely to confer cytoprotective or antiapoptotic effects exerted by these cyPGs.	prostaglandin A2	87-93	heme oxygenase 1	Homo sapiens	23-27
15504750-0	2004	The HIV protease inhibitor ritonavir synergizes with butyrate for induction of apoptotic cell death and mediates expression of heme oxygenase-1 in DLD-1 colon carcinoma cells.	Ritonavir	27-36	heme oxygenase 1	Homo sapiens	127-143
15560792-5	2004	PCC 6803 (Syn HO-1), in complex with heme at 2.5 A resolution.	Heme	37-41	heme oxygenase 1	Homo sapiens	14-18
15504750-9	2004	Ritonavir-induced HO-1 protein was suppressed by SB203580 or SB202190 and preceded by immediate upregulation of cellular c-Fos and c-Jun protein levels.	Ritonavir	0-9	heme oxygenase 1	Homo sapiens	18-22
15504750-9	2004	Ritonavir-induced HO-1 protein was suppressed by SB203580 or SB202190 and preceded by immediate upregulation of cellular c-Fos and c-Jun protein levels.	SB 203580	49-57	heme oxygenase 1	Homo sapiens	18-22
15504750-9	2004	Ritonavir-induced HO-1 protein was suppressed by SB203580 or SB202190 and preceded by immediate upregulation of cellular c-Fos and c-Jun protein levels.	4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)imidazole	61-69	heme oxygenase 1	Homo sapiens	18-22
15504750-11	2004	The present data suggest that ritonavir has the potential to curb colon carcinogenesis by reducing cell growth via mechanisms that include apoptosis and by simultaneously modulating colonic inflammation via induction of anti-inflammatory HO-1.	Ritonavir	30-39	heme oxygenase 1	Homo sapiens	238-242
15642322-9	2004	Analysis with real-time PCR showed a maximum 3-6-fold increase in mRNA levels 9 hr after the 3 hr O2-exposure for the enzymes heme oxygenase-1 (HO-1), MnSOD and TrxR1 (the cytoplasmic form of TrxR).	Oxygen	98-100	heme oxygenase 1	Homo sapiens	126-142
15642322-9	2004	Analysis with real-time PCR showed a maximum 3-6-fold increase in mRNA levels 9 hr after the 3 hr O2-exposure for the enzymes heme oxygenase-1 (HO-1), MnSOD and TrxR1 (the cytoplasmic form of TrxR).	Oxygen	98-100	heme oxygenase 1	Homo sapiens	144-148
15642322-11	2004	Initial upregulation of message for HO-1 occurred a few hours before any upregulation of MnSOD could be detected, suggesting that release of free iron from the degradation of heme by HO-1 may have played a role in the upregulation of the dismutase.	Iron	146-150	heme oxygenase 1	Homo sapiens	36-40
15642322-11	2004	Initial upregulation of message for HO-1 occurred a few hours before any upregulation of MnSOD could be detected, suggesting that release of free iron from the degradation of heme by HO-1 may have played a role in the upregulation of the dismutase.	Iron	146-150	heme oxygenase 1	Homo sapiens	183-187
15547665-3	2004	Heme oxygenase-1 (HO-1) is known to be induced not only by its substrate, heme, but also by various oxidative stresses, and thought to play an important role in the protection of the host from oxidative tissue injuries.	Heme	74-78	heme oxygenase 1	Homo sapiens	0-16
15547665-3	2004	Heme oxygenase-1 (HO-1) is known to be induced not only by its substrate, heme, but also by various oxidative stresses, and thought to play an important role in the protection of the host from oxidative tissue injuries.	Heme	74-78	heme oxygenase 1	Homo sapiens	18-22
15547665-8	2004	These findings suggest that, in the liver of ALF patients, there may be an increase in free heme concentration which up-regulates HO-1 gene expression, while down-regulating ALAS1 gene expression, resulting in markedly altered heme metabolism and liver function.	Heme	92-96	heme oxygenase 1	Homo sapiens	130-134
15642322-11	2004	Initial upregulation of message for HO-1 occurred a few hours before any upregulation of MnSOD could be detected, suggesting that release of free iron from the degradation of heme by HO-1 may have played a role in the upregulation of the dismutase.	Heme	175-179	heme oxygenase 1	Homo sapiens	36-40
15642322-11	2004	Initial upregulation of message for HO-1 occurred a few hours before any upregulation of MnSOD could be detected, suggesting that release of free iron from the degradation of heme by HO-1 may have played a role in the upregulation of the dismutase.	Heme	175-179	heme oxygenase 1	Homo sapiens	183-187
15531134-0	2004	Effects of 1alpha,25 dihydroxyvitamin D3 on the expression of HO-1 and GFAP in glial cells of the photothrombotically lesioned cerebral cortex.	Calcitriol	11-40	heme oxygenase 1	Homo sapiens	62-66
15531134-3	2004	The inducible enzyme, heme oxygenase-1 metabolizes and thus detoxifies free heme to the powerful endogenous antioxidants biliverdin and bilirubin therefore enhancing neuroprotection.	Biliverdine	121-131	heme oxygenase 1	Homo sapiens	22-38
15531134-3	2004	The inducible enzyme, heme oxygenase-1 metabolizes and thus detoxifies free heme to the powerful endogenous antioxidants biliverdin and bilirubin therefore enhancing neuroprotection.	Bilirubin	136-145	heme oxygenase 1	Homo sapiens	22-38
15531134-5	2004	We studied the effects of 1,25-D3 treatment on heme oxygenase-1 expression following focal cortical ischemia elicited by photothrombosis.	Calcitriol	26-33	heme oxygenase 1	Homo sapiens	47-63
15531134-6	2004	Postlesional treatment with 1,25-D3 (4 microg/kg body weight) resulted in a transient, but significant upregulation of glial heme oxygenase-1 immunoreactivity concomitant with a reduction in glial fibrillary acidic protein immunoreactivity in remote cortical regions affected by a secondary spread of injury, whereas the size of the lesion"s core remained unaffected.	Calcitriol	28-35	heme oxygenase 1	Homo sapiens	125-141
15450936-5	2004	Total GSH level decreased markedly (50% of control) by 2 h, began to recover at 4 h, returned to control level by 6 h and increased above the control level during 10-24 h. Collectively, these results indicated that overproduced O2*- depletes GSH and triggers induction of xCT, HO-1, iNOS and HO-1 expression in sequence.	Glutathione	6-9	heme oxygenase 1	Homo sapiens	277-281
15450936-5	2004	Total GSH level decreased markedly (50% of control) by 2 h, began to recover at 4 h, returned to control level by 6 h and increased above the control level during 10-24 h. Collectively, these results indicated that overproduced O2*- depletes GSH and triggers induction of xCT, HO-1, iNOS and HO-1 expression in sequence.	Glutathione	6-9	heme oxygenase 1	Homo sapiens	292-296
15450936-5	2004	Total GSH level decreased markedly (50% of control) by 2 h, began to recover at 4 h, returned to control level by 6 h and increased above the control level during 10-24 h. Collectively, these results indicated that overproduced O2*- depletes GSH and triggers induction of xCT, HO-1, iNOS and HO-1 expression in sequence.	Oxygen	228-230	heme oxygenase 1	Homo sapiens	277-281
15450936-5	2004	Total GSH level decreased markedly (50% of control) by 2 h, began to recover at 4 h, returned to control level by 6 h and increased above the control level during 10-24 h. Collectively, these results indicated that overproduced O2*- depletes GSH and triggers induction of xCT, HO-1, iNOS and HO-1 expression in sequence.	Oxygen	228-230	heme oxygenase 1	Homo sapiens	292-296
15450936-7	2004	When this iNOS-derived delivery of NO* was combined with prior depletion of GSH using buthioninesulfoximine, an inhibitor of GSH biosynthesis, induction of HO-1 was potentiated.	Glutathione	76-79	heme oxygenase 1	Homo sapiens	156-160
15450936-7	2004	When this iNOS-derived delivery of NO* was combined with prior depletion of GSH using buthioninesulfoximine, an inhibitor of GSH biosynthesis, induction of HO-1 was potentiated.	Buthionine Sulfoximine	86-107	heme oxygenase 1	Homo sapiens	156-160
15450936-7	2004	When this iNOS-derived delivery of NO* was combined with prior depletion of GSH using buthioninesulfoximine, an inhibitor of GSH biosynthesis, induction of HO-1 was potentiated.	Glutathione	125-128	heme oxygenase 1	Homo sapiens	156-160
15571180-5	2004	PATIENTS AND METHODS: To this end, the gene expression of p22phox, a NAD(P)H oxidase subunit closely linked with the generation of superoxide anions and of Heme oxygenase-1 (HO-1), induced by and protective from oxidative stress, were evaluated by RT-PCR in mononuclear cells from 5 patients under 3 times a week chronic bicarbonate dialysis.	Bicarbonates	321-332	heme oxygenase 1	Homo sapiens	156-172
15560792-7	2004	Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity.	Heme	13-17	heme oxygenase 1	Homo sapiens	37-41
15560792-7	2004	Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity.	Heme	28-32	heme oxygenase 1	Homo sapiens	37-41
15560792-7	2004	Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity.	Heme	28-32	heme oxygenase 1	Homo sapiens	94-98
15560792-10	2004	The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO-1 is narrow compared to that of mammalian HO-1.	Heme	20-24	heme oxygenase 1	Homo sapiens	90-94
15560792-10	2004	The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO-1 is narrow compared to that of mammalian HO-1.	Heme	20-24	heme oxygenase 1	Homo sapiens	135-139
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Iron	92-96	heme oxygenase 1	Homo sapiens	28-32
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Iron	92-96	heme oxygenase 1	Homo sapiens	155-159
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Sulfur	97-103	heme oxygenase 1	Homo sapiens	28-32
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Sulfur	97-103	heme oxygenase 1	Homo sapiens	155-159
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Heme	19-23	heme oxygenase 1	Homo sapiens	28-32
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Heme	19-23	heme oxygenase 1	Homo sapiens	155-159
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Iron	138-142	heme oxygenase 1	Homo sapiens	28-32
15560792-12	2004	A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.	Iron	138-142	heme oxygenase 1	Homo sapiens	155-159
15451438-0	2004	Augmented heme oxygenase-1 induces prostaglandin uptake via the prostaglandin transporter in micro-vascular endothelial cells.	Prostaglandins	35-48	heme oxygenase 1	Homo sapiens	10-26
15591777-4	2004	Scavenging carbon monoxide (CO), one of the by-products of heme degradation by HO-1, significantly attenuated HO-1-mediated suppression of iNOS gene induction as revealed by Northern blot analysis.	Carbon Monoxide	11-26	heme oxygenase 1	Homo sapiens	79-83
15591777-4	2004	Scavenging carbon monoxide (CO), one of the by-products of heme degradation by HO-1, significantly attenuated HO-1-mediated suppression of iNOS gene induction as revealed by Northern blot analysis.	Carbon Monoxide	11-26	heme oxygenase 1	Homo sapiens	110-114
15591777-4	2004	Scavenging carbon monoxide (CO), one of the by-products of heme degradation by HO-1, significantly attenuated HO-1-mediated suppression of iNOS gene induction as revealed by Northern blot analysis.	Carbon Monoxide	28-30	heme oxygenase 1	Homo sapiens	79-83
15591777-4	2004	Scavenging carbon monoxide (CO), one of the by-products of heme degradation by HO-1, significantly attenuated HO-1-mediated suppression of iNOS gene induction as revealed by Northern blot analysis.	Carbon Monoxide	28-30	heme oxygenase 1	Homo sapiens	110-114
15591777-9	2004	CO appears to mediate the suppressive effect of HO-1, at least in part, through downregulating transcriptional activation of the iNOS gene via a cGMP-dependent pathway.	Cyclic GMP	145-149	heme oxygenase 1	Homo sapiens	48-52
15519649-5	2004	HO-1 enzyme activity was highest during warm hypoxia, followed by cold hypoxia and CM which was confirmed by intracellular Fe(2+) formation.	ammonium ferrous sulfate	123-129	heme oxygenase 1	Homo sapiens	0-4
15474356-9	2004	These results support the hypothesis that HO-1 protects astrocytes from heme-mediated oxidative injury.	Heme	72-76	heme oxygenase 1	Homo sapiens	42-46
15530192-12	2004	Bilirubin, but not carboxyhemoglobin, correlated with heme oxygenase-1 expression (p = .0013).	Bilirubin	0-9	heme oxygenase 1	Homo sapiens	54-70
15530192-14	2004	Heme oxygenase-1 expression correlated with serum bilirubin levels.	Bilirubin	50-59	heme oxygenase 1	Homo sapiens	0-16
15530192-15	2004	The increase in heme oxygenase-1 expression may add to the understanding of the increase in serum bilirubin observed in patients with SIRS/sepsis.	Bilirubin	98-107	heme oxygenase 1	Homo sapiens	16-32
15522396-0	2004	Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage.	ammonium ferrous sulfate	22-29	heme oxygenase 1	Homo sapiens	88-104
15522396-0	2004	Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage.	ammonium ferrous sulfate	34-41	heme oxygenase 1	Homo sapiens	88-104
15522396-0	2004	Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage.	Heme	59-63	heme oxygenase 1	Homo sapiens	88-104
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	mesophorphyrin	163-177	heme oxygenase 1	Homo sapiens	145-149
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	mesophorphyrin	163-177	heme oxygenase 1	Homo sapiens	145-149
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	Prostaglandins	98-100	heme oxygenase 1	Homo sapiens	57-61
15451438-1	2004	Previous studies show that expression of heme oxygenase-1 (HO-1) in endothelial cells results in decreased cyclooxygenase expression and prostaglandin (PG) levels through limiting heme availability.	Prostaglandins	137-150	heme oxygenase 1	Homo sapiens	41-57
15451438-7	2004	Therefore, PG clearance via PGT may contribute to the cellular regulation of PG levels by HO-1.	Prostaglandins	11-13	heme oxygenase 1	Homo sapiens	90-94
15451438-1	2004	Previous studies show that expression of heme oxygenase-1 (HO-1) in endothelial cells results in decreased cyclooxygenase expression and prostaglandin (PG) levels through limiting heme availability.	Prostaglandins	137-150	heme oxygenase 1	Homo sapiens	59-63
15451438-1	2004	Previous studies show that expression of heme oxygenase-1 (HO-1) in endothelial cells results in decreased cyclooxygenase expression and prostaglandin (PG) levels through limiting heme availability.	Prostaglandins	152-154	heme oxygenase 1	Homo sapiens	41-57
15451438-7	2004	Therefore, PG clearance via PGT may contribute to the cellular regulation of PG levels by HO-1.	pgt	28-31	heme oxygenase 1	Homo sapiens	90-94
15451438-1	2004	Previous studies show that expression of heme oxygenase-1 (HO-1) in endothelial cells results in decreased cyclooxygenase expression and prostaglandin (PG) levels through limiting heme availability.	Prostaglandins	152-154	heme oxygenase 1	Homo sapiens	59-63
15451438-7	2004	Therefore, PG clearance via PGT may contribute to the cellular regulation of PG levels by HO-1.	Prostaglandins	28-30	heme oxygenase 1	Homo sapiens	90-94
15451438-1	2004	Previous studies show that expression of heme oxygenase-1 (HO-1) in endothelial cells results in decreased cyclooxygenase expression and prostaglandin (PG) levels through limiting heme availability.	Heme	41-45	heme oxygenase 1	Homo sapiens	59-63
15451438-2	2004	Regulation of PGs, important inflammatory mediators, may contribute to the anti-inflammatory potential of HO-1.	Phosphatidylglycerols	14-17	heme oxygenase 1	Homo sapiens	106-110
15451438-3	2004	Here we examine the effects of HO-1 expression on PG clearance via the prostaglandin transporter (PGT).	Prostaglandins	50-52	heme oxygenase 1	Homo sapiens	31-35
15451438-4	2004	Endothelial cells expressing human HO-1 via retroviral transfer exhibit approximately 7-fold higher levels of PGT RNA and equivalently elevated uptake of [(3)H]PGE(2).	Prostaglandins E	160-163	heme oxygenase 1	Homo sapiens	35-39
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	stannous chloride	24-41	heme oxygenase 1	Homo sapiens	57-61
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	stannous chloride	24-41	heme oxygenase 1	Homo sapiens	145-149
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	stannous chloride	24-41	heme oxygenase 1	Homo sapiens	145-149
15451438-6	2004	Treatment of cells with stannous chloride, an inducer of HO-1, results in increased expression of PGT while incubation of cells expressing human HO-1 with stannic mesophorphyrin, a substrate inhibitor of HO-1, decreases PG uptake.	pgt	98-101	heme oxygenase 1	Homo sapiens	57-61
15242350-2	2004	HO-1 transcription is induced by a vast array of compounds including, but certainly not limited to, haem and heavy metals such as cadmium.	Cadmium	130-137	heme oxygenase 1	Homo sapiens	0-4
15242350-4	2004	Dimethylsulphate in vivo footprinting studies have identified three protected guanine residues in the E-box of the HO-1 proximal promoter.	dimethyl sulfate	0-16	heme oxygenase 1	Homo sapiens	115-119
15242350-4	2004	Dimethylsulphate in vivo footprinting studies have identified three protected guanine residues in the E-box of the HO-1 proximal promoter.	Guanine	78-85	heme oxygenase 1	Homo sapiens	115-119
15242350-8	2004	These results demonstrate for the first time that USF proteins bind to the human HO-1 promoter in vivo and are required for high-level expression of HO-1 by haem and cadmium in human renal epithelial cells.	Heme	157-161	heme oxygenase 1	Homo sapiens	81-85
15242350-8	2004	These results demonstrate for the first time that USF proteins bind to the human HO-1 promoter in vivo and are required for high-level expression of HO-1 by haem and cadmium in human renal epithelial cells.	Heme	157-161	heme oxygenase 1	Homo sapiens	149-153
15242350-8	2004	These results demonstrate for the first time that USF proteins bind to the human HO-1 promoter in vivo and are required for high-level expression of HO-1 by haem and cadmium in human renal epithelial cells.	Cadmium	166-173	heme oxygenase 1	Homo sapiens	81-85
15242350-8	2004	These results demonstrate for the first time that USF proteins bind to the human HO-1 promoter in vivo and are required for high-level expression of HO-1 by haem and cadmium in human renal epithelial cells.	Cadmium	166-173	heme oxygenase 1	Homo sapiens	149-153
15378604-4	2004	Effect of HO-1 production on the cell injury induced by hydrogen peroxide was evaluated after hemin stimulation and after HO-1 gene transfection.	Hydrogen Peroxide	56-73	heme oxygenase 1	Homo sapiens	10-14
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Oxygen	45-47	heme oxygenase 1	Homo sapiens	6-22
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Oxygen	45-47	heme oxygenase 1	Homo sapiens	24-29
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Heme	6-10	heme oxygenase 1	Homo sapiens	24-29
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Biliverdine	79-89	heme oxygenase 1	Homo sapiens	6-22
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Biliverdine	79-89	heme oxygenase 1	Homo sapiens	24-29
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Carbon Monoxide	91-93	heme oxygenase 1	Homo sapiens	6-22
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Carbon Monoxide	91-93	heme oxygenase 1	Homo sapiens	24-29
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Iron	104-108	heme oxygenase 1	Homo sapiens	6-22
15297453-1	2004	Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron.	Iron	104-108	heme oxygenase 1	Homo sapiens	24-29
15297453-6	2004	We report here that hHO-1 cleaves 5-phenylheme to biliverdin IXalpha and oxidizes 15-phenylheme at the alpha-meso position to give 10-phenylbiliverdin IXalpha.	5-phenylheme	34-46	heme oxygenase 1	Homo sapiens	20-25
15297453-6	2004	We report here that hHO-1 cleaves 5-phenylheme to biliverdin IXalpha and oxidizes 15-phenylheme at the alpha-meso position to give 10-phenylbiliverdin IXalpha.	Biliverdine	50-68	heme oxygenase 1	Homo sapiens	20-25
15297453-6	2004	We report here that hHO-1 cleaves 5-phenylheme to biliverdin IXalpha and oxidizes 15-phenylheme at the alpha-meso position to give 10-phenylbiliverdin IXalpha.	15-phenylheme	82-95	heme oxygenase 1	Homo sapiens	20-25
15297453-6	2004	We report here that hHO-1 cleaves 5-phenylheme to biliverdin IXalpha and oxidizes 15-phenylheme at the alpha-meso position to give 10-phenylbiliverdin IXalpha.	10-phenylbiliverdin ixalpha	131-158	heme oxygenase 1	Homo sapiens	20-25
15297453-8	2004	The 2.29- and 2.11-A crystal structures of the hHO-1 complexes with 1- and 15-phenylheme, respectively, show clear electron density for both the 5- and 15-phenyl rings in both molecules of the asymmetric unit.	phenylheme	78-88	heme oxygenase 1	Homo sapiens	47-52
15297453-9	2004	The overall structure of 15-phenylheme-hHO-1 is similar to that of heme-hHO-1 except for small changes in distal residues 141-150 and in the proximal Lys18 and Lys22.	octadeca(lysine)	150-155	heme oxygenase 1	Homo sapiens	39-44
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	phenyl-substituted heme	41-64	heme oxygenase 1	Homo sapiens	20-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	phenyl-substituted heme	41-64	heme oxygenase 1	Homo sapiens	21-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	Heme	15-19	heme oxygenase 1	Homo sapiens	20-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	Heme	15-19	heme oxygenase 1	Homo sapiens	21-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	meso	251-255	heme oxygenase 1	Homo sapiens	20-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	meso	251-255	heme oxygenase 1	Homo sapiens	21-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	Carbon	256-262	heme oxygenase 1	Homo sapiens	20-25
15297453-10	2004	In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon.	Carbon	256-262	heme oxygenase 1	Homo sapiens	21-25
15345146-3	2004	Moreover, heme oxygenase-1 (HO-1), a ubiquitous stress-inducible enzyme that is induced by ROS and NO, was recently discovered to be involved in angiogenesis.	Reactive Oxygen Species	91-94	heme oxygenase 1	Homo sapiens	10-26
15345141-4	2004	Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1).	Heme	5-9	heme oxygenase 1	Homo sapiens	232-248
15345146-3	2004	Moreover, heme oxygenase-1 (HO-1), a ubiquitous stress-inducible enzyme that is induced by ROS and NO, was recently discovered to be involved in angiogenesis.	Reactive Oxygen Species	91-94	heme oxygenase 1	Homo sapiens	28-32
15345141-4	2004	Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1).	Heme	5-9	heme oxygenase 1	Homo sapiens	250-254
15345141-4	2004	Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1).	Heme	35-39	heme oxygenase 1	Homo sapiens	232-248
15345147-2	2004	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
15345141-4	2004	Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1).	Heme	35-39	heme oxygenase 1	Homo sapiens	250-254
15345147-2	2004	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
15345141-5	2004	The latter gene expression occurs by way of free heme-mediated derepression of Bach1, a mammalian heme-responsive transcription factor that suppresses the activation of the HO-1 gene.	Heme	49-53	heme oxygenase 1	Homo sapiens	173-177
15345143-3	2004	Free heme, an entity that can be generated by UVA irradiation of cells, also appears to be a critical intermediate that can directly influence both the transcriptional activation and repression of the HO-1 gene.	Heme	5-9	heme oxygenase 1	Homo sapiens	201-205
15345147-2	2004	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress.	Heme	109-113	heme oxygenase 1	Homo sapiens	0-16
15345147-2	2004	Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress.	Heme	109-113	heme oxygenase 1	Homo sapiens	18-22
15345147-3	2004	In various models of oxidative tissue injuries, the induction of HO-1 confers protection on tissues from further damages by removing the prooxidant heme, or by virtue of the antioxidative, antiinflammatory, and/or antiapoptotic actions of one or more of the three products, i.e., carbon monoxide, biliverdin IXalpha, and iron by HO reaction.	Heme	148-152	heme oxygenase 1	Homo sapiens	65-69
15345147-3	2004	In various models of oxidative tissue injuries, the induction of HO-1 confers protection on tissues from further damages by removing the prooxidant heme, or by virtue of the antioxidative, antiinflammatory, and/or antiapoptotic actions of one or more of the three products, i.e., carbon monoxide, biliverdin IXalpha, and iron by HO reaction.	Carbon Monoxide	280-295	heme oxygenase 1	Homo sapiens	65-69
15345147-3	2004	In various models of oxidative tissue injuries, the induction of HO-1 confers protection on tissues from further damages by removing the prooxidant heme, or by virtue of the antioxidative, antiinflammatory, and/or antiapoptotic actions of one or more of the three products, i.e., carbon monoxide, biliverdin IXalpha, and iron by HO reaction.	Biliverdine	297-315	heme oxygenase 1	Homo sapiens	65-69
15345147-3	2004	In various models of oxidative tissue injuries, the induction of HO-1 confers protection on tissues from further damages by removing the prooxidant heme, or by virtue of the antioxidative, antiinflammatory, and/or antiapoptotic actions of one or more of the three products, i.e., carbon monoxide, biliverdin IXalpha, and iron by HO reaction.	Iron	321-325	heme oxygenase 1	Homo sapiens	65-69
15345152-3	2004	As a further complication, heme and cadmium, two potent inducers of the hmox-1 gene, inhibit Bach1 function by different mechanisms-by inhibition of DNA binding or promotion of nuclear export, respectively.	Heme	27-31	heme oxygenase 1	Homo sapiens	72-78
15345152-3	2004	As a further complication, heme and cadmium, two potent inducers of the hmox-1 gene, inhibit Bach1 function by different mechanisms-by inhibition of DNA binding or promotion of nuclear export, respectively.	Cadmium	36-43	heme oxygenase 1	Homo sapiens	72-78
15602829-0	2004	Induction of heme oxygenase-1 in human hepatocytes to protect them from ethanol-induced cytotoxicity.	Ethanol	72-79	heme oxygenase 1	Homo sapiens	13-29
15636365-1	2004	Human Heme Oxygenase-1 (hHO-1) is the rate-limiting enzyme in the catabolism reaction of heme, which directly regulates the concentration of bilirubin in human body.	Heme	89-93	heme oxygenase 1	Homo sapiens	6-22
15636365-1	2004	Human Heme Oxygenase-1 (hHO-1) is the rate-limiting enzyme in the catabolism reaction of heme, which directly regulates the concentration of bilirubin in human body.	Heme	89-93	heme oxygenase 1	Homo sapiens	24-29
15636365-1	2004	Human Heme Oxygenase-1 (hHO-1) is the rate-limiting enzyme in the catabolism reaction of heme, which directly regulates the concentration of bilirubin in human body.	Bilirubin	141-150	heme oxygenase 1	Homo sapiens	6-22
15636365-1	2004	Human Heme Oxygenase-1 (hHO-1) is the rate-limiting enzyme in the catabolism reaction of heme, which directly regulates the concentration of bilirubin in human body.	Bilirubin	141-150	heme oxygenase 1	Homo sapiens	24-29
15636365-5	2004	The concentration of hHO-1 in 30%-60% saturation (NH4)2SO4 components and in fractions through twice column chromatography was 3.6-fold and 30-fold higher than that in initial product, respectively.	Ammonium Sulfate	49-58	heme oxygenase 1	Homo sapiens	21-26
15458743-0	2004	Heme oxygenase-1 mediates up-regulation of adhesion molecule expression induced by peroxynitrite in endothelial cells.	Peroxynitrous Acid	83-96	heme oxygenase 1	Homo sapiens	0-16
15458743-3	2004	This study was to test whether EC oxidative stress induced by peroxynitrite could up-regulate EC CAM expression, and whether heme oxygenase-1 (HO-1) has protective effects on this peroxynitrite-induced cellular response.	Peroxynitrous Acid	180-193	heme oxygenase 1	Homo sapiens	125-141
15458743-3	2004	This study was to test whether EC oxidative stress induced by peroxynitrite could up-regulate EC CAM expression, and whether heme oxygenase-1 (HO-1) has protective effects on this peroxynitrite-induced cellular response.	Peroxynitrous Acid	180-193	heme oxygenase 1	Homo sapiens	143-147
15458743-13	2004	CONCLUSIONS: Peroxynitrite-induced EC oxidative stress produces differential effects on CAM expression, which may be mediated by HO-1 regulation.	Peroxynitrous Acid	13-26	heme oxygenase 1	Homo sapiens	129-133
15337692-0	2004	Simvastatin induces heme oxygenase-1: a novel mechanism of vessel protection.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	20-36
15337692-3	2004	Here, we studied whether heme oxygenase-1 (HO-1), an important cytoprotective molecule, is induced by simvastatin and the role of HO-1 in the pleiotropic effects of simvastatin.	Simvastatin	102-113	heme oxygenase 1	Homo sapiens	25-41
15337692-3	2004	Here, we studied whether heme oxygenase-1 (HO-1), an important cytoprotective molecule, is induced by simvastatin and the role of HO-1 in the pleiotropic effects of simvastatin.	Simvastatin	102-113	heme oxygenase 1	Homo sapiens	43-47
15337692-5	2004	The induction of HO-1 by simvastatin was not found in cultured endothelial cells and macrophages.	Simvastatin	25-36	heme oxygenase 1	Homo sapiens	17-21
15337692-7	2004	Treating VSMCs with zinc protoporphyrin, an HO-1 inhibitor, or HO-1 small interfering RNA (siRNA) blocked the antiinflammatory effect of simvastatin, including the inhibition of nuclear factor-kappaB activation and nitric oxide production.	Simvastatin	137-148	heme oxygenase 1	Homo sapiens	44-48
15337692-7	2004	Treating VSMCs with zinc protoporphyrin, an HO-1 inhibitor, or HO-1 small interfering RNA (siRNA) blocked the antiinflammatory effect of simvastatin, including the inhibition of nuclear factor-kappaB activation and nitric oxide production.	Simvastatin	137-148	heme oxygenase 1	Homo sapiens	63-67
15337692-7	2004	Treating VSMCs with zinc protoporphyrin, an HO-1 inhibitor, or HO-1 small interfering RNA (siRNA) blocked the antiinflammatory effect of simvastatin, including the inhibition of nuclear factor-kappaB activation and nitric oxide production.	Nitric Oxide	215-227	heme oxygenase 1	Homo sapiens	63-67
15337692-8	2004	Blockade of HO-1 also abolished the simvastatin-induced p21(Waf1) and the associated antiproliferative effect.	Simvastatin	36-47	heme oxygenase 1	Homo sapiens	12-16
15337692-9	2004	Simvastatin activated p38 and Akt in VSMCs, and the respective inhibitors of p38 and phosphoinositide 3-kinase (PI3K) greatly reduced the level of simvastatin-induced HO-1, which suggests the involvement of p38 and the PI3K-Akt pathway in HO-1 induction.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	167-171
15337692-9	2004	Simvastatin activated p38 and Akt in VSMCs, and the respective inhibitors of p38 and phosphoinositide 3-kinase (PI3K) greatly reduced the level of simvastatin-induced HO-1, which suggests the involvement of p38 and the PI3K-Akt pathway in HO-1 induction.	Simvastatin	0-11	heme oxygenase 1	Homo sapiens	239-243
15337692-9	2004	Simvastatin activated p38 and Akt in VSMCs, and the respective inhibitors of p38 and phosphoinositide 3-kinase (PI3K) greatly reduced the level of simvastatin-induced HO-1, which suggests the involvement of p38 and the PI3K-Akt pathway in HO-1 induction.	Simvastatin	147-158	heme oxygenase 1	Homo sapiens	167-171
15337692-9	2004	Simvastatin activated p38 and Akt in VSMCs, and the respective inhibitors of p38 and phosphoinositide 3-kinase (PI3K) greatly reduced the level of simvastatin-induced HO-1, which suggests the involvement of p38 and the PI3K-Akt pathway in HO-1 induction.	Simvastatin	147-158	heme oxygenase 1	Homo sapiens	239-243
15337692-10	2004	CONCLUSIONS: Simvastatin activates HO-1 in VSMCs in vitro and in vivo.	Simvastatin	13-24	heme oxygenase 1	Homo sapiens	35-39
15337692-11	2004	The antiinflammatory and antiproliferative effects of simvastatin occur largely through the induced HO-1.	Simvastatin	54-65	heme oxygenase 1	Homo sapiens	100-104
15602829-7	2004	We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes.	ammonium ferrous sulfate	506-510	heme oxygenase 1	Homo sapiens	49-53
15602829-9	2004	Furthermore, we demonstrated that pre-administration of cobalt protoporphyrin (CoPP) induced HO-1 in human hepatocytes, and prevented an increase of MDA and a decrease of GSH.	cobaltiprotoporphyrin	56-77	heme oxygenase 1	Homo sapiens	93-97
15602829-9	2004	Furthermore, we demonstrated that pre-administration of cobalt protoporphyrin (CoPP) induced HO-1 in human hepatocytes, and prevented an increase of MDA and a decrease of GSH.	cobaltiprotoporphyrin	79-83	heme oxygenase 1	Homo sapiens	93-97
15602829-10	2004	These effects could be partially reversed by zinc protoporphyrin (ZnPP), an antagonist of HO-1 induction.	zinc protoporphyrin	45-64	heme oxygenase 1	Homo sapiens	90-94
15602829-10	2004	These effects could be partially reversed by zinc protoporphyrin (ZnPP), an antagonist of HO-1 induction.	zinc protoporphyrin	66-70	heme oxygenase 1	Homo sapiens	90-94
15602829-11	2004	CONCLUSION: HO-1 expression in cells or organs could lead to new strategies for better prevention and treatment of ethanol-induced oxidative damage in human liver.	Ethanol	115-122	heme oxygenase 1	Homo sapiens	12-16
15602829-1	2004	UNLABELLED: We investigated the relationship between ethanol exposure and heme oxygenase (HO-1) in human hepatocytes in order to ascertain if induction of HO-1 can prevent ethanol induced cellular damage.	Ethanol	53-60	heme oxygenase 1	Homo sapiens	90-94
15602829-1	2004	UNLABELLED: We investigated the relationship between ethanol exposure and heme oxygenase (HO-1) in human hepatocytes in order to ascertain if induction of HO-1 can prevent ethanol induced cellular damage.	Ethanol	172-179	heme oxygenase 1	Homo sapiens	155-159
15602829-4	2004	HO-1 activity was indicated by bilirubin and Fe2+ formation.	Bilirubin	31-40	heme oxygenase 1	Homo sapiens	0-4
15602829-4	2004	HO-1 activity was indicated by bilirubin and Fe2+ formation.	ammonium ferrous sulfate	45-49	heme oxygenase 1	Homo sapiens	0-4
15602829-6	2004	RESULTS: We first demonstrated a dose-dependent response between ethanol exposure and HO-1 mRNA and protein expression in human hepatocytes.	Ethanol	65-72	heme oxygenase 1	Homo sapiens	86-90
15602829-7	2004	We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes.	Ethanol	87-94	heme oxygenase 1	Homo sapiens	49-53
15602829-7	2004	We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes.	Ethanol	121-128	heme oxygenase 1	Homo sapiens	49-53
15602829-7	2004	We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes.	Ethanol	121-128	heme oxygenase 1	Homo sapiens	49-53
15602829-7	2004	We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes.	Ethanol	121-128	heme oxygenase 1	Homo sapiens	49-53
15602829-7	2004	We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes.	Bilirubin	492-501	heme oxygenase 1	Homo sapiens	49-53
15518801-1	2004	To study the effect of treatment with cobalt-protoporphyrin (CoPP) for the induction of the heme oxygenase-1 (HO-1) enzyme on islet engraftment donor mice received either a single intraperitoneal injection of CoPP (20 mg/kg body weight) 1 day prior to islet isolation or this injection plus a 9 day posttransplantation course of Copp.	cobaltiprotoporphyrin	38-59	heme oxygenase 1	Homo sapiens	92-108
15240748-7	2004	Also, inhibition of HO-1 activity by the specific inhibitor zinc-II-protoporphyrin-IX had no effect on the anti-inflammatory function of IL-10.	zinc-ii-protoporphyrin-ix	60-85	heme oxygenase 1	Homo sapiens	20-24
15339982-8	2004	Heme catabolism is regulated by (inducible) heme oxygenase-1 (HO-1).	Heme	0-4	heme oxygenase 1	Homo sapiens	44-60
15339982-8	2004	Heme catabolism is regulated by (inducible) heme oxygenase-1 (HO-1).	Heme	0-4	heme oxygenase 1	Homo sapiens	62-66
15339982-10	2004	Stimulation of cells for 6 h with CdCl(2), which markedly increased HO-1 expression before the addition of VT, blunted subsequent hemin injury.	cdcl	34-38	heme oxygenase 1	Homo sapiens	68-72
15339982-11	2004	In conclusion, VT augments hemin-induced toxicity in renal tubular epithelial cells that can be reversed by prior induction of HO-1.	Hemin	27-32	heme oxygenase 1	Homo sapiens	127-131
15322212-5	2004	We demonstrate that aromatic and polar DEP fractions, which are enriched in polycyclic aromatic hydrocarbons and quinones, respectively, induce the expression of HO-1, GST, and other phase II enzymes in macrophages and epithelial cells.	Polycyclic Aromatic Hydrocarbons	76-108	heme oxygenase 1	Homo sapiens	162-166
15322212-5	2004	We demonstrate that aromatic and polar DEP fractions, which are enriched in polycyclic aromatic hydrocarbons and quinones, respectively, induce the expression of HO-1, GST, and other phase II enzymes in macrophages and epithelial cells.	Quinones	113-121	heme oxygenase 1	Homo sapiens	162-166
15518801-1	2004	To study the effect of treatment with cobalt-protoporphyrin (CoPP) for the induction of the heme oxygenase-1 (HO-1) enzyme on islet engraftment donor mice received either a single intraperitoneal injection of CoPP (20 mg/kg body weight) 1 day prior to islet isolation or this injection plus a 9 day posttransplantation course of Copp.	cobaltiprotoporphyrin	38-59	heme oxygenase 1	Homo sapiens	110-114
15518801-1	2004	To study the effect of treatment with cobalt-protoporphyrin (CoPP) for the induction of the heme oxygenase-1 (HO-1) enzyme on islet engraftment donor mice received either a single intraperitoneal injection of CoPP (20 mg/kg body weight) 1 day prior to islet isolation or this injection plus a 9 day posttransplantation course of Copp.	cobaltiprotoporphyrin	61-65	heme oxygenase 1	Homo sapiens	92-108
15518801-1	2004	To study the effect of treatment with cobalt-protoporphyrin (CoPP) for the induction of the heme oxygenase-1 (HO-1) enzyme on islet engraftment donor mice received either a single intraperitoneal injection of CoPP (20 mg/kg body weight) 1 day prior to islet isolation or this injection plus a 9 day posttransplantation course of Copp.	cobaltiprotoporphyrin	61-65	heme oxygenase 1	Homo sapiens	110-114
15271722-2	2004	HO-1 catalyzes the conversion of the heme moiety of hemeproteins, such as hemoglobin, myoglobin, and cytochrome P450, to biliverdin, liberating carbon monoxide (CO) in the process.	Heme	37-41	heme oxygenase 1	Homo sapiens	0-4
15311945-3	2004	We have observed that pretreatment of cells with PTIO boosted expression of IL-8 and heme oxygenase 1 (HOX) genes to a high level in cells treated with the NO donor DPTA-NO.	dpta-no	165-172	heme oxygenase 1	Homo sapiens	85-101
15311945-3	2004	We have observed that pretreatment of cells with PTIO boosted expression of IL-8 and heme oxygenase 1 (HOX) genes to a high level in cells treated with the NO donor DPTA-NO.	dpta-no	165-172	heme oxygenase 1	Homo sapiens	103-106
15311945-5	2004	The effect of PTIO was abrogated by reduced glutathione, suggesting that upregulation of the IL-8 and HOX genes is dependent on RNI-mediated S-nitrosation of specific regulator(s).	Glutathione	44-55	heme oxygenase 1	Homo sapiens	102-105
15311945-6	2004	The concentration of PTIO required to enhance mRNA level was different for IL-8 and HOX genes.	2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide	21-25	heme oxygenase 1	Homo sapiens	84-87
15258907-0	2004	Heme oxygenase-1 protects against apoptosis induced by tumor necrosis factor-alpha and cycloheximide in papillary thyroid carcinoma cells.	Cycloheximide	87-100	heme oxygenase 1	Homo sapiens	0-16
15258907-3	2004	The results show that HO-1 is significantly induced by hemin and cadmium.	Hemin	55-60	heme oxygenase 1	Homo sapiens	22-26
15258907-3	2004	The results show that HO-1 is significantly induced by hemin and cadmium.	Cadmium	65-72	heme oxygenase 1	Homo sapiens	22-26
15258907-4	2004	In addition to inducing HO-1, hemin and cadmium also cause a rise in the levels of p21, a cyclin-dependent kinase inhibitor.	Hemin	30-35	heme oxygenase 1	Homo sapiens	24-28
15258907-4	2004	In addition to inducing HO-1, hemin and cadmium also cause a rise in the levels of p21, a cyclin-dependent kinase inhibitor.	Cadmium	40-47	heme oxygenase 1	Homo sapiens	24-28
15612472-0	2004	[Effect of acute ethanol exposure on HO-1 enzyme activity in human primary hepatocytes].	Ethanol	17-24	heme oxygenase 1	Homo sapiens	37-41
15612472-1	2004	OBJECTIVE: To study the effect of ethanol exposure on the expression of HO-1 enzymes in human primary culture hepatocytes.	Ethanol	34-41	heme oxygenase 1	Homo sapiens	72-76
15612472-6	2004	Moreover, we also observed that ethanol exposure could affect HO-1 enzyme activity and HO-1 protein level, at the beginning, it went up significantly then went down.	Ethanol	32-39	heme oxygenase 1	Homo sapiens	62-91
15612472-7	2004	CONCLUSION: The increase of HO-1 enzyme activity and protein level after ethanol exposure may be relative to prevent against ethanol-induced oxidative injury in human primary hepatocytes.	Ethanol	73-80	heme oxygenase 1	Homo sapiens	28-32
15612472-7	2004	CONCLUSION: The increase of HO-1 enzyme activity and protein level after ethanol exposure may be relative to prevent against ethanol-induced oxidative injury in human primary hepatocytes.	Ethanol	125-132	heme oxygenase 1	Homo sapiens	28-32
15271722-2	2004	HO-1 catalyzes the conversion of the heme moiety of hemeproteins, such as hemoglobin, myoglobin, and cytochrome P450, to biliverdin, liberating carbon monoxide (CO) in the process.	Biliverdine	121-131	heme oxygenase 1	Homo sapiens	0-4
15271722-2	2004	HO-1 catalyzes the conversion of the heme moiety of hemeproteins, such as hemoglobin, myoglobin, and cytochrome P450, to biliverdin, liberating carbon monoxide (CO) in the process.	Carbon Monoxide	144-159	heme oxygenase 1	Homo sapiens	0-4
15271722-2	2004	HO-1 catalyzes the conversion of the heme moiety of hemeproteins, such as hemoglobin, myoglobin, and cytochrome P450, to biliverdin, liberating carbon monoxide (CO) in the process.	Carbon Monoxide	161-163	heme oxygenase 1	Homo sapiens	0-4
15271722-7	2004	These results suggest that oxidative stress caused by anesthesia and/or surgery may induce HO-1, which catalyzes heme to produce CO, leading to increased exhaled CO concentration.	Heme	113-117	heme oxygenase 1	Homo sapiens	91-95
15271722-7	2004	These results suggest that oxidative stress caused by anesthesia and/or surgery may induce HO-1, which catalyzes heme to produce CO, leading to increased exhaled CO concentration.	Carbon Monoxide	129-131	heme oxygenase 1	Homo sapiens	91-95
15231239-4	2004	These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD.	Biliverdine	185-195	heme oxygenase 1	Homo sapiens	107-123
15313669-4	2004	The recombinant plasmid pcDNA3-HO-1 was transfected into endothelial cells, and recombinant HO-1 was expressed in the endothelial cells under G418 selection.	antibiotic G 418	142-146	heme oxygenase 1	Homo sapiens	92-96
15231239-4	2004	These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD.	Iron	39-43	heme oxygenase 1	Homo sapiens	107-123
15276427-11	2004	mRNA levels of heme oxygenase-1 (HO-1) were decreased by NAC in DMA(V)-exposed, but MMA(V)-exposed cells.	N-myristoyl-alaninol	64-67	heme oxygenase 1	Homo sapiens	15-31
15298625-7	2004	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by trinitrobenzene sulphonic acid or dextran sulphate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the intestinal tract.	trinitrobenzene sulphonic acid	133-163	heme oxygenase 1	Homo sapiens	45-49
15298625-7	2004	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by trinitrobenzene sulphonic acid or dextran sulphate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the intestinal tract.	trinitrobenzene sulphonic acid	133-163	heme oxygenase 1	Homo sapiens	222-226
15231239-4	2004	These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD.	Heme	95-99	heme oxygenase 1	Homo sapiens	107-123
15264013-2	2004	The present study was carried out to examine the effect of dopamine on the expression of heme oxygenase-1 and -2 (HO-1 and HO-2) in human neuroblastomas (SK-N-SH cell line) and the effects of selegiline and antioxidants on this expression.	Dopamine	59-67	heme oxygenase 1	Homo sapiens	89-112
15231239-4	2004	These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD.	Iron	176-180	heme oxygenase 1	Homo sapiens	107-123
15356994-3	2004	Curcumin possesses anti-inflammatory activity and is a potent inhibitor of reactive oxygen-generating enzymes such as lipoxygenase/cyclooxygenase, xanthine dehydrogenase/oxidase and inducible nitric oxide synthase; and an effective inducer of heme oxygenase-1.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	243-259
15356994-3	2004	Curcumin possesses anti-inflammatory activity and is a potent inhibitor of reactive oxygen-generating enzymes such as lipoxygenase/cyclooxygenase, xanthine dehydrogenase/oxidase and inducible nitric oxide synthase; and an effective inducer of heme oxygenase-1.	reactive oxygen	75-90	heme oxygenase 1	Homo sapiens	243-259
15298625-7	2004	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by trinitrobenzene sulphonic acid or dextran sulphate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the intestinal tract.	dextran sulphate sodium	167-190	heme oxygenase 1	Homo sapiens	45-49
15298625-7	2004	Recent studies suggest that the induction of HO-1 expression plays a critical protective role in intestinal damage models induced by trinitrobenzene sulphonic acid or dextran sulphate sodium, indicating that activation of HO-1 may act as an endogenous defensive mechanism to reduce inflammation and tissue injury in the intestinal tract.	dextran sulphate sodium	167-190	heme oxygenase 1	Homo sapiens	222-226
15264013-2	2004	The present study was carried out to examine the effect of dopamine on the expression of heme oxygenase-1 and -2 (HO-1 and HO-2) in human neuroblastomas (SK-N-SH cell line) and the effects of selegiline and antioxidants on this expression.	Dopamine	59-67	heme oxygenase 1	Homo sapiens	114-127
15264013-5	2004	The levels of HO-1 mRNA increased after dopamine treatment, in a dose-dependent manner, in all cell lines studied, whereas levels of the two HO-2 transcripts did not.	Dopamine	40-48	heme oxygenase 1	Homo sapiens	14-18
15264013-7	2004	HO-1 protein was undetectable in untreated SK-N-SH cells and increased after treatment with dopamine.	Dopamine	92-100	heme oxygenase 1	Homo sapiens	0-4
15264013-10	2004	Selegiline (10 microM) produced significant increase (P &lt; 0.01) in the induction of HO-1 by dopamine (more than six times the control values).	Selegiline	0-10	heme oxygenase 1	Homo sapiens	87-91
15264013-10	2004	Selegiline (10 microM) produced significant increase (P &lt; 0.01) in the induction of HO-1 by dopamine (more than six times the control values).	Dopamine	95-103	heme oxygenase 1	Homo sapiens	87-91
15264013-11	2004	The increased expression of HO-1 following dopamine treatment indicates that dopamine produces oxidative stress in this cell line.	Dopamine	43-51	heme oxygenase 1	Homo sapiens	28-32
15264013-11	2004	The increased expression of HO-1 following dopamine treatment indicates that dopamine produces oxidative stress in this cell line.	Dopamine	77-85	heme oxygenase 1	Homo sapiens	28-32
15233805-3	2004	HO-1 catalyzes heme breakdown to release iron, carbon monoxide, and biliverdin, which is reduced to bilirubin, a potent radical scavenger.	Iron	41-45	heme oxygenase 1	Homo sapiens	0-4
15233805-3	2004	HO-1 catalyzes heme breakdown to release iron, carbon monoxide, and biliverdin, which is reduced to bilirubin, a potent radical scavenger.	Carbon Monoxide	47-62	heme oxygenase 1	Homo sapiens	0-4
15233805-3	2004	HO-1 catalyzes heme breakdown to release iron, carbon monoxide, and biliverdin, which is reduced to bilirubin, a potent radical scavenger.	Biliverdine	68-78	heme oxygenase 1	Homo sapiens	0-4
15233805-3	2004	HO-1 catalyzes heme breakdown to release iron, carbon monoxide, and biliverdin, which is reduced to bilirubin, a potent radical scavenger.	Bilirubin	100-109	heme oxygenase 1	Homo sapiens	0-4
15213272-4	2004	SSAT overexpression increased the expression of heme oxygenase-1 (HO-1) by 350% 24 h after addition of tetracycline, indicating the induction of oxidative stress.	Tetracycline	103-115	heme oxygenase 1	Homo sapiens	48-64
15213272-4	2004	SSAT overexpression increased the expression of heme oxygenase-1 (HO-1) by 350% 24 h after addition of tetracycline, indicating the induction of oxidative stress.	Tetracycline	103-115	heme oxygenase 1	Homo sapiens	66-70
15213272-5	2004	The presence of catalase significantly prevented the upregulation of HO-1 in SSAT overexpressing cells, indicating that generation of H2O2 is partially responsible for the induction of oxidative stress.	Hydrogen Peroxide	134-138	heme oxygenase 1	Homo sapiens	69-73
15219989-0	2004	Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex.	Hydroxylamine	0-13	heme oxygenase 1	Homo sapiens	71-87
15219989-0	2004	Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex.	hydrazine	18-27	heme oxygenase 1	Homo sapiens	71-87
15551655-11	2004	Dopamine is capable of stimulating the induction of protective enzymes like heme oxygenase-1 (HO-1) rendering the organ more resistant to the insult of ischemia/reperfusion and inflammation.	Dopamine	0-8	heme oxygenase 1	Homo sapiens	76-92
15219989-0	2004	Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex.	Heme	49-53	heme oxygenase 1	Homo sapiens	71-87
15219989-0	2004	Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex.	Iron	54-58	heme oxygenase 1	Homo sapiens	71-87
15213303-0	2004	Roles of heme oxygenase-1 in the antiproliferative and antiapoptotic effects of nitric oxide on Jurkat T cells.	Nitric Oxide	80-92	heme oxygenase 1	Homo sapiens	9-25
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Heme	40-44	heme oxygenase 1	Homo sapiens	0-16
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Heme	40-44	heme oxygenase 1	Homo sapiens	18-22
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Biliverdine	50-60	heme oxygenase 1	Homo sapiens	0-16
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Biliverdine	50-60	heme oxygenase 1	Homo sapiens	18-22
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Iron	67-71	heme oxygenase 1	Homo sapiens	0-16
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Iron	67-71	heme oxygenase 1	Homo sapiens	18-22
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	ammonium ferrous sulfate	73-79	heme oxygenase 1	Homo sapiens	0-16
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	ammonium ferrous sulfate	73-79	heme oxygenase 1	Homo sapiens	18-22
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	0-16
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Carbon Monoxide	86-101	heme oxygenase 1	Homo sapiens	18-22
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Carbon Monoxide	103-105	heme oxygenase 1	Homo sapiens	0-16
15213303-2	2004	Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects.	Carbon Monoxide	103-105	heme oxygenase 1	Homo sapiens	18-22
15213303-5	2004	Using human Jurkat T cells, we found that the NO donor sodium nitroprusside (SNP) induced HO-1 expression and that preincubation with SNP suppressed T cell proliferation induced by concanavalin A and apoptosis triggered by anti-Fas antibody.	Nitroprusside	55-75	heme oxygenase 1	Homo sapiens	90-94
15213303-6	2004	Suppressions of T cell proliferation and apoptosis comparable with SNP were also observed when the T cells were preincubated with the HO-1 inducer cobalt protoporphyrin.	cobaltiprotoporphyrin	147-168	heme oxygenase 1	Homo sapiens	134-138
15213303-7	2004	A phosphorothioate-linked HO-1 antisense oligonucleotide blocked HO-1 expression, and subsequently abrogated the antiproliferative and antiapoptotic effects of SNP.	Parathion	2-18	heme oxygenase 1	Homo sapiens	26-30
15213303-7	2004	A phosphorothioate-linked HO-1 antisense oligonucleotide blocked HO-1 expression, and subsequently abrogated the antiproliferative and antiapoptotic effects of SNP.	Parathion	2-18	heme oxygenase 1	Homo sapiens	65-69
15213303-7	2004	A phosphorothioate-linked HO-1 antisense oligonucleotide blocked HO-1 expression, and subsequently abrogated the antiproliferative and antiapoptotic effects of SNP.	Oligonucleotides	41-56	heme oxygenase 1	Homo sapiens	26-30
15213303-7	2004	A phosphorothioate-linked HO-1 antisense oligonucleotide blocked HO-1 expression, and subsequently abrogated the antiproliferative and antiapoptotic effects of SNP.	Oligonucleotides	41-56	heme oxygenase 1	Homo sapiens	65-69
15188507-7	2004	The specific HO-1 inhibitor- ZnPPIX could worsen LPS-induced injuries and weaken the protective effect of CCK-8.	zinc protoporphyrin	29-35	heme oxygenase 1	Homo sapiens	13-17
15207648-4	2004	Immunoblot experiments showed that Pb2+ exposure (100 nM to 10 microM, 1-14 days) induces HO-1 synthesis in astrocytes, but not in neurons; this is probably the 32-kDa protein.	Lead	35-39	heme oxygenase 1	Homo sapiens	90-94
15207648-7	2004	We found that HO-1 induction in astrocytes is increased by combined exposure to Pb2+ and many other stresses, including heat, nitric oxide, H2O2, and superoxide.	Nitric Oxide	126-138	heme oxygenase 1	Homo sapiens	14-18
15207648-7	2004	We found that HO-1 induction in astrocytes is increased by combined exposure to Pb2+ and many other stresses, including heat, nitric oxide, H2O2, and superoxide.	Hydrogen Peroxide	140-144	heme oxygenase 1	Homo sapiens	14-18
15207648-7	2004	We found that HO-1 induction in astrocytes is increased by combined exposure to Pb2+ and many other stresses, including heat, nitric oxide, H2O2, and superoxide.	Superoxides	150-160	heme oxygenase 1	Homo sapiens	14-18
15207648-10	2004	Induction of HO-1 by Pb2+ is reduced by the hydroxyl radical scavengers dimethylthiourea (DMTU) and mannitol, but not by inhibitors of calmodulin, calmodulin-dependent protein kinases, protein kinase C, or extracellular signal-regulated kinases (ERK).	Lead	21-25	heme oxygenase 1	Homo sapiens	13-17
15207648-10	2004	Induction of HO-1 by Pb2+ is reduced by the hydroxyl radical scavengers dimethylthiourea (DMTU) and mannitol, but not by inhibitors of calmodulin, calmodulin-dependent protein kinases, protein kinase C, or extracellular signal-regulated kinases (ERK).	Hydroxyl Radical	44-60	heme oxygenase 1	Homo sapiens	13-17
15207648-10	2004	Induction of HO-1 by Pb2+ is reduced by the hydroxyl radical scavengers dimethylthiourea (DMTU) and mannitol, but not by inhibitors of calmodulin, calmodulin-dependent protein kinases, protein kinase C, or extracellular signal-regulated kinases (ERK).	1,3-dimethylthiourea	72-88	heme oxygenase 1	Homo sapiens	13-17
15207648-10	2004	Induction of HO-1 by Pb2+ is reduced by the hydroxyl radical scavengers dimethylthiourea (DMTU) and mannitol, but not by inhibitors of calmodulin, calmodulin-dependent protein kinases, protein kinase C, or extracellular signal-regulated kinases (ERK).	1,3-dimethylthiourea	90-94	heme oxygenase 1	Homo sapiens	13-17
15207648-10	2004	Induction of HO-1 by Pb2+ is reduced by the hydroxyl radical scavengers dimethylthiourea (DMTU) and mannitol, but not by inhibitors of calmodulin, calmodulin-dependent protein kinases, protein kinase C, or extracellular signal-regulated kinases (ERK).	Mannitol	100-108	heme oxygenase 1	Homo sapiens	13-17
15188507-7	2004	The specific HO-1 inhibitor- ZnPPIX could worsen LPS-induced injuries and weaken the protective effect of CCK-8.	Sincalide	106-111	heme oxygenase 1	Homo sapiens	13-17
15188507-9	2004	CONCLUSION: HO-1 may be a key factor in CCK-8 attenuated injuries of PASMCs induced by LPS, and HO-1 expression may be related to the activation of JNK and activator protein (AP-1).	pasmcs	69-75	heme oxygenase 1	Homo sapiens	12-16
15161651-6	2004	A rapid increase in the expression of genes involved in reactive oxygen species metabolism and cell stress, eg, heme oxygenase-1, thioredoxin reductase, cytochrome b5 reductase, Gadd 153, amino acid transporter E16, and HSP70 was found after HOCl-LDL treatment of HK-2 cells.	Reactive Oxygen Species	56-79	heme oxygenase 1	Homo sapiens	112-128
15024026-0	2004	15-deoxy-delta 12,14-prostaglandin J2 induces heme oxygenase-1 gene expression in a reactive oxygen species-dependent manner in human lymphocytes.	15-deoxy-delta(12,14)-prostaglandin J2	0-37	heme oxygenase 1	Homo sapiens	46-62
15180563-3	2004	Exposure of mammalian cells to oxidative stimuli induces heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, as well as a 33-kDa heat shock protein.	Heme	57-61	heme oxygenase 1	Homo sapiens	75-79
15158123-3	2004	In this study, we found that a 30-min incubation in the absence of glucose resulted in a rapid increased expression of COX-2 and HO-1 in cardiac fibroblasts as examined by real-time quantitative polymerase chain reaction (PCR) and western blot analysis.	Glucose	67-74	heme oxygenase 1	Homo sapiens	129-133
15158123-7	2004	In addition, the induction of COX-2 and HO-1 expression by TGD was prevented by pretreatment with NAC or SB203580, a p38 MAPK inhibitor.	Acetylcysteine	98-101	heme oxygenase 1	Homo sapiens	40-44
15158123-7	2004	In addition, the induction of COX-2 and HO-1 expression by TGD was prevented by pretreatment with NAC or SB203580, a p38 MAPK inhibitor.	SB 203580	105-113	heme oxygenase 1	Homo sapiens	40-44
15158123-8	2004	Surprisingly, pretreatment with chelerythrine, an inhibitor of PKC, strongly augmented the HO-1 mRNA expression but blocked the COX-2 mRNA induction by TGD.	chelerythrine	32-45	heme oxygenase 1	Homo sapiens	91-95
15158123-9	2004	These results demonstrate that briefly removing glucose from cultured cardiac fibroblasts induces COX-2 and HO-1 expression via generation of ROS and p38 MAPK phosphorylation, while the translocation of PKC- to the membrane fraction may participate in the induction of COX-2 but not in the HO-1 expression.	Glucose	48-55	heme oxygenase 1	Homo sapiens	108-112
15158123-9	2004	These results demonstrate that briefly removing glucose from cultured cardiac fibroblasts induces COX-2 and HO-1 expression via generation of ROS and p38 MAPK phosphorylation, while the translocation of PKC- to the membrane fraction may participate in the induction of COX-2 but not in the HO-1 expression.	Glucose	48-55	heme oxygenase 1	Homo sapiens	290-294
15158123-9	2004	These results demonstrate that briefly removing glucose from cultured cardiac fibroblasts induces COX-2 and HO-1 expression via generation of ROS and p38 MAPK phosphorylation, while the translocation of PKC- to the membrane fraction may participate in the induction of COX-2 but not in the HO-1 expression.	Reactive Oxygen Species	142-145	heme oxygenase 1	Homo sapiens	108-112
15158359-9	2004	These results showing a CO-mediated decrease in 59Fe uptake from 59Fe-Tf using exogenous CO were in agreement with studies implementing cells transfected with HO1.	Iron-59	48-52	heme oxygenase 1	Homo sapiens	159-162
15024026-0	2004	15-deoxy-delta 12,14-prostaglandin J2 induces heme oxygenase-1 gene expression in a reactive oxygen species-dependent manner in human lymphocytes.	Reactive Oxygen Species	84-107	heme oxygenase 1	Homo sapiens	46-62
15024026-6	2004	Inhibition of intracellular ROS production by N-acetylcysteine, TEMPO, Me(2)SO, 1,10-phenanthroline, or allopurinol resulted in a decreased 15dPGJ(2)-dependent HO-1 expression in the cells.	Reactive Oxygen Species	28-31	heme oxygenase 1	Homo sapiens	160-164
15024026-6	2004	Inhibition of intracellular ROS production by N-acetylcysteine, TEMPO, Me(2)SO, 1,10-phenanthroline, or allopurinol resulted in a decreased 15dPGJ(2)-dependent HO-1 expression in the cells.	Acetylcysteine	46-62	heme oxygenase 1	Homo sapiens	160-164
15024026-6	2004	Inhibition of intracellular ROS production by N-acetylcysteine, TEMPO, Me(2)SO, 1,10-phenanthroline, or allopurinol resulted in a decreased 15dPGJ(2)-dependent HO-1 expression in the cells.	1,10-phenanthroline	80-99	heme oxygenase 1	Homo sapiens	160-164
15024026-6	2004	Inhibition of intracellular ROS production by N-acetylcysteine, TEMPO, Me(2)SO, 1,10-phenanthroline, or allopurinol resulted in a decreased 15dPGJ(2)-dependent HO-1 expression in the cells.	Allopurinol	104-115	heme oxygenase 1	Homo sapiens	160-164
15024026-7	2004	Furthermore, buthionine sulfoximine, an inhibitor of reduced glutathione synthesis, or Fe(2+)/Cu(2+) ions enhanced the positive effect of 15dPGJ(2) on HO-1 expression.	Buthionine Sulfoximine	13-35	heme oxygenase 1	Homo sapiens	151-155
15024026-7	2004	Furthermore, buthionine sulfoximine, an inhibitor of reduced glutathione synthesis, or Fe(2+)/Cu(2+) ions enhanced the positive effect of 15dPGJ(2) on HO-1 expression.	Glutathione	61-72	heme oxygenase 1	Homo sapiens	151-155
15024026-7	2004	Furthermore, buthionine sulfoximine, an inhibitor of reduced glutathione synthesis, or Fe(2+)/Cu(2+) ions enhanced the positive effect of 15dPGJ(2) on HO-1 expression.	ammonium ferrous sulfate	87-93	heme oxygenase 1	Homo sapiens	151-155
15024026-7	2004	Furthermore, buthionine sulfoximine, an inhibitor of reduced glutathione synthesis, or Fe(2+)/Cu(2+) ions enhanced the positive effect of 15dPGJ(2) on HO-1 expression.	cupric ion	94-100	heme oxygenase 1	Homo sapiens	151-155
15084179-2	2004	The induction of HO-1 expression is modulated by a (GT)(n) dinucleotide polymorphism in the promoter of the gene, of which increased activity is associated with short (S) (&lt;or=27) repeats.	(n) dinucleotide	55-71	heme oxygenase 1	Homo sapiens	17-21
14988408-14	2004	hBVR modulation of ATF-2 and HO-1 expression suggests it has a potential role in regulation of AP-1 and cAMP-regulated genes and a role in cell signaling.	Cyclic AMP	104-108	heme oxygenase 1	Homo sapiens	29-33
14731112-9	2004	The half-life of HO-1 protein was prolonged by MG132, indicating that the upregulation of HO-1 by proteasome inhibitor is partially attributable to the inhibition of protein degradation.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	47-52	heme oxygenase 1	Homo sapiens	90-94
14731112-11	2004	We found HO-1 upregulation by MG132 and pyrrolidine dithiocarbamate is unrelated to their inhibition of NF-kappaB, since leptomycin B, another NF-kappaB inhibitor, did not elicit similar induction of HO-1.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	30-35	heme oxygenase 1	Homo sapiens	9-13
14731112-3	2004	In the present study, we found a novel action of proteasome inhibitors MG132 and MG262 on HO-1 induction, and characterized the underlying mechanisms.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	71-76	heme oxygenase 1	Homo sapiens	90-94
14731112-11	2004	We found HO-1 upregulation by MG132 and pyrrolidine dithiocarbamate is unrelated to their inhibition of NF-kappaB, since leptomycin B, another NF-kappaB inhibitor, did not elicit similar induction of HO-1.	pyrrolidine dithiocarbamic acid	40-67	heme oxygenase 1	Homo sapiens	9-13
14731112-3	2004	In the present study, we found a novel action of proteasome inhibitors MG132 and MG262 on HO-1 induction, and characterized the underlying mechanisms.	MG 262	81-86	heme oxygenase 1	Homo sapiens	90-94
14731112-4	2004	MG132 (&gt; or =0.1 microM) treatment resulted in a marked time- and concentration-dependent induction of the steady-state level of HO-1 mRNA in RAW264.7 macrophages, followed by a corresponding increase in HO-1 protein.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	heme oxygenase 1	Homo sapiens	132-136
14731112-4	2004	MG132 (&gt; or =0.1 microM) treatment resulted in a marked time- and concentration-dependent induction of the steady-state level of HO-1 mRNA in RAW264.7 macrophages, followed by a corresponding increase in HO-1 protein.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	0-5	heme oxygenase 1	Homo sapiens	207-211
14731112-5	2004	Actinomycin D and cycloheximide inhibited MG132-responsive HO-1 protein expression, indicating a requirement for transcription and de novo protein synthesis.	Dactinomycin	0-13	heme oxygenase 1	Homo sapiens	59-63
14731112-5	2004	Actinomycin D and cycloheximide inhibited MG132-responsive HO-1 protein expression, indicating a requirement for transcription and de novo protein synthesis.	Cycloheximide	18-31	heme oxygenase 1	Homo sapiens	59-63
14731112-5	2004	Actinomycin D and cycloheximide inhibited MG132-responsive HO-1 protein expression, indicating a requirement for transcription and de novo protein synthesis.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	42-47	heme oxygenase 1	Homo sapiens	59-63
14731112-6	2004	The involvement of signal pathways in MG132-induced HO-1 gene expression was examined using chemical inhibitors.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	38-43	heme oxygenase 1	Homo sapiens	52-56
14731112-7	2004	Antioxidant N -acetylcysteine and SB203580, an antioxidant and inhibitor of p38 MAPK (mitogen-activated protein kinase), abolished MG132-inducible HO-1 expression.	Acetylcysteine	12-29	heme oxygenase 1	Homo sapiens	147-151
14731112-7	2004	Antioxidant N -acetylcysteine and SB203580, an antioxidant and inhibitor of p38 MAPK (mitogen-activated protein kinase), abolished MG132-inducible HO-1 expression.	SB 203580	34-42	heme oxygenase 1	Homo sapiens	147-151
15190962-1	2004	OBJECTIVE: We aimed to quantify concentrations of inducible heme oxygenase (HO)-1 in the lungs of patients with acute respiratory distress syndrome (ARDS) and to investigate its role as a source of ferrous iron and as a signaling agent for iron regulation.	Iron	206-210	heme oxygenase 1	Homo sapiens	60-81
14731112-7	2004	Antioxidant N -acetylcysteine and SB203580, an antioxidant and inhibitor of p38 MAPK (mitogen-activated protein kinase), abolished MG132-inducible HO-1 expression.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	131-136	heme oxygenase 1	Homo sapiens	147-151
14731112-9	2004	The half-life of HO-1 protein was prolonged by MG132, indicating that the upregulation of HO-1 by proteasome inhibitor is partially attributable to the inhibition of protein degradation.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	47-52	heme oxygenase 1	Homo sapiens	17-21
15126353-2	2004	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the degradation of heme and has recently been implicated in the regulation of growth and survival of various neoplastic cells.	Heme	89-93	heme oxygenase 1	Homo sapiens	0-16
15126353-2	2004	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the degradation of heme and has recently been implicated in the regulation of growth and survival of various neoplastic cells.	Heme	89-93	heme oxygenase 1	Homo sapiens	18-22
15126353-5	2004	Exposure of these cells to the BCR/ABL tyrosine kinase inhibitor STI571 resulted in decreased expression of HO-1 mRNA and protein.	Imatinib Mesylate	65-71	heme oxygenase 1	Homo sapiens	108-112
15126353-8	2004	Hemin-induced expression of HO-1 was found to protect CML cells from STI571-induced cell death.	Imatinib Mesylate	69-75	heme oxygenase 1	Homo sapiens	28-32
15126353-9	2004	In addition, inhibition of HO-1 by zinc-(II)-deuteroporphyrin-IX-2,4-bisethyleneglycol resulted in a substantial decrease of cell viability.	zinc-(ii)-deuteroporphyrin-ix-2,4-bisethyleneglycol	35-86	heme oxygenase 1	Homo sapiens	27-31
14726403-8	2004	Increased HO-1 enzymatic activity in vitro enhanced proliferation of KSHV-infected DMVECs in the presence of free heme.	dmvecs	83-89	heme oxygenase 1	Homo sapiens	10-14
14726403-8	2004	Increased HO-1 enzymatic activity in vitro enhanced proliferation of KSHV-infected DMVECs in the presence of free heme.	Heme	114-118	heme oxygenase 1	Homo sapiens	10-14
14726403-9	2004	Treatment with the HO-1 inhibitor chromium mesoporphyrin IX abolished heme-induced proliferation.	chromium mesoporphyrin ix	34-59	heme oxygenase 1	Homo sapiens	19-23
14726403-9	2004	Treatment with the HO-1 inhibitor chromium mesoporphyrin IX abolished heme-induced proliferation.	Heme	70-74	heme oxygenase 1	Homo sapiens	19-23
15126353-10	2004	Furthermore, overexpression of HO-1 in the CML-derived cell line K562 was found to counteract STI571-induced apoptosis.	Imatinib Mesylate	94-100	heme oxygenase 1	Homo sapiens	31-35
15190962-1	2004	OBJECTIVE: We aimed to quantify concentrations of inducible heme oxygenase (HO)-1 in the lungs of patients with acute respiratory distress syndrome (ARDS) and to investigate its role as a source of ferrous iron and as a signaling agent for iron regulation.	Iron	240-244	heme oxygenase 1	Homo sapiens	60-81
15086901-7	2004	In TALH cells infected with Ad-NKCC2-HO-1, Ang II-stimulated prostaglandin E(2) (PGE(2)) levels were reduced by 40%.	Dinoprostone	61-79	heme oxygenase 1	Homo sapiens	37-41
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	15-20
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	36-52
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	54-58
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	140-144
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	237-246	heme oxygenase 1	Homo sapiens	15-20
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	237-246	heme oxygenase 1	Homo sapiens	36-52
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	237-246	heme oxygenase 1	Homo sapiens	54-58
15341181-8	2004	In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury.	Bilirubin	237-246	heme oxygenase 1	Homo sapiens	140-144
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Heme	64-68	heme oxygenase 1	Homo sapiens	12-28
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Heme	64-68	heme oxygenase 1	Homo sapiens	30-34
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Bilirubin	72-81	heme oxygenase 1	Homo sapiens	12-28
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Bilirubin	72-81	heme oxygenase 1	Homo sapiens	30-34
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	12-28
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Carbon Monoxide	83-98	heme oxygenase 1	Homo sapiens	30-34
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Carbon Monoxide	100-102	heme oxygenase 1	Homo sapiens	12-28
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Carbon Monoxide	100-102	heme oxygenase 1	Homo sapiens	30-34
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Iron	114-118	heme oxygenase 1	Homo sapiens	12-28
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Iron	114-118	heme oxygenase 1	Homo sapiens	30-34
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Heme	159-163	heme oxygenase 1	Homo sapiens	12-28
15086901-7	2004	In TALH cells infected with Ad-NKCC2-HO-1, Ang II-stimulated prostaglandin E(2) (PGE(2)) levels were reduced by 40%.	Prostaglandins E	81-84	heme oxygenase 1	Homo sapiens	37-41
15086901-1	2004	BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme.	Heme	159-163	heme oxygenase 1	Homo sapiens	30-34
15086901-8	2004	Ang II caused a marked decrease in GSH levels and this decrease was greatly attenuated in TALH cells transduced with Ad-NKCC2-HO-1.	Glutathione	35-38	heme oxygenase 1	Homo sapiens	126-130
15086901-3	2004	We hypothesize that selective upregulation of HO-1 in TALH by gene transfer attenuates oxidative stress caused by angiotensin II (Ang II).	talh	54-58	heme oxygenase 1	Homo sapiens	46-50
14977878-1	2004	Biliverdin, a product of heme oxygenase-1 (HO-1) enzymatic action, is converted into bilirubin, which has been considered a waste product in the past.	Biliverdine	0-10	heme oxygenase 1	Homo sapiens	25-41
15067050-0	2004	Carbon monoxide produced by heme oxygenase-1 suppresses T cell proliferation via inhibition of IL-2 production.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	28-44
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Heme	36-40	heme oxygenase 1	Homo sapiens	0-16
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Heme	36-40	heme oxygenase 1	Homo sapiens	18-22
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Carbon Monoxide	46-48	heme oxygenase 1	Homo sapiens	0-16
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Carbon Monoxide	46-48	heme oxygenase 1	Homo sapiens	18-22
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Biliverdine	50-60	heme oxygenase 1	Homo sapiens	0-16
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Biliverdine	50-60	heme oxygenase 1	Homo sapiens	18-22
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Iron	71-75	heme oxygenase 1	Homo sapiens	0-16
15067050-1	2004	Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions.	Iron	71-75	heme oxygenase 1	Homo sapiens	18-22
15049686-0	2004	Crystal structure of human heme oxygenase-1 in a complex with biliverdin.	Biliverdine	62-72	heme oxygenase 1	Homo sapiens	27-43
14977878-1	2004	Biliverdin, a product of heme oxygenase-1 (HO-1) enzymatic action, is converted into bilirubin, which has been considered a waste product in the past.	Bilirubin	85-94	heme oxygenase 1	Homo sapiens	25-41
14977880-0	2004	Heme oxygenase-1-derived carbon monoxide protects hearts from transplant associated ischemia reperfusion injury.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Heme	33-37	heme oxygenase 1	Homo sapiens	0-16
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Heme	33-37	heme oxygenase 1	Homo sapiens	18-22
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Iron	43-47	heme oxygenase 1	Homo sapiens	0-16
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Heme	23-27	heme oxygenase 1	Homo sapiens	41-45
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Iron	43-47	heme oxygenase 1	Homo sapiens	18-22
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Carbon Monoxide	96-111	heme oxygenase 1	Homo sapiens	23-39
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Carbon Monoxide	96-111	heme oxygenase 1	Homo sapiens	41-45
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Carbon Monoxide	113-115	heme oxygenase 1	Homo sapiens	23-39
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Carbon Monoxide	113-115	heme oxygenase 1	Homo sapiens	41-45
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Biliverdine	118-129	heme oxygenase 1	Homo sapiens	23-39
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Biliverdine	118-129	heme oxygenase 1	Homo sapiens	41-45
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Iron	139-143	heme oxygenase 1	Homo sapiens	23-39
14973545-1	2004	Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models.	Iron	139-143	heme oxygenase 1	Homo sapiens	41-45
15019971-0	2004	Overexpression of heme oxygenase (HO)-1 renders Jurkat T cells resistant to fas-mediated apoptosis: involvement of iron released by HO-1.	ammonium ferrous sulfate	76-79	heme oxygenase 1	Homo sapiens	18-39
15019971-0	2004	Overexpression of heme oxygenase (HO)-1 renders Jurkat T cells resistant to fas-mediated apoptosis: involvement of iron released by HO-1.	Iron	115-119	heme oxygenase 1	Homo sapiens	18-39
15019971-0	2004	Overexpression of heme oxygenase (HO)-1 renders Jurkat T cells resistant to fas-mediated apoptosis: involvement of iron released by HO-1.	Iron	115-119	heme oxygenase 1	Homo sapiens	132-136
15019971-4	2004	Surprisingly, however, HO-1-overexpressing Jurkat T cells showed strong resistance to Fas-mediated apoptosis.	ammonium ferrous sulfate	86-89	heme oxygenase 1	Homo sapiens	23-27
15019971-5	2004	In contrast, abrogation of HO-1 expression by antisense oligomer against HO-1 gene from CoPP-treated cells or depletion of iron by desferrioxamine from HO-1-transfected cells abolished the resistance.	cobaltiprotoporphyrin	88-92	heme oxygenase 1	Homo sapiens	27-31
15019971-5	2004	In contrast, abrogation of HO-1 expression by antisense oligomer against HO-1 gene from CoPP-treated cells or depletion of iron by desferrioxamine from HO-1-transfected cells abolished the resistance.	cobaltiprotoporphyrin	88-92	heme oxygenase 1	Homo sapiens	73-77
15019971-5	2004	In contrast, abrogation of HO-1 expression by antisense oligomer against HO-1 gene from CoPP-treated cells or depletion of iron by desferrioxamine from HO-1-transfected cells abolished the resistance.	cobaltiprotoporphyrin	88-92	heme oxygenase 1	Homo sapiens	73-77
15019971-8	2004	Primary CD4+ T cells induced by CoPP to express HO-1 also showed more resistance to Fas-mediated apoptosis than untreated cells.	cobaltiprotoporphyrin	32-36	heme oxygenase 1	Homo sapiens	48-52
15019971-8	2004	Primary CD4+ T cells induced by CoPP to express HO-1 also showed more resistance to Fas-mediated apoptosis than untreated cells.	ammonium ferrous sulfate	84-87	heme oxygenase 1	Homo sapiens	48-52
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Biliverdine	49-59	heme oxygenase 1	Homo sapiens	0-16
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Biliverdine	49-59	heme oxygenase 1	Homo sapiens	18-22
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	65-80	heme oxygenase 1	Homo sapiens	0-16
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	65-80	heme oxygenase 1	Homo sapiens	18-22
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	82-84	heme oxygenase 1	Homo sapiens	0-16
14977880-1	2004	Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	82-84	heme oxygenase 1	Homo sapiens	18-22
14977880-4	2004	Induction of HO-1 expression by administration of cobalt protoporphyrin IX (CoPPIX) to the graft donor restored graft function.	cobaltiprotoporphyrin	50-74	heme oxygenase 1	Homo sapiens	13-17
14977880-4	2004	Induction of HO-1 expression by administration of cobalt protoporphyrin IX (CoPPIX) to the graft donor restored graft function.	cobaltiprotoporphyrin	76-82	heme oxygenase 1	Homo sapiens	13-17
14977880-5	2004	Inhibition of HO-1 enzymatic activity, by administration of zinc protoporphyrin (ZnPPIX) at the time of transplantation, reversed the protective effect of HO-1.	zinc protoporphyrin	60-79	heme oxygenase 1	Homo sapiens	14-18
14977880-5	2004	Inhibition of HO-1 enzymatic activity, by administration of zinc protoporphyrin (ZnPPIX) at the time of transplantation, reversed the protective effect of HO-1.	zinc protoporphyrin	60-79	heme oxygenase 1	Homo sapiens	155-159
14977880-5	2004	Inhibition of HO-1 enzymatic activity, by administration of zinc protoporphyrin (ZnPPIX) at the time of transplantation, reversed the protective effect of HO-1.	zinc protoporphyrin	81-87	heme oxygenase 1	Homo sapiens	14-18
14977880-5	2004	Inhibition of HO-1 enzymatic activity, by administration of zinc protoporphyrin (ZnPPIX) at the time of transplantation, reversed the protective effect of HO-1.	zinc protoporphyrin	81-87	heme oxygenase 1	Homo sapiens	155-159
15085064-7	2004	Manidipine increased monocyte HO-1 mRNA production (1.6 +/- 0.4 versus 1.2 +/- 0.4, P &lt; 0.008), while nifedipine and captopril showed no effect (1.2 +/- 0.3 and 1.1 +/- 0.3, respectively).	manidipine	0-10	heme oxygenase 1	Homo sapiens	30-34
15085064-0	2004	Effect of manidipine on gene expression and protein level of oxidative stress-related proteins: p22phox and HO-1: relevance for antihypertensive and anti-remodeling effects.	manidipine	10-20	heme oxygenase 1	Homo sapiens	108-112
15085064-9	2004	In conclusion, manidipine decreases p22(phox) and increases HO-1 mRNA production and protein level.	manidipine	15-25	heme oxygenase 1	Homo sapiens	60-64
15085064-10	2004	The manidipine-induced increase of HO-1 gene and protein expression seems to be a peculiar effect of this drug since it is not observed with captopril and nifedipine.	manidipine	4-14	heme oxygenase 1	Homo sapiens	35-39
15085064-10	2004	The manidipine-induced increase of HO-1 gene and protein expression seems to be a peculiar effect of this drug since it is not observed with captopril and nifedipine.	Captopril	141-150	heme oxygenase 1	Homo sapiens	35-39
15010533-7	2004	Inhibition of the Fenton reaction by the.OH scavenger DHR attenuated HIF-prolyl hydroxylase activity and interaction with von Hippel-Lindau protein, leading to enhanced HIF-1alpha levels, HIF-1alpha transactivation, and activated expression of the HIF-1 target genes plasminogen activator inhibitor 1 and heme oxygenase 1.	dhr	54-57	heme oxygenase 1	Homo sapiens	305-321
14998722-0	2004	Thiol antioxidant and thiol-reducing agents attenuate 15-deoxy-delta 12,14-prostaglandin J2-induced heme oxygenase-1 expression.	Sulfhydryl Compounds	0-5	heme oxygenase 1	Homo sapiens	100-116
14998722-0	2004	Thiol antioxidant and thiol-reducing agents attenuate 15-deoxy-delta 12,14-prostaglandin J2-induced heme oxygenase-1 expression.	Sulfhydryl Compounds	22-27	heme oxygenase 1	Homo sapiens	100-116
14998722-0	2004	Thiol antioxidant and thiol-reducing agents attenuate 15-deoxy-delta 12,14-prostaglandin J2-induced heme oxygenase-1 expression.	15-deoxy-delta(12,14)-prostaglandin J2	54-91	heme oxygenase 1	Homo sapiens	100-116
14998722-2	2004	Herein we examined how various eicosanoids affect the induction of HO-1, and the possible mechanism underlying 15-deoxy-Delta(12,14)- prostaglandin J(2) (15d-PGJ(2))-induced HO-1 expression.	Eicosanoids	31-42	heme oxygenase 1	Homo sapiens	67-71
14998722-2	2004	Herein we examined how various eicosanoids affect the induction of HO-1, and the possible mechanism underlying 15-deoxy-Delta(12,14)- prostaglandin J(2) (15d-PGJ(2))-induced HO-1 expression.	15-deoxy-delta	111-125	heme oxygenase 1	Homo sapiens	174-178
14998722-2	2004	Herein we examined how various eicosanoids affect the induction of HO-1, and the possible mechanism underlying 15-deoxy-Delta(12,14)- prostaglandin J(2) (15d-PGJ(2))-induced HO-1 expression.	prostaglandin j	134-149	heme oxygenase 1	Homo sapiens	174-178
14998722-3	2004	PGH(2), PGD(2) and its metabolites of the PGJ(2) series, and PGA(1) markedly induced the protein expression of HO-1.	GH2 protein, human	0-3	heme oxygenase 1	Homo sapiens	111-115
14998722-3	2004	PGH(2), PGD(2) and its metabolites of the PGJ(2) series, and PGA(1) markedly induced the protein expression of HO-1.	Prostaglandins D	8-11	heme oxygenase 1	Homo sapiens	111-115
14998722-3	2004	PGH(2), PGD(2) and its metabolites of the PGJ(2) series, and PGA(1) markedly induced the protein expression of HO-1.	2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE	42-45	heme oxygenase 1	Homo sapiens	111-115
14998722-3	2004	PGH(2), PGD(2) and its metabolites of the PGJ(2) series, and PGA(1) markedly induced the protein expression of HO-1.	Prostaglandins A	61-64	heme oxygenase 1	Homo sapiens	111-115
14998722-8	2004	15d-PGJ(2) significantly decreased the intracellular level of reduced glutathione; and the thiol antioxidant, N-acetyl-L-cysteine (NAC), and the thiol-reducing agent, dithiothreitol (DTT), inhibited the induction of HO-1 by 15d-PGJ(2).	15d-pgj	0-7	heme oxygenase 1	Homo sapiens	216-220
14998722-9	2004	Finally, NAC and DTT exhibited significant inhibition of HO-1 mRNA and HO-1 promoter reporter activity induced by 15d-PGJ(2).	Dithiothreitol	17-20	heme oxygenase 1	Homo sapiens	57-61
14998722-9	2004	Finally, NAC and DTT exhibited significant inhibition of HO-1 mRNA and HO-1 promoter reporter activity induced by 15d-PGJ(2).	Dithiothreitol	17-20	heme oxygenase 1	Homo sapiens	71-75
14998722-9	2004	Finally, NAC and DTT exhibited significant inhibition of HO-1 mRNA and HO-1 promoter reporter activity induced by 15d-PGJ(2).	15d-pgj	114-121	heme oxygenase 1	Homo sapiens	57-61
14998722-9	2004	Finally, NAC and DTT exhibited significant inhibition of HO-1 mRNA and HO-1 promoter reporter activity induced by 15d-PGJ(2).	15d-pgj	114-121	heme oxygenase 1	Homo sapiens	71-75
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Sulfhydryl Compounds	27-32	heme oxygenase 1	Homo sapiens	93-97
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Sulfhydryl Compounds	27-32	heme oxygenase 1	Homo sapiens	189-193
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	15d-pgj	109-116	heme oxygenase 1	Homo sapiens	93-97
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Sulfhydryl Compounds	143-148	heme oxygenase 1	Homo sapiens	189-193
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Disulfides	149-158	heme oxygenase 1	Homo sapiens	93-97
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Disulfides	149-158	heme oxygenase 1	Homo sapiens	189-193
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Iron	87-91	heme oxygenase 1	Homo sapiens	0-16
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Heme	54-58	heme oxygenase 1	Homo sapiens	0-16
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Heme	54-58	heme oxygenase 1	Homo sapiens	18-22
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	0-16
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	18-22
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	ammonium ferrous sulfate	81-85	heme oxygenase 1	Homo sapiens	0-16
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	ammonium ferrous sulfate	81-85	heme oxygenase 1	Homo sapiens	18-22
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	0-16
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Biliverdine	91-101	heme oxygenase 1	Homo sapiens	18-22
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Bilirubin	132-141	heme oxygenase 1	Homo sapiens	0-16
15004156-1	2004	Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin.	Bilirubin	132-141	heme oxygenase 1	Homo sapiens	18-22
15004156-8	2004	Bilirubin and/or Fe2+ chelation mimicked the effects of HO-1, whereas biliverdin or carbon monoxide did not.	Bilirubin	0-9	heme oxygenase 1	Homo sapiens	56-60
15004156-8	2004	Bilirubin and/or Fe2+ chelation mimicked the effects of HO-1, whereas biliverdin or carbon monoxide did not.	ammonium ferrous sulfate	17-21	heme oxygenase 1	Homo sapiens	56-60
15004156-10	2004	This effect of HO-1 is mediated by bilirubin and/or by a decrease of free intracellular Fe2+ but probably not by biliverdin or carbon monoxide.	Bilirubin	35-44	heme oxygenase 1	Homo sapiens	15-19
15004156-10	2004	This effect of HO-1 is mediated by bilirubin and/or by a decrease of free intracellular Fe2+ but probably not by biliverdin or carbon monoxide.	ammonium ferrous sulfate	88-92	heme oxygenase 1	Homo sapiens	15-19
15028349-3	2004	A dinucleotide repeat in the HO-1 gene promoter shows a length polymorphism that modulates HO-1 gene transcription.	Dinucleoside Phosphates	2-14	heme oxygenase 1	Homo sapiens	29-33
15028349-3	2004	A dinucleotide repeat in the HO-1 gene promoter shows a length polymorphism that modulates HO-1 gene transcription.	Dinucleoside Phosphates	2-14	heme oxygenase 1	Homo sapiens	91-95
15028349-4	2004	Short (&lt;25 guanosine thymidine [GT]) repeats are associated with a 10-fold greater up-regulation of HO-1 than are longer repeats.	guanosine thymidine	14-33	heme oxygenase 1	Homo sapiens	103-107
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Iron	87-91	heme oxygenase 1	Homo sapiens	18-22
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	0-16
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	18-22
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	110-112	heme oxygenase 1	Homo sapiens	0-16
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Carbon Monoxide	110-112	heme oxygenase 1	Homo sapiens	18-22
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Biliverdine	119-129	heme oxygenase 1	Homo sapiens	0-16
14766239-1	2004	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin.	Biliverdine	119-129	heme oxygenase 1	Homo sapiens	18-22
14660625-11	2004	Heme oxygenase-1 expression was increased in rho(0) cells, and a heme oxygenase-1 inhibitor decreased the induction of MnSOD in rho(0) cells and their resistance against ROS donors.	ros	170-173	heme oxygenase 1	Homo sapiens	0-16
15069378-3	2004	The HO enzyme exists in three isophorms: HO-1 is expressed at low levels under physiological conditions, but is induced by numerous factors, including oxidative stress, inflammation, nitric oxide, an elevated level of substrate, and hypoxia.	Nitric Oxide	183-195	heme oxygenase 1	Homo sapiens	41-45
14761930-5	2004	Several stimuli implicated in the pathogenesis of renal injury, such as heme, nitric oxide, growth factors, angiotensin II, cytokines, and nephrotoxins, induce HO-1.	Heme	72-76	heme oxygenase 1	Homo sapiens	160-164
14761930-5	2004	Several stimuli implicated in the pathogenesis of renal injury, such as heme, nitric oxide, growth factors, angiotensin II, cytokines, and nephrotoxins, induce HO-1.	Nitric Oxide	78-90	heme oxygenase 1	Homo sapiens	160-164
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Iron	135-139	heme oxygenase 1	Homo sapiens	18-22
15105257-0	2004	Heme oxygenase-1: transducer of pathological brain iron sequestration under oxidative stress.	Iron	51-55	heme oxygenase 1	Homo sapiens	0-16
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Heme	65-69	heme oxygenase 1	Homo sapiens	0-16
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Heme	65-69	heme oxygenase 1	Homo sapiens	18-22
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Biliverdine	73-83	heme oxygenase 1	Homo sapiens	0-16
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Biliverdine	73-83	heme oxygenase 1	Homo sapiens	18-22
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Iron	90-94	heme oxygenase 1	Homo sapiens	0-16
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Iron	90-94	heme oxygenase 1	Homo sapiens	18-22
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Carbon Monoxide	100-115	heme oxygenase 1	Homo sapiens	0-16
15105257-2	2004	Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide.	Carbon Monoxide	100-115	heme oxygenase 1	Homo sapiens	18-22
15105257-4	2004	A model is presented implicating glial HO-1 induction as a "final common pathway" leading to pathological iron sequestration and mitochondrial insufficiency in a host of human CNS disorders.	Iron	106-110	heme oxygenase 1	Homo sapiens	39-43
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Heme	85-89	heme oxygenase 1	Homo sapiens	0-16
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Heme	85-89	heme oxygenase 1	Homo sapiens	18-22
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Biliverdine	98-108	heme oxygenase 1	Homo sapiens	0-16
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Biliverdine	98-108	heme oxygenase 1	Homo sapiens	18-22
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	0-16
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	18-22
14735461-1	2004	Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo.	Iron	135-139	heme oxygenase 1	Homo sapiens	0-16
14660625-11	2004	Heme oxygenase-1 expression was increased in rho(0) cells, and a heme oxygenase-1 inhibitor decreased the induction of MnSOD in rho(0) cells and their resistance against ROS donors.	ros	170-173	heme oxygenase 1	Homo sapiens	65-81
14733911-0	2004	Antioxidant action of L-alanine: heme oxygenase-1 and ferritin as possible mediators.	Alanine	22-31	heme oxygenase 1	Homo sapiens	33-49
15084931-2	2004	Inducibility of this enzyme is modulated by a (GT)n dinucleotide length polymorphism in the HO-1 gene promoter.	Dinucleoside Phosphates	52-64	heme oxygenase 1	Homo sapiens	92-96
14733911-5	2004	A protective effect similar to L-alanine was observed when preincubating the cells with iron-free apoferritin or the antioxidant HO-1 product, bilirubin.	Bilirubin	143-152	heme oxygenase 1	Homo sapiens	129-133
14733911-6	2004	The present study demonstrates that L-alanine stimulates expression of the antioxidant defense proteins HO-1 and ferritin in endothelial cells.	Alanine	36-45	heme oxygenase 1	Homo sapiens	104-121
14715242-9	2004	We conclude that induction of HO-1 by 15d-PGJ(2) results in augmentation of VEGF synthesis in normoxia.	15d-pgj	38-45	heme oxygenase 1	Homo sapiens	30-34
14525760-9	2004	Furthermore, in the LPS-induced model of inflammatory angiogenesis, induction of HO-1 with cobalt protoporphyrin significantly inhibited leukocyte invasion into LPS-conditioned Matrigel and thus prevented the subsequent angiogenesis.	cobaltiprotoporphyrin	91-112	heme oxygenase 1	Homo sapiens	81-85
14968347-7	2004	Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells.	pentrinitrol	14-20	heme oxygenase 1	Homo sapiens	56-60
14968347-7	2004	Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells.	pentrinitrol	14-20	heme oxygenase 1	Homo sapiens	90-94
14968347-7	2004	Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells.	Bilirubin	107-116	heme oxygenase 1	Homo sapiens	56-60
14968347-7	2004	Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells.	Bilirubin	107-116	heme oxygenase 1	Homo sapiens	90-94
14968347-7	2004	Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells.	Carbon Monoxide	132-147	heme oxygenase 1	Homo sapiens	56-60
14968347-8	2004	HO-1 induction subsequently led to a marked increase in protein expression of a second antioxidant protein, ferritin, via the HO-1-dependent release of free iron from endogenous heme sources (Figures 1 and 5).	Iron	157-161	heme oxygenase 1	Homo sapiens	0-4
14968347-8	2004	HO-1 induction subsequently led to a marked increase in protein expression of a second antioxidant protein, ferritin, via the HO-1-dependent release of free iron from endogenous heme sources (Figures 1 and 5).	Iron	157-161	heme oxygenase 1	Homo sapiens	126-130
14968347-8	2004	HO-1 induction subsequently led to a marked increase in protein expression of a second antioxidant protein, ferritin, via the HO-1-dependent release of free iron from endogenous heme sources (Figures 1 and 5).	Heme	178-182	heme oxygenase 1	Homo sapiens	0-4
14968347-8	2004	HO-1 induction subsequently led to a marked increase in protein expression of a second antioxidant protein, ferritin, via the HO-1-dependent release of free iron from endogenous heme sources (Figures 1 and 5).	Heme	178-182	heme oxygenase 1	Homo sapiens	126-130
14968347-19	2004	Thus, the ability to activate HO-1 induction and associated antioxidant pathways apparently distinguishes PETN from other long-acting nitrates and may explain their different patterns of action in vivo (Figure 9).	Pentaerythritol Tetranitrate	106-110	heme oxygenase 1	Homo sapiens	30-34
14968347-19	2004	Thus, the ability to activate HO-1 induction and associated antioxidant pathways apparently distinguishes PETN from other long-acting nitrates and may explain their different patterns of action in vivo (Figure 9).	Nitrates	134-142	heme oxygenase 1	Homo sapiens	30-34
14707100-2	2004	We have recently shown that carbon monoxide (CO), an enzymatic product of heme oxygenase-1 (HO-1), confers potent antiproliferative effects in airway and vascular smooth muscle cells.	Carbon Monoxide	28-43	heme oxygenase 1	Homo sapiens	74-90
14707100-2	2004	We have recently shown that carbon monoxide (CO), an enzymatic product of heme oxygenase-1 (HO-1), confers potent antiproliferative effects in airway and vascular smooth muscle cells.	Carbon Monoxide	45-47	heme oxygenase 1	Homo sapiens	74-90
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Heme	100-104	heme oxygenase 1	Homo sapiens	14-30
14647439-4	2004	The cells were treated with hemin and cadmium to induce HO-1.	Hemin	28-33	heme oxygenase 1	Homo sapiens	56-60
14647439-4	2004	The cells were treated with hemin and cadmium to induce HO-1.	Cadmium	38-45	heme oxygenase 1	Homo sapiens	56-60
14647439-5	2004	The result showed that HO-1 protein was significantly induced by hemin and cadmium in both cells tested.	Hemin	65-70	heme oxygenase 1	Homo sapiens	23-27
14647439-5	2004	The result showed that HO-1 protein was significantly induced by hemin and cadmium in both cells tested.	Cadmium	75-82	heme oxygenase 1	Homo sapiens	23-27
14647439-8	2004	The levels of HO-1 and p21 induced were significantly inhibited by p38 mitogen-activated protein kinase (p38 MAPK) inhibitor (SB203580) and extracellular-regulated kinase (ERK) inhibitor (PD098059).	SB 203580	126-134	heme oxygenase 1	Homo sapiens	14-18
14647439-8	2004	The levels of HO-1 and p21 induced were significantly inhibited by p38 mitogen-activated protein kinase (p38 MAPK) inhibitor (SB203580) and extracellular-regulated kinase (ERK) inhibitor (PD098059).	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	188-196	heme oxygenase 1	Homo sapiens	14-18
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Heme	100-104	heme oxygenase 1	Homo sapiens	32-36
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Biliverdine	110-123	heme oxygenase 1	Homo sapiens	14-30
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Biliverdine	110-123	heme oxygenase 1	Homo sapiens	32-36
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	14-30
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	32-36
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Iron	159-163	heme oxygenase 1	Homo sapiens	14-30
14960194-1	2004	INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron.	Iron	159-163	heme oxygenase 1	Homo sapiens	32-36
14960194-4	2004	RESULTS: HO-1 induction with cobalt protoporphorin (Co-PP) dose-dependently protected against apoptotic cell death as well as neutrophil-mediated oncosis in the galactosamine/endotoxin (Gal/ET) shock model.	cobalt protoporphorin	29-50	heme oxygenase 1	Homo sapiens	9-13
14960194-4	2004	RESULTS: HO-1 induction with cobalt protoporphorin (Co-PP) dose-dependently protected against apoptotic cell death as well as neutrophil-mediated oncosis in the galactosamine/endotoxin (Gal/ET) shock model.	co-pp	52-57	heme oxygenase 1	Homo sapiens	9-13
14960194-4	2004	RESULTS: HO-1 induction with cobalt protoporphorin (Co-PP) dose-dependently protected against apoptotic cell death as well as neutrophil-mediated oncosis in the galactosamine/endotoxin (Gal/ET) shock model.	Galactosamine	161-174	heme oxygenase 1	Homo sapiens	9-13
14960194-5	2004	Induction of HO-1 with Co-PP dose-dependently protected against neutrophil-mediated oncosis as indicated by attenuated ALT release and TNF-mediated apoptotic cell death as indicated by reduced caspase-3 activation.	co-pp	23-28	heme oxygenase 1	Homo sapiens	13-17
14683741-11	2004	These findings suggest the genetic contribution to stent restenosis and support the notion that the long dinucleotide GT repeat in promotor region may interfere with HO-1 gene transcription, leading to decreased vascular protection upon injury.	Dinucleoside Phosphates	105-117	heme oxygenase 1	Homo sapiens	166-170
15777021-6	2004	The existence of a constitutive haem oxygenase (HO-2), mainly present in the vasculature and nervous system, and an inducible haem oxygenase (HO-1), which is highly expressed during stress conditions in all tissues, also suggests that cells have evolved a fine control of this enzymic pathway to ultimately regulate haem consumption and to ensure production of CO, biliverdin/bilirubin and iron during physiological and pathophysiological situations.	Carbon Monoxide	361-363	heme oxygenase 1	Homo sapiens	142-146
15777021-6	2004	The existence of a constitutive haem oxygenase (HO-2), mainly present in the vasculature and nervous system, and an inducible haem oxygenase (HO-1), which is highly expressed during stress conditions in all tissues, also suggests that cells have evolved a fine control of this enzymic pathway to ultimately regulate haem consumption and to ensure production of CO, biliverdin/bilirubin and iron during physiological and pathophysiological situations.	Biliverdine	365-375	heme oxygenase 1	Homo sapiens	142-146
15777021-6	2004	The existence of a constitutive haem oxygenase (HO-2), mainly present in the vasculature and nervous system, and an inducible haem oxygenase (HO-1), which is highly expressed during stress conditions in all tissues, also suggests that cells have evolved a fine control of this enzymic pathway to ultimately regulate haem consumption and to ensure production of CO, biliverdin/bilirubin and iron during physiological and pathophysiological situations.	Bilirubin	376-385	heme oxygenase 1	Homo sapiens	142-146
15777021-6	2004	The existence of a constitutive haem oxygenase (HO-2), mainly present in the vasculature and nervous system, and an inducible haem oxygenase (HO-1), which is highly expressed during stress conditions in all tissues, also suggests that cells have evolved a fine control of this enzymic pathway to ultimately regulate haem consumption and to ensure production of CO, biliverdin/bilirubin and iron during physiological and pathophysiological situations.	Iron	390-394	heme oxygenase 1	Homo sapiens	142-146
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Heme	59-63	heme oxygenase 1	Homo sapiens	6-22
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Heme	59-63	heme oxygenase 1	Homo sapiens	24-28
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Iron	111-115	heme oxygenase 1	Homo sapiens	6-22
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Iron	111-115	heme oxygenase 1	Homo sapiens	24-28
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Biliverdine	117-127	heme oxygenase 1	Homo sapiens	6-22
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Biliverdine	117-127	heme oxygenase 1	Homo sapiens	24-28
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	133-148	heme oxygenase 1	Homo sapiens	6-22
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	133-148	heme oxygenase 1	Homo sapiens	24-28
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	150-152	heme oxygenase 1	Homo sapiens	6-22
14683741-1	2004	AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO).	Carbon Monoxide	150-152	heme oxygenase 1	Homo sapiens	24-28
14683741-3	2004	A dinucleotide GT repeat in the promotor region of human HO-1 gene shows a length polymorphism that modulates the level of gene transcription.	Dinucleoside Phosphates	2-14	heme oxygenase 1	Homo sapiens	57-61
14523007-0	2003	Oxidized phospholipids induce expression of human heme oxygenase-1 involving activation of cAMP-responsive element-binding protein.	Phospholipids	9-22	heme oxygenase 1	Homo sapiens	50-66
14702110-7	2004	Avicins inhibited epidermal hyperplasia, reduced p53 mutation, enhanced apoptosis, decreased generation of 8-hydroxy-2"-deoxyguanosine, and enhanced expression of NADPH:quinone oxidoreductase 1 and heme oxygenase-1.	avicins	0-7	heme oxygenase 1	Homo sapiens	198-214
15140586-2	2004	A (GT)n dinucleotide repeat polymorphism in the HO-1 promoter has been shown to modulate HO-1 gene expression.	Dinucleoside Phosphates	8-20	heme oxygenase 1	Homo sapiens	48-52
15140586-2	2004	A (GT)n dinucleotide repeat polymorphism in the HO-1 promoter has been shown to modulate HO-1 gene expression.	Dinucleoside Phosphates	8-20	heme oxygenase 1	Homo sapiens	89-93
14691581-0	2004	A microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with increased bilirubin and HDL levels but not with coronary artery disease.	Bilirubin	97-106	heme oxygenase 1	Homo sapiens	37-53
14691581-1	2004	Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous anti-oxidant bilirubin which exerts beneficial effects against arteriosclerosis.	Bilirubin	85-94	heme oxygenase 1	Homo sapiens	0-16
14691581-1	2004	Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous anti-oxidant bilirubin which exerts beneficial effects against arteriosclerosis.	Bilirubin	85-94	heme oxygenase 1	Homo sapiens	18-22
14523007-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, protects against oxidative stress, and shows potent anti-inflammatory effects.	Heme	60-64	heme oxygenase 1	Homo sapiens	0-16
14523007-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, protects against oxidative stress, and shows potent anti-inflammatory effects.	Heme	60-64	heme oxygenase 1	Homo sapiens	18-22
14523007-2	2003	Oxidized phospholipids, which are generated during inflammation and apoptosis, modulate the inflammatory response by inducing the expression of several genes including HO-1.	Phospholipids	9-22	heme oxygenase 1	Homo sapiens	168-172
14523007-3	2003	Here we investigated the signaling pathways and transcriptional events involved in the induction of HO-1 gene expression by oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (OxPAPC) in human umbilical vein endothelial cells.	1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine	133-190	heme oxygenase 1	Homo sapiens	100-104
14523007-3	2003	Here we investigated the signaling pathways and transcriptional events involved in the induction of HO-1 gene expression by oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine (OxPAPC) in human umbilical vein endothelial cells.	oxpapc	192-198	heme oxygenase 1	Homo sapiens	100-104
14523007-7	2003	We identified a cAMP-responsive element and a Maf recognition element to be involved in the transcriptional activation of the HO-1 promoter by OxPAPC.	Cyclic AMP	16-20	heme oxygenase 1	Homo sapiens	126-130
14644359-5	2003	The expression of hsp 32 and hsp70 was studied in human diploid lung fibroblasts (HEL cells) and human monocytic leukaemia cells (THP-1 cells) incubated in vitro with different concentrations of dibenzo[a,l]pyrene (DB[a,l]P), 1-nitropyrene, (NP), 4-aminobiphenyl (ABP), ACN and EOM for different periods of time.	dibenzo(a,l)pyrene	195-213	heme oxygenase 1	Homo sapiens	18-24
14635185-1	2003	The purpose of the present study was to examine the role of human heme oxygenase (human HO-1) in cell cycle progression following exposure to heme or human HO-1 gene transfer and to identify target genes associated with human HO-1-meditated increases in cell cycle progression using cDNA microarray technology.	Heme	66-70	heme oxygenase 1	Homo sapiens	88-92
14635185-1	2003	The purpose of the present study was to examine the role of human heme oxygenase (human HO-1) in cell cycle progression following exposure to heme or human HO-1 gene transfer and to identify target genes associated with human HO-1-meditated increases in cell cycle progression using cDNA microarray technology.	Heme	66-70	heme oxygenase 1	Homo sapiens	156-160
14635185-1	2003	The purpose of the present study was to examine the role of human heme oxygenase (human HO-1) in cell cycle progression following exposure to heme or human HO-1 gene transfer and to identify target genes associated with human HO-1-meditated increases in cell cycle progression using cDNA microarray technology.	Heme	66-70	heme oxygenase 1	Homo sapiens	156-160
14635185-2	2003	Heme-induced robust human HO-1 expression in quiescent human microvessel endothelial cells cultured in 1% FBS and the levels of human HO-1 expression progressively declined without a change in the cell cyclin.	Heme	0-4	heme oxygenase 1	Homo sapiens	26-30
14635185-2	2003	Heme-induced robust human HO-1 expression in quiescent human microvessel endothelial cells cultured in 1% FBS and the levels of human HO-1 expression progressively declined without a change in the cell cyclin.	Heme	0-4	heme oxygenase 1	Homo sapiens	134-138
14637166-0	2003	Gastroprotection by vitamin C--a heme oxygenase-1-dependent mechanism?	Ascorbic Acid	20-29	heme oxygenase 1	Homo sapiens	33-49
14637166-5	2003	HO-1 mRNA was significantly elevated by either ASA or vitamin C in gastric epithelial cells, combination of both substances further increased expression.	Aspirin	47-50	heme oxygenase 1	Homo sapiens	0-4
14637166-5	2003	HO-1 mRNA was significantly elevated by either ASA or vitamin C in gastric epithelial cells, combination of both substances further increased expression.	Ascorbic Acid	54-63	heme oxygenase 1	Homo sapiens	0-4
14637166-6	2003	HO-1 protein and enzyme activity rose in cells exposed to vitamin C alone or combined with ASA, but not after stimulation with ASA alone.	Ascorbic Acid	58-67	heme oxygenase 1	Homo sapiens	0-4
14637166-6	2003	HO-1 protein and enzyme activity rose in cells exposed to vitamin C alone or combined with ASA, but not after stimulation with ASA alone.	Aspirin	91-94	heme oxygenase 1	Homo sapiens	0-4
14637166-6	2003	HO-1 protein and enzyme activity rose in cells exposed to vitamin C alone or combined with ASA, but not after stimulation with ASA alone.	Aspirin	127-130	heme oxygenase 1	Homo sapiens	0-4
14637166-7	2003	In contrast to endothelia, in which ASA simultaneously induces HO-1 mRNA and protein expression, gastric epithelial cells require vitamin C to translate HO-1 mRNA into active protein, which then may exert gastroprotection by its antioxidant and vasodilative properties.	Aspirin	36-39	heme oxygenase 1	Homo sapiens	63-67
14637166-7	2003	In contrast to endothelia, in which ASA simultaneously induces HO-1 mRNA and protein expression, gastric epithelial cells require vitamin C to translate HO-1 mRNA into active protein, which then may exert gastroprotection by its antioxidant and vasodilative properties.	Ascorbic Acid	130-139	heme oxygenase 1	Homo sapiens	153-157
14644359-7	2003	ACN induced the expression of hsp 32 as well as hsp70 in HEL and THP-1 cells, which probably reflects its ability to induce oxidative stress.	Acrylonitrile	0-3	heme oxygenase 1	Homo sapiens	30-36
14615405-6	2003	Preexposure (24 h) in a combination of low O2 and low glucose concentrations decreased the protein content of the HO-1 isoform by 59.6% (P &lt; 0.05), whereas preexposure (24 h) to low glucose concentration alone increased HO-2 content by 28.2% in chorionic villi explants (P &lt; 0.05).	Oxygen	43-45	heme oxygenase 1	Homo sapiens	114-118
14504288-3	2003	The small Maf proteins appear to be critical regulators of heme oxygenase (HO)-1, an anti-oxidant defense enzyme that degrades heme into iron, carbon monoxide, and biliverdin.	Iron	137-141	heme oxygenase 1	Homo sapiens	59-80
14504288-3	2003	The small Maf proteins appear to be critical regulators of heme oxygenase (HO)-1, an anti-oxidant defense enzyme that degrades heme into iron, carbon monoxide, and biliverdin.	Carbon Monoxide	143-158	heme oxygenase 1	Homo sapiens	59-80
14504288-3	2003	The small Maf proteins appear to be critical regulators of heme oxygenase (HO)-1, an anti-oxidant defense enzyme that degrades heme into iron, carbon monoxide, and biliverdin.	Biliverdine	164-174	heme oxygenase 1	Homo sapiens	59-80
14615405-6	2003	Preexposure (24 h) in a combination of low O2 and low glucose concentrations decreased the protein content of the HO-1 isoform by 59.6% (P &lt; 0.05), whereas preexposure (24 h) to low glucose concentration alone increased HO-2 content by 28.2% in chorionic villi explants (P &lt; 0.05).	Glucose	54-61	heme oxygenase 1	Homo sapiens	114-118
14615405-6	2003	Preexposure (24 h) in a combination of low O2 and low glucose concentrations decreased the protein content of the HO-1 isoform by 59.6% (P &lt; 0.05), whereas preexposure (24 h) to low glucose concentration alone increased HO-2 content by 28.2% in chorionic villi explants (P &lt; 0.05).	Glucose	185-192	heme oxygenase 1	Homo sapiens	114-118
14638927-9	2003	Renal function at the first week posttransplantation (analyzed by serum creatinine levels) showed a significant correlation with both HO-1 and VEGF mRNA expression, reinforcing the protective role of both genes in the early events of transplantation.	Creatinine	72-82	heme oxygenase 1	Homo sapiens	134-138
12907459-8	2003	Comparative Northern analyses of iron-related genes after erythrophagocytosis revealed a 16-fold increase in FPN1 levels after 3 hours, a 10-fold increase in heme oxygenase-1 (HO-1) after 3 hours, a 2-fold increase in natural resistance macrophage-associated protein 1 (Nramp1) levels after 6 hours, but no change in divalent metal ion transporter 1 (DMT1) levels.	Iron	33-37	heme oxygenase 1	Homo sapiens	158-174
14522998-9	2003	Heme oxygenase-1 was induced at low extract dose and with minimal decline in the GSH/GSSG ratio, whereas MAP kinase activation required a higher chemical dose and incremental levels of oxidative stress.	Glutathione Disulfide	81-84	heme oxygenase 1	Homo sapiens	0-16
14598260-4	2003	Our aim was to explore the role of the heme oxygenase-1/carbon monoxide pathway in the pathogenesis of experimental hepatopulmonary syndrome.	Carbon Monoxide	56-71	heme oxygenase 1	Homo sapiens	39-55
14562166-1	2003	INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO).	Heme	80-84	heme oxygenase 1	Homo sapiens	44-48
14562166-1	2003	INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO).	Iron	98-102	heme oxygenase 1	Homo sapiens	44-48
14562166-1	2003	INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO).	Carbon Monoxide	107-122	heme oxygenase 1	Homo sapiens	44-48
14624702-1	2003	BACKGROUND: As well as being inducible by haem, haemoxygenase -1 (HO-1) is also induced by interleukin-10 and an anti-inflammatory prostaglandin, 15d PGJ2, the carbon monoxide thus produced mediating the anti-inflammatory effects of these molecules.	Prostaglandins	131-144	heme oxygenase 1	Homo sapiens	48-70
14624702-1	2003	BACKGROUND: As well as being inducible by haem, haemoxygenase -1 (HO-1) is also induced by interleukin-10 and an anti-inflammatory prostaglandin, 15d PGJ2, the carbon monoxide thus produced mediating the anti-inflammatory effects of these molecules.	9-deoxy-delta-9-prostaglandin D2	150-154	heme oxygenase 1	Homo sapiens	48-70
14624702-1	2003	BACKGROUND: As well as being inducible by haem, haemoxygenase -1 (HO-1) is also induced by interleukin-10 and an anti-inflammatory prostaglandin, 15d PGJ2, the carbon monoxide thus produced mediating the anti-inflammatory effects of these molecules.	Carbon Monoxide	160-175	heme oxygenase 1	Homo sapiens	48-70
14562166-1	2003	INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO).	Carbon Monoxide	124-126	heme oxygenase 1	Homo sapiens	44-48
14598260-10	2003	CONCLUSIONS: The heme oxygenase-1/carbon monoxide system is an important contributor to the progression of experimental hepatopulmonary syndrome in addition to alterations in the endothelial nitric oxide synthase/nitric oxide pathway.	Carbon Monoxide	34-49	heme oxygenase 1	Homo sapiens	17-33
14696395-1	2003	BACKGROUND/AIMS: Hemeoxygenase-1 produces carbon monoxide as a byproduct of hemoglobin metabolism.	Carbon Monoxide	42-57	heme oxygenase 1	Homo sapiens	17-32
14614191-6	2003	Heme oxygenase-1 (HO-1) protein level is increased 24 h after HBO exposure and inhibition of HO-1 activity by tin-mesoporphyrin increased HBO genotoxicity.	tin mesoporphyrin	110-127	heme oxygenase 1	Homo sapiens	0-16
12882997-3	2003	Using antisense oligonucleotides, we achieved a block of iNOS protein formation, accompanied by a strong decrease in the expression of the protective stress response genes bcl-2, vascular endothelial growth factor, and heme oxygenase-1 (HO-1).	Oligonucleotides	16-32	heme oxygenase 1	Homo sapiens	219-235
14614191-6	2003	Heme oxygenase-1 (HO-1) protein level is increased 24 h after HBO exposure and inhibition of HO-1 activity by tin-mesoporphyrin increased HBO genotoxicity.	tin mesoporphyrin	110-127	heme oxygenase 1	Homo sapiens	93-97
12969148-6	2003	RESULTS: In HRPTECs, both HO-1 mRNA expression and protein production peaked at around 12 h and persisted until 24 h after hemin stimulation.	Hemin	123-128	heme oxygenase 1	Homo sapiens	26-30
12969148-10	2003	Tin protoporphyrin (SnPP), an inhibitor of HO function, significantly reversed the cytoprotection by HO-1.	tin protoporphyrin IX	0-18	heme oxygenase 1	Homo sapiens	101-105
12969148-10	2003	Tin protoporphyrin (SnPP), an inhibitor of HO function, significantly reversed the cytoprotection by HO-1.	S-Nitroso-N-propionyl-D,L-penicillamine	20-24	heme oxygenase 1	Homo sapiens	101-105
12933701-0	2003	Heme oxygenase-1 attenuates glucose-mediated cell growth arrest and apoptosis in human microvessel endothelial cells.	Glucose	28-35	heme oxygenase 1	Homo sapiens	0-16
12933701-8	2003	These findings identify a novel effect of HO-1 on endothelial cell growth and indicate that heme metabolism and HO-1 expression regulate signaling systems in cells exposed to high glucose, which controls cell-cycle progression.	Glucose	180-187	heme oxygenase 1	Homo sapiens	42-46
12933701-1	2003	Heme oxygenase-1 (HO-1) is a stress protein that has been suggested to participate in defense mechanisms against agents that may induce oxidative injury, such as heme and inflammatory molecules.	Heme	162-166	heme oxygenase 1	Homo sapiens	0-16
12933701-8	2003	These findings identify a novel effect of HO-1 on endothelial cell growth and indicate that heme metabolism and HO-1 expression regulate signaling systems in cells exposed to high glucose, which controls cell-cycle progression.	Glucose	180-187	heme oxygenase 1	Homo sapiens	112-116
12933701-1	2003	Heme oxygenase-1 (HO-1) is a stress protein that has been suggested to participate in defense mechanisms against agents that may induce oxidative injury, such as heme and inflammatory molecules.	Heme	162-166	heme oxygenase 1	Homo sapiens	18-22
12933701-2	2003	Incubation of endothelial cells in a high-glucose (33 mmol/L) medium for 7 days resulted in a decrease of HO activity by 34% and a decrease in HO-1 and HO-2 proteins compared with cells exposed to low glucose (5 mmol/L) (P&lt;0.05) or cells exposed to mannitol (33 mmol/L).	Glucose	42-49	heme oxygenase 1	Homo sapiens	143-156
12933701-3	2003	Overexpression of HO-1 was coupled with an increase in HO activity and carbon monoxide synthesis, decreased cellular heme, and acceleration in all phases of the cell cycle (P&lt;0.001).	Carbon Monoxide	71-86	heme oxygenase 1	Homo sapiens	18-22
12933701-3	2003	Overexpression of HO-1 was coupled with an increase in HO activity and carbon monoxide synthesis, decreased cellular heme, and acceleration in all phases of the cell cycle (P&lt;0.001).	Heme	117-121	heme oxygenase 1	Homo sapiens	18-22
12933701-5	2003	Exposure to high glucose significantly decreased cell-cycle progression in control cells and in cells underexpressing HO-1 but did not decrease cell-cycle progression in cells overexpressing HO-1.	Glucose	17-24	heme oxygenase 1	Homo sapiens	118-122
12933701-7	2003	The addition of tin-mesoporphyrin (SnMP), an inhibitor of HO activity, reversed the HO-1-mediated decrease of p21 and p27 in cells overexpressing HO-1.	tin mesoporphyrin	16-33	heme oxygenase 1	Homo sapiens	84-88
12933701-7	2003	The addition of tin-mesoporphyrin (SnMP), an inhibitor of HO activity, reversed the HO-1-mediated decrease of p21 and p27 in cells overexpressing HO-1.	tin mesoporphyrin	16-33	heme oxygenase 1	Homo sapiens	146-150
12933701-7	2003	The addition of tin-mesoporphyrin (SnMP), an inhibitor of HO activity, reversed the HO-1-mediated decrease of p21 and p27 in cells overexpressing HO-1.	tin mesoporphyrin	35-39	heme oxygenase 1	Homo sapiens	84-88
12933701-7	2003	The addition of tin-mesoporphyrin (SnMP), an inhibitor of HO activity, reversed the HO-1-mediated decrease of p21 and p27 in cells overexpressing HO-1.	tin mesoporphyrin	35-39	heme oxygenase 1	Homo sapiens	146-150
12933701-8	2003	These findings identify a novel effect of HO-1 on endothelial cell growth and indicate that heme metabolism and HO-1 expression regulate signaling systems in cells exposed to high glucose, which controls cell-cycle progression.	Heme	92-96	heme oxygenase 1	Homo sapiens	42-46
12927812-2	2003	In cultured endothelial cells derived from human umbilical vein, aspirin (30-300 microM) increased heme oxygenase-1 (HO-1) protein levels in a concentration-dependent fashion up to fivefold over basal levels.	Aspirin	65-72	heme oxygenase 1	Homo sapiens	99-115
12819228-11	2003	Although the active site residues differ between nm-HO and human HO-1, the close similarity in the H-bonded water network suggests a common mechanism shared by all heme oxygenases.	Water	108-113	heme oxygenase 1	Homo sapiens	65-69
12927811-0	2003	Changes in temperature modulate heme oxygenase-1 induction by curcumin in renal epithelial cells.	Curcumin	62-70	heme oxygenase 1	Homo sapiens	32-48
12927812-2	2003	In cultured endothelial cells derived from human umbilical vein, aspirin (30-300 microM) increased heme oxygenase-1 (HO-1) protein levels in a concentration-dependent fashion up to fivefold over basal levels.	Aspirin	65-72	heme oxygenase 1	Homo sapiens	117-121
12927812-0	2003	Heme oxygenase-1 induction may explain the antioxidant profile of aspirin.	Aspirin	66-73	heme oxygenase 1	Homo sapiens	0-16
12927812-3	2003	HO-1 induction was accompanied by a marked increase in catalytic activity of the enzyme as reflected by enhanced formation of both carbon monoxide and bilirubin.	Carbon Monoxide	131-146	heme oxygenase 1	Homo sapiens	0-4
12927812-3	2003	HO-1 induction was accompanied by a marked increase in catalytic activity of the enzyme as reflected by enhanced formation of both carbon monoxide and bilirubin.	Bilirubin	151-160	heme oxygenase 1	Homo sapiens	0-4
12927812-6	2003	The nitric oxide (NO) synthase blocker L-NAME prevented aspirin-dependent HO-1 induction.	Nitric Oxide	4-16	heme oxygenase 1	Homo sapiens	74-78
12927812-6	2003	The nitric oxide (NO) synthase blocker L-NAME prevented aspirin-dependent HO-1 induction.	NG-Nitroarginine Methyl Ester	39-45	heme oxygenase 1	Homo sapiens	74-78
12927812-6	2003	The nitric oxide (NO) synthase blocker L-NAME prevented aspirin-dependent HO-1 induction.	Aspirin	56-63	heme oxygenase 1	Homo sapiens	74-78
12927812-7	2003	These findings demonstrate that aspirin targets HO-1, presumably via NO-dependent pathways.	Aspirin	32-39	heme oxygenase 1	Homo sapiens	48-52
12927812-8	2003	Induction of HO-1 expression and activity may be a novel mechanism by which aspirin prevents cellular injury under inflammatory conditions and in cardiovascular disease.	Aspirin	76-83	heme oxygenase 1	Homo sapiens	13-17
12927819-6	2003	Inhibition of HO-1, by Stannis mesoporphyrin (SnMP), potentiated Ang II-mediated DNA damage and generation of 8-epi-isoprostane PGF(2 alpha).	stannis mesoporphyrin	23-44	heme oxygenase 1	Homo sapiens	14-18
12927819-6	2003	Inhibition of HO-1, by Stannis mesoporphyrin (SnMP), potentiated Ang II-mediated DNA damage and generation of 8-epi-isoprostane PGF(2 alpha).	tin mesoporphyrin	46-50	heme oxygenase 1	Homo sapiens	14-18
12927819-6	2003	Inhibition of HO-1, by Stannis mesoporphyrin (SnMP), potentiated Ang II-mediated DNA damage and generation of 8-epi-isoprostane PGF(2 alpha).	8-epi-isoprostane	110-127	heme oxygenase 1	Homo sapiens	14-18
12783778-0	2003	An internal enhancer regulates heme- and cadmium-mediated induction of human heme oxygenase-1.	Heme	31-35	heme oxygenase 1	Homo sapiens	77-93
12783778-0	2003	An internal enhancer regulates heme- and cadmium-mediated induction of human heme oxygenase-1.	Cadmium	41-48	heme oxygenase 1	Homo sapiens	77-93
12927819-6	2003	Inhibition of HO-1, by Stannis mesoporphyrin (SnMP), potentiated Ang II-mediated DNA damage and generation of 8-epi-isoprostane PGF(2 alpha).	Prostaglandins F	128-131	heme oxygenase 1	Homo sapiens	14-18
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Heme	60-64	heme oxygenase 1	Homo sapiens	0-16
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Heme	60-64	heme oxygenase 1	Homo sapiens	18-22
12927819-9	2003	Upregulation of HO-1 ensures the generation of bilirubin and carbon monoxide (CO) in G(0)/G(1) phase to counteract Ang II-mediated oxidative DNA damage.	Bilirubin	47-56	heme oxygenase 1	Homo sapiens	16-20
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Iron	88-92	heme oxygenase 1	Homo sapiens	0-16
12927819-9	2003	Upregulation of HO-1 ensures the generation of bilirubin and carbon monoxide (CO) in G(0)/G(1) phase to counteract Ang II-mediated oxidative DNA damage.	Carbon Monoxide	61-76	heme oxygenase 1	Homo sapiens	16-20
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Iron	88-92	heme oxygenase 1	Homo sapiens	18-22
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	0-16
12927819-9	2003	Upregulation of HO-1 ensures the generation of bilirubin and carbon monoxide (CO) in G(0)/G(1) phase to counteract Ang II-mediated oxidative DNA damage.	Carbon Monoxide	78-80	heme oxygenase 1	Homo sapiens	16-20
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	18-22
12927819-10	2003	Inducibility of HO-1 in G(0)/G(1) phase is essential and probably regulated by a complex system involving oxygen species to assure controlled cell growth.	Oxygen	106-112	heme oxygenase 1	Homo sapiens	16-20
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	0-16
12783778-1	2003	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	18-22
12941774-4	2003	Both basal HSP72 (r = 0.75, P &lt; 0.001) and HO-1 (r = 0.50, P &lt; 0.05) mRNA expression correlated with the glucose infusion rate during the clamp.	Glucose	111-118	heme oxygenase 1	Homo sapiens	46-50
12783778-3	2003	The purpose of this study was to characterize the regulation of the human HO-1 gene in renal proximal tubule and aortic endothelial cells in response to heme and cadmium.	Heme	153-157	heme oxygenase 1	Homo sapiens	74-78
12783778-3	2003	The purpose of this study was to characterize the regulation of the human HO-1 gene in renal proximal tubule and aortic endothelial cells in response to heme and cadmium.	Cadmium	162-169	heme oxygenase 1	Homo sapiens	74-78
12783778-4	2003	Evaluation of multiple human HO-1 promoter-reporter constructs up to -9.1 kb demonstrated only a partial response to heme and cadmium.	Heme	117-121	heme oxygenase 1	Homo sapiens	29-33
12783778-4	2003	Evaluation of multiple human HO-1 promoter-reporter constructs up to -9.1 kb demonstrated only a partial response to heme and cadmium.	Cadmium	126-133	heme oxygenase 1	Homo sapiens	29-33
12783778-7	2003	Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene.	Heme	131-135	heme oxygenase 1	Homo sapiens	62-66
12783778-7	2003	Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene.	Heme	131-135	heme oxygenase 1	Homo sapiens	102-106
12783778-7	2003	Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene.	Heme	131-135	heme oxygenase 1	Homo sapiens	102-106
12783778-7	2003	Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene.	Cadmium	141-148	heme oxygenase 1	Homo sapiens	62-66
12783778-7	2003	Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene.	Cadmium	141-148	heme oxygenase 1	Homo sapiens	102-106
12783778-7	2003	Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene.	Cadmium	141-148	heme oxygenase 1	Homo sapiens	102-106
12925221-5	2003	Lomefloxacin also triggered various stress responses: heme-oxygenase-1 expression in fibroblasts, changes in p53 status as shown by the accumulation of p53 and p21 proteins or the induction of MDM2 and GADD45 genes, and stimulation of melanogenesis by increasing the tyrosinase activity in melanocytes.	lomefloxacin	0-12	heme oxygenase 1	Homo sapiens	54-70
12958189-2	2003	HO-1 cleaves the heme porphyrin ring releasing Fe2+, which induces the expression of the Fe2+ sequestering protein ferritin.	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4
12958189-2	2003	HO-1 cleaves the heme porphyrin ring releasing Fe2+, which induces the expression of the Fe2+ sequestering protein ferritin.	ammonium ferrous sulfate	47-51	heme oxygenase 1	Homo sapiens	0-4
12958189-2	2003	HO-1 cleaves the heme porphyrin ring releasing Fe2+, which induces the expression of the Fe2+ sequestering protein ferritin.	ammonium ferrous sulfate	89-93	heme oxygenase 1	Homo sapiens	0-4
12878207-1	2003	Vascular endothelial cells respond to nitric oxide by activating MAPK pathways and upregulating stress-activated proteins such as gamma-glutamylcysteine synthetase (gamma-GCS) and heme oxygenase-1 (HO-1).	Nitric Oxide	38-50	heme oxygenase 1	Homo sapiens	180-196
12777398-8	2003	Increasing oxidative stress by the addition of arachidonic acid or depletion of glutathione further increased HO-1 induction.	Arachidonic Acid	47-63	heme oxygenase 1	Homo sapiens	110-114
12777398-8	2003	Increasing oxidative stress by the addition of arachidonic acid or depletion of glutathione further increased HO-1 induction.	Glutathione	80-91	heme oxygenase 1	Homo sapiens	110-114
12878207-1	2003	Vascular endothelial cells respond to nitric oxide by activating MAPK pathways and upregulating stress-activated proteins such as gamma-glutamylcysteine synthetase (gamma-GCS) and heme oxygenase-1 (HO-1).	Nitric Oxide	38-50	heme oxygenase 1	Homo sapiens	198-202
12777398-10	2003	PD98059, a specific inhibitor of ERK MAPK, blocked the activity of a HO-1 reporter in E47 cells but not in C34 cells.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	0-7	heme oxygenase 1	Homo sapiens	69-73
12878207-7	2003	Pretreatment with N-acetylcysteine, PD 98059, and SB 203580 decreased HO-1 upregulation in spermine NONOate-treated cells.	Acetylcysteine	18-34	heme oxygenase 1	Homo sapiens	70-74
12878207-7	2003	Pretreatment with N-acetylcysteine, PD 98059, and SB 203580 decreased HO-1 upregulation in spermine NONOate-treated cells.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	36-44	heme oxygenase 1	Homo sapiens	70-74
12878207-7	2003	Pretreatment with N-acetylcysteine, PD 98059, and SB 203580 decreased HO-1 upregulation in spermine NONOate-treated cells.	SB 203580	50-59	heme oxygenase 1	Homo sapiens	70-74
12878207-7	2003	Pretreatment with N-acetylcysteine, PD 98059, and SB 203580 decreased HO-1 upregulation in spermine NONOate-treated cells.	spermine nitric oxide complex	91-107	heme oxygenase 1	Homo sapiens	70-74
12700136-6	2003	Induction of HO-1 gene expression by phorone, a glutathione depletor, and 4-hydroxy-2,3-nonenal (4-HNE), an end product of lipid peroxidation, was suppressed by a specific PKC inhibitor, Ro-31-8220, at concentrations that inhibit all isoforms in WI-38 cells.	phorone	37-44	heme oxygenase 1	Homo sapiens	13-17
12700136-6	2003	Induction of HO-1 gene expression by phorone, a glutathione depletor, and 4-hydroxy-2,3-nonenal (4-HNE), an end product of lipid peroxidation, was suppressed by a specific PKC inhibitor, Ro-31-8220, at concentrations that inhibit all isoforms in WI-38 cells.	Glutathione	48-59	heme oxygenase 1	Homo sapiens	13-17
12700136-6	2003	Induction of HO-1 gene expression by phorone, a glutathione depletor, and 4-hydroxy-2,3-nonenal (4-HNE), an end product of lipid peroxidation, was suppressed by a specific PKC inhibitor, Ro-31-8220, at concentrations that inhibit all isoforms in WI-38 cells.	4-hydroxy-2-nonenal	97-102	heme oxygenase 1	Homo sapiens	13-17
13678532-0	2003	Induction of heme oxygenase-1 in monocytes suppresses angiotensin II-elicited chemotactic activity through inhibition of CCR2: role of bilirubin and carbon monoxide generated by the enzyme.	Bilirubin	135-144	heme oxygenase 1	Homo sapiens	13-29
13678532-0	2003	Induction of heme oxygenase-1 in monocytes suppresses angiotensin II-elicited chemotactic activity through inhibition of CCR2: role of bilirubin and carbon monoxide generated by the enzyme.	Carbon Monoxide	149-164	heme oxygenase 1	Homo sapiens	13-29
13678532-2	2003	Heme oxygenase (HO) is a microsomal enzyme that catalyzes the degradation of heme into biliverdin, which is subsequently reduced to bilirubin, free iron, and carbon monoxide, and induction of HO-1 is potentially associated with cellular protection, especially against oxidative insults.	Heme	77-81	heme oxygenase 1	Homo sapiens	192-196
13678532-2	2003	Heme oxygenase (HO) is a microsomal enzyme that catalyzes the degradation of heme into biliverdin, which is subsequently reduced to bilirubin, free iron, and carbon monoxide, and induction of HO-1 is potentially associated with cellular protection, especially against oxidative insults.	Biliverdine	87-97	heme oxygenase 1	Homo sapiens	192-196
12872043-11	2003	As carbon monoxide, which is one of the products of HO-1, can attenuate nitric oxide-induced vasodilatation, a high expression of HO-1 may cause hypertension, especially in women.	Carbon Monoxide	3-18	heme oxygenase 1	Homo sapiens	52-56
13678532-2	2003	Heme oxygenase (HO) is a microsomal enzyme that catalyzes the degradation of heme into biliverdin, which is subsequently reduced to bilirubin, free iron, and carbon monoxide, and induction of HO-1 is potentially associated with cellular protection, especially against oxidative insults.	Bilirubin	132-141	heme oxygenase 1	Homo sapiens	192-196
13678532-2	2003	Heme oxygenase (HO) is a microsomal enzyme that catalyzes the degradation of heme into biliverdin, which is subsequently reduced to bilirubin, free iron, and carbon monoxide, and induction of HO-1 is potentially associated with cellular protection, especially against oxidative insults.	Iron	148-152	heme oxygenase 1	Homo sapiens	192-196
13678532-2	2003	Heme oxygenase (HO) is a microsomal enzyme that catalyzes the degradation of heme into biliverdin, which is subsequently reduced to bilirubin, free iron, and carbon monoxide, and induction of HO-1 is potentially associated with cellular protection, especially against oxidative insults.	Carbon Monoxide	158-173	heme oxygenase 1	Homo sapiens	192-196
13678532-6	2003	The induction of HO-1 in monocytes suppresses not only Ang II-stimulated superoxide formation, but also Ang II-enhanced chemotactic activity.	Superoxides	73-83	heme oxygenase 1	Homo sapiens	17-21
13678532-7	2003	Exogenously applied bilirubin and carbon monoxide mimicked the inhibitory effect of HO-1 on the chemotactic response.	Bilirubin	20-29	heme oxygenase 1	Homo sapiens	84-88
13678532-7	2003	Exogenously applied bilirubin and carbon monoxide mimicked the inhibitory effect of HO-1 on the chemotactic response.	Carbon Monoxide	34-49	heme oxygenase 1	Homo sapiens	84-88
12891549-3	2003	The aim of the present study was to investigate the role of a stress-inducible protein, heme oxygenase-1 (HO-1), in the action of 15-d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	130-139	heme oxygenase 1	Homo sapiens	88-104
12891549-3	2003	The aim of the present study was to investigate the role of a stress-inducible protein, heme oxygenase-1 (HO-1), in the action of 15-d-PGJ2.	15-deoxy-delta(12,14)-prostaglandin J2	130-139	heme oxygenase 1	Homo sapiens	106-110
12891549-8	2003	HO-1 messenger RNA (mRNA) and protein also were detected in cultured human hepatic myofibroblasts and increased in response to 15-d-PGJ2 in a time- and dose-dependent manner.	15-deoxy-delta(12,14)-prostaglandin J2	127-136	heme oxygenase 1	Homo sapiens	0-4
12891549-9	2003	Induction of HO-1 in human hepatic myofibroblasts mediated 2 major antifibrogenic properties of 15-d-PGJ2, namely, inhibition of proliferation and of procollagen I mRNA expression.	15-deoxy-delta(12,14)-prostaglandin J2	96-105	heme oxygenase 1	Homo sapiens	13-17
12891549-10	2003	These effects were ascribed to bilirubin, one of the products of HO-1-mediated heme degradation.	Bilirubin	31-40	heme oxygenase 1	Homo sapiens	65-69
12891549-10	2003	These effects were ascribed to bilirubin, one of the products of HO-1-mediated heme degradation.	Heme	79-83	heme oxygenase 1	Homo sapiens	65-69
12805077-1	2003	OBJECTIVE: Several proatherogenic agents including oxidized LDL and its major component, 13-hydroperoxyoctadecadienoic acid (13-HPODE), upregulate heme oxygenase-1 (HO-1).	13-Hydroperoxyoctadecadienoic acid	89-123	heme oxygenase 1	Homo sapiens	147-163
12805077-1	2003	OBJECTIVE: Several proatherogenic agents including oxidized LDL and its major component, 13-hydroperoxyoctadecadienoic acid (13-HPODE), upregulate heme oxygenase-1 (HO-1).	13-Hydroperoxyoctadecadienoic acid	89-123	heme oxygenase 1	Homo sapiens	165-169
12805077-5	2003	Antioxidants such as N-acetylcysteine, iron chelation with deferoxamine mesylate, and protein kinase C inhibition with Go6976 blocked HO-1 induction.	Go 6976	119-125	heme oxygenase 1	Homo sapiens	134-138
12872043-11	2003	As carbon monoxide, which is one of the products of HO-1, can attenuate nitric oxide-induced vasodilatation, a high expression of HO-1 may cause hypertension, especially in women.	Carbon Monoxide	3-18	heme oxygenase 1	Homo sapiens	130-134
12872043-11	2003	As carbon monoxide, which is one of the products of HO-1, can attenuate nitric oxide-induced vasodilatation, a high expression of HO-1 may cause hypertension, especially in women.	Nitric Oxide	72-84	heme oxygenase 1	Homo sapiens	52-56
12872043-11	2003	As carbon monoxide, which is one of the products of HO-1, can attenuate nitric oxide-induced vasodilatation, a high expression of HO-1 may cause hypertension, especially in women.	Nitric Oxide	72-84	heme oxygenase 1	Homo sapiens	130-134
12909459-0	2003	Heme oxygenase-1: unleashing the protective properties of heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	0-16
12865654-8	2003	Pyrrolidine dithiocarbamate, an inhibitor of nuclear factor kappaB-dependent gene expression, dose dependently decreased HO-1 mRNA transcripts in human mononuclear cells subjected to oxidative stress while slightly increasing HO-1 gene expression in HepG2 cells.	pyrrolidine dithiocarbamic acid	0-27	heme oxygenase 1	Homo sapiens	121-125
12865654-8	2003	Pyrrolidine dithiocarbamate, an inhibitor of nuclear factor kappaB-dependent gene expression, dose dependently decreased HO-1 mRNA transcripts in human mononuclear cells subjected to oxidative stress while slightly increasing HO-1 gene expression in HepG2 cells.	pyrrolidine dithiocarbamic acid	0-27	heme oxygenase 1	Homo sapiens	226-230
12865654-9	2003	In contrast, HO-1 induction upon oxidative stress was attenuated in HepG2 cells by cycloheximide and dexamethasone.	Cycloheximide	83-96	heme oxygenase 1	Homo sapiens	13-17
12865654-9	2003	In contrast, HO-1 induction upon oxidative stress was attenuated in HepG2 cells by cycloheximide and dexamethasone.	Dexamethasone	101-114	heme oxygenase 1	Homo sapiens	13-17
12865654-12	2003	These data suggest a differential regulation of HO-1 gene expression in parenchymal and non-parenchymal human liver cells and may provide a topographic basis for the understanding of the role of the heme oxygenase/carbon monoxide pathway in human liver disease.	Carbon Monoxide	214-229	heme oxygenase 1	Homo sapiens	48-52
12947311-5	2003	METHODS: Human umbilical vein endothelial cells were pretreated with hemin (100 micromol/L) for 5 hours, and the induction of HO-1 was confirmed by Western blot.	Hemin	69-74	heme oxygenase 1	Homo sapiens	126-130
12947311-8	2003	RESULTS: HO-1 protein was increased 3-fold by exposure to hemin under all conditions.	Hemin	58-63	heme oxygenase 1	Homo sapiens	9-13
12947311-11	2003	CONCLUSIONS: The induction of HO-1 by hemin results in inhibition of the proinflammatory response of endothelial cells, as evidenced by the inhibition of IL-8 production without affecting PGI(2) production.	Epoprostenol	188-194	heme oxygenase 1	Homo sapiens	30-34
12909459-1	2003	Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein).	Heme	34-38	heme oxygenase 1	Homo sapiens	0-21
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Heme	0-4	heme oxygenase 1	Homo sapiens	69-85
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Heme	0-4	heme oxygenase 1	Homo sapiens	87-91
12909459-1	2003	Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein).	Carbon Monoxide	60-75	heme oxygenase 1	Homo sapiens	0-21
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Biliverdine	123-133	heme oxygenase 1	Homo sapiens	69-85
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Biliverdine	123-133	heme oxygenase 1	Homo sapiens	87-91
12909459-1	2003	Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein).	Carbon Monoxide	77-79	heme oxygenase 1	Homo sapiens	0-21
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Bilirubin	134-143	heme oxygenase 1	Homo sapiens	69-85
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Bilirubin	134-143	heme oxygenase 1	Homo sapiens	87-91
12909459-1	2003	Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein).	Biliverdine	82-92	heme oxygenase 1	Homo sapiens	0-21
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Carbon Monoxide	145-147	heme oxygenase 1	Homo sapiens	69-85
12909459-1	2003	Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein).	Bilirubin	124-133	heme oxygenase 1	Homo sapiens	0-21
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Carbon Monoxide	145-147	heme oxygenase 1	Homo sapiens	87-91
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Iron	153-157	heme oxygenase 1	Homo sapiens	69-85
12909459-1	2003	Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein).	Iron	144-148	heme oxygenase 1	Homo sapiens	0-21
14580148-2	2003	Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron.	Iron	153-157	heme oxygenase 1	Homo sapiens	87-91
12909459-4	2003	We suggest that the products of HO-1 action could be valuable therapeutic agents and speculate that HO-1 functions as a "therapeutic funnel", mediating the beneficial effects attributed to other molecules, such as interleukin-10 (IL-10), inducible nitric oxide synthase (NOS2; iNOS) and prostaglandins.	Prostaglandins	287-301	heme oxygenase 1	Homo sapiens	32-36
14580148-7	2003	Notably, HO-1 expression is induced by heme in all mammalian cells examined, but is repressed by hypoxia in certain types of cultured human cells.	Heme	39-43	heme oxygenase 1	Homo sapiens	9-13
14580148-8	2003	The recent discovery of Bach1 as a heme-regulated and hypoxia-inducible repressor for transcription of the HO-1 gene has provided a missing link in the feedback control of heme catabolism.	Heme	35-39	heme oxygenase 1	Homo sapiens	107-111
12909459-4	2003	We suggest that the products of HO-1 action could be valuable therapeutic agents and speculate that HO-1 functions as a "therapeutic funnel", mediating the beneficial effects attributed to other molecules, such as interleukin-10 (IL-10), inducible nitric oxide synthase (NOS2; iNOS) and prostaglandins.	Prostaglandins	287-301	heme oxygenase 1	Homo sapiens	100-104
12832044-0	2003	Heme oxygenase-1 induction by endogenous nitric oxide: influence of intracellular glutathione.	Nitric Oxide	41-53	heme oxygenase 1	Homo sapiens	0-16
12832044-0	2003	Heme oxygenase-1 induction by endogenous nitric oxide: influence of intracellular glutathione.	Glutathione	82-93	heme oxygenase 1	Homo sapiens	0-16
12832044-2	2003	Protein levels of oxidative stress-sensitive heme oxygenase-1 (HO-1) were analyzed in the presence or absence of GSH depletion using L-buthionine-[S,R]-sulfoximine and iNOS induction.	L-Buthionine	133-145	heme oxygenase 1	Homo sapiens	45-61
12842469-0	2003	Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications.	Ferric enterobactin ion	26-32	heme oxygenase 1	Homo sapiens	97-113
12842469-0	2003	Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications.	ammonium ferrous sulfate	34-41	heme oxygenase 1	Homo sapiens	97-113
12842469-0	2003	Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications.	ferrous-no	47-57	heme oxygenase 1	Homo sapiens	97-113
12832044-3	2003	While no effect was observed in the presence of iNOS activity alone, a synergistic effect on HO-1 expression was observed in the presence of iNOS expression and GSH depletion.	Glutathione	161-164	heme oxygenase 1	Homo sapiens	93-97
12839943-6	2003	In vitro studies with cultured SW480 cells, which express HO-1, showed that PEG-ZnPP induced oxidative stress, and consequently apoptotic death, of these cells.	peg-znpp	76-84	heme oxygenase 1	Homo sapiens	58-62
12810075-5	2003	In addition, transfection of human Jurkat T cells with HO-1 suppressed the cellular proliferation, and this effect was reversed by zinc protoporphyrin, a specific HO competitive inhibitor.	zinc protoporphyrin	131-150	heme oxygenase 1	Homo sapiens	55-59
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
14592553-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene attenuated heme and Ang II-induced prostaglandin synthesis.	Heme	103-107	heme oxygenase 1	Homo sapiens	16-20
14592553-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene attenuated heme and Ang II-induced prostaglandin synthesis.	Heme	103-107	heme oxygenase 1	Homo sapiens	82-86
14592553-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene attenuated heme and Ang II-induced prostaglandin synthesis.	Prostaglandins	127-140	heme oxygenase 1	Homo sapiens	16-20
14592553-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene attenuated heme and Ang II-induced prostaglandin synthesis.	Prostaglandins	127-140	heme oxygenase 1	Homo sapiens	82-86
12622689-0	2003	Haem and nitric oxide: synergism in the modulation of the endothelial haem oxygenase-1 pathway.	Nitric Oxide	9-21	heme oxygenase 1	Homo sapiens	70-86
12622689-1	2003	NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin.	Iron	116-120	heme oxygenase 1	Homo sapiens	34-50
12622689-1	2003	NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin.	Iron	116-120	heme oxygenase 1	Homo sapiens	52-56
12622689-1	2003	NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin.	Bilirubin	141-150	heme oxygenase 1	Homo sapiens	34-50
12622689-1	2003	NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin.	Bilirubin	141-150	heme oxygenase 1	Homo sapiens	52-56
12622689-5	2003	A role for haem metabolites in modulating HO-1 expression by NO was assessed by exposing cells to SNAP, SNP or DETA/NO in medium derived from cells treated with haemin, which contained increased bilirubin levels.	DEET	111-115	heme oxygenase 1	Homo sapiens	42-46
12622689-5	2003	A role for haem metabolites in modulating HO-1 expression by NO was assessed by exposing cells to SNAP, SNP or DETA/NO in medium derived from cells treated with haemin, which contained increased bilirubin levels.	Hemin	161-167	heme oxygenase 1	Homo sapiens	42-46
12622689-5	2003	A role for haem metabolites in modulating HO-1 expression by NO was assessed by exposing cells to SNAP, SNP or DETA/NO in medium derived from cells treated with haemin, which contained increased bilirubin levels.	Bilirubin	195-204	heme oxygenase 1	Homo sapiens	42-46
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Carbon Monoxide	61-76	heme oxygenase 1	Homo sapiens	0-16
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Carbon Monoxide	61-76	heme oxygenase 1	Homo sapiens	18-22
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Carbon Monoxide	78-80	heme oxygenase 1	Homo sapiens	0-16
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Carbon Monoxide	78-80	heme oxygenase 1	Homo sapiens	18-22
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Iron	83-87	heme oxygenase 1	Homo sapiens	0-16
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Iron	83-87	heme oxygenase 1	Homo sapiens	18-22
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	0-16
12704646-1	2003	Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin.	Biliverdine	93-103	heme oxygenase 1	Homo sapiens	18-22
12704646-3	2003	Although interest in HO-1 originally centered on its heme-degrading function, recent findings indicate that HO-1 exerts other biologically important actions.	Heme	53-57	heme oxygenase 1	Homo sapiens	21-25
12704646-6	2003	Although the mechanisms responsible for the growth promoting properties of HO-1 are not well established, HO-1 can indirectly influence growth by regulating the synthesis of growth factors and by modulating the delivery of oxygen or nutrients to specific target tissues.	Oxygen	223-229	heme oxygenase 1	Homo sapiens	75-79
12704646-6	2003	Although the mechanisms responsible for the growth promoting properties of HO-1 are not well established, HO-1 can indirectly influence growth by regulating the synthesis of growth factors and by modulating the delivery of oxygen or nutrients to specific target tissues.	Oxygen	223-229	heme oxygenase 1	Homo sapiens	106-110
12570874-0	2003	Curcumin activates the haem oxygenase-1 gene via regulation of Nrf2 and the antioxidant-responsive element.	Curcumin	0-8	heme oxygenase 1	Homo sapiens	23-39
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Heme	6-10	heme oxygenase 1	Homo sapiens	24-29
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Biliverdine	108-118	heme oxygenase 1	Homo sapiens	6-22
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Biliverdine	108-118	heme oxygenase 1	Homo sapiens	24-29
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Carbon Monoxide	120-122	heme oxygenase 1	Homo sapiens	6-22
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Carbon Monoxide	120-122	heme oxygenase 1	Homo sapiens	24-29
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Iron	133-137	heme oxygenase 1	Homo sapiens	6-22
12626517-1	2003	Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron.	Iron	133-137	heme oxygenase 1	Homo sapiens	24-29
12626517-3	2003	Earlier kinetic studies suggested that biliverdin reductase facilitates the release of biliverdin from hHO-1 (Liu, Y., and Ortiz de Montellano, P. R. (2000) J. Biol.	Biliverdine	39-49	heme oxygenase 1	Homo sapiens	103-108
12626517-9	2003	Mutation of surface ionic residues shows that hHO-1 residues Lys18, Lys22, Lys179, Arg183, Arg198, Glu19, Glu127, and Glu190 contribute to the binding of cytochrome P450 reductase.	octadeca(lysine)	61-66	heme oxygenase 1	Homo sapiens	46-51
12585963-4	2003	Either N-acetylcysteine, an antioxidant, or deferoxamine, an iron chelator, resulted in a dose-dependent inhibition of HO-1 mRNA and protein induction during glucose deprivation, suggesting a redox- and iron-dependent mechanism.	Iron	203-207	heme oxygenase 1	Homo sapiens	119-123
12585963-5	2003	Inhibitors of electron-transport chain complex III, antimycin A and myxothiazol, the ATP synthase inhibitor oligomycin and ATP depletion with 2-deoxyglucose or glucosamine also blocked HO-1 induction.	myxothiazol	68-79	heme oxygenase 1	Homo sapiens	185-189
12585963-5	2003	Inhibitors of electron-transport chain complex III, antimycin A and myxothiazol, the ATP synthase inhibitor oligomycin and ATP depletion with 2-deoxyglucose or glucosamine also blocked HO-1 induction.	Oligomycins	108-118	heme oxygenase 1	Homo sapiens	185-189
12585963-5	2003	Inhibitors of electron-transport chain complex III, antimycin A and myxothiazol, the ATP synthase inhibitor oligomycin and ATP depletion with 2-deoxyglucose or glucosamine also blocked HO-1 induction.	Deoxyglucose	142-156	heme oxygenase 1	Homo sapiens	185-189
12585963-5	2003	Inhibitors of electron-transport chain complex III, antimycin A and myxothiazol, the ATP synthase inhibitor oligomycin and ATP depletion with 2-deoxyglucose or glucosamine also blocked HO-1 induction.	Glucosamine	160-171	heme oxygenase 1	Homo sapiens	185-189
12585963-6	2003	To address the involvement of ROS further, specifically H(2)O(2), we showed that overexpression of catalase completely blocked HO-1 activation by glucose deprivation.	Reactive Oxygen Species	30-33	heme oxygenase 1	Homo sapiens	127-131
12585963-8	2003	These results demonstrate that activation of the HO-1 gene by glucose deprivation is mediated by a "glucose metabolic response" pathway via generation of ROS and that the pathway requires a functional electron-transport chain.	Glucose	62-69	heme oxygenase 1	Homo sapiens	49-53
12585963-8	2003	These results demonstrate that activation of the HO-1 gene by glucose deprivation is mediated by a "glucose metabolic response" pathway via generation of ROS and that the pathway requires a functional electron-transport chain.	Reactive Oxygen Species	154-157	heme oxygenase 1	Homo sapiens	49-53
12649278-0	2003	Activation of the prolyl hydroxylase oxygen-sensor results in induction of GLUT1, heme oxygenase-1, and nitric-oxide synthase proteins and confers protection from metabolic inhibition to cardiomyocytes.	Oxygen	37-43	heme oxygenase 1	Homo sapiens	82-98
12649278-7	2003	In addition, ethyl-3,4 dihydroxybenzoate, dimethyloxalylglycine, and hypoxia treatments were found to induce protein levels of nitricoxide synthase-2 and heme oxygenase-1, two important cardioregulatory proteins whose expression in response to hypoxic conditions is poorly understood.	ethyl protocatechuate	13-40	heme oxygenase 1	Homo sapiens	139-170
12649278-7	2003	In addition, ethyl-3,4 dihydroxybenzoate, dimethyloxalylglycine, and hypoxia treatments were found to induce protein levels of nitricoxide synthase-2 and heme oxygenase-1, two important cardioregulatory proteins whose expression in response to hypoxic conditions is poorly understood.	oxalylglycine	42-63	heme oxygenase 1	Homo sapiens	139-170
12853318-10	2003	Using primary neuronal cultures, resveratrol was able to significantly induce heme oxygenase 1, whereas vehicle control showed no effect.	Resveratrol	33-44	heme oxygenase 1	Homo sapiens	78-94
12570874-7	2003	From several lines of investigation we also report that curcumin (and, by inference, CAPE) stimulates ho-1 gene activity by promoting inactivation of the Nrf2-Keap1 complex, leading to increased Nrf2 binding to the resident ho-1 AREs.	Curcumin	56-64	heme oxygenase 1	Homo sapiens	224-228
12570874-8	2003	Moreover, using antibodies and specific inhibitors of the mitogen-activated protein kinase (MAPK) pathways, we provide data implicating p38 MAPK in curcumin-mediated ho-1 induction.	Curcumin	148-156	heme oxygenase 1	Homo sapiens	166-170
12570874-9	2003	Taken together, these results demonstrate that induction of HO-1 by curcumin and CAPE requires the activation of the Nrf2/ARE pathway.	Curcumin	68-76	heme oxygenase 1	Homo sapiens	60-64
12570874-9	2003	Taken together, these results demonstrate that induction of HO-1 by curcumin and CAPE requires the activation of the Nrf2/ARE pathway.	caffeic acid phenethyl ester	81-85	heme oxygenase 1	Homo sapiens	60-64
12585963-0	2003	Haem oxygenase 1 gene induction by glucose deprivation is mediated by reactive oxygen species via the mitochondrial electron-transport chain.	Reactive Oxygen Species	70-93	heme oxygenase 1	Homo sapiens	0-16
12585963-2	2003	One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin.	Iron	145-149	heme oxygenase 1	Homo sapiens	49-65
12585963-2	2003	One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin.	Iron	145-149	heme oxygenase 1	Homo sapiens	67-71
12585963-2	2003	One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin.	Carbon Monoxide	151-153	heme oxygenase 1	Homo sapiens	49-65
12585963-2	2003	One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin.	Carbon Monoxide	151-153	heme oxygenase 1	Homo sapiens	67-71
12585963-2	2003	One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin.	Biliverdine	158-168	heme oxygenase 1	Homo sapiens	49-65
12585963-2	2003	One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin.	Biliverdine	158-168	heme oxygenase 1	Homo sapiens	67-71
12585963-3	2003	The present study evaluated the role of ROS and the mitochondrial electron-transport chain in the induction of HO-1 by glucose deprivation in HepG2 hepatoma cells.	Reactive Oxygen Species	40-43	heme oxygenase 1	Homo sapiens	111-115
12585963-4	2003	Either N-acetylcysteine, an antioxidant, or deferoxamine, an iron chelator, resulted in a dose-dependent inhibition of HO-1 mRNA and protein induction during glucose deprivation, suggesting a redox- and iron-dependent mechanism.	Acetylcysteine	7-23	heme oxygenase 1	Homo sapiens	119-123
12585963-4	2003	Either N-acetylcysteine, an antioxidant, or deferoxamine, an iron chelator, resulted in a dose-dependent inhibition of HO-1 mRNA and protein induction during glucose deprivation, suggesting a redox- and iron-dependent mechanism.	Deferoxamine	44-56	heme oxygenase 1	Homo sapiens	119-123
12585963-4	2003	Either N-acetylcysteine, an antioxidant, or deferoxamine, an iron chelator, resulted in a dose-dependent inhibition of HO-1 mRNA and protein induction during glucose deprivation, suggesting a redox- and iron-dependent mechanism.	Iron	61-65	heme oxygenase 1	Homo sapiens	119-123
12570874-4	2003	Recently, the natural antioxidants curcumin and caffeic acid phenethyl ester (CAPE) have been identified as potent inducers of haem oxygenase-1 (HO-1), a redox-sensitive inducible protein that provides protection against various forms of stress.	Curcumin	35-43	heme oxygenase 1	Homo sapiens	127-143
12570874-4	2003	Recently, the natural antioxidants curcumin and caffeic acid phenethyl ester (CAPE) have been identified as potent inducers of haem oxygenase-1 (HO-1), a redox-sensitive inducible protein that provides protection against various forms of stress.	Curcumin	35-43	heme oxygenase 1	Homo sapiens	145-149
12570874-4	2003	Recently, the natural antioxidants curcumin and caffeic acid phenethyl ester (CAPE) have been identified as potent inducers of haem oxygenase-1 (HO-1), a redox-sensitive inducible protein that provides protection against various forms of stress.	caffeic acid phenethyl ester	48-76	heme oxygenase 1	Homo sapiens	127-143
12570874-4	2003	Recently, the natural antioxidants curcumin and caffeic acid phenethyl ester (CAPE) have been identified as potent inducers of haem oxygenase-1 (HO-1), a redox-sensitive inducible protein that provides protection against various forms of stress.	caffeic acid phenethyl ester	48-76	heme oxygenase 1	Homo sapiens	145-149
12570874-4	2003	Recently, the natural antioxidants curcumin and caffeic acid phenethyl ester (CAPE) have been identified as potent inducers of haem oxygenase-1 (HO-1), a redox-sensitive inducible protein that provides protection against various forms of stress.	caffeic acid phenethyl ester	78-82	heme oxygenase 1	Homo sapiens	127-143
12570874-4	2003	Recently, the natural antioxidants curcumin and caffeic acid phenethyl ester (CAPE) have been identified as potent inducers of haem oxygenase-1 (HO-1), a redox-sensitive inducible protein that provides protection against various forms of stress.	caffeic acid phenethyl ester	78-82	heme oxygenase 1	Homo sapiens	145-149
12570874-7	2003	From several lines of investigation we also report that curcumin (and, by inference, CAPE) stimulates ho-1 gene activity by promoting inactivation of the Nrf2-Keap1 complex, leading to increased Nrf2 binding to the resident ho-1 AREs.	Curcumin	56-64	heme oxygenase 1	Homo sapiens	102-106
12709592-9	2003	The effect of a HO-1 enzyme activity inhibitor, tin protoporphyrin (SnPP), on Caco-2 cell proliferation and differentiation was examined.	S-Nitroso-N-propionyl-D,L-penicillamine	68-72	heme oxygenase 1	Homo sapiens	16-20
12770927-12	2003	Furthermore, reducing sugars have been shown to induce oxidative stress, and ribose could be a possible cause for the upregulation of HO-1, which has been implicated in the release of angiogenic factors.	Ribose	77-83	heme oxygenase 1	Homo sapiens	134-138
12709581-6	2003	Elevation of HO-1 protein was accompanied by a marked increase in catalytic activity of the enzyme as reflected by enhanced formation of both carbon monoxide and the endogenous antioxidant, bilirubin.	Carbon Monoxide	142-157	heme oxygenase 1	Homo sapiens	13-17
12709581-6	2003	Elevation of HO-1 protein was accompanied by a marked increase in catalytic activity of the enzyme as reflected by enhanced formation of both carbon monoxide and the endogenous antioxidant, bilirubin.	Bilirubin	190-199	heme oxygenase 1	Homo sapiens	13-17
12800860-1	2003	Haem-oxygenase-1 (HO-1) is an antioxidant stress protein that is mainly induced by reactive oxygen species, inflammatory cytokines and hyperthermia.	Reactive Oxygen Species	83-106	heme oxygenase 1	Homo sapiens	0-16
12709581-10	2003	Increased HO-1 expression and ensuing formation of bilirubin and carbon monoxide may contribute to and explain the specific antioxidant and antiatherogenic actions of PETN.	Carbon Monoxide	65-80	heme oxygenase 1	Homo sapiens	10-14
12709582-0	2003	Influence of heme and heme oxygenase-1 transfection of pulmonary microvascular endothelium on oxidant generation and cGMP.	Cyclic GMP	117-121	heme oxygenase 1	Homo sapiens	22-38
12709582-3	2003	Culture of PMEC with low serum heme decreased cGMP and the detection of peroxide with 10 microM 2",7"-dichlorofluorescin diacetate and increased HO-1 further decreased cGMP without altering the peroxide detection under these conditions.	Heme	31-35	heme oxygenase 1	Homo sapiens	145-149
12709582-3	2003	Culture of PMEC with low serum heme decreased cGMP and the detection of peroxide with 10 microM 2",7"-dichlorofluorescin diacetate and increased HO-1 further decreased cGMP without altering the peroxide detection under these conditions.	Cyclic GMP	168-172	heme oxygenase 1	Homo sapiens	145-149
12709585-2	2003	Although most of the monocyte-derived cytokines exhibit proinflammatory functions in vivo, heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, exerts potent anti-inflammatory effect through production of carbon monoxide and bilirubin.	Heme	91-95	heme oxygenase 1	Homo sapiens	109-113
12709585-2	2003	Although most of the monocyte-derived cytokines exhibit proinflammatory functions in vivo, heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, exerts potent anti-inflammatory effect through production of carbon monoxide and bilirubin.	Carbon Monoxide	213-228	heme oxygenase 1	Homo sapiens	91-107
12709585-2	2003	Although most of the monocyte-derived cytokines exhibit proinflammatory functions in vivo, heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, exerts potent anti-inflammatory effect through production of carbon monoxide and bilirubin.	Carbon Monoxide	213-228	heme oxygenase 1	Homo sapiens	109-113
12709585-2	2003	Although most of the monocyte-derived cytokines exhibit proinflammatory functions in vivo, heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, exerts potent anti-inflammatory effect through production of carbon monoxide and bilirubin.	Bilirubin	233-242	heme oxygenase 1	Homo sapiens	91-107
12709585-2	2003	Although most of the monocyte-derived cytokines exhibit proinflammatory functions in vivo, heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, exerts potent anti-inflammatory effect through production of carbon monoxide and bilirubin.	Bilirubin	233-242	heme oxygenase 1	Homo sapiens	109-113
12709592-8	2003	HO-1 activity was determined by the ability of the enzyme to generate bilirubin from hemin.	Bilirubin	70-79	heme oxygenase 1	Homo sapiens	0-4
12709592-8	2003	HO-1 activity was determined by the ability of the enzyme to generate bilirubin from hemin.	Hemin	85-90	heme oxygenase 1	Homo sapiens	0-4
12709592-9	2003	The effect of a HO-1 enzyme activity inhibitor, tin protoporphyrin (SnPP), on Caco-2 cell proliferation and differentiation was examined.	tin protoporphyrin IX	48-66	heme oxygenase 1	Homo sapiens	16-20
12720199-1	2003	BACKGROUND/PURPOSE: Heme oxygenase (HO-1), an inducible isoform of HO is a regulator of vascular tone and cell proliferation through the production of endogenous carbon monoxide (CO).	Carbon Monoxide	162-177	heme oxygenase 1	Homo sapiens	36-40
12720199-1	2003	BACKGROUND/PURPOSE: Heme oxygenase (HO-1), an inducible isoform of HO is a regulator of vascular tone and cell proliferation through the production of endogenous carbon monoxide (CO).	Carbon Monoxide	179-181	heme oxygenase 1	Homo sapiens	36-40
12720199-10	2003	HO-1 and eNOS immunoreactivity was reduced markedly reduced in the endothelium and arterial wall in the CDH samples compared with normal lung.	CDw17 antigen	104-107	heme oxygenase 1	Homo sapiens	0-4
12709568-2	2003	We examined the effect of delivery of the human HO-1 gene on cellular heme in renal tissue using a retroviral vector.	Heme	70-74	heme oxygenase 1	Homo sapiens	48-52
12709568-9	2003	Compared with nontransduced rats, human HO-1 gene overexpression in transduced rats was associated with a 35% decrease in urinary 20-hydroxyeicosatetraenoic acid, a potent vasoconstrictor and an inhibitor of tubular Na(+) transport, which may be related to the decrease in blood pressure.	20-hydroxy-5,8,11,14-eicosatetraenoic acid	130-161	heme oxygenase 1	Homo sapiens	40-44
12709570-5	2003	This plasmid contains the H-2K(b) promoter, which transcribes the tet transactivator (tTA) and expression of a human HO-1 cDNA is obtained in the absence of tetracycline.	Tetracycline	157-169	heme oxygenase 1	Homo sapiens	117-121
12709571-1	2003	Heme oxygenase-1 (HO-1) is an essential enzyme in heme catabolism and is characterized by its inducibility in response to various environmental factors, including its substrate heme.	Heme	50-54	heme oxygenase 1	Homo sapiens	0-16
12709571-1	2003	Heme oxygenase-1 (HO-1) is an essential enzyme in heme catabolism and is characterized by its inducibility in response to various environmental factors, including its substrate heme.	Heme	50-54	heme oxygenase 1	Homo sapiens	18-22
12709571-4	2003	The downregulation of HO-1 expression may reduce energy expenditure and local production of carbon monoxide, iron, and bilirubin and transiently increase intracellular heme pool.	Carbon Monoxide	92-107	heme oxygenase 1	Homo sapiens	22-26
12709571-4	2003	The downregulation of HO-1 expression may reduce energy expenditure and local production of carbon monoxide, iron, and bilirubin and transiently increase intracellular heme pool.	Iron	109-113	heme oxygenase 1	Homo sapiens	22-26
12709571-4	2003	The downregulation of HO-1 expression may reduce energy expenditure and local production of carbon monoxide, iron, and bilirubin and transiently increase intracellular heme pool.	Bilirubin	119-128	heme oxygenase 1	Homo sapiens	22-26
12709571-4	2003	The downregulation of HO-1 expression may reduce energy expenditure and local production of carbon monoxide, iron, and bilirubin and transiently increase intracellular heme pool.	Heme	168-172	heme oxygenase 1	Homo sapiens	22-26
12800860-1	2003	Haem-oxygenase-1 (HO-1) is an antioxidant stress protein that is mainly induced by reactive oxygen species, inflammatory cytokines and hyperthermia.	Reactive Oxygen Species	83-106	heme oxygenase 1	Homo sapiens	18-22
12678694-6	2003	HO1-mediated metabolism of heme groups released from NO-damaged proteins leads to a change in the levels of redox-active iron and a release of carbon monoxide (CO) and bilirubin, all of which have been implicated in cellular resistance to oxidative stress.	Heme	27-31	heme oxygenase 1	Homo sapiens	0-3
12578834-0	2003	Nerve growth factor protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner.	Oxidopamine	37-54	heme oxygenase 1	Homo sapiens	108-124
12578834-4	2003	The effect of NGF was mimicked by induction of HO-1 expression with CoCl(2); by treatment with bilirubin, an end product of heme catabolism; and by infection with a retroviral expression vector for human HO-1.	cocl(	68-73	heme oxygenase 1	Homo sapiens	47-51
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	Reactive Oxygen Species	37-40	heme oxygenase 1	Homo sapiens	17-21
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	Reactive Oxygen Species	37-40	heme oxygenase 1	Homo sapiens	120-124
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	tin protoporphyrin IX	135-153	heme oxygenase 1	Homo sapiens	17-21
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	tin protoporphyrin IX	135-153	heme oxygenase 1	Homo sapiens	120-124
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	Reactive Oxygen Species	240-243	heme oxygenase 1	Homo sapiens	17-21
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	Reactive Oxygen Species	240-243	heme oxygenase 1	Homo sapiens	120-124
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	Oxidopamine	267-273	heme oxygenase 1	Homo sapiens	17-21
12578834-5	2003	The relevance of HO-1 in NGF-induced ROS reduction was further demonstrated by the evidence that cells treated with the HO-1 inhibitor tin-protoporphyrin or infected with a retroviral expression vector for antisense HO-1 exhibited enhanced ROS release in response to 6-OHDA, despite the presence of the neurotrophin.	Oxidopamine	267-273	heme oxygenase 1	Homo sapiens	120-124
12578834-8	2003	These observations indicate that the PI3K/Akt pathway controls the intracellular levels of ROS by regulating the expression of the antioxidant enzyme HO-1.	Reactive Oxygen Species	91-94	heme oxygenase 1	Homo sapiens	150-154
12727804-7	2003	Genes whose transcription was altered in common among all the treated keratinocytes included those induced by reactive oxygen, of which heme oxygenase-1 displayed the highest fold induction.	reactive oxygen	110-125	heme oxygenase 1	Homo sapiens	136-152
12727804-10	2003	Comparison with other agents producing reactive oxygen in the cells, as reflected in heme oxygenase-1 induction, suggested cellular differentiation was suppressed by sustained but not transient generation of reactive oxygen.	reactive	39-47	heme oxygenase 1	Homo sapiens	85-101
12727804-10	2003	Comparison with other agents producing reactive oxygen in the cells, as reflected in heme oxygenase-1 induction, suggested cellular differentiation was suppressed by sustained but not transient generation of reactive oxygen.	Oxygen	48-54	heme oxygenase 1	Homo sapiens	85-101
12678694-6	2003	HO1-mediated metabolism of heme groups released from NO-damaged proteins leads to a change in the levels of redox-active iron and a release of carbon monoxide (CO) and bilirubin, all of which have been implicated in cellular resistance to oxidative stress.	Iron	121-125	heme oxygenase 1	Homo sapiens	0-3
12678694-6	2003	HO1-mediated metabolism of heme groups released from NO-damaged proteins leads to a change in the levels of redox-active iron and a release of carbon monoxide (CO) and bilirubin, all of which have been implicated in cellular resistance to oxidative stress.	Carbon Monoxide	143-158	heme oxygenase 1	Homo sapiens	0-3
12678694-6	2003	HO1-mediated metabolism of heme groups released from NO-damaged proteins leads to a change in the levels of redox-active iron and a release of carbon monoxide (CO) and bilirubin, all of which have been implicated in cellular resistance to oxidative stress.	Carbon Monoxide	160-162	heme oxygenase 1	Homo sapiens	0-3
12678694-6	2003	HO1-mediated metabolism of heme groups released from NO-damaged proteins leads to a change in the levels of redox-active iron and a release of carbon monoxide (CO) and bilirubin, all of which have been implicated in cellular resistance to oxidative stress.	Bilirubin	168-177	heme oxygenase 1	Homo sapiens	0-3
12676598-5	2003	HO-1 expression, a sensitive marker for oxidative stress, is directly correlated with the high organic carbon and polycyclic aromatic hydrocarbon (PAH) content of UFPs.	Carbon	103-109	heme oxygenase 1	Homo sapiens	0-4
12678694-7	2003	Perhaps one or more of the products of HO1 heme metabolism is involved in induced adaptive resistance or perhaps a heme-independent mechanism is involved.	Heme	43-47	heme oxygenase 1	Homo sapiens	39-42
12676598-5	2003	HO-1 expression, a sensitive marker for oxidative stress, is directly correlated with the high organic carbon and polycyclic aromatic hydrocarbon (PAH) content of UFPs.	Polycyclic Aromatic Hydrocarbons	114-145	heme oxygenase 1	Homo sapiens	0-4
12676598-5	2003	HO-1 expression, a sensitive marker for oxidative stress, is directly correlated with the high organic carbon and polycyclic aromatic hydrocarbon (PAH) content of UFPs.	Polycyclic Aromatic Hydrocarbons	147-150	heme oxygenase 1	Homo sapiens	0-4
12572666-6	2003	Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron.	Biliverdine	78-88	heme oxygenase 1	Homo sapiens	0-16
12676598-6	2003	The dithiothreitol (DTT) assay, a quantitative measure of in vitro ROS formation, was correlated with PAH content and HO-1 expression.	Dithiothreitol	4-18	heme oxygenase 1	Homo sapiens	118-122
12676598-6	2003	The dithiothreitol (DTT) assay, a quantitative measure of in vitro ROS formation, was correlated with PAH content and HO-1 expression.	Dithiothreitol	20-23	heme oxygenase 1	Homo sapiens	118-122
12676598-6	2003	The dithiothreitol (DTT) assay, a quantitative measure of in vitro ROS formation, was correlated with PAH content and HO-1 expression.	Reactive Oxygen Species	67-70	heme oxygenase 1	Homo sapiens	118-122
12500973-0	2003	Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1.	Heme	18-22	heme oxygenase 1	Homo sapiens	67-83
12594185-9	2003	HO-1 plays an important protective role in the defense against reactive oxygen species (ROS).	Reactive Oxygen Species	63-86	heme oxygenase 1	Homo sapiens	0-4
12594185-9	2003	HO-1 plays an important protective role in the defense against reactive oxygen species (ROS).	Reactive Oxygen Species	88-91	heme oxygenase 1	Homo sapiens	0-4
12668974-0	2003	Nitric oxide-mediated cytoprotection of hepatocytes from glucose deprivation-induced cytotoxicity: involvement of heme oxygenase-1.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	114-130
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	105-120	heme oxygenase 1	Homo sapiens	0-16
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	105-120	heme oxygenase 1	Homo sapiens	18-22
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	122-124	heme oxygenase 1	Homo sapiens	0-16
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Carbon Monoxide	122-124	heme oxygenase 1	Homo sapiens	18-22
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Biliverdine	127-137	heme oxygenase 1	Homo sapiens	0-16
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Biliverdine	127-137	heme oxygenase 1	Homo sapiens	18-22
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Iron	148-152	heme oxygenase 1	Homo sapiens	0-16
12668974-1	2003	Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron.	Iron	148-152	heme oxygenase 1	Homo sapiens	18-22
12511571-1	2003	Heme oxygenase 1 (HO-1) catalyzes heme breakdown, eventually releasing iron, carbon monoxide, and bilirubin IXalpha.	Iron	71-75	heme oxygenase 1	Homo sapiens	0-16
12511571-1	2003	Heme oxygenase 1 (HO-1) catalyzes heme breakdown, eventually releasing iron, carbon monoxide, and bilirubin IXalpha.	Carbon Monoxide	77-92	heme oxygenase 1	Homo sapiens	0-16
12511571-1	2003	Heme oxygenase 1 (HO-1) catalyzes heme breakdown, eventually releasing iron, carbon monoxide, and bilirubin IXalpha.	Bilirubin	98-107	heme oxygenase 1	Homo sapiens	0-16
12511571-2	2003	HO-1 is induced by its substrate heme and various environmental factors, which represents a protective response against oxidative stresses.	Heme	33-37	heme oxygenase 1	Homo sapiens	0-4
12511571-6	2003	Expression of HO-1 was also reduced in human cells when exposed to interferon-gamma or an iron chelator desferrioxamine, each of which induced Bach1 expression.	Iron	90-94	heme oxygenase 1	Homo sapiens	14-18
12511571-6	2003	Expression of HO-1 was also reduced in human cells when exposed to interferon-gamma or an iron chelator desferrioxamine, each of which induced Bach1 expression.	Deferoxamine	104-119	heme oxygenase 1	Homo sapiens	14-18
12511571-7	2003	In contrast, induction of HO-1 expression by CoCl(2) is associated with reduced expression of Bach1 mRNA.	cobaltous chloride	45-52	heme oxygenase 1	Homo sapiens	26-30
12511571-10	2003	Therefore, Bach1 functions as a hypoxia-inducible repressor for the HO-1 gene, thereby contributing to fine-tuning of oxygen homeostasis in human cells.	Oxygen	118-124	heme oxygenase 1	Homo sapiens	68-72
12572666-6	2003	Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron.	Heme	61-65	heme oxygenase 1	Homo sapiens	0-16
12572666-6	2003	Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron.	Iron	69-73	heme oxygenase 1	Homo sapiens	0-16
12572666-6	2003	Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron.	Heme	145-149	heme oxygenase 1	Homo sapiens	0-16
12572666-6	2003	Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron.	Iron	187-191	heme oxygenase 1	Homo sapiens	0-16
12586756-10	2003	Endogenously produced cGMP also induced HO-1 because phosphodiesterase inhibition markedly elevated HO-1.	8-bromocyclic GMP	22-26	heme oxygenase 1	Homo sapiens	40-44
12586756-10	2003	Endogenously produced cGMP also induced HO-1 because phosphodiesterase inhibition markedly elevated HO-1.	8-bromocyclic GMP	22-26	heme oxygenase 1	Homo sapiens	100-104
12586756-14	2003	Abrogation of HO-1 induction by PD-98059 showed also a role for ERK.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	32-40	heme oxygenase 1	Homo sapiens	14-18
12531245-8	2003	Endotoxin and SnMP showed more prominent effect on the expression of VEGF and suppression of TGF-beta in HO-1 transduced endothelial cells, suggesting that their effect is most probably mediated through induction of HO-1.	tin mesoporphyrin	14-18	heme oxygenase 1	Homo sapiens	105-109
12623985-3	2003	In the present study, we determined the effect of interventions that suppress HO activity or induce HO-1 gene expression on Ang II-mediated increase in 6-keto-PGF1alpha and PGE2 in cultures of human femoral artery endothelial cells.	6-Ketoprostaglandin F1 alpha	152-168	heme oxygenase 1	Homo sapiens	100-104
12623985-3	2003	In the present study, we determined the effect of interventions that suppress HO activity or induce HO-1 gene expression on Ang II-mediated increase in 6-keto-PGF1alpha and PGE2 in cultures of human femoral artery endothelial cells.	Dinoprostone	173-177	heme oxygenase 1	Homo sapiens	100-104
12623985-5	2003	This effect of Ang II on prostaglandin production by endothelial cells was attenuated in cells treated with SnCl2 (10 micromol/L), an inducer of HO-1, but was magnified in cells treated with the HO inhibitor ZnDPP or heme.	Prostaglandins	25-38	heme oxygenase 1	Homo sapiens	145-149
12623985-5	2003	This effect of Ang II on prostaglandin production by endothelial cells was attenuated in cells treated with SnCl2 (10 micromol/L), an inducer of HO-1, but was magnified in cells treated with the HO inhibitor ZnDPP or heme.	stannous chloride	108-113	heme oxygenase 1	Homo sapiens	145-149
12531245-8	2003	Endotoxin and SnMP showed more prominent effect on the expression of VEGF and suppression of TGF-beta in HO-1 transduced endothelial cells, suggesting that their effect is most probably mediated through induction of HO-1.	tin mesoporphyrin	14-18	heme oxygenase 1	Homo sapiens	216-220
12623985-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene also attenuated heme and Ang II-induced prostaglandin synthesis.	Heme	108-112	heme oxygenase 1	Homo sapiens	16-20
12623985-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene also attenuated heme and Ang II-induced prostaglandin synthesis.	Heme	108-112	heme oxygenase 1	Homo sapiens	82-86
12591764-0	2003	Rapamycin induces heme oxygenase-1 in human pulmonary vascular cells: implications in the antiproliferative response to rapamycin.	Sirolimus	0-9	heme oxygenase 1	Homo sapiens	18-34
12623985-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene also attenuated heme and Ang II-induced prostaglandin synthesis.	Prostaglandins	132-145	heme oxygenase 1	Homo sapiens	16-20
12623985-6	2003	Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene also attenuated heme and Ang II-induced prostaglandin synthesis.	Prostaglandins	132-145	heme oxygenase 1	Homo sapiens	82-86
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Heme	76-80	heme oxygenase 1	Homo sapiens	0-16
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Heme	76-80	heme oxygenase 1	Homo sapiens	18-22
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Biliverdine	84-94	heme oxygenase 1	Homo sapiens	0-16
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Biliverdine	84-94	heme oxygenase 1	Homo sapiens	18-22
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Iron	101-105	heme oxygenase 1	Homo sapiens	0-16
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Iron	101-105	heme oxygenase 1	Homo sapiens	18-22
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	0-16
12935634-1	2003	Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	18-22
12591764-0	2003	Rapamycin induces heme oxygenase-1 in human pulmonary vascular cells: implications in the antiproliferative response to rapamycin.	Sirolimus	120-129	heme oxygenase 1	Homo sapiens	18-34
12591764-3	2003	In this study, we evaluated whether there is an interaction between rapamycin and HO-1.	Sirolimus	68-77	heme oxygenase 1	Homo sapiens	82-86
12591764-4	2003	METHODS AND RESULTS: In human pulmonary artery endothelial or smooth muscle cells, HO-1 expression was evaluated in response to rapamycin or wortmannin, an inhibitor of the upstream modulator of mammalian target of rapamycin (mTOR) PI-3K.	Sirolimus	128-137	heme oxygenase 1	Homo sapiens	83-87
12591764-4	2003	METHODS AND RESULTS: In human pulmonary artery endothelial or smooth muscle cells, HO-1 expression was evaluated in response to rapamycin or wortmannin, an inhibitor of the upstream modulator of mammalian target of rapamycin (mTOR) PI-3K.	Wortmannin	141-151	heme oxygenase 1	Homo sapiens	83-87
12591764-6	2003	Rapamycin induced HO-1 expression in both pulmonary endothelial and smooth muscle cells, whereas no to little increase was seen in response to another immunosuppressive agent, cyclosporin A.	Sirolimus	0-9	heme oxygenase 1	Homo sapiens	18-22
12591764-7	2003	HO-1 expression was also increased in response to wortmannin, suggesting that the PI-3K-mTOR pathway is required for this induction.	Wortmannin	50-60	heme oxygenase 1	Homo sapiens	0-4
12591764-9	2003	CONCLUSIONS: The induction of HO-1 expression by rapamycin and, more importantly, the effects of tin protoporphyrin, an inhibitor of HO activity, on the antiproliferative actions of rapamycin suggest that the effects of rapamycin may be, at least in part, modulated by its actions on HO-1.	tin protoporphyrin IX	97-115	heme oxygenase 1	Homo sapiens	284-288
12591764-9	2003	CONCLUSIONS: The induction of HO-1 expression by rapamycin and, more importantly, the effects of tin protoporphyrin, an inhibitor of HO activity, on the antiproliferative actions of rapamycin suggest that the effects of rapamycin may be, at least in part, modulated by its actions on HO-1.	Sirolimus	49-58	heme oxygenase 1	Homo sapiens	30-34
12591764-9	2003	CONCLUSIONS: The induction of HO-1 expression by rapamycin and, more importantly, the effects of tin protoporphyrin, an inhibitor of HO activity, on the antiproliferative actions of rapamycin suggest that the effects of rapamycin may be, at least in part, modulated by its actions on HO-1.	Sirolimus	182-191	heme oxygenase 1	Homo sapiens	30-34
12591764-9	2003	CONCLUSIONS: The induction of HO-1 expression by rapamycin and, more importantly, the effects of tin protoporphyrin, an inhibitor of HO activity, on the antiproliferative actions of rapamycin suggest that the effects of rapamycin may be, at least in part, modulated by its actions on HO-1.	Sirolimus	182-191	heme oxygenase 1	Homo sapiens	284-288
12420309-4	2002	Catecholamines caused a reduction in intracellular glutathione levels, an accumulation in reactive oxygen species and in heme oxygenase-1, the 32 kDa stress-induced protein.	Catecholamines	0-14	heme oxygenase 1	Homo sapiens	121-137
12566071-0	2003	Beta-carotene suppresses UVA-induced HO-1 gene expression in cultured FEK4.	beta Carotene	0-13	heme oxygenase 1	Homo sapiens	37-41
12566071-4	2003	Carotenoids, as the most potent singlet oxygen quenchers in nature, are expected to effectively suppress the UVA-induced HO-1 gene activation in human cells.	Carotenoids	0-11	heme oxygenase 1	Homo sapiens	121-125
12566071-5	2003	In this study, we measured the suppression of UVA-induced levels of HO-1 mRNA after the addition of a series of six all-trans-beta-carotene concentrations (0.07, 0.2, 0.8, 2.3, 8.0, and 21 microM) to the culture medium of exponentially growing FEK4 cells.	beta Carotene	126-139	heme oxygenase 1	Homo sapiens	68-72
12566071-7	2003	The results of this study show a concentration-dependent suppression of UVA- (250 kJ/m(2)) induced transcriptional activation of HO-1 in exponentially growing FEK4 cells by beta-carotene.	beta Carotene	173-186	heme oxygenase 1	Homo sapiens	129-133
21207851-1	2003	AIM: To explore the effects of heme- heme oxygenase-1 (HO-1)-carbon monoxide(CO)-cyclic GMP (cGMP)on aortic vascular reactivity in endotoxemic rats and its molecular mechanism.	Carbon Monoxide	61-76	heme oxygenase 1	Homo sapiens	55-59
21207851-1	2003	AIM: To explore the effects of heme- heme oxygenase-1 (HO-1)-carbon monoxide(CO)-cyclic GMP (cGMP)on aortic vascular reactivity in endotoxemic rats and its molecular mechanism.	Carbon Monoxide	77-80	heme oxygenase 1	Homo sapiens	55-59
21207851-1	2003	AIM: To explore the effects of heme- heme oxygenase-1 (HO-1)-carbon monoxide(CO)-cyclic GMP (cGMP)on aortic vascular reactivity in endotoxemic rats and its molecular mechanism.	Cyclic GMP	81-91	heme oxygenase 1	Homo sapiens	55-59
21207851-1	2003	AIM: To explore the effects of heme- heme oxygenase-1 (HO-1)-carbon monoxide(CO)-cyclic GMP (cGMP)on aortic vascular reactivity in endotoxemic rats and its molecular mechanism.	Cyclic GMP	93-97	heme oxygenase 1	Homo sapiens	55-59
14753445-0	2003	Transient elevation of serum bilirubin (a heme oxygenase-1 metabolite) level in hemorrhagic stroke: bilirubin is a marker of oxidant stress.	Bilirubin	29-38	heme oxygenase 1	Homo sapiens	42-58
14753445-0	2003	Transient elevation of serum bilirubin (a heme oxygenase-1 metabolite) level in hemorrhagic stroke: bilirubin is a marker of oxidant stress.	Bilirubin	100-109	heme oxygenase 1	Homo sapiens	42-58
14753445-2	2003	The production of Bil reflects heme oxygenase-1 expression in response to oxidative stress in various diseases.	Bilirubin	18-21	heme oxygenase 1	Homo sapiens	31-47
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	Oxygen	33-39	heme oxygenase 1	Homo sapiens	0-21
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	Oxygen	33-39	heme oxygenase 1	Homo sapiens	23-28
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	C-1027 AROMATIZED CHROMOPHORE	89-92	heme oxygenase 1	Homo sapiens	0-21
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	C-1027 AROMATIZED CHROMOPHORE	89-92	heme oxygenase 1	Homo sapiens	23-28
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	Heme	107-111	heme oxygenase 1	Homo sapiens	0-21
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	Heme	107-111	heme oxygenase 1	Homo sapiens	23-28
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	Bilirubin	152-161	heme oxygenase 1	Homo sapiens	0-21
15115285-1	2003	Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin.	Bilirubin	152-161	heme oxygenase 1	Homo sapiens	23-28
15115285-6	2003	Hsp32 expression in formalin-fixed sections was assessed by avidin-biotin peroxidase immunohistochemistry using a polyclonal rabbit anti-Hsp32 as the primary antibody.	Formaldehyde	20-28	heme oxygenase 1	Homo sapiens	0-5
12551835-0	2003	Contribution of the induction of heme oxygenase-1 to etoposide-induced apoptosis in acute myeloblastic leukemia.	Etoposide	53-62	heme oxygenase 1	Homo sapiens	33-49
12964953-2	2003	In addition to its physiological role in heme degradation, HO-1 may influence a number of cellular processes, including growth, inflammation, and apoptosis.	Heme	41-45	heme oxygenase 1	Homo sapiens	59-63
12964953-4	2003	The transcriptional upregulation of HO-1 responds to many agents, such as hypoxia, bacterial lipopolysaccharide, and reactive oxygen/nitrogen species.	bacterial lipopolysaccharide	83-111	heme oxygenase 1	Homo sapiens	36-40
12964953-4	2003	The transcriptional upregulation of HO-1 responds to many agents, such as hypoxia, bacterial lipopolysaccharide, and reactive oxygen/nitrogen species.	reactive oxygen/nitrogen species	117-149	heme oxygenase 1	Homo sapiens	36-40
12964953-5	2003	HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO).	Heme	47-51	heme oxygenase 1	Homo sapiens	0-4
12964953-5	2003	HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO).	Bilirubin	143-160	heme oxygenase 1	Homo sapiens	0-4
12964953-5	2003	HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO).	Iron	170-174	heme oxygenase 1	Homo sapiens	0-4
12964953-5	2003	HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO).	Carbon Monoxide	180-195	heme oxygenase 1	Homo sapiens	0-4
12964953-5	2003	HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO).	Carbon Monoxide	197-199	heme oxygenase 1	Homo sapiens	0-4
12444034-2	2002	Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	33-37
12444034-2	2002	Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties.	Carbon Monoxide	120-135	heme oxygenase 1	Homo sapiens	193-197
12444034-2	2002	Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties.	Carbon Monoxide	137-139	heme oxygenase 1	Homo sapiens	33-37
12444034-2	2002	Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties.	Carbon Monoxide	137-139	heme oxygenase 1	Homo sapiens	193-197
12444034-2	2002	Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties.	Heme	174-178	heme oxygenase 1	Homo sapiens	33-37
12444034-2	2002	Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties.	Heme	174-178	heme oxygenase 1	Homo sapiens	193-197
12699247-0	2002	Interaction of heme with nitroxyl or nitric oxide amplifies heme oxygenase-1 induction: involvement of the transcription factor Nrf2.	Heme	15-19	heme oxygenase 1	Homo sapiens	60-76
12699247-0	2002	Interaction of heme with nitroxyl or nitric oxide amplifies heme oxygenase-1 induction: involvement of the transcription factor Nrf2.	nitroxyl	25-33	heme oxygenase 1	Homo sapiens	60-76
12699247-0	2002	Interaction of heme with nitroxyl or nitric oxide amplifies heme oxygenase-1 induction: involvement of the transcription factor Nrf2.	Nitric Oxide	37-49	heme oxygenase 1	Homo sapiens	60-76
12699247-1	2002	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species.	Heme	156-160	heme oxygenase 1	Homo sapiens	0-16
12699247-1	2002	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species.	Heme	156-160	heme oxygenase 1	Homo sapiens	18-22
12699247-1	2002	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species.	Reactive Oxygen Species	165-188	heme oxygenase 1	Homo sapiens	0-16
12699247-1	2002	Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species.	Reactive Oxygen Species	165-188	heme oxygenase 1	Homo sapiens	18-22
12699247-2	2002	Conceptually, the perception that HO-1 plays a key role in response to oxidative damage is paralleled by evidence showing high expression of HO-1 in a variety of cell systems challenged with nitric oxide (NO) or NO-derivatives, thus revealing a potential biological function for HO-1 against nitrosative stress.	Nitric Oxide	191-203	heme oxygenase 1	Homo sapiens	34-38
12699247-2	2002	Conceptually, the perception that HO-1 plays a key role in response to oxidative damage is paralleled by evidence showing high expression of HO-1 in a variety of cell systems challenged with nitric oxide (NO) or NO-derivatives, thus revealing a potential biological function for HO-1 against nitrosative stress.	Nitric Oxide	191-203	heme oxygenase 1	Homo sapiens	141-145
12699247-2	2002	Conceptually, the perception that HO-1 plays a key role in response to oxidative damage is paralleled by evidence showing high expression of HO-1 in a variety of cell systems challenged with nitric oxide (NO) or NO-derivatives, thus revealing a potential biological function for HO-1 against nitrosative stress.	Nitric Oxide	191-203	heme oxygenase 1	Homo sapiens	141-145
12699247-3	2002	In this study, we report that exposure of cardiac cells to hemin (5-20 microM) in combination with compounds that liberate nitroxyl (HNO/NO-) or release NO significantly potentiates HO-1 mRNA and protein expression leading to a remarkable increase in heme oxygenase activity under both normoxic and hypoxic conditions.	Hemin	59-64	heme oxygenase 1	Homo sapiens	182-186
12699247-3	2002	In this study, we report that exposure of cardiac cells to hemin (5-20 microM) in combination with compounds that liberate nitroxyl (HNO/NO-) or release NO significantly potentiates HO-1 mRNA and protein expression leading to a remarkable increase in heme oxygenase activity under both normoxic and hypoxic conditions.	nitroxyl	123-131	heme oxygenase 1	Homo sapiens	182-186
12699247-3	2002	In this study, we report that exposure of cardiac cells to hemin (5-20 microM) in combination with compounds that liberate nitroxyl (HNO/NO-) or release NO significantly potentiates HO-1 mRNA and protein expression leading to a remarkable increase in heme oxygenase activity under both normoxic and hypoxic conditions.	nitroxyl	133-136	heme oxygenase 1	Homo sapiens	182-186
12699247-4	2002	The amplification of the heme oxygenase pathway appears to involve a direct interaction between heme and the NO groups, as the ability of both NO(-)- and NO-releasing agents to induce HO-1 is totally lost by their pre-incubation for 1 hr in complete medium prior to cell treatment but is highly preserved by addition of hemin during the preincubation step.	Heme	25-29	heme oxygenase 1	Homo sapiens	184-188
12699247-4	2002	The amplification of the heme oxygenase pathway appears to involve a direct interaction between heme and the NO groups, as the ability of both NO(-)- and NO-releasing agents to induce HO-1 is totally lost by their pre-incubation for 1 hr in complete medium prior to cell treatment but is highly preserved by addition of hemin during the preincubation step.	Hemin	320-325	heme oxygenase 1	Homo sapiens	184-188
12699247-8	2002	We propose that modification of the iron protoporphyrin centers by NO groups to modulate HO-1 expression might be regarded as a molecular switch to maximize heme oxygenase enzymatic activity and consequently mitigate the redox imbalance imposed by oxidative and nitrosative stress.	Heme	36-55	heme oxygenase 1	Homo sapiens	89-93
12646399-6	2003	Pretreatment of monolayers with hemin for 2 h followed by 18 h in complete medium resulted in HO-1 induction and the attenuation of H(2)O(2)-mediated increases in endothelial permeability, and significantly improved the restoration of endothelial barrier function 48 h later.	Hemin	32-37	heme oxygenase 1	Homo sapiens	94-98
12646399-8	2003	This potentiation was inhibited by incubation with the HO inhibitor tin protoporphyrin IX, supporting a role for HO-1 in the potentiation of the cytotoxic response.	tin protoporphyrin IX	68-89	heme oxygenase 1	Homo sapiens	113-117
12433915-0	2003	Interaction of nitric oxide with human heme oxygenase-1.	Nitric Oxide	15-27	heme oxygenase 1	Homo sapiens	39-55
12433915-2	2003	We have examined the binding of NO to human heme oxygenase-1 (hHO-1), an enzyme that oxidizes heme to biliverdin, CO, and free iron, to determine whether inhibition of hHO-1 by NO can contribute to the signaling interplay of NO and CO. An Fe(3+)-NO hHO-1-heme complex is formed with NO or the NO donors NOC9 or 2-(N,N-diethylamino)-diazenolate-2-oxide.sodium salt.	Heme	44-48	heme oxygenase 1	Homo sapiens	62-67
12433915-2	2003	We have examined the binding of NO to human heme oxygenase-1 (hHO-1), an enzyme that oxidizes heme to biliverdin, CO, and free iron, to determine whether inhibition of hHO-1 by NO can contribute to the signaling interplay of NO and CO. An Fe(3+)-NO hHO-1-heme complex is formed with NO or the NO donors NOC9 or 2-(N,N-diethylamino)-diazenolate-2-oxide.sodium salt.	Biliverdine	102-112	heme oxygenase 1	Homo sapiens	62-67
12433915-5	2003	The Fe(3+)-NO complex of hHO-1 is much more stable than that of met-Mb.	fe(3+)-no	4-13	heme oxygenase 1	Homo sapiens	25-30
12433915-6	2003	Stopped-flow studies indicate that k(on) for formation of the hHO-1-heme Fe(3+)-NO complex is approximately 50-times faster, and k(off) 10 times slower, than for met-Mb, resulting in K(d) = 1.4 microm for NO.	fe(3+)-no	73-82	heme oxygenase 1	Homo sapiens	62-67
14529548-3	2003	An inducible form of HO, HO-1, is induced by a variety of stresses such as oxidized lipoproteins, cytokines, hemodynamic changes, angiotensin II and nitric oxide (NO) in vascular wall.	Nitric Oxide	149-161	heme oxygenase 1	Homo sapiens	25-29
14529548-5	2003	HO-1 induction in artery wall scavenges reactive oxygen species, which leads to the attenuation of monocyte adhesion and chemotaxis.	Reactive Oxygen Species	40-63	heme oxygenase 1	Homo sapiens	0-4
14529549-1	2003	The heme oxygenase-1 (HO-1) enzyme catalyzes the rate-limiting reaction in the catabolism of heme yielding products with pleiotropic, but ultimately, cytoprotective activities.	Heme	4-8	heme oxygenase 1	Homo sapiens	22-26
14529549-4	2003	Extensive analysis of the mouse gene, and to a lesser extent of the human gene, has identified a common mechanism the stress response element (StRE)/Nrf2 transcription factor pathway for gene regulation in response to a diverse array of HO-1 inducers including the substrate heme, various environmental and industrial toxins, and plant-derived polyphenolic compounds.	Heme	275-279	heme oxygenase 1	Homo sapiens	237-241
14529549-4	2003	Extensive analysis of the mouse gene, and to a lesser extent of the human gene, has identified a common mechanism the stress response element (StRE)/Nrf2 transcription factor pathway for gene regulation in response to a diverse array of HO-1 inducers including the substrate heme, various environmental and industrial toxins, and plant-derived polyphenolic compounds.	polyphenolic compounds	344-366	heme oxygenase 1	Homo sapiens	237-241
14529550-9	2003	Human HO-1 gene transfer into endothelial cells has been shown to attenuate Ang II- TNF- and heme-mediated DNA damage.	Heme	93-97	heme oxygenase 1	Homo sapiens	6-10
14529552-3	2003	HO-1 is induced by nitric oxide (NO) in different biological systems and can control the increased production of this mediator observed in many inflammatory situations.	Nitric Oxide	19-31	heme oxygenase 1	Homo sapiens	0-4
14529552-5	2003	Modulation of signal transduction pathways by HO-1 or products derived from its activity, such as carbon monoxide (CO), may mediate the anti-inflammatory effects of this protein.	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	46-50
14529552-5	2003	Modulation of signal transduction pathways by HO-1 or products derived from its activity, such as carbon monoxide (CO), may mediate the anti-inflammatory effects of this protein.	Carbon Monoxide	115-117	heme oxygenase 1	Homo sapiens	46-50
12498987-1	2003	In many models, a protective role for heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, has been demonstrated.	Heme	38-42	heme oxygenase 1	Homo sapiens	56-60
12498987-5	2003	Disrupted HO-1 expression was associated with decreased lung reactive iron and iron-associated proteins, decreased NADPH cytochrome cp450 reductase activity, and decreased lung peroxidase activity compared to WT.	Iron	70-74	heme oxygenase 1	Homo sapiens	10-14
12498987-5	2003	Disrupted HO-1 expression was associated with decreased lung reactive iron and iron-associated proteins, decreased NADPH cytochrome cp450 reductase activity, and decreased lung peroxidase activity compared to WT.	Iron	79-83	heme oxygenase 1	Homo sapiens	10-14
12498987-7	2003	This suggests that disruption of HO-1 protects against hyperoxia by diminishing the generation of toxic reactive intermediates in the lung via iron and H(2)O(2).	Iron	143-147	heme oxygenase 1	Homo sapiens	33-37
12498987-7	2003	This suggests that disruption of HO-1 protects against hyperoxia by diminishing the generation of toxic reactive intermediates in the lung via iron and H(2)O(2).	Water	152-157	heme oxygenase 1	Homo sapiens	33-37
12469218-4	2003	Treatment of HLE/2E1 cells with succinylacetone (SA), a potent inhibitor of delta-aminolevulinate dehydratase and thereby heme synthesis, resulted in a further increase in ALAS-N mRNA but a decrease in HO-1 mRNA levels.	succinylacetone	32-47	heme oxygenase 1	Homo sapiens	202-206
12469218-4	2003	Treatment of HLE/2E1 cells with succinylacetone (SA), a potent inhibitor of delta-aminolevulinate dehydratase and thereby heme synthesis, resulted in a further increase in ALAS-N mRNA but a decrease in HO-1 mRNA levels.	succinylacetone	49-51	heme oxygenase 1	Homo sapiens	202-206
12469218-6	2003	These findings suggest that the overexpression of CYP2E1 results in the up-regulation of ALAS-N in order to meet with an increased demand for heme synthesis for CYP2E1 formation, while it also results in the up-regulation of HO-1 presumably by enzyme induction by free heme released from CYP2E1, which then results in the elimination of toxic excess free heme and ultimately restores the physiologic milieu.	Heme	269-273	heme oxygenase 1	Homo sapiens	225-229
12469218-6	2003	These findings suggest that the overexpression of CYP2E1 results in the up-regulation of ALAS-N in order to meet with an increased demand for heme synthesis for CYP2E1 formation, while it also results in the up-regulation of HO-1 presumably by enzyme induction by free heme released from CYP2E1, which then results in the elimination of toxic excess free heme and ultimately restores the physiologic milieu.	Heme	269-273	heme oxygenase 1	Homo sapiens	225-229
12598705-0	2003	The induction of heme oxygenase-1 by exogenous nitric oxide in ex vivo normal human skin.	Nitric Oxide	47-59	heme oxygenase 1	Homo sapiens	17-33
12598705-3	2003	Many reports have revealed that exogenous nitric oxide (NO) can induce HO-1 in vitro, which is the induced isoform of HO.	Nitric Oxide	42-54	heme oxygenase 1	Homo sapiens	71-75
12452690-0	2002	1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1.	Hydrogen	0-2	heme oxygenase 1	Homo sapiens	121-137
12452690-0	2002	1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1.	Water	32-37	heme oxygenase 1	Homo sapiens	121-137
12452690-0	2002	1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1.	Hydrogen	71-79	heme oxygenase 1	Homo sapiens	121-137
12376363-5	2002	Actinomycin D and cycloheximide inhibited TGF-beta1-responsive HO-1 mRNA expression, indicating a requirement for transcription and de novo protein synthesis.	Dactinomycin	0-13	heme oxygenase 1	Homo sapiens	63-67
12376366-8	2002	These results indicate that prolonged overexpression of HO-1 ultimately decreases sGC activity by limiting the availability of cellular heme.	Heme	136-140	heme oxygenase 1	Homo sapiens	56-60
12376363-5	2002	Actinomycin D and cycloheximide inhibited TGF-beta1-responsive HO-1 mRNA expression, indicating a requirement for transcription and de novo protein synthesis.	Cycloheximide	18-31	heme oxygenase 1	Homo sapiens	63-67
12376363-7	2002	A chemical inhibitor of p38 MAPK (SB-203580) abolished TGF-beta1-inducible HO-1 mRNA expression.	SB 203580	34-43	heme oxygenase 1	Homo sapiens	75-79
12376363-8	2002	Both SB-203580 and expression of a dominant-negative mutant of p38 MAPK inhibited TGF-beta1-induced ho-1 gene activation, as assayed by luciferase activity of an ho-1 enhancer/luciferase fusion construct (pMHO1luc-33+SX2).	SB 203580	5-14	heme oxygenase 1	Homo sapiens	100-104
12376366-0	2002	Modulation of cGMP by human HO-1 retrovirus gene transfer in pulmonary microvessel endothelial cells.	Cyclic GMP	14-18	heme oxygenase 1	Homo sapiens	28-32
12376366-3	2002	Pulmonary cells that expressed hHO-1 exhibited a fourfold increase in HO activity associated with decreases in the steady-state levels of heme and cGMP without changes in soluble GC (sGC) and endothelial nitric oxide synthase (NOS) proteins or basal nitrite production.	Heme	138-142	heme oxygenase 1	Homo sapiens	31-36
12376366-3	2002	Pulmonary cells that expressed hHO-1 exhibited a fourfold increase in HO activity associated with decreases in the steady-state levels of heme and cGMP without changes in soluble GC (sGC) and endothelial nitric oxide synthase (NOS) proteins or basal nitrite production.	Cyclic GMP	147-151	heme oxygenase 1	Homo sapiens	31-36
12376366-3	2002	Pulmonary cells that expressed hHO-1 exhibited a fourfold increase in HO activity associated with decreases in the steady-state levels of heme and cGMP without changes in soluble GC (sGC) and endothelial nitric oxide synthase (NOS) proteins or basal nitrite production.	Nitrites	250-257	heme oxygenase 1	Homo sapiens	31-36
12376366-4	2002	Heme elicited significant increases in CO production and intracellular cGMP levels in both pulmonary endothelial and pulmonary hHO-1-expressing cells.	Heme	0-4	heme oxygenase 1	Homo sapiens	127-132
12376366-5	2002	N(omega)-nitro-L-arginine methyl ester (L-NAME), an inhibitor of NOS, significantly decreased cGMP levels in heme-treated pulmonary endothelial cells but not heme-treated hHO-1-expressing cells.	Heme	109-113	heme oxygenase 1	Homo sapiens	171-176
12376366-6	2002	In the presence of exogenous heme, CO and cGMP levels in hHO-1-expressing cells exceeded the corresponding levels in pulmonary endothelial cells.	Heme	29-33	heme oxygenase 1	Homo sapiens	57-62
12376366-6	2002	In the presence of exogenous heme, CO and cGMP levels in hHO-1-expressing cells exceeded the corresponding levels in pulmonary endothelial cells.	Carbon Monoxide	35-37	heme oxygenase 1	Homo sapiens	57-62
12376366-6	2002	In the presence of exogenous heme, CO and cGMP levels in hHO-1-expressing cells exceeded the corresponding levels in pulmonary endothelial cells.	Cyclic GMP	42-46	heme oxygenase 1	Homo sapiens	57-62
12396617-6	2002	However, inhibition of HO-1 after treatment with tin protoporphyrin reversed the immunomodulatory/antiapoptotic effects of Ad-IL-13 both in vivo (infectious transplantation tolerance), and in vitro (HUVECs).	tin protoporphyrin IX	49-67	heme oxygenase 1	Homo sapiens	23-27
12394829-1	2002	The heme oxygenase-1 (HO-1) system, the rate-limiting step in the conversion of heme, is among the most critical of cytoprotective mechanisms activated during cellular stress.	Heme	4-8	heme oxygenase 1	Homo sapiens	22-26
12394829-2	2002	The cytoprotection may result from the elimination of heme and the function of HO-1 downstream mediators, that is, biliverdin, carbon monoxide, and free iron.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	79-83
12394829-2	2002	The cytoprotection may result from the elimination of heme and the function of HO-1 downstream mediators, that is, biliverdin, carbon monoxide, and free iron.	Carbon Monoxide	127-142	heme oxygenase 1	Homo sapiens	79-83
12394829-2	2002	The cytoprotection may result from the elimination of heme and the function of HO-1 downstream mediators, that is, biliverdin, carbon monoxide, and free iron.	Iron	153-157	heme oxygenase 1	Homo sapiens	79-83
12352326-9	2002	Endothelial NOS mRNA was increased in cyclosporine-and tacrolimus-treated patients in comparison with controls (0.92 +/- 0.09, 0.96 +/- 0.04, and 0.37 +/- 0.05 respectively; p &lt; 0.001), whereas no difference was found between patients and controls in HO-1 mRNA.	Cyclosporine	38-50	heme oxygenase 1	Homo sapiens	254-258
12352326-9	2002	Endothelial NOS mRNA was increased in cyclosporine-and tacrolimus-treated patients in comparison with controls (0.92 +/- 0.09, 0.96 +/- 0.04, and 0.37 +/- 0.05 respectively; p &lt; 0.001), whereas no difference was found between patients and controls in HO-1 mRNA.	Tacrolimus	55-65	heme oxygenase 1	Homo sapiens	254-258
12352326-11	2002	Ramipril also reduced p22 (to 0.83 +/- 0.05 in cyclosporine, p &lt; 0.03 and to 0.81 +/- 0.08 in tacrolimus; p &lt; 0.01) and TGF-beta mRNA (to 0.72 +/- 01 in cyclosporine, p &lt; 0.02, and to 0.73 +/- 0.05 in tacrolimus; p &lt; 0.01) with no difference between groups, but it did not change HO-1 and ecNOS mRNA.	Ramipril	0-8	heme oxygenase 1	Homo sapiens	292-296
12221210-5	2002	Histologic examination revealed that HO-1 was constitutively expressed in intestinal epithelial cells (IEC), and that glutamine increased the grade of HO-1 immunostaining (P &lt;/= 0.01).	Glutamine	118-127	heme oxygenase 1	Homo sapiens	151-155
12382200-12	2002	Heme oxygenase 1 is essential for the catabolism of heme and in the recycling of hemoglobin iron in macrophages.	Heme	52-56	heme oxygenase 1	Homo sapiens	0-16
12382200-12	2002	Heme oxygenase 1 is essential for the catabolism of heme and in the recycling of hemoglobin iron in macrophages.	Iron	92-96	heme oxygenase 1	Homo sapiens	0-16
12352873-0	2002	Inhibition of ischemia/reperfusion injury and chronic graft deterioration by a single-donor treatment with cobalt-protoporphyrin for the induction of heme oxygenase-1.	cobaltiprotoporphyrin	107-128	heme oxygenase 1	Homo sapiens	150-166
12352873-5	2002	Induction of HO-1 expression following cobalt-protoporphyrin (CoPP) treatment in organ donors prolonged graft survival and long-term function remarkably following extended periods of ischemia.	cobaltiprotoporphyrin	39-60	heme oxygenase 1	Homo sapiens	13-17
12352873-5	2002	Induction of HO-1 expression following cobalt-protoporphyrin (CoPP) treatment in organ donors prolonged graft survival and long-term function remarkably following extended periods of ischemia.	cobaltiprotoporphyrin	62-66	heme oxygenase 1	Homo sapiens	13-17
12207883-4	2002	The addition of SnMP (10 microM), an inhibitor of HO activity, to EC or SMC for 24h, resulted in significant abnormalities in DNA distribution and cell cycle progression compared to cells treated with the HO-1 inducers, heme (10 microM) or SnCl(2) (10 microM).	tin mesoporphyrin	16-20	heme oxygenase 1	Homo sapiens	205-209
12221210-0	2002	Acute enteral glutamine infusion enhances heme oxygenase-1 expression in human duodenal mucosa.	Glutamine	14-23	heme oxygenase 1	Homo sapiens	42-58
12221210-2	2002	Some experimental models suggest that induction of HO-1 by glutamine may contribute to the preservation of intestinal mucosa.	Glutamine	59-68	heme oxygenase 1	Homo sapiens	51-55
12221210-3	2002	The effect of an enteral infusion of glutamine for 6 h on HO-1 expression in duodenal mucosa was studied in healthy men and women and compared with an isonitrogenous mixture of amino acids.	Glutamine	37-46	heme oxygenase 1	Homo sapiens	58-62
12398878-3	2002	HO-1 expression was correlated with increased tissue iron and/or ferritin expression and increased inflammatory/oxidant load as measured by myeloperoxidase expression.	Iron	53-57	heme oxygenase 1	Homo sapiens	0-4
12221210-6	2002	Glutamine also increased the percentage of HO-1 immunoreactive lamina propria cells (LPC, 10.5 vs. 7.5%, P &lt;/= 0.05).	Glutamine	0-9	heme oxygenase 1	Homo sapiens	43-47
12221210-6	2002	Glutamine also increased the percentage of HO-1 immunoreactive lamina propria cells (LPC, 10.5 vs. 7.5%, P &lt;/= 0.05).	lpc	85-88	heme oxygenase 1	Homo sapiens	43-47
12221210-7	2002	Glutamine significantly increased HO-1 mRNA expression compared with control amino acids: median (range) 156 (102-182) vs. 100 (68-179)%, P &lt;/= 0.05.	Glutamine	0-9	heme oxygenase 1	Homo sapiens	34-38
12221210-9	2002	In conclusion, glutamine enhanced HO-1 mRNA and protein expression in human duodenal mucosa.	Glutamine	15-24	heme oxygenase 1	Homo sapiens	34-38
12221210-10	2002	These data support further evaluation of the effects of glutamine on intestinal HO-1 during states of intestinal inflammation.	Glutamine	56-65	heme oxygenase 1	Homo sapiens	80-84
12147246-6	2002	alpha-Naphthoflavone, which is known as an antagonist to 2,3,7,8-tetrachlorodibenzo-p-dioxin, inhibited the inductions of heme oxygenase 1, glutamate-cysteine ligase (modifier unit), and thioredoxin reductase by beta-naphthoflavone but not those of CYP1A1 and CYP1A2.	alpha-naphthoflavone	0-20	heme oxygenase 1	Homo sapiens	122-138
12147246-6	2002	alpha-Naphthoflavone, which is known as an antagonist to 2,3,7,8-tetrachlorodibenzo-p-dioxin, inhibited the inductions of heme oxygenase 1, glutamate-cysteine ligase (modifier unit), and thioredoxin reductase by beta-naphthoflavone but not those of CYP1A1 and CYP1A2.	Polychlorinated Dibenzodioxins	57-92	heme oxygenase 1	Homo sapiens	122-138
12147246-6	2002	alpha-Naphthoflavone, which is known as an antagonist to 2,3,7,8-tetrachlorodibenzo-p-dioxin, inhibited the inductions of heme oxygenase 1, glutamate-cysteine ligase (modifier unit), and thioredoxin reductase by beta-naphthoflavone but not those of CYP1A1 and CYP1A2.	beta-Naphthoflavone	212-231	heme oxygenase 1	Homo sapiens	122-138
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Heme	61-65	heme oxygenase 1	Homo sapiens	18-22
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	0-16
12230868-3	2002	HO-1 is a cytoprotective enzyme that degrades heme, a potent oxidant, to generate carbon monoxide, biliverdin (subsequently reduced to bilirubin), and iron.	Heme	46-50	heme oxygenase 1	Homo sapiens	0-4
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	18-22
12230868-3	2002	HO-1 is a cytoprotective enzyme that degrades heme, a potent oxidant, to generate carbon monoxide, biliverdin (subsequently reduced to bilirubin), and iron.	Carbon Monoxide	82-97	heme oxygenase 1	Homo sapiens	0-4
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Iron	86-90	heme oxygenase 1	Homo sapiens	0-16
12230868-3	2002	HO-1 is a cytoprotective enzyme that degrades heme, a potent oxidant, to generate carbon monoxide, biliverdin (subsequently reduced to bilirubin), and iron.	Biliverdine	99-109	heme oxygenase 1	Homo sapiens	0-4
12230868-3	2002	HO-1 is a cytoprotective enzyme that degrades heme, a potent oxidant, to generate carbon monoxide, biliverdin (subsequently reduced to bilirubin), and iron.	Bilirubin	135-144	heme oxygenase 1	Homo sapiens	0-4
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Iron	86-90	heme oxygenase 1	Homo sapiens	18-22
12230868-3	2002	HO-1 is a cytoprotective enzyme that degrades heme, a potent oxidant, to generate carbon monoxide, biliverdin (subsequently reduced to bilirubin), and iron.	Iron	151-155	heme oxygenase 1	Homo sapiens	0-4
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Biliverdine	101-111	heme oxygenase 1	Homo sapiens	0-16
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Biliverdine	101-111	heme oxygenase 1	Homo sapiens	18-22
12230869-0	2002	Effect of prostaglandin-J(2) on VEGF synthesis depends on the induction of heme oxygenase-1.	prostaglandin-j	10-25	heme oxygenase 1	Homo sapiens	75-91
12230869-4	2002	Here we investigated the involvement of HO-1 in the 15d-PGJ(2)-mediated regulation of VEGF production by human microvascular endothelial cells (HMEC-1).	9-deoxy-delta-9-prostaglandin D2	56-62	heme oxygenase 1	Homo sapiens	40-44
12230869-1	2002	Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin.	Heme	61-65	heme oxygenase 1	Homo sapiens	0-16
12230869-8	2002	Activation of HO-1 with hemin or ectopic overexpression of HO-1 in HMEC-1 perfectly mimicked the effect of 15d-PGJ(2) and led to increased VEGF production.	15d-pgj	107-114	heme oxygenase 1	Homo sapiens	14-18
12230869-8	2002	Activation of HO-1 with hemin or ectopic overexpression of HO-1 in HMEC-1 perfectly mimicked the effect of 15d-PGJ(2) and led to increased VEGF production.	15d-pgj	107-114	heme oxygenase 1	Homo sapiens	59-63
12230869-9	2002	Importantly, the inhibition of the HO-1 pathway by tin protoporphyrin-IX significantly reduced the stimulatory effect of 15d-PGJ(2) on VEGF synthesis.	tin protoporphyrin IX	51-72	heme oxygenase 1	Homo sapiens	35-39
12230869-9	2002	Importantly, the inhibition of the HO-1 pathway by tin protoporphyrin-IX significantly reduced the stimulatory effect of 15d-PGJ(2) on VEGF synthesis.	15d-pgj	121-128	heme oxygenase 1	Homo sapiens	35-39
12230871-3	2002	Here we present an overview of the heme degradation processes and relevant disorders by focusing on heme oxygenase-1 (HO-1), a key enzyme in heme catabolism.	Heme	35-39	heme oxygenase 1	Homo sapiens	100-116
12230871-3	2002	Here we present an overview of the heme degradation processes and relevant disorders by focusing on heme oxygenase-1 (HO-1), a key enzyme in heme catabolism.	Heme	35-39	heme oxygenase 1	Homo sapiens	118-122
12130498-2	2002	Deficiency of the heme-catabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium.	Heme	18-22	heme oxygenase 1	Homo sapiens	44-60
12130498-2	2002	Deficiency of the heme-catabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium.	Heme	18-22	heme oxygenase 1	Homo sapiens	62-66
12130498-2	2002	Deficiency of the heme-catabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium.	Heme	44-48	heme oxygenase 1	Homo sapiens	62-66
12230871-4	2002	HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin.	Oxygen	74-80	heme oxygenase 1	Homo sapiens	0-4
12230871-4	2002	HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin.	tetrapyrrole biliverdin	101-124	heme oxygenase 1	Homo sapiens	0-4
12230871-4	2002	HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin.	Carbon Monoxide	126-141	heme oxygenase 1	Homo sapiens	0-4
12230871-4	2002	HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin.	Iron	155-159	heme oxygenase 1	Homo sapiens	0-4
12230871-4	2002	HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin.	Biliverdine	114-124	heme oxygenase 1	Homo sapiens	0-4
12151344-0	2002	Expression of interleukin-8, heme oxygenase-1 and vascular endothelial growth factor in DLD-1 colon carcinoma cells exposed to pyrrolidine dithiocarbamate.	pyrrolidine dithiocarbamic acid	127-154	heme oxygenase 1	Homo sapiens	29-45
12230871-4	2002	HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin.	Bilirubin	194-203	heme oxygenase 1	Homo sapiens	0-4
12230873-0	2002	Regulation of heme oxygenase-1 by redox signals involving nitric oxide.	Nitric Oxide	58-70	heme oxygenase 1	Homo sapiens	14-30
12230873-2	2002	The importance of this protein in physiology and disease is underlined by the versatility of HO-1 inducers and the functional role attributed to HO-1 products (carbon monoxide and bilirubin) in conditions that are associated with moderate or severe cellular stress.	Carbon Monoxide	160-175	heme oxygenase 1	Homo sapiens	145-149
12230873-2	2002	The importance of this protein in physiology and disease is underlined by the versatility of HO-1 inducers and the functional role attributed to HO-1 products (carbon monoxide and bilirubin) in conditions that are associated with moderate or severe cellular stress.	Bilirubin	180-189	heme oxygenase 1	Homo sapiens	145-149
12230873-3	2002	An intriguing aspect is the recent evidence showing that nitric oxide, a ubiquitous signaling molecule, finely modulates the activation of HO-1 expression.	Nitric Oxide	57-69	heme oxygenase 1	Homo sapiens	139-143
12230873-4	2002	As the effects of oxidative stress on the regulation of the HO-1 gene have been well established and characterized, this review will focus on the biological relevance of redox signals involving nitric oxide and reactive nitrogen species that lead to up-regulation of the HO-1 pathway, with particular emphasis on vascular tissues and the cardiovascular system.	Nitric Oxide	194-206	heme oxygenase 1	Homo sapiens	60-64
12230873-4	2002	As the effects of oxidative stress on the regulation of the HO-1 gene have been well established and characterized, this review will focus on the biological relevance of redox signals involving nitric oxide and reactive nitrogen species that lead to up-regulation of the HO-1 pathway, with particular emphasis on vascular tissues and the cardiovascular system.	Nitric Oxide	194-206	heme oxygenase 1	Homo sapiens	271-275
12230873-4	2002	As the effects of oxidative stress on the regulation of the HO-1 gene have been well established and characterized, this review will focus on the biological relevance of redox signals involving nitric oxide and reactive nitrogen species that lead to up-regulation of the HO-1 pathway, with particular emphasis on vascular tissues and the cardiovascular system.	reactive nitrogen	211-228	heme oxygenase 1	Homo sapiens	60-64
12230873-4	2002	As the effects of oxidative stress on the regulation of the HO-1 gene have been well established and characterized, this review will focus on the biological relevance of redox signals involving nitric oxide and reactive nitrogen species that lead to up-regulation of the HO-1 pathway, with particular emphasis on vascular tissues and the cardiovascular system.	reactive nitrogen	211-228	heme oxygenase 1	Homo sapiens	271-275
12222997-4	2002	An association of the relative increase (Delta, %) of these inflammatory markers with short (&lt;25) (GT)(n) dinucleotide repeats in the HO-1 gene promoter was assessed.	(n) dinucleotide	105-121	heme oxygenase 1	Homo sapiens	137-141
12227681-8	2002	Carvedilol increased plasma antioxidant power and HO-1 mRNA and reduced 3-nitrotyrosine and TGFbeta mRNA levels, while the same was not observed with nifedipine.	Carvedilol	0-10	heme oxygenase 1	Homo sapiens	50-54
12176442-0	2002	Heme oxygenase-1 gene transfer prevents CD95/FasL-mediated apoptosis and improves liver allograft survival via carbon monoxide signaling pathway.	Carbon Monoxide	111-126	heme oxygenase 1	Homo sapiens	0-16
12420741-0	2002	Management of oxidative stress by heme oxygenase-1 in cisplatin-induced toxicity in renal tubular cells.	Cisplatin	54-63	heme oxygenase 1	Homo sapiens	34-50
12420741-1	2002	Induction of heme oxygenase-1 (HO-1) may serve as an immediate protective response during treatment with the cytostatic drug cisplatin (CDDP).	Cisplatin	125-134	heme oxygenase 1	Homo sapiens	13-29
12420741-1	2002	Induction of heme oxygenase-1 (HO-1) may serve as an immediate protective response during treatment with the cytostatic drug cisplatin (CDDP).	Cisplatin	136-140	heme oxygenase 1	Homo sapiens	13-29
12057767-10	2002	Indeed, beta-carotene or lycopene (0.5-1.0 microM) led to a further 1.5-fold rise in the UVA-induced HO-1 mRNA levels.	beta Carotene	8-21	heme oxygenase 1	Homo sapiens	101-105
12082007-0	2002	Heme oxygenase-1-mediated protection: potential role of nonheme iron-nitric oxide complexes.	Iron	64-68	heme oxygenase 1	Homo sapiens	0-16
12082007-0	2002	Heme oxygenase-1-mediated protection: potential role of nonheme iron-nitric oxide complexes.	Nitric Oxide	69-81	heme oxygenase 1	Homo sapiens	0-16
12036874-0	2002	Heme oxygenase-1-derived carbon monoxide is an autocrine inhibitor of vascular smooth muscle cell growth.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
12036874-3	2002	The induction of HO-1 expression by serum was inhibited by actinomycin D or cycloheximide.	Dactinomycin	59-72	heme oxygenase 1	Homo sapiens	17-21
12036874-3	2002	The induction of HO-1 expression by serum was inhibited by actinomycin D or cycloheximide.	Cycloheximide	76-89	heme oxygenase 1	Homo sapiens	17-21
12057767-10	2002	Indeed, beta-carotene or lycopene (0.5-1.0 microM) led to a further 1.5-fold rise in the UVA-induced HO-1 mRNA levels.	Lycopene	25-33	heme oxygenase 1	Homo sapiens	101-105
12118938-4	2002	However, the resistance of the HO-1 transfected VSMC against H2O2 was significantly raised.	Hydrogen Peroxide	61-65	heme oxygenase 1	Homo sapiens	31-35
12118938-5	2002	This protective effect was dramatically diminished when the transfected VSMC were pretreated with ZnPP-IX, a specific inhibitor of HO, for 24 h. In addition, we found that the growth potential of the transfected cells was significantly inhibited directly by increased activity of HO-1, and this effect might be related to decreased phosphorylation of MAPK.	zinc protoporphyrin	98-105	heme oxygenase 1	Homo sapiens	280-284
12182912-3	2002	A (GT)(n) dinucleotide repeat in the HO-1 gene promoter shows a length polymorphism that modulates the level of gene transcription.	(n) dinucleotide	6-22	heme oxygenase 1	Homo sapiens	37-41
11880364-0	2002	Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	0-16
11880364-1	2002	We have shown that carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) protects endothelial cells (EC) from tumor necrosis alpha (TNF-alpha)-mediated apoptosis.	Carbon Monoxide	19-34	heme oxygenase 1	Homo sapiens	53-69
11880364-1	2002	We have shown that carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) protects endothelial cells (EC) from tumor necrosis alpha (TNF-alpha)-mediated apoptosis.	Carbon Monoxide	19-34	heme oxygenase 1	Homo sapiens	71-75
11880364-1	2002	We have shown that carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) protects endothelial cells (EC) from tumor necrosis alpha (TNF-alpha)-mediated apoptosis.	Carbon Monoxide	36-38	heme oxygenase 1	Homo sapiens	53-69
11880364-1	2002	We have shown that carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) protects endothelial cells (EC) from tumor necrosis alpha (TNF-alpha)-mediated apoptosis.	Carbon Monoxide	36-38	heme oxygenase 1	Homo sapiens	71-75
12166345-6	2002	These results suggest that HO-1 is up-regulated through heme-independent stimuli according to the development of portal hypertension, and that induced HO-1 plays a pathophysiological role in portal hypertension through carbon monoxide production.	Carbon Monoxide	219-234	heme oxygenase 1	Homo sapiens	27-31
12166345-6	2002	These results suggest that HO-1 is up-regulated through heme-independent stimuli according to the development of portal hypertension, and that induced HO-1 plays a pathophysiological role in portal hypertension through carbon monoxide production.	Carbon Monoxide	219-234	heme oxygenase 1	Homo sapiens	151-155
12028803-6	2002	Moreover, HO-1 expression was positively correlated to the higher organic carbon (OC) and polyaromatic hydrocarbons (PAHs) content of fine versus coarse PM, as well as the rise in PAH content that occurs in coarse PM during the winter months.	Carbon	74-80	heme oxygenase 1	Homo sapiens	10-14
12028803-6	2002	Moreover, HO-1 expression was positively correlated to the higher organic carbon (OC) and polyaromatic hydrocarbons (PAHs) content of fine versus coarse PM, as well as the rise in PAH content that occurs in coarse PM during the winter months.	polyaromatic hydrocarbons	90-115	heme oxygenase 1	Homo sapiens	10-14
12028803-6	2002	Moreover, HO-1 expression was positively correlated to the higher organic carbon (OC) and polyaromatic hydrocarbons (PAHs) content of fine versus coarse PM, as well as the rise in PAH content that occurs in coarse PM during the winter months.	pahs	117-121	heme oxygenase 1	Homo sapiens	10-14
12028803-6	2002	Moreover, HO-1 expression was positively correlated to the higher organic carbon (OC) and polyaromatic hydrocarbons (PAHs) content of fine versus coarse PM, as well as the rise in PAH content that occurs in coarse PM during the winter months.	p-Aminohippuric Acid	117-120	heme oxygenase 1	Homo sapiens	10-14
11773068-10	2002	The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected.	carbonyl sulfide	105-108	heme oxygenase 1	Homo sapiens	96-100
12006180-4	2002	Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin.	Carbon Monoxide	129-144	heme oxygenase 1	Homo sapiens	62-78
12006180-4	2002	Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin.	Carbon Monoxide	129-144	heme oxygenase 1	Homo sapiens	80-84
12006180-4	2002	Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin.	Carbon Monoxide	146-148	heme oxygenase 1	Homo sapiens	62-78
12006180-4	2002	Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin.	Carbon Monoxide	146-148	heme oxygenase 1	Homo sapiens	80-84
12006180-4	2002	Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin.	Bilirubin	154-163	heme oxygenase 1	Homo sapiens	62-78
12006180-4	2002	Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin.	Bilirubin	154-163	heme oxygenase 1	Homo sapiens	80-84
12006183-0	2002	Modulation of endothelial cell apoptosis by heme oxygenase-1-derived carbon monoxide.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	44-60
12006183-3	2002	We have also shown that the antiapoptotic effect of HO-1 is mediated through heme catabolism into the gas carbon monoxide (CO).	Heme	77-81	heme oxygenase 1	Homo sapiens	52-56
12006183-3	2002	We have also shown that the antiapoptotic effect of HO-1 is mediated through heme catabolism into the gas carbon monoxide (CO).	Carbon Monoxide	106-121	heme oxygenase 1	Homo sapiens	52-56
12006183-3	2002	We have also shown that the antiapoptotic effect of HO-1 is mediated through heme catabolism into the gas carbon monoxide (CO).	Carbon Monoxide	123-125	heme oxygenase 1	Homo sapiens	52-56
12042071-8	2002	Okadaic acid also induced heme oxygenase-1 mRNA in both cell lines, but the magnitude of induction was only twofold, and was rapid and transient.	Okadaic Acid	0-12	heme oxygenase 1	Homo sapiens	26-42
12042071-9	2002	Okadaic acid and phorbol 12-myristate 13-acetate significantly decreased heme-mediated induction of heme oxygenase-1 mRNA in both Huh-7 and HepG2 cells.	Okadaic Acid	0-12	heme oxygenase 1	Homo sapiens	100-116
12042071-9	2002	Okadaic acid and phorbol 12-myristate 13-acetate significantly decreased heme-mediated induction of heme oxygenase-1 mRNA in both Huh-7 and HepG2 cells.	Tetradecanoylphorbol Acetate	17-48	heme oxygenase 1	Homo sapiens	100-116
12042071-9	2002	Okadaic acid and phorbol 12-myristate 13-acetate significantly decreased heme-mediated induction of heme oxygenase-1 mRNA in both Huh-7 and HepG2 cells.	Heme	73-77	heme oxygenase 1	Homo sapiens	100-116
12042071-10	2002	Wortmannin diminished the heme-mediated induction of heme oxygenase-1 mRNA in HepG2 cells, but not Huh-7 cells.	Wortmannin	0-10	heme oxygenase 1	Homo sapiens	53-69
12042071-10	2002	Wortmannin diminished the heme-mediated induction of heme oxygenase-1 mRNA in HepG2 cells, but not Huh-7 cells.	Heme	26-30	heme oxygenase 1	Homo sapiens	53-69
12042074-1	2002	Heme-hemopexin coordinately regulates genes encoding protective proteins including metallothionein-I (MT-I) and heme oxygenase 1 (HO-1).	Heme	0-4	heme oxygenase 1	Homo sapiens	112-128
12042074-1	2002	Heme-hemopexin coordinately regulates genes encoding protective proteins including metallothionein-I (MT-I) and heme oxygenase 1 (HO-1).	Heme	0-4	heme oxygenase 1	Homo sapiens	130-134
12042074-2	2002	Hexamethylene-bisacetamide (HMBA), which induces differentiation and activates protein kinase C (PKC), synergistically augments the induction of both MT-I and MT-II mRNAs in response to heme-hemopexin, but attenuates the induction of HO-1.	hexamethylene bisacetamide	0-26	heme oxygenase 1	Homo sapiens	234-238
12042074-2	2002	Hexamethylene-bisacetamide (HMBA), which induces differentiation and activates protein kinase C (PKC), synergistically augments the induction of both MT-I and MT-II mRNAs in response to heme-hemopexin, but attenuates the induction of HO-1.	hexamethylene bisacetamide	28-32	heme oxygenase 1	Homo sapiens	234-238
12042074-2	2002	Hexamethylene-bisacetamide (HMBA), which induces differentiation and activates protein kinase C (PKC), synergistically augments the induction of both MT-I and MT-II mRNAs in response to heme-hemopexin, but attenuates the induction of HO-1.	Heme	186-190	heme oxygenase 1	Homo sapiens	234-238
12042074-4	2002	Unlike the PKC-activating phorbol esters that induce MT-I and HO-1, HMBA has minimal effects on MT-I or HO-1.	Phorbol Esters	26-40	heme oxygenase 1	Homo sapiens	62-66
12449018-6	2002	Finally, OxPAPC-induced expression of HO-1 was blocked by a platelet-activating factor (PAF) receptor antagonist.	oxpapc	9-15	heme oxygenase 1	Homo sapiens	38-42
11773068-10	2002	The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected.	Superoxides	189-205	heme oxygenase 1	Homo sapiens	96-100
11773068-10	2002	The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected.	Superoxides	207-211	heme oxygenase 1	Homo sapiens	96-100
11773068-10	2002	The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected.	Vitamin K 3	225-234	heme oxygenase 1	Homo sapiens	96-100
11773068-10	2002	The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected.	Heme	271-275	heme oxygenase 1	Homo sapiens	96-100
11854143-7	2002	The levels of the CYP1A1 and CYP1B1 mRNAs induced by BAP were not significantly affected by coexposure to NaAsO(2); however, heme oxygenase 1 mRNA levels were markedly induced by coexposure to BAP and NaAsO(2).	naaso	201-206	heme oxygenase 1	Homo sapiens	125-141
11854435-0	2002	Caffeic acid phenethyl ester and curcumin: a novel class of heme oxygenase-1 inducers.	caffeic acid phenethyl ester	0-28	heme oxygenase 1	Homo sapiens	60-76
11854435-0	2002	Caffeic acid phenethyl ester and curcumin: a novel class of heme oxygenase-1 inducers.	Curcumin	33-41	heme oxygenase 1	Homo sapiens	60-76
11854435-2	2002	Curcumin, a polyphenolic natural compound that possesses anti-tumor and anti-inflammatory properties, has been reported recently to induce potently HO-1 expression in vascular endothelial cells (Free Rad Biol Med 28:1303-1312, 2000).	Curcumin	0-8	heme oxygenase 1	Homo sapiens	148-152
11854435-3	2002	Here, we extend our previous findings by showing that caffeic acid phenethyl ester (CAPE), another plant-derived phenolic agent, markedly increases heme oxygenase activity and HO-1 protein in astrocytes.	caffeic acid phenethyl ester	54-82	heme oxygenase 1	Homo sapiens	176-180
11854435-3	2002	Here, we extend our previous findings by showing that caffeic acid phenethyl ester (CAPE), another plant-derived phenolic agent, markedly increases heme oxygenase activity and HO-1 protein in astrocytes.	caffeic acid phenethyl ester	84-88	heme oxygenase 1	Homo sapiens	176-180
11854435-9	2002	These data suggest that regulation of HO-1 expression by polyphenolic compounds is evoked by a distinctive mechanism which is not necessarily linked to changes in glutathione but might depend on redox signals sustained by specific and targeted sulfydryl groups.	Glutathione	163-174	heme oxygenase 1	Homo sapiens	38-42
11854435-9	2002	These data suggest that regulation of HO-1 expression by polyphenolic compounds is evoked by a distinctive mechanism which is not necessarily linked to changes in glutathione but might depend on redox signals sustained by specific and targeted sulfydryl groups.	sulfydryl	244-253	heme oxygenase 1	Homo sapiens	38-42
11930234-1	2002	The heme oxygenase-1 (HO-1), a rate-limiting enzyme in heme metabolism, has been recently defined as a novel stress-stimulated protein, since the intracellular expression of HO-1 in response to various stimuli as oxidation, ischemia and endotoxin injury has been proved to be able to protect the cells from damage.	Heme	4-8	heme oxygenase 1	Homo sapiens	174-178
11930234-5	2002	It was found that the HO-1 transfected-VSMCs presented dominant resistance to toxicity produced by exposure to H2O2, as a significant protective effect of HO-1 marked by cell survival and LDH leakage was observed when 200, 400 and 600 micromol/L of H2O2 were used.	Hydrogen Peroxide	111-115	heme oxygenase 1	Homo sapiens	22-26
11930234-1	2002	The heme oxygenase-1 (HO-1), a rate-limiting enzyme in heme metabolism, has been recently defined as a novel stress-stimulated protein, since the intracellular expression of HO-1 in response to various stimuli as oxidation, ischemia and endotoxin injury has been proved to be able to protect the cells from damage.	Heme	4-8	heme oxygenase 1	Homo sapiens	22-26
11930234-5	2002	It was found that the HO-1 transfected-VSMCs presented dominant resistance to toxicity produced by exposure to H2O2, as a significant protective effect of HO-1 marked by cell survival and LDH leakage was observed when 200, 400 and 600 micromol/L of H2O2 were used.	Hydrogen Peroxide	111-115	heme oxygenase 1	Homo sapiens	155-159
11930234-5	2002	It was found that the HO-1 transfected-VSMCs presented dominant resistance to toxicity produced by exposure to H2O2, as a significant protective effect of HO-1 marked by cell survival and LDH leakage was observed when 200, 400 and 600 micromol/L of H2O2 were used.	Hydrogen Peroxide	249-253	heme oxygenase 1	Homo sapiens	22-26
11930234-6	2002	The protection of HO-1 rapidly declined after the transfected-VSMCs were pretreated 24 h with an HO-1 specific inhibitor (ZnPP-IX).	zinc protoporphyrin	122-129	heme oxygenase 1	Homo sapiens	18-22
11930234-6	2002	The protection of HO-1 rapidly declined after the transfected-VSMCs were pretreated 24 h with an HO-1 specific inhibitor (ZnPP-IX).	zinc protoporphyrin	122-129	heme oxygenase 1	Homo sapiens	97-101
11930234-7	2002	The results of this investigation suggest that the functional expression of HO-1 gene within VSMCs raises an alternative ability to protect the vascular cells against active oxygen injury.	Oxygen	174-180	heme oxygenase 1	Homo sapiens	76-80
11829463-11	2002	We conclude that an increase in endothelial cell HO-1 activity with subsequent generation of carbon monoxide, elicited by gene transfer, reversed the PDTC-mediated abnormalities in cell cycle progression and is thus a potential therapeutic means for attenuating the effects of oxidative stress-causing agents.	Carbon Monoxide	93-108	heme oxygenase 1	Homo sapiens	49-53
11854317-2	2002	This study examined the induction of heme oxygenase-1 (HO-1), a carbon monoxide-generating inducible enzyme, in modulation of spermatogenesis.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	37-53
11820797-0	2002	Heme oxygenase-1 induction may explain the antioxidant profile of pentaerythrityl trinitrate.	pentrinitrol	66-92	heme oxygenase 1	Homo sapiens	0-16
11820797-2	2002	In cultured endothelial cells derived from human umbilical vein, the active PETN metabolite PETriN (0.01-1 mM) increased heme oxygenase (HO)-1 mRNA and protein levels in a concentration-dependent fashion.	Pentaerythritol Tetranitrate	76-80	heme oxygenase 1	Homo sapiens	121-142
11820797-2	2002	In cultured endothelial cells derived from human umbilical vein, the active PETN metabolite PETriN (0.01-1 mM) increased heme oxygenase (HO)-1 mRNA and protein levels in a concentration-dependent fashion.	pentrinitrol	92-98	heme oxygenase 1	Homo sapiens	121-142
11854317-2	2002	This study examined the induction of heme oxygenase-1 (HO-1), a carbon monoxide-generating inducible enzyme, in modulation of spermatogenesis.	Carbon Monoxide	64-79	heme oxygenase 1	Homo sapiens	55-59
11854317-4	2002	CdCl(2)-treated testes increased HO-1 activity and suppressed microsomal cytochromes P450, which are required for steroidogenesis.	Cadmium Chloride	0-7	heme oxygenase 1	Homo sapiens	33-37
11854317-5	2002	CdCl(2)-elicited HO-1 occurred mostly in Leydig cells and coincided with CO generation, as judged by bilirubin-IXalpha immunoreactivity.	Cadmium Chloride	0-7	heme oxygenase 1	Homo sapiens	17-21
11854317-5	2002	CdCl(2)-elicited HO-1 occurred mostly in Leydig cells and coincided with CO generation, as judged by bilirubin-IXalpha immunoreactivity.	Bilirubin	101-110	heme oxygenase 1	Homo sapiens	17-21
11928711-3	2002	Exposure of mammalian cells to oxidative stimuli induces heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, as well as the 32-kDa heat shock protein.	Heme	57-61	heme oxygenase 1	Homo sapiens	75-79
12112002-2	2002	Here we show that NO donors including sodium nitroprusside (SNP) and spermine nonoate (SP-NO), and PGE(2) significantly stimulate HO-1 expression in RAW264.7 macrophages, associated with alternative induction on NO and PGE(2) in medium, respectively.	Nitroprusside	38-58	heme oxygenase 1	Homo sapiens	130-134
11707454-2	2002	Depletion of nutrients results in cellular stress, which evokes adaptive and protective responses, one of which is the induction of heme oxygenase-1 (HO-1), a 32-kDa endoplasmic reticulum enzyme that catalyzes the rate-limiting step in heme degradation.	Heme	132-136	heme oxygenase 1	Homo sapiens	150-154
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Glucose	44-51	heme oxygenase 1	Homo sapiens	89-93
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Glucose	44-51	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Glucose	187-194	heme oxygenase 1	Homo sapiens	89-93
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Glucose	187-194	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Fructose	307-315	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Galactose	317-326	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Mannose	328-335	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Deoxyglucose	341-355	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Glucose	187-194	heme oxygenase 1	Homo sapiens	89-93
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	Glucose	187-194	heme oxygenase 1	Homo sapiens	218-222
11707454-3	2002	Incubation of HepG2 human hepatoma cells in glucose-free medium resulted in an increased HO-1 mRNA content, reaching a maximum of approximately 25-fold over control cells after 12 h. The glucose-dependent induction of HO-1 mRNA was concentration-dependent (k(12) approximately 0.5 mm) and was attenuated by fructose, galactose, mannose, and 2-deoxyglucose, but not by the non-metabolizable glucose analog, 3-O-methylglucose.	3-O-Methylglucose	406-423	heme oxygenase 1	Homo sapiens	218-222
11707454-5	2002	These results demonstrate that glucose availability regulates transcription of the HO-1 gene via a pathway that is different from the unfolded protein response.	Glucose	31-38	heme oxygenase 1	Homo sapiens	83-87
12489116-3	2002	Using treatment of cell cultures with hyperbaric oxygen (HBO) as a model for oxidative stress, we have shown an induction of HO-1 in isolated human lymphocytes after a single HBO exposure and protection of these cells against DNA damage by subsequent oxidative stress.	Oxygen	49-55	heme oxygenase 1	Homo sapiens	125-129
11948696-4	2002	In cells transduced by HOP-driven HO-1 gene, there was a decrease in basal cyclooxygenase (COX) activity as measured by PGE(2).	Prostaglandins E	120-123	heme oxygenase 1	Homo sapiens	34-38
11948696-5	2002	The degree of HO-1 expression and, consequently, the levels of cellular heme were directly related to COX activity.	Heme	72-76	heme oxygenase 1	Homo sapiens	14-18
12112002-6	2002	And, NSAIDs aspirin and diclofenase dose dependently inhibited LPS/IFN-gamma-induced HO-1 protein accompanied by suppression of PGE(2) (not NO) production.	diclofenase	24-35	heme oxygenase 1	Homo sapiens	85-89
12112002-7	2002	PD98059 (a specific inhibitor of MEKK), but not SB203580 (a specific inhibitor of p38 kinase), attenuated PGE(2) (not SP-NO) induced HO-1 protein.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	0-7	heme oxygenase 1	Homo sapiens	133-137
12112002-7	2002	PD98059 (a specific inhibitor of MEKK), but not SB203580 (a specific inhibitor of p38 kinase), attenuated PGE(2) (not SP-NO) induced HO-1 protein.	Prostaglandins E	106-109	heme oxygenase 1	Homo sapiens	133-137
12112002-8	2002	Under UVC (100 J/m(2)) and UVB (50 J/m(2)) irradiation, PGE(2) or SP-NO treatment prevents cells from UVC or UVB-induced cell death, and HO-1 inhibitor tin protoporphyrin (SnPP) reverses the preventive effects of PGE(2) and SP-NO.	Prostaglandins E	56-59	heme oxygenase 1	Homo sapiens	137-141
12112002-8	2002	Under UVC (100 J/m(2)) and UVB (50 J/m(2)) irradiation, PGE(2) or SP-NO treatment prevents cells from UVC or UVB-induced cell death, and HO-1 inhibitor tin protoporphyrin (SnPP) reverses the preventive effects of PGE(2) and SP-NO.	sp-no	66-71	heme oxygenase 1	Homo sapiens	137-141
12112002-8	2002	Under UVC (100 J/m(2)) and UVB (50 J/m(2)) irradiation, PGE(2) or SP-NO treatment prevents cells from UVC or UVB-induced cell death, and HO-1 inhibitor tin protoporphyrin (SnPP) reverses the preventive effects of PGE(2) and SP-NO.	tin protoporphyrin IX	152-170	heme oxygenase 1	Homo sapiens	137-141
12112002-10	2002	These results demonstrated that inflammatory molecules NO and PGE(2) were potent inducers of HO-1 gene, and protected cells from UV-irradiation-induced cell death through HO-1 induction.	Prostaglandins E	62-65	heme oxygenase 1	Homo sapiens	93-97
12112002-10	2002	These results demonstrated that inflammatory molecules NO and PGE(2) were potent inducers of HO-1 gene, and protected cells from UV-irradiation-induced cell death through HO-1 induction.	Prostaglandins E	62-65	heme oxygenase 1	Homo sapiens	171-175
12112002-2	2002	Here we show that NO donors including sodium nitroprusside (SNP) and spermine nonoate (SP-NO), and PGE(2) significantly stimulate HO-1 expression in RAW264.7 macrophages, associated with alternative induction on NO and PGE(2) in medium, respectively.	spermine nitric oxide complex	69-85	heme oxygenase 1	Homo sapiens	130-134
12112002-2	2002	Here we show that NO donors including sodium nitroprusside (SNP) and spermine nonoate (SP-NO), and PGE(2) significantly stimulate HO-1 expression in RAW264.7 macrophages, associated with alternative induction on NO and PGE(2) in medium, respectively.	sp-no	87-92	heme oxygenase 1	Homo sapiens	130-134
12112002-2	2002	Here we show that NO donors including sodium nitroprusside (SNP) and spermine nonoate (SP-NO), and PGE(2) significantly stimulate HO-1 expression in RAW264.7 macrophages, associated with alternative induction on NO and PGE(2) in medium, respectively.	Prostaglandins E	99-102	heme oxygenase 1	Homo sapiens	130-134
12112002-4	2002	In the presence of lipopolysaccharide and interferon-gamma (LPS/IFN-gamma), HO-1 protein was induced slightly but significantly, and SNP, SP-NO, and PGE(2) enhanced HO-1 protein induced by LPS/IFN-gamma.	sp-no	138-143	heme oxygenase 1	Homo sapiens	165-169
12112002-4	2002	In the presence of lipopolysaccharide and interferon-gamma (LPS/IFN-gamma), HO-1 protein was induced slightly but significantly, and SNP, SP-NO, and PGE(2) enhanced HO-1 protein induced by LPS/IFN-gamma.	Prostaglandins E	149-152	heme oxygenase 1	Homo sapiens	165-169
12112002-5	2002	L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production.	Arginine	0-10	heme oxygenase 1	Homo sapiens	109-113
12112002-5	2002	L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production.	n-nitro-l-arginine methyl ester	19-50	heme oxygenase 1	Homo sapiens	109-113
12397597-5	2002	Endothelial cells stably transfected with the retrovirus containing the human HO-1 gene exhibited a several-fold increase in HO-1 protein levels, which was accompanied by an increase in HO activity and a marked decrease in PGE(2) and 6-keto PGF(1alpha) levels.	Prostaglandins E	223-226	heme oxygenase 1	Homo sapiens	78-82
12112002-5	2002	L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production.	NG-Nitroarginine Methyl Ester	52-58	heme oxygenase 1	Homo sapiens	109-113
12397597-5	2002	Endothelial cells stably transfected with the retrovirus containing the human HO-1 gene exhibited a several-fold increase in HO-1 protein levels, which was accompanied by an increase in HO activity and a marked decrease in PGE(2) and 6-keto PGF(1alpha) levels.	6-keto pgf	234-244	heme oxygenase 1	Homo sapiens	78-82
12112002-5	2002	L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production.	Nitroarginine	19-37	heme oxygenase 1	Homo sapiens	109-113
12397597-5	2002	Endothelial cells stably transfected with the retrovirus containing the human HO-1 gene exhibited a several-fold increase in HO-1 protein levels, which was accompanied by an increase in HO activity and a marked decrease in PGE(2) and 6-keto PGF(1alpha) levels.	6-keto pgf	234-244	heme oxygenase 1	Homo sapiens	125-129
12397597-10	2002	The levels of PGI(2) decreased in cells transduced with HO-1 sense and increased in cells transduced with HO-1 in antisense orientation.	Epoprostenol	14-20	heme oxygenase 1	Homo sapiens	56-60
12112002-5	2002	L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production.	Nitroarginine	84-87	heme oxygenase 1	Homo sapiens	109-113
12397597-10	2002	The levels of PGI(2) decreased in cells transduced with HO-1 sense and increased in cells transduced with HO-1 in antisense orientation.	Epoprostenol	14-20	heme oxygenase 1	Homo sapiens	106-110
12112002-5	2002	L-Arginine analogs N-nitro-L-arginine methyl ester (L-NAME) and N-nitro-L-arginine (NLA) significantly block HO-1 protein induced by LPS/IFN-gamma associated with a decrease in NO (not PGE(2)) production.	Prostaglandins E	185-188	heme oxygenase 1	Homo sapiens	109-113
12397597-13	2002	Tin mesoporphyrin (SnMP) reversed the protective effect of HO-1.	tin mesoporphyrin	0-17	heme oxygenase 1	Homo sapiens	59-63
12397597-13	2002	Tin mesoporphyrin (SnMP) reversed the protective effect of HO-1.	tin mesoporphyrin	19-23	heme oxygenase 1	Homo sapiens	59-63
12112002-6	2002	And, NSAIDs aspirin and diclofenase dose dependently inhibited LPS/IFN-gamma-induced HO-1 protein accompanied by suppression of PGE(2) (not NO) production.	Aspirin	12-19	heme oxygenase 1	Homo sapiens	85-89
11925914-8	2002	Third, we demonstrated that exhaled carbon monoxide concentrations caused by heme oxygenase-1 upregulation, may be a useful noninvasive means of monitoring airway inflammation and of controlling elderly patients with bronchial asthma.	Carbon Monoxide	36-51	heme oxygenase 1	Homo sapiens	77-93
11752115-5	2002	Endothelial cells stably transfected with the human HO-1 gene exhibited a severalfold increase in human HO-1 mRNA levels, which was accompanied by an increase in HO activity and a marked decrease in prostaglandin (PG) E(2) and 6-keto-PGF(1alpha) levels.	Prostaglandins E	199-219	heme oxygenase 1	Homo sapiens	52-56
11752115-5	2002	Endothelial cells stably transfected with the human HO-1 gene exhibited a severalfold increase in human HO-1 mRNA levels, which was accompanied by an increase in HO activity and a marked decrease in prostaglandin (PG) E(2) and 6-keto-PGF(1alpha) levels.	Prostaglandins E	199-219	heme oxygenase 1	Homo sapiens	104-108
11752115-5	2002	Endothelial cells stably transfected with the human HO-1 gene exhibited a severalfold increase in human HO-1 mRNA levels, which was accompanied by an increase in HO activity and a marked decrease in prostaglandin (PG) E(2) and 6-keto-PGF(1alpha) levels.	6-keto-pgf	227-237	heme oxygenase 1	Homo sapiens	52-56
11752115-5	2002	Endothelial cells stably transfected with the human HO-1 gene exhibited a severalfold increase in human HO-1 mRNA levels, which was accompanied by an increase in HO activity and a marked decrease in prostaglandin (PG) E(2) and 6-keto-PGF(1alpha) levels.	6-keto-pgf	227-237	heme oxygenase 1	Homo sapiens	104-108
11752115-6	2002	Exposure of cells to CoCl(2), an inducer of HO-1 gene expression, resulted in increases in HO-1 protein levels and HO activity.	cobaltous chloride	21-28	heme oxygenase 1	Homo sapiens	44-48
11752115-6	2002	Exposure of cells to CoCl(2), an inducer of HO-1 gene expression, resulted in increases in HO-1 protein levels and HO activity.	cobaltous chloride	21-28	heme oxygenase 1	Homo sapiens	91-95
11752115-9	2002	The degree of HO-1 expression and, consequently, the level of cellular heme, were directly related to COX activity.	Heme	71-75	heme oxygenase 1	Homo sapiens	14-18
15499991-3	2002	Three isoforms of heme oxygenase (HO) have been described: two constitutively expressed isoforms, HO-2 and HO-3, and an inducible isoform, HO-1 that is increased as an adaptive response to several injurious stimuli including heme, hyperoxia, hypoxia, endotoxin and heavy metals.	Heme	18-22	heme oxygenase 1	Homo sapiens	139-143
11592943-0	2001	Mechanism of heme oxygenase-1 gene induction by curcumin in human renal proximal tubule cells.	Curcumin	48-56	heme oxygenase 1	Homo sapiens	13-29
11741586-0	2001	The effect of beta-carotene on the expression of interleukin-6 and heme oxygenase-1 in UV-irradiated human skin fibroblasts in vitro.	beta Carotene	14-27	heme oxygenase 1	Homo sapiens	67-83
11741586-2	2001	However, we recently demonstrated that beta-carotene has a pro-oxidant potential in cultured human skin fibroblasts because it enhances the UVA induction of heme oxygenase-1 (HO-1).	beta Carotene	39-52	heme oxygenase 1	Homo sapiens	157-173
11741586-2	2001	However, we recently demonstrated that beta-carotene has a pro-oxidant potential in cultured human skin fibroblasts because it enhances the UVA induction of heme oxygenase-1 (HO-1).	beta Carotene	39-52	heme oxygenase 1	Homo sapiens	175-179
11741586-4	2001	Singlet oxygen quencher sodium azide abrogated up-regulation of IL-6, and likewise also of HO-1.	Sodium Azide	24-36	heme oxygenase 1	Homo sapiens	91-95
11592943-5	2001	Surprisingly, curcumin by itself was a very potent inducer of HO-1.	Curcumin	14-22	heme oxygenase 1	Homo sapiens	62-66
11592943-7	2001	To evaluate the mechanism of curcumin-mediated induction of HO-1, confluent human renal proximal tubule cells were exposed to curcumin (1-8 microM).	Curcumin	29-37	heme oxygenase 1	Homo sapiens	60-64
11751428-0	2001	Involvement of heme oxygenase-1 (HO-1) in the adaptive protection of human lymphocytes after hyperbaric oxygen (HBO) treatment.	Oxygen	20-26	heme oxygenase 1	Homo sapiens	33-37
11751428-2	2001	Our previous studies on hyperbaric oxygen (HBO; i.e. exposure to pure oxygen under high ambient pressure) indicated clearly increased levels of HO-1 in lymphocytes of volunteers 24 h after HBO treatment (1 h at 1.5 bar).	Oxygen	35-41	heme oxygenase 1	Homo sapiens	144-148
11751428-2	2001	Our previous studies on hyperbaric oxygen (HBO; i.e. exposure to pure oxygen under high ambient pressure) indicated clearly increased levels of HO-1 in lymphocytes of volunteers 24 h after HBO treatment (1 h at 1.5 bar).	Oxygen	70-76	heme oxygenase 1	Homo sapiens	144-148
11751428-8	2001	Treatment with the specific HO-1 inhibitor tin-mesoporphyrin IX (SnMP) led to a complete abrogation of HBO-induced adaptive protection in human lymphocytes.	tin-mesoporphyrin ix	43-63	heme oxygenase 1	Homo sapiens	28-32
11751428-8	2001	Treatment with the specific HO-1 inhibitor tin-mesoporphyrin IX (SnMP) led to a complete abrogation of HBO-induced adaptive protection in human lymphocytes.	tin mesoporphyrin	65-69	heme oxygenase 1	Homo sapiens	28-32
11728461-0	2001	Homocysteine attenuates endothelial haem oxygenase-1 induction by nitric oxide (NO) and hypoxia.	Homocysteine	0-12	heme oxygenase 1	Homo sapiens	36-52
11728461-0	2001	Homocysteine attenuates endothelial haem oxygenase-1 induction by nitric oxide (NO) and hypoxia.	Nitric Oxide	66-78	heme oxygenase 1	Homo sapiens	36-52
11728461-2	2001	Here, we examined how Hcy modulates the induction of the stress protein haem oxygenase-1 (HO-1) evoked by NO releasing agents and hypoxia in vascular endothelial cells.	Homocysteine	22-25	heme oxygenase 1	Homo sapiens	72-88
11728461-2	2001	Here, we examined how Hcy modulates the induction of the stress protein haem oxygenase-1 (HO-1) evoked by NO releasing agents and hypoxia in vascular endothelial cells.	Homocysteine	22-25	heme oxygenase 1	Homo sapiens	90-94
11728461-3	2001	We found that Hcy (0.5 mM) markedly reduced the increase in haem oxygenase activity and HO-1 protein expression induced by sodium nitroprusside (SNP, 0.5 mM) but did not affect HO-1 activation mediated by S-nitroso-N-acetyl-penicillamine.	Homocysteine	14-17	heme oxygenase 1	Homo sapiens	88-92
11728461-3	2001	We found that Hcy (0.5 mM) markedly reduced the increase in haem oxygenase activity and HO-1 protein expression induced by sodium nitroprusside (SNP, 0.5 mM) but did not affect HO-1 activation mediated by S-nitroso-N-acetyl-penicillamine.	Nitroprusside	123-143	heme oxygenase 1	Homo sapiens	88-92
11728461-5	2001	Interestingly, high levels of Hcy were also able to abolish hypoxia-mediated HO-1 expression in a concentration-dependent manner.	Homocysteine	30-33	heme oxygenase 1	Homo sapiens	77-81
11707736-5	2001	Increased HO-1 protein was associated with a brisk and early increase in catalytically active iron and a robust increase in cellular ferritin.	Iron	94-98	heme oxygenase 1	Homo sapiens	10-14
11592943-9	2001	Coincubation of curcumin with actinomycin D completely blocked the upregulation of HO-1 mRNA.	Curcumin	16-24	heme oxygenase 1	Homo sapiens	83-87
11592943-9	2001	Coincubation of curcumin with actinomycin D completely blocked the upregulation of HO-1 mRNA.	Dactinomycin	30-43	heme oxygenase 1	Homo sapiens	83-87
11592943-10	2001	Blockade of nuclear factor-kappaB (NF-kappaB) with an IkappaBalpha phosphorylation inhibitor attenuated curcumin-mediated induction of HO-1 mRNA and protein.	Curcumin	104-112	heme oxygenase 1	Homo sapiens	135-139
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Heme	60-64	heme oxygenase 1	Homo sapiens	0-16
11592943-11	2001	These data demonstrate that curcumin induces HO-1 mRNA and protein in renal proximal tubule cells.	Curcumin	28-36	heme oxygenase 1	Homo sapiens	45-49
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Heme	60-64	heme oxygenase 1	Homo sapiens	18-22
11592943-12	2001	HO-1 induction by curcumin is mediated, at least in part, via transcriptional mechanisms and involves the NF-kappaB pathway.	Curcumin	18-26	heme oxygenase 1	Homo sapiens	0-4
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Iron	88-92	heme oxygenase 1	Homo sapiens	0-16
11592948-2	2001	By Northern blot analysis, HO-1 mRNA expression was found to significantly increase in response to reduction of PO(2) in culture medium.	PO-2	112-117	heme oxygenase 1	Homo sapiens	27-31
11592948-4	2001	This hypoxia-induced upregulation of HO-1 mRNA was significantly blocked by HIF-1alpha inhibition with ferrous ammonium sulfate.	ammonium ferrous sulfate	103-127	heme oxygenase 1	Homo sapiens	37-41
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Heme	63-67	heme oxygenase 1	Homo sapiens	0-16
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Iron	88-92	heme oxygenase 1	Homo sapiens	18-22
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Heme	63-67	heme oxygenase 1	Homo sapiens	18-22
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Carbon Monoxide	71-86	heme oxygenase 1	Homo sapiens	0-16
11592948-6	2001	Both desferrioxamine and CoCl(2) markedly increased HIF-1alpha mRNA and protein levels and resulted in the upregulation of HO-1 mRNA but not HO-2.	Deferoxamine	5-20	heme oxygenase 1	Homo sapiens	123-127
11592948-6	2001	Both desferrioxamine and CoCl(2) markedly increased HIF-1alpha mRNA and protein levels and resulted in the upregulation of HO-1 mRNA but not HO-2.	cobaltous chloride	25-32	heme oxygenase 1	Homo sapiens	123-127
11592948-7	2001	Furthermore, inhibition of HIF-1alpha degradation by CBZ-LLL, an inhibitor of ubiquitin-proteasome, significantly increased HIF-1alpha protein and HO-1 mRNA but not HO-2 in these cells.	carbobenzoxy-leucyl-leucyl-leucine	53-60	heme oxygenase 1	Homo sapiens	147-151
11592948-8	2001	Using cis-element oligodeoxynucleotide transfection to specifically decoy HIF-1alpha and block HIF-1alpha binding, increased mRNA expression of HO-1 in response to hypoxia and CoCl(2) was attenuated.	cobaltous chloride	176-183	heme oxygenase 1	Homo sapiens	144-148
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Carbon Monoxide	71-86	heme oxygenase 1	Homo sapiens	18-22
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Bilirubin	88-97	heme oxygenase 1	Homo sapiens	0-16
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Bilirubin	88-97	heme oxygenase 1	Homo sapiens	18-22
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Iron	103-107	heme oxygenase 1	Homo sapiens	0-16
11668058-1	2001	Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron.	Iron	103-107	heme oxygenase 1	Homo sapiens	18-22
11668058-3	2001	Here, we investigated the effect of severe hypoxia and reoxygenation on HO-1 expression in cardiomyocytes and determined whether HO-1 and its product, bilirubin, have a protective role against reoxygenation damage.	Bilirubin	151-160	heme oxygenase 1	Homo sapiens	129-133
11668058-9	2001	These results indicate that the HO-1-bilirubin pathway can effectively defend hypoxic cardiomyocytes against reoxygenation injury and highlight the issue of heme availability in the cytoprotective action afforded by HO-1.	Bilirubin	37-46	heme oxygenase 1	Homo sapiens	32-36
11668058-9	2001	These results indicate that the HO-1-bilirubin pathway can effectively defend hypoxic cardiomyocytes against reoxygenation injury and highlight the issue of heme availability in the cytoprotective action afforded by HO-1.	Bilirubin	37-46	heme oxygenase 1	Homo sapiens	216-220
11668058-9	2001	These results indicate that the HO-1-bilirubin pathway can effectively defend hypoxic cardiomyocytes against reoxygenation injury and highlight the issue of heme availability in the cytoprotective action afforded by HO-1.	Heme	157-161	heme oxygenase 1	Homo sapiens	216-220
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	0-16
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Carbon Monoxide	94-109	heme oxygenase 1	Homo sapiens	18-22
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	0-16
11592943-1	2001	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin.	Biliverdine	115-125	heme oxygenase 1	Homo sapiens	18-22
11593038-5	2001	Overexpression of HO-1 AS was associated with a long-term decrease (45%) of endogenous HO-1 protein and an increase (167%) in unmetabolized exogenous heme in HMEC-1 cells.	Heme	150-154	heme oxygenase 1	Homo sapiens	18-22
11593038-6	2001	Carbon monoxide (CO) production in HO-1 S- or AS-transduced HMEC-1 cells after heme treatment was increased (159%) or decreased (50%), respectively, compared with nontransduced cells.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	35-39
11593038-6	2001	Carbon monoxide (CO) production in HO-1 S- or AS-transduced HMEC-1 cells after heme treatment was increased (159%) or decreased (50%), respectively, compared with nontransduced cells.	Carbon Monoxide	17-19	heme oxygenase 1	Homo sapiens	35-39
11593038-6	2001	Carbon monoxide (CO) production in HO-1 S- or AS-transduced HMEC-1 cells after heme treatment was increased (159%) or decreased (50%), respectively, compared with nontransduced cells.	Heme	79-83	heme oxygenase 1	Homo sapiens	35-39
11600581-6	2001	The detection of mRNA and protein for HO-1 and HO-2 in normal human endometrium suggests that the carbon monoxide/HO system may play a role in the local control of endometrial function.	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	38-51
11581219-6	2001	Differentiated ARPE-19 cells treated with tBH or H2O2 resulted in upregulation of the HO-1 and FGFR1 transcripts.	tert-Butylhydroperoxide	42-45	heme oxygenase 1	Homo sapiens	86-90
11581219-6	2001	Differentiated ARPE-19 cells treated with tBH or H2O2 resulted in upregulation of the HO-1 and FGFR1 transcripts.	Hydrogen Peroxide	49-53	heme oxygenase 1	Homo sapiens	86-90
11572959-7	2001	Macrophage-inducible NOS generates NO to kill other cells, whereas HO1 generates bilirubin to exert antioxidant cytoprotective effects and also provides cytoprotection by facilitating iron extrusion from cells.	Bilirubin	81-90	heme oxygenase 1	Homo sapiens	67-70
11571246-3	2001	METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells.	Hemin	204-209	heme oxygenase 1	Homo sapiens	100-104
11718398-1	2001	PURPOSE: To determine if an association exists between postdilation restenosis and heme oxygenase-1 (HO-1), which is induced by balloon injury and inhibits neointimal formation through the action of endogenous carbon monoxide.	Carbon Monoxide	210-225	heme oxygenase 1	Homo sapiens	83-99
11718398-1	2001	PURPOSE: To determine if an association exists between postdilation restenosis and heme oxygenase-1 (HO-1), which is induced by balloon injury and inhibits neointimal formation through the action of endogenous carbon monoxide.	Carbon Monoxide	210-225	heme oxygenase 1	Homo sapiens	101-105
11718398-2	2001	A dinucleotide repeat in the promoter region of the HO-1 gene shows a length polymorphism that modulates the level of gene transcription.	Dinucleoside Phosphates	2-14	heme oxygenase 1	Homo sapiens	52-56
11718398-7	2001	Patients with short (&lt;25 GT) dinucleotide repeats in the HO-1 gene promoter on either allele had restenosis significantly less often than patients with longer (&gt; or = 25 GT) dinucleotide repeats (p = 0.01).	Dinucleoside Phosphates	32-44	heme oxygenase 1	Homo sapiens	60-64
11768235-0	2001	Induction of heme oxygenase-1 by phenylarsine oxide.	oxophenylarsine	33-51	heme oxygenase 1	Homo sapiens	13-29
11768235-2	2001	Heme oxygenase-1, the major inducible isoform of heme oxygenase (HO), can be induced by heme and numerous other physical and chemical factors, many of which cause cellular "stress".	Heme	49-53	heme oxygenase 1	Homo sapiens	0-16
11768235-5	2001	We hypothesized that phenylarsine oxide (PAO), an inhibitor of protein tyrosine phosphatases (PTPs), might up-regulate the HO-1 gene.	oxophenylarsine	21-39	heme oxygenase 1	Homo sapiens	123-127
11768235-5	2001	We hypothesized that phenylarsine oxide (PAO), an inhibitor of protein tyrosine phosphatases (PTPs), might up-regulate the HO-1 gene.	oxophenylarsine	41-44	heme oxygenase 1	Homo sapiens	123-127
11768235-6	2001	Here, we show that a remarkably brief (1-15 min) exposure of normal hepatocytes to low concentrations (0.5-3 microM) of PAO produces a marked increase in mRNA and protein of HO-1.	oxophenylarsine	120-123	heme oxygenase 1	Homo sapiens	174-178
11768235-9	2001	Addition of thiol donors abrogated the PAO-mediated induction of HO-1 in a dose dependent fashion.	Sulfhydryl Compounds	12-17	heme oxygenase 1	Homo sapiens	65-69
11768235-9	2001	Addition of thiol donors abrogated the PAO-mediated induction of HO-1 in a dose dependent fashion.	oxophenylarsine	39-42	heme oxygenase 1	Homo sapiens	65-69
11768235-12	2001	Our results are consistent with the proposition that induction of HO-1 by PAO involves inhibition of specific PTP(s), and that the mechanisms of induction of HO-1 by PAO and by heme may share some common pathways.	oxophenylarsine	74-77	heme oxygenase 1	Homo sapiens	66-70
11768235-12	2001	Our results are consistent with the proposition that induction of HO-1 by PAO involves inhibition of specific PTP(s), and that the mechanisms of induction of HO-1 by PAO and by heme may share some common pathways.	oxophenylarsine	166-169	heme oxygenase 1	Homo sapiens	158-162
11768235-12	2001	Our results are consistent with the proposition that induction of HO-1 by PAO involves inhibition of specific PTP(s), and that the mechanisms of induction of HO-1 by PAO and by heme may share some common pathways.	Heme	177-181	heme oxygenase 1	Homo sapiens	66-70
11768235-12	2001	Our results are consistent with the proposition that induction of HO-1 by PAO involves inhibition of specific PTP(s), and that the mechanisms of induction of HO-1 by PAO and by heme may share some common pathways.	Heme	177-181	heme oxygenase 1	Homo sapiens	158-162
11571246-3	2001	METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells.	Hemin	204-209	heme oxygenase 1	Homo sapiens	115-119
11571246-3	2001	METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells.	Iron	218-222	heme oxygenase 1	Homo sapiens	100-104
11571246-3	2001	METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells.	Iron	218-222	heme oxygenase 1	Homo sapiens	115-119
11572959-7	2001	Macrophage-inducible NOS generates NO to kill other cells, whereas HO1 generates bilirubin to exert antioxidant cytoprotective effects and also provides cytoprotection by facilitating iron extrusion from cells.	Iron	184-188	heme oxygenase 1	Homo sapiens	67-70
11429414-3	2001	Once bound to its recognition DNA sequence termed antioxidant-responsive element or Maf-recognition element, Nrf2/small Maf induces a set of antioxidative stress genes, including heme oxygenase-1 and gamma-glutamylcysteine synthetase, whose products have been demonstrated to contribute to the scavenging of reactive oxygen species and to exhibit anti-inflammatory effects.	Reactive Oxygen Species	308-331	heme oxygenase 1	Homo sapiens	179-195
11481283-4	2001	The degree of oxidative stress in cells was estimated by flow cytometric analysis of reactive oxygen intermediate (ROI)-induced 2",7"-dichlorodihydrofluorescein diacetate fluorescence and Northern blot analysis of heme oxygenase-1 (HO-1) mRNA induction.	reactive oxygen intermediate	85-113	heme oxygenase 1	Homo sapiens	214-230
11481283-4	2001	The degree of oxidative stress in cells was estimated by flow cytometric analysis of reactive oxygen intermediate (ROI)-induced 2",7"-dichlorodihydrofluorescein diacetate fluorescence and Northern blot analysis of heme oxygenase-1 (HO-1) mRNA induction.	reactive oxygen intermediate	85-113	heme oxygenase 1	Homo sapiens	232-236
11481283-7	2001	The degree of ROI production and HO-1 mRNA induction was greater in cells treated with 40% than 20% O(2), an effect that was also larger in old than young passaged cells.	o(2)	100-104	heme oxygenase 1	Homo sapiens	33-37
11454666-9	2001	NOS inhibition by L-N(G)-nitroarginine methyl ester (L-NAME) or 1400 W abolished nitrite production and strongly reduced HO-1 expression.	NG-Nitroarginine Methyl Ester	53-59	heme oxygenase 1	Homo sapiens	121-125
11448133-6	2001	In addition to HSP72, HSP32 was significantly increased by PGA1.	prostaglandin A1	59-63	heme oxygenase 1	Homo sapiens	22-27
11448133-7	2001	The HSP32 induction was more vigorous with a marked increase with only 4 microg/ml of PGA1.	prostaglandin A1	86-90	heme oxygenase 1	Homo sapiens	4-9
11551744-7	2001	Preconditioning induction of stress proteins (i.e., hemeoxygenase-1 and neuronal nitric oxide synthase) and hypothermia therapy suppress the generation of toxic reactive oxygen, lipid, and thiol species evoked by bioactive iron complexes in the brain.	Sulfhydryl Compounds	189-194	heme oxygenase 1	Homo sapiens	52-67
11551744-7	2001	Preconditioning induction of stress proteins (i.e., hemeoxygenase-1 and neuronal nitric oxide synthase) and hypothermia therapy suppress the generation of toxic reactive oxygen, lipid, and thiol species evoked by bioactive iron complexes in the brain.	Iron	223-227	heme oxygenase 1	Homo sapiens	52-67
11435909-3	2001	HO-1 metabolizes heme to the antioxidant bilirubin and carbon monoxide, and represents a powerful endogenous defensive mechanism against free radicals in many diseases.	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4
11435909-3	2001	HO-1 metabolizes heme to the antioxidant bilirubin and carbon monoxide, and represents a powerful endogenous defensive mechanism against free radicals in many diseases.	Bilirubin	41-50	heme oxygenase 1	Homo sapiens	0-4
11435909-3	2001	HO-1 metabolizes heme to the antioxidant bilirubin and carbon monoxide, and represents a powerful endogenous defensive mechanism against free radicals in many diseases.	Carbon Monoxide	55-70	heme oxygenase 1	Homo sapiens	0-4
11435909-3	2001	HO-1 metabolizes heme to the antioxidant bilirubin and carbon monoxide, and represents a powerful endogenous defensive mechanism against free radicals in many diseases.	Free Radicals	137-150	heme oxygenase 1	Homo sapiens	0-4
11435909-5	2001	In this study, we showed high expression of HO-1 in lesions of EAE, and demonstrated that hemin, an inducer of HO-1, inhibited EAE effectively.	Hemin	90-95	heme oxygenase 1	Homo sapiens	44-48
11435909-5	2001	In this study, we showed high expression of HO-1 in lesions of EAE, and demonstrated that hemin, an inducer of HO-1, inhibited EAE effectively.	Hemin	90-95	heme oxygenase 1	Homo sapiens	111-115
11435909-6	2001	In contrast, tin mesoporphyrin, an inhibitor of HO-1, markedly exacerbated EAE.	tin mesoporphyrin	13-30	heme oxygenase 1	Homo sapiens	48-52
11454666-0	2001	Modulation of haem oxygenase-1 expression by nitric oxide and leukotrienes in zymosan-activated macrophages.	Nitric Oxide	45-57	heme oxygenase 1	Homo sapiens	14-30
11454666-0	2001	Modulation of haem oxygenase-1 expression by nitric oxide and leukotrienes in zymosan-activated macrophages.	Leukotrienes	62-74	heme oxygenase 1	Homo sapiens	14-30
11454666-0	2001	Modulation of haem oxygenase-1 expression by nitric oxide and leukotrienes in zymosan-activated macrophages.	Zymosan	78-85	heme oxygenase 1	Homo sapiens	14-30
11274184-2	2001	Nrf2 regulates expression of genes encoding enzymes with antioxidant (e.g. heme oxygenase-1 (HO-1)) or xenobiotic detoxification (e.g. NAD(P)H:quinone oxidoreductase, glutathione S-transferase) functions via the stress- or antioxidant-response elements (StRE/ARE).	nad(p)h	135-142	heme oxygenase 1	Homo sapiens	75-91
11454666-1	2001	Phagocytosis of unopsonized zymosan by RAW 264.7 macrophages upregulated protein expression of haem oxygenase-1 (HO-1), inducible nitric oxide synthase (iNOS) and cyclo-oxygenase-2 (COX-2) in a time- and concentration-dependent manner.	Zymosan	28-35	heme oxygenase 1	Homo sapiens	95-111
11454666-1	2001	Phagocytosis of unopsonized zymosan by RAW 264.7 macrophages upregulated protein expression of haem oxygenase-1 (HO-1), inducible nitric oxide synthase (iNOS) and cyclo-oxygenase-2 (COX-2) in a time- and concentration-dependent manner.	Zymosan	28-35	heme oxygenase 1	Homo sapiens	113-117
11454666-4	2001	The COX inhibitors indomethacin and NS398 weakly inhibited HO-1 expression but had no effect on iNOS and COX-2 expression or nitrite.	Indomethacin	19-31	heme oxygenase 1	Homo sapiens	59-63
11454666-4	2001	The COX inhibitors indomethacin and NS398 weakly inhibited HO-1 expression but had no effect on iNOS and COX-2 expression or nitrite.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	36-41	heme oxygenase 1	Homo sapiens	59-63
11454666-5	2001	In contrast, the 5-lipoxygenase (5-LO) inhibitor ZM 230,487 significantly decreased HO-1, iNOS and nitrite, which were not affected by zileuton.	zm 230	49-55	heme oxygenase 1	Homo sapiens	84-88
11454666-6	2001	Dexamethasone showed an inhibitory effect on HO-1 expression induced by zymosan.	Dexamethasone	0-13	heme oxygenase 1	Homo sapiens	45-49
11454666-6	2001	Dexamethasone showed an inhibitory effect on HO-1 expression induced by zymosan.	Zymosan	72-79	heme oxygenase 1	Homo sapiens	45-49
11454666-9	2001	NOS inhibition by L-N(G)-nitroarginine methyl ester (L-NAME) or 1400 W abolished nitrite production and strongly reduced HO-1 expression.	l-n(g)-nitroarginine methyl ester	18-51	heme oxygenase 1	Homo sapiens	121-125
11274184-10	2001	These results indicate that ATF4 regulates basal and CdCl(2)-induced expression of the ho-1 gene in a cell-specific manner and possibly in a complex with Nrf2.	Cadmium Chloride	53-60	heme oxygenase 1	Homo sapiens	87-91
11274184-2	2001	Nrf2 regulates expression of genes encoding enzymes with antioxidant (e.g. heme oxygenase-1 (HO-1)) or xenobiotic detoxification (e.g. NAD(P)H:quinone oxidoreductase, glutathione S-transferase) functions via the stress- or antioxidant-response elements (StRE/ARE).	nad(p)h	135-142	heme oxygenase 1	Homo sapiens	93-97
23045067-1	2001	Heme oxygenase 1 and 2 activities are responsible for initiating most of the degradation of heme, although other enzyme pathways play a role as well.	Heme	92-96	heme oxygenase 1	Homo sapiens	0-22
23045070-2	2001	This unit describes protocols for assessing the expression and regulation of specific HO-1 and HO-2 mRNAs by in situ hybridization using digoxigenin-tagged probes.	Digoxigenin	137-148	heme oxygenase 1	Homo sapiens	86-90
11340095-1	2001	The possible beneficial effect of supplemental glutamine (Gln) in critically ill patients has been suggested to be mediated by the induction of the cytoprotective heat shock proteins (HSP)32 and HSP72.	Glutamine	47-56	heme oxygenase 1	Homo sapiens	184-190
11340095-1	2001	The possible beneficial effect of supplemental glutamine (Gln) in critically ill patients has been suggested to be mediated by the induction of the cytoprotective heat shock proteins (HSP)32 and HSP72.	Glutamine	58-61	heme oxygenase 1	Homo sapiens	184-190
11278277-5	2001	Expression of recombinant ATM in AT fibroblasts, however, reduced the extent of the effects of CdCl(2) on both c-Jun phosphorylation and heme oxygenase-1 induction.	cdcl	95-99	heme oxygenase 1	Homo sapiens	137-153
11121422-0	2001	Disruption of an active site hydrogen bond converts human heme oxygenase-1 into a peroxidase.	Hydrogen	29-37	heme oxygenase 1	Homo sapiens	58-74
11121422-1	2001	The crystal structure of heme oxygenase-1 suggests that Asp-140 may participate in a hydrogen bonding network involving ligands coordinated to the heme iron atom.	Aspartic Acid	56-59	heme oxygenase 1	Homo sapiens	25-41
11121422-1	2001	The crystal structure of heme oxygenase-1 suggests that Asp-140 may participate in a hydrogen bonding network involving ligands coordinated to the heme iron atom.	Hydrogen	85-93	heme oxygenase 1	Homo sapiens	25-41
11121422-1	2001	The crystal structure of heme oxygenase-1 suggests that Asp-140 may participate in a hydrogen bonding network involving ligands coordinated to the heme iron atom.	Iron	152-156	heme oxygenase 1	Homo sapiens	25-41
11287117-0	2001	Heme oxygenase-1 induction by nitric oxide in RAW 264.7 macrophages is upregulated by a cyclo-oxygenase-2 inhibitor.	Nitric Oxide	30-42	heme oxygenase 1	Homo sapiens	0-16
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	Nitric Oxide	110-122	heme oxygenase 1	Homo sapiens	166-170
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	spermine nitric oxide complex	134-150	heme oxygenase 1	Homo sapiens	54-70
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	spermine nitric oxide complex	134-150	heme oxygenase 1	Homo sapiens	72-76
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	spermine nitric oxide complex	134-150	heme oxygenase 1	Homo sapiens	166-170
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	spermine nitric oxide complex	152-156	heme oxygenase 1	Homo sapiens	54-70
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	spermine nitric oxide complex	152-156	heme oxygenase 1	Homo sapiens	72-76
11287117-1	2001	Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein.	spermine nitric oxide complex	152-156	heme oxygenase 1	Homo sapiens	166-170
11287117-3	2001	Cells incubated with SPNO showed a strong increase in HO-1 mRNA levels after 4 h with a significant potentiation in the presence of SC58125, which did not modify HO-1 mRNA stability.	spermine nitric oxide complex	21-25	heme oxygenase 1	Homo sapiens	54-58
11287117-3	2001	Cells incubated with SPNO showed a strong increase in HO-1 mRNA levels after 4 h with a significant potentiation in the presence of SC58125, which did not modify HO-1 mRNA stability.	spermine nitric oxide complex	21-25	heme oxygenase 1	Homo sapiens	162-166
11688356-10	2001	In conclusion, carvedilol reduces oxidative stress and normalizes blood pressure; ecNOS remains upregulated while mRNA for transforming growth factor beta, a key fibrogenic cytokine, is reduced by carvedilol, which seems to preserve protective mechanisms such as NO and heme oxygenase-1 against long-term complications of oxidative stress, e.g., endothelial dysfunction, fibrogenesis and chronic rejection.	Carvedilol	15-25	heme oxygenase 1	Homo sapiens	270-286
11688356-10	2001	In conclusion, carvedilol reduces oxidative stress and normalizes blood pressure; ecNOS remains upregulated while mRNA for transforming growth factor beta, a key fibrogenic cytokine, is reduced by carvedilol, which seems to preserve protective mechanisms such as NO and heme oxygenase-1 against long-term complications of oxidative stress, e.g., endothelial dysfunction, fibrogenesis and chronic rejection.	Carvedilol	197-207	heme oxygenase 1	Homo sapiens	270-286
11247059-12	2001	CONCLUSIONS: The increase in bilirubin level by HO-1 might protect OSAHS patients from disorders related to hypoxemia.	Bilirubin	29-38	heme oxygenase 1	Homo sapiens	48-52
11283857-4	2001	Administration of the NO donor, molsidomine (MOL) (3 mg. kg(-1)), during resuscitation attenuated the accumulation of HO-1 mRNA and protein and the rise in HO activity.	Molsidomine	32-43	heme oxygenase 1	Homo sapiens	118-122
11283857-4	2001	Administration of the NO donor, molsidomine (MOL) (3 mg. kg(-1)), during resuscitation attenuated the accumulation of HO-1 mRNA and protein and the rise in HO activity.	Molsidomine	45-48	heme oxygenase 1	Homo sapiens	118-122
11247059-0	2001	Increase in bilirubin levels of patients with obstructive sleep apnea in the morning--a possible explanation of induced heme oxygenase-1.	Bilirubin	12-21	heme oxygenase 1	Homo sapiens	120-136
11171041-12	2001	In vitro studies with cultured keratinocytes revealed a potential role for reactive oxygen species (ROS), but not for growth factors and pro-inflammatory cytokines, as inducers of HO-1 expression in inflamed skin.	Reactive Oxygen Species	75-98	heme oxygenase 1	Homo sapiens	180-184
11247059-1	2001	STUDY OBJECTIVES: In the absence of heme oxygenase-1 (HO-1), which catalyzes the oxidation of heme to generate carbon monoxide and indirect bilirubin, hypoxia induces severe right ventricular dilation and infarction.	Heme	36-40	heme oxygenase 1	Homo sapiens	54-58
11247059-1	2001	STUDY OBJECTIVES: In the absence of heme oxygenase-1 (HO-1), which catalyzes the oxidation of heme to generate carbon monoxide and indirect bilirubin, hypoxia induces severe right ventricular dilation and infarction.	Carbon Monoxide	111-126	heme oxygenase 1	Homo sapiens	36-52
11247059-1	2001	STUDY OBJECTIVES: In the absence of heme oxygenase-1 (HO-1), which catalyzes the oxidation of heme to generate carbon monoxide and indirect bilirubin, hypoxia induces severe right ventricular dilation and infarction.	Carbon Monoxide	111-126	heme oxygenase 1	Homo sapiens	54-58
11247059-1	2001	STUDY OBJECTIVES: In the absence of heme oxygenase-1 (HO-1), which catalyzes the oxidation of heme to generate carbon monoxide and indirect bilirubin, hypoxia induces severe right ventricular dilation and infarction.	Bilirubin	140-149	heme oxygenase 1	Homo sapiens	36-52
11247059-1	2001	STUDY OBJECTIVES: In the absence of heme oxygenase-1 (HO-1), which catalyzes the oxidation of heme to generate carbon monoxide and indirect bilirubin, hypoxia induces severe right ventricular dilation and infarction.	Bilirubin	140-149	heme oxygenase 1	Homo sapiens	54-58
11245628-3	2001	There are three isoforms of HO: HO-1 is inducible by inflammatory cytokines and oxidants, including nitric oxide (NO), whereas HO-2 and HO-3 are expressed constitutively.	Nitric Oxide	100-112	heme oxygenase 1	Homo sapiens	32-36
11171043-0	2001	Tobacco-smoke-inducible human haem oxygenase-1 gene expression: role of distinct transcription factors and reactive oxygen intermediates.	reactive oxygen	107-122	heme oxygenase 1	Homo sapiens	30-46
11171043-1	2001	Exposure of eukaryotic cells to a variety of reactive-oxygen-intermediate (ROI)-mediated sources of cellular injury, including heavy metals and UV radiation, induces the expression of heat-shock (HS) and stress-related genes among which is a 32-34 kDa protein identified as inducible haem oxygenase-1 (HO-1).	reactive	45-53	heme oxygenase 1	Homo sapiens	284-300
11171043-1	2001	Exposure of eukaryotic cells to a variety of reactive-oxygen-intermediate (ROI)-mediated sources of cellular injury, including heavy metals and UV radiation, induces the expression of heat-shock (HS) and stress-related genes among which is a 32-34 kDa protein identified as inducible haem oxygenase-1 (HO-1).	reactive	45-53	heme oxygenase 1	Homo sapiens	302-306
11171043-1	2001	Exposure of eukaryotic cells to a variety of reactive-oxygen-intermediate (ROI)-mediated sources of cellular injury, including heavy metals and UV radiation, induces the expression of heat-shock (HS) and stress-related genes among which is a 32-34 kDa protein identified as inducible haem oxygenase-1 (HO-1).	Oxygen	54-60	heme oxygenase 1	Homo sapiens	284-300
11171043-1	2001	Exposure of eukaryotic cells to a variety of reactive-oxygen-intermediate (ROI)-mediated sources of cellular injury, including heavy metals and UV radiation, induces the expression of heat-shock (HS) and stress-related genes among which is a 32-34 kDa protein identified as inducible haem oxygenase-1 (HO-1).	Oxygen	54-60	heme oxygenase 1	Homo sapiens	302-306
11171043-8	2001	We report an inhibition of NF-kappaB activation by TS, no effect on AP-1 and a strong activation of CdRE-binding activity, whereas cadmium chelation from TS only partially prevented HO-1 induction.	Cadmium	131-138	heme oxygenase 1	Homo sapiens	182-186
11171043-9	2001	H(2)O(2) also activated the CdRE-binding activity, and pretreatment with N-acetyl-L-cysteine, which replenishes the intracellular levels of GSH, suppressed, in TS-treated cells, both the CdRE-binding activity and the increased HO-1 expression.	Hydrogen Peroxide	0-8	heme oxygenase 1	Homo sapiens	227-231
11171043-9	2001	H(2)O(2) also activated the CdRE-binding activity, and pretreatment with N-acetyl-L-cysteine, which replenishes the intracellular levels of GSH, suppressed, in TS-treated cells, both the CdRE-binding activity and the increased HO-1 expression.	Acetylcysteine	73-92	heme oxygenase 1	Homo sapiens	227-231
11171043-9	2001	H(2)O(2) also activated the CdRE-binding activity, and pretreatment with N-acetyl-L-cysteine, which replenishes the intracellular levels of GSH, suppressed, in TS-treated cells, both the CdRE-binding activity and the increased HO-1 expression.	Glutathione	140-143	heme oxygenase 1	Homo sapiens	227-231
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Heme	57-61	heme oxygenase 1	Homo sapiens	0-16
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Heme	57-61	heme oxygenase 1	Homo sapiens	18-22
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	0-16
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Carbon Monoxide	88-103	heme oxygenase 1	Homo sapiens	18-22
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Carbon Monoxide	105-107	heme oxygenase 1	Homo sapiens	0-16
11950143-2	2001	Heme oxygenase isozymes, HO-1, HO-2 and HO-3, are HSP32 protein cognates, with a known function of catalyzing the isomer specific oxidation of the heme molecule, including that of NO synthase.	Heme	147-151	heme oxygenase 1	Homo sapiens	25-44
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Carbon Monoxide	105-107	heme oxygenase 1	Homo sapiens	18-22
11950143-2	2001	Heme oxygenase isozymes, HO-1, HO-2 and HO-3, are HSP32 protein cognates, with a known function of catalyzing the isomer specific oxidation of the heme molecule, including that of NO synthase.	Heme	147-151	heme oxygenase 1	Homo sapiens	50-55
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Biliverdine	113-123	heme oxygenase 1	Homo sapiens	0-16
11950143-11	2001	In the case of severe tissue injury, such as compression injury, HO-1 is induced and colocalizes with cGMP and pro-apoptotic oncogenes.	Cyclic GMP	102-106	heme oxygenase 1	Homo sapiens	65-69
11194943-4	2001	Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant.	Biliverdine	113-123	heme oxygenase 1	Homo sapiens	18-22
11135063-10	2001	CONCLUSION: We conclude that up-regulation of HO-1 occurs in the kidney in humans and rats repetitively exposed to heme proteins.	Heme	115-119	heme oxygenase 1	Homo sapiens	46-50
11124818-1	2001	This study was designed to determine changes in expression of heme oxygenase (HO)-1, the stress-inducible and carbon monoxide-producing enzyme, in normotensive and portal hypertensive human livers.	Carbon Monoxide	110-125	heme oxygenase 1	Homo sapiens	62-83
11208917-3	2001	We have also shown that reactive iron (Fe3+) and cGMP staining spatially resemble that of HO-1; which, in turn, colocalizes in motor neurons with transcription factors: Fas-associated protein containing death domain (FADD), tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and p53.	Iron	33-37	heme oxygenase 1	Homo sapiens	90-94
11208917-3	2001	We have also shown that reactive iron (Fe3+) and cGMP staining spatially resemble that of HO-1; which, in turn, colocalizes in motor neurons with transcription factors: Fas-associated protein containing death domain (FADD), tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and p53.	ferric sulfate	39-43	heme oxygenase 1	Homo sapiens	90-94
11208917-3	2001	We have also shown that reactive iron (Fe3+) and cGMP staining spatially resemble that of HO-1; which, in turn, colocalizes in motor neurons with transcription factors: Fas-associated protein containing death domain (FADD), tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and p53.	Cyclic GMP	49-53	heme oxygenase 1	Homo sapiens	90-94
11208917-11	2001	Tissue Fe3+ and cGMP staining were increased and prominently mapped below the site of injury, where cGMP colocalized with HO-1 in the nucleus of the motor neurons.	ferric sulfate	7-11	heme oxygenase 1	Homo sapiens	122-126
11208917-11	2001	Tissue Fe3+ and cGMP staining were increased and prominently mapped below the site of injury, where cGMP colocalized with HO-1 in the nucleus of the motor neurons.	Cyclic GMP	16-20	heme oxygenase 1	Homo sapiens	122-126
11208917-11	2001	Tissue Fe3+ and cGMP staining were increased and prominently mapped below the site of injury, where cGMP colocalized with HO-1 in the nucleus of the motor neurons.	Cyclic GMP	100-104	heme oxygenase 1	Homo sapiens	122-126
11018038-5	2000	TGF-beta1 treatment in conjunction with actinomycin D or cycloheximide demonstrated that induction of HO-1 mRNA requires de novo transcription and, in part, protein synthesis.	Dactinomycin	40-53	heme oxygenase 1	Homo sapiens	102-106
11018038-5	2000	TGF-beta1 treatment in conjunction with actinomycin D or cycloheximide demonstrated that induction of HO-1 mRNA requires de novo transcription and, in part, protein synthesis.	Cycloheximide	57-70	heme oxygenase 1	Homo sapiens	102-106
10942763-0	2000	Replacement of the distal glycine 139 transforms human heme oxygenase-1 into a peroxidase.	Glycine	26-33	heme oxygenase 1	Homo sapiens	55-71
11078701-6	2000	15-d-PGJ(2) and its precursors, but not the thiazolidinediones, induced gene expression for heme oxygenase-1 (HO-1), a stress-related protein, and strongly inhibited interleukin-1 (IL-1)-induced nitric oxide (NO) production.	15-d-pgj	0-8	heme oxygenase 1	Homo sapiens	92-108
11078701-6	2000	15-d-PGJ(2) and its precursors, but not the thiazolidinediones, induced gene expression for heme oxygenase-1 (HO-1), a stress-related protein, and strongly inhibited interleukin-1 (IL-1)-induced nitric oxide (NO) production.	15-d-pgj	0-8	heme oxygenase 1	Homo sapiens	110-114
11078701-6	2000	15-d-PGJ(2) and its precursors, but not the thiazolidinediones, induced gene expression for heme oxygenase-1 (HO-1), a stress-related protein, and strongly inhibited interleukin-1 (IL-1)-induced nitric oxide (NO) production.	Nitric Oxide	195-207	heme oxygenase 1	Homo sapiens	92-108
11078701-6	2000	15-d-PGJ(2) and its precursors, but not the thiazolidinediones, induced gene expression for heme oxygenase-1 (HO-1), a stress-related protein, and strongly inhibited interleukin-1 (IL-1)-induced nitric oxide (NO) production.	Nitric Oxide	195-207	heme oxygenase 1	Homo sapiens	110-114
11078701-8	2000	On the other hand, sodium arsenite, a known activator of the stress response pathway, induced HO-1 mRNA expression but lacked a promoting effect on TG production.	sodium arsenite	19-34	heme oxygenase 1	Homo sapiens	94-98
11076874-0	2000	Inhibition of inducible nitric oxide synthase in the human intestinal epithelial cell line, DLD-1, by the inducers of heme oxygenase 1, bismuth salts, heme, and nitric oxide donors.	nitric	24-30	heme oxygenase 1	Homo sapiens	118-134
11076874-0	2000	Inhibition of inducible nitric oxide synthase in the human intestinal epithelial cell line, DLD-1, by the inducers of heme oxygenase 1, bismuth salts, heme, and nitric oxide donors.	Nitric Oxide	24-36	heme oxygenase 1	Homo sapiens	118-134
11076874-8	2000	This inhibitory effect was abolished by the HO-1 specific inhibitor tin protoporphyrin.	tin protoporphyrin IX	68-86	heme oxygenase 1	Homo sapiens	44-48
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Heme	63-67	heme oxygenase 1	Homo sapiens	81-85
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Iron	134-138	heme oxygenase 1	Homo sapiens	63-79
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Iron	134-138	heme oxygenase 1	Homo sapiens	81-85
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Biliverdine	140-150	heme oxygenase 1	Homo sapiens	63-79
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Biliverdine	140-150	heme oxygenase 1	Homo sapiens	81-85
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Carbon Monoxide	156-171	heme oxygenase 1	Homo sapiens	63-79
11085891-2	2000	Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide.	Carbon Monoxide	156-171	heme oxygenase 1	Homo sapiens	81-85
11115065-0	2000	Dopamine induces the expression of heme oxygenase-1 by human endothelial cells in vitro.	Dopamine	0-8	heme oxygenase 1	Homo sapiens	35-51
11115065-2	2000	To study the mechanisms underlying the organ protection associated with the administration of DA prior to transplantation, we questioned whether DA induces the antioxidative enzyme heme oxygenase-1 (HO-1) in cultured endothelial cells.	Dopamine	145-147	heme oxygenase 1	Homo sapiens	199-203
11115065-5	2000	RESULTS: The presence of DA resulted in a dose- and time-dependent up-regulation of HO-1 both on RNA and protein level, whereas HO-1 was barely detectable under basal conditions.	Dopamine	25-27	heme oxygenase 1	Homo sapiens	84-88
11115065-8	2000	The addition of the antioxidant agents ascorbic acid and N-acetyl-cysteine both lead to dose-dependent inhibition of DA-mediated HO-1 induction.	Ascorbic Acid	39-52	heme oxygenase 1	Homo sapiens	129-133
11115065-8	2000	The addition of the antioxidant agents ascorbic acid and N-acetyl-cysteine both lead to dose-dependent inhibition of DA-mediated HO-1 induction.	Acetylcysteine	57-74	heme oxygenase 1	Homo sapiens	129-133
11115065-10	2000	CONCLUSION: We conclude that DA induces the expression of the protective enzyme HO-1 in cultured endothelial cells by an oxidative mechanism.	Dopamine	29-31	heme oxygenase 1	Homo sapiens	80-84
10942763-1	2000	The human heme oxygenase-1 crystal structure suggests that Gly-139 and Gly-143 interact directly with iron-bound ligands.	Glycine	59-62	heme oxygenase 1	Homo sapiens	10-26
10942763-1	2000	The human heme oxygenase-1 crystal structure suggests that Gly-139 and Gly-143 interact directly with iron-bound ligands.	Glycine	71-74	heme oxygenase 1	Homo sapiens	10-26
10942763-1	2000	The human heme oxygenase-1 crystal structure suggests that Gly-139 and Gly-143 interact directly with iron-bound ligands.	Iron	102-106	heme oxygenase 1	Homo sapiens	10-26
11032845-0	2000	Nitric oxide-inducible expression of heme oxygenase-1 in human cells.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	37-53
11032845-3	2000	Nitric oxide (NO) induces HO-1 in many cell types, but the specific contribution of transcriptional or post-transcriptional effects to this induction have remained unresolved.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	26-30
11032845-5	2000	We used a specific NO scavenger (2-(4-carboxylphenyl)-4,4,5,5-tetramethylimidazolin-1-oxyl 3-oxide) that completely prevented the inducible expression of HO-1 by NO, pointing to direct signaling action of NO in this induction.	2-(4-carboxylphenyl)-4,4,5,5-tetramethylimidazolin-1-oxyl 3-oxide	33-98	heme oxygenase 1	Homo sapiens	154-158
11007950-1	2000	Heme oxygenase (HO)-1 is the inducible isoform of the rate-limiting enzyme of heme degradation.	Heme	78-82	heme oxygenase 1	Homo sapiens	0-21
11015442-5	2000	Exposure of ECs to exogenous CO, under inhibition of HO-1 activity by SnPPIX, substitutes HO-1 in preventing EC apoptosis.	Carbon Monoxide	29-31	heme oxygenase 1	Homo sapiens	53-57
11015442-0	2000	Carbon monoxide generated by heme oxygenase 1 suppresses endothelial cell apoptosis.	Carbon Monoxide	0-15	heme oxygenase 1	Homo sapiens	29-45
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Heme	14-18	heme oxygenase 1	Homo sapiens	119-141
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Heme	14-18	heme oxygenase 1	Homo sapiens	143-149
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Carbon Monoxide	198-213	heme oxygenase 1	Homo sapiens	119-141
11015442-1	2000	Heme oxygenase 1 (HO-1) inhibits apoptosis by regulating cellular prooxidant iron.	Iron	77-81	heme oxygenase 1	Homo sapiens	0-22
11015442-5	2000	Exposure of ECs to exogenous CO, under inhibition of HO-1 activity by SnPPIX, substitutes HO-1 in preventing EC apoptosis.	Carbon Monoxide	29-31	heme oxygenase 1	Homo sapiens	90-94
11015442-2	2000	We now show that there is an additional mechanism by which HO-1 inhibits apoptosis, namely by generating the gaseous molecule carbon monoxide (CO).	Carbon Monoxide	126-141	heme oxygenase 1	Homo sapiens	59-63
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Carbon Monoxide	198-213	heme oxygenase 1	Homo sapiens	143-149
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Carbon Monoxide	215-217	heme oxygenase 1	Homo sapiens	119-141
11015442-2	2000	We now show that there is an additional mechanism by which HO-1 inhibits apoptosis, namely by generating the gaseous molecule carbon monoxide (CO).	Carbon Monoxide	143-145	heme oxygenase 1	Homo sapiens	59-63
11015442-5	2000	Exposure of ECs to exogenous CO, under inhibition of HO-1 activity by SnPPIX, substitutes HO-1 in preventing EC apoptosis.	tin protoporphyrin IX	70-76	heme oxygenase 1	Homo sapiens	53-57
11015442-3	2000	Overexpression of HO-1, or induction of HO-1 expression by heme, protects endothelial cells (ECs) from apoptosis.	Heme	59-63	heme oxygenase 1	Homo sapiens	40-44
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Carbon Monoxide	215-217	heme oxygenase 1	Homo sapiens	143-149
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Iron	220-224	heme oxygenase 1	Homo sapiens	119-141
11015442-4	2000	When HO-1 enzymatic activity is blocked by tin protoporphyrin (SnPPIX) or the action of CO is inhibited by hemoglobin (Hb), HO-1 no longer prevents EC apoptosis while these reagents do not affect the antiapoptotic action of bcl-2.	tin protoporphyrin IX	43-61	heme oxygenase 1	Homo sapiens	5-9
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Iron	220-224	heme oxygenase 1	Homo sapiens	143-149
11015442-8	2000	Specific inhibition of p38 MAPK activation by the pyridinyl imidazol SB203580 or through overexpression of a p38 MAPK dominant negative mutant abrogated the antiapoptotic effect of HO-1.	pyridinyl imidazol	50-68	heme oxygenase 1	Homo sapiens	181-185
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Iron	226-228	heme oxygenase 1	Homo sapiens	119-141
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Iron	226-228	heme oxygenase 1	Homo sapiens	143-149
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Biliverdine	234-244	heme oxygenase 1	Homo sapiens	119-141
10985695-1	2000	Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin.	Biliverdine	234-244	heme oxygenase 1	Homo sapiens	143-149
11015442-4	2000	When HO-1 enzymatic activity is blocked by tin protoporphyrin (SnPPIX) or the action of CO is inhibited by hemoglobin (Hb), HO-1 no longer prevents EC apoptosis while these reagents do not affect the antiapoptotic action of bcl-2.	tin protoporphyrin IX	63-69	heme oxygenase 1	Homo sapiens	5-9
11015442-8	2000	Specific inhibition of p38 MAPK activation by the pyridinyl imidazol SB203580 or through overexpression of a p38 MAPK dominant negative mutant abrogated the antiapoptotic effect of HO-1.	SB 203580	69-77	heme oxygenase 1	Homo sapiens	181-185
11023535-8	2000	Our results suggest that increased sequestration of iron as a consequence of induced HO-1 might be involved in the adaptive protection after HBO treatment and that the induction of DNA damage is not the trigger for adaptive protection.	Iron	52-56	heme oxygenase 1	Homo sapiens	85-89
10997923-0	2000	Mechanisms underlying induction of heme oxygenase-1 by nitric oxide in renal tubular epithelial cells.	Nitric Oxide	55-67	heme oxygenase 1	Homo sapiens	35-51
10997923-1	2000	We examined whether nitric oxide-generating agents influence expression of heme oxygenase-1 (HO-1) in renal proximal tubular epithelial cells, LLC-PK(1) cells, and the mechanisms underlying any such effects.	Nitric Oxide	20-32	heme oxygenase 1	Homo sapiens	75-91
10997923-1	2000	We examined whether nitric oxide-generating agents influence expression of heme oxygenase-1 (HO-1) in renal proximal tubular epithelial cells, LLC-PK(1) cells, and the mechanisms underlying any such effects.	Nitric Oxide	20-32	heme oxygenase 1	Homo sapiens	93-97
10997923-2	2000	In sublytic amounts, the nitric oxide donor sodium nitroprusside induced HO-1 mRNA and protein and HO activity in a dose-dependent and time-dependent fashion; this induction was specific for nitric oxide since the nitric oxide scavenger carboxy-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide significantly reduced such induction.	Nitric Oxide	25-37	heme oxygenase 1	Homo sapiens	73-77
10997923-2	2000	In sublytic amounts, the nitric oxide donor sodium nitroprusside induced HO-1 mRNA and protein and HO activity in a dose-dependent and time-dependent fashion; this induction was specific for nitric oxide since the nitric oxide scavenger carboxy-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide significantly reduced such induction.	Nitroprusside	44-64	heme oxygenase 1	Homo sapiens	73-77
10997923-2	2000	In sublytic amounts, the nitric oxide donor sodium nitroprusside induced HO-1 mRNA and protein and HO activity in a dose-dependent and time-dependent fashion; this induction was specific for nitric oxide since the nitric oxide scavenger carboxy-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide significantly reduced such induction.	Nitric Oxide	191-203	heme oxygenase 1	Homo sapiens	73-77
10997923-2	2000	In sublytic amounts, the nitric oxide donor sodium nitroprusside induced HO-1 mRNA and protein and HO activity in a dose-dependent and time-dependent fashion; this induction was specific for nitric oxide since the nitric oxide scavenger carboxy-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide significantly reduced such induction.	Nitric Oxide	191-203	heme oxygenase 1	Homo sapiens	73-77
10997923-2	2000	In sublytic amounts, the nitric oxide donor sodium nitroprusside induced HO-1 mRNA and protein and HO activity in a dose-dependent and time-dependent fashion; this induction was specific for nitric oxide since the nitric oxide scavenger carboxy-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide significantly reduced such induction.	carboxy-2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide	237-299	heme oxygenase 1	Homo sapiens	73-77
10997923-8	2000	We thus provide the novel description of the induction of HO-1 in renal proximal tubular epithelial cells exposed to nitric oxide donors and provide the first demonstration in kidney-derived cells for the involvement of a redox-based mechanism in such expression.	Nitric Oxide	117-129	heme oxygenase 1	Homo sapiens	58-62
10997923-9	2000	We also demonstrate that, in LLC-PK(1) cells exposed to nitric oxide donors, chelatable iron is involved in eliciting the HO-1 response observed at lower concentrations of these donors, and in mediating the cytotoxic effects of these donors when present in higher concentrations.	Nitric Oxide	56-68	heme oxygenase 1	Homo sapiens	122-126
10997923-9	2000	We also demonstrate that, in LLC-PK(1) cells exposed to nitric oxide donors, chelatable iron is involved in eliciting the HO-1 response observed at lower concentrations of these donors, and in mediating the cytotoxic effects of these donors when present in higher concentrations.	Iron	88-92	heme oxygenase 1	Homo sapiens	122-126
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Heme	64-68	heme oxygenase 1	Homo sapiens	0-16
10874044-0	2000	Mechanism of heme oxygenase-1 gene activation by cadmium in MCF-7 mammary epithelial cells.	Cadmium	49-56	heme oxygenase 1	Homo sapiens	13-29
10874044-5	2000	Exposure of MCF-7 cells to 10 micrometer CdCl(2) stimulates phosphorylation of ERK, JNK, and p38 mitogen-activated protein kinases, implicating one or more of these signaling pathways in ho-1 gene induction.	cdcl	41-45	heme oxygenase 1	Homo sapiens	187-191
10874044-6	2000	SB203580, an inhibitor of p38, diminishes cadmium-stimulated pE1-luc expression and HO-1 mRNA levels by up to 70-80%.	SB 203580	0-8	heme oxygenase 1	Homo sapiens	84-88
10874044-13	2000	Taken together, these results indicate that cadmium induces ho-1 gene expression via sequential activation of the p38 kinase pathway and Nrf2.	Cadmium	44-51	heme oxygenase 1	Homo sapiens	60-64
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Heme	64-68	heme oxygenase 1	Homo sapiens	18-22
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Biliverdine	72-82	heme oxygenase 1	Homo sapiens	0-16
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Biliverdine	72-82	heme oxygenase 1	Homo sapiens	18-22
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Iron	89-93	heme oxygenase 1	Homo sapiens	0-16
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Iron	89-93	heme oxygenase 1	Homo sapiens	18-22
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	0-16
11053673-2	2000	Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide.	Carbon Monoxide	98-113	heme oxygenase 1	Homo sapiens	18-22
11053673-4	2000	In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone.	Iron	88-92	heme oxygenase 1	Homo sapiens	63-67
10975414-6	2000	Total RNA from EPS was used for gene expression of heme oxygenase-1 (HO-1) and granzyme B.	eps	15-18	heme oxygenase 1	Homo sapiens	51-67
11053673-4	2000	In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone.	Iron	88-92	heme oxygenase 1	Homo sapiens	122-126
11053673-4	2000	In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone.	tin mesoporphyrin	139-156	heme oxygenase 1	Homo sapiens	63-67
11053673-4	2000	In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone.	tin mesoporphyrin	139-156	heme oxygenase 1	Homo sapiens	122-126
11053673-4	2000	In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone.	Dexamethasone	161-174	heme oxygenase 1	Homo sapiens	63-67
11053673-4	2000	In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone.	Dexamethasone	161-174	heme oxygenase 1	Homo sapiens	122-126
11053673-7	2000	Collectively, our findings suggest that HO-1 over-expression contributes to the pathological iron deposition and mitochondrial damage documented in these aging-related neurodegenerative disorders.	Iron	93-97	heme oxygenase 1	Homo sapiens	40-44
10906077-6	2000	Treatments of isolated tubules with either sodium arsenite, known to induce HO-1, or hematin, an HO substrate, resulted in 4.4- and 1.8-fold, respectively, increases in cGMP levels.	sodium arsenite	43-58	heme oxygenase 1	Homo sapiens	76-80
10906077-6	2000	Treatments of isolated tubules with either sodium arsenite, known to induce HO-1, or hematin, an HO substrate, resulted in 4.4- and 1.8-fold, respectively, increases in cGMP levels.	Cyclic GMP	169-173	heme oxygenase 1	Homo sapiens	76-80
10906077-9	2000	These findings, demonstrating for the first time a link between HO-1 activity in Sertoli cells and sGC-dependent cGMP production in seminiferous tubules, suggest a functional role of CO in the human testis.	Cyclic GMP	113-117	heme oxygenase 1	Homo sapiens	64-68
10894889-2	2000	Arsenite is also a potent inducer of heme oxygenase (HO)-1.	arsenite	0-8	heme oxygenase 1	Homo sapiens	37-58
10788478-2	2000	The stress protein heme oxygenase-1 (HO-1) is induced in endothelial cells exposed to nitric oxide (NO)-releasing agents, and this process is finely modulated by thiols (Foresti, R., Clark, J. E., Green, C. J., and Motterlini R. (1997) J. Biol.	Nitric Oxide	86-98	heme oxygenase 1	Homo sapiens	19-35
11229523-12	2000	In addition, surface redox-active copper is the first link shown for the concomitant regulation of HO-1 and MT-1 and is required for the activation of the amino-terminal c-Jun kinase (JNK) by heme-hemopexin.	Copper	34-40	heme oxygenase 1	Homo sapiens	99-112
10938455-6	2000	In lymphocytes isolated from individuals receiving antioxidant supplements and subjected to a heat shock in the presence of the free radical generator 2, 2"-azobis-(2-amidinopropane)-dihydrochloride, enhanced synthesis of heat shock proteins hsp 105, hsp 90, hsp 70, and hsp 40 by contrast with decreased synthesis of heme oxygenase HO-1 (hsp 32) were noted.	Free Radicals	128-140	heme oxygenase 1	Homo sapiens	333-337
10938455-6	2000	In lymphocytes isolated from individuals receiving antioxidant supplements and subjected to a heat shock in the presence of the free radical generator 2, 2"-azobis-(2-amidinopropane)-dihydrochloride, enhanced synthesis of heat shock proteins hsp 105, hsp 90, hsp 70, and hsp 40 by contrast with decreased synthesis of heme oxygenase HO-1 (hsp 32) were noted.	Free Radicals	128-140	heme oxygenase 1	Homo sapiens	339-345
10938455-6	2000	In lymphocytes isolated from individuals receiving antioxidant supplements and subjected to a heat shock in the presence of the free radical generator 2, 2"-azobis-(2-amidinopropane)-dihydrochloride, enhanced synthesis of heat shock proteins hsp 105, hsp 90, hsp 70, and hsp 40 by contrast with decreased synthesis of heme oxygenase HO-1 (hsp 32) were noted.	2,2'-azobis(2-amidinopropane)	151-198	heme oxygenase 1	Homo sapiens	333-337
10938455-6	2000	In lymphocytes isolated from individuals receiving antioxidant supplements and subjected to a heat shock in the presence of the free radical generator 2, 2"-azobis-(2-amidinopropane)-dihydrochloride, enhanced synthesis of heat shock proteins hsp 105, hsp 90, hsp 70, and hsp 40 by contrast with decreased synthesis of heme oxygenase HO-1 (hsp 32) were noted.	2,2'-azobis(2-amidinopropane)	151-198	heme oxygenase 1	Homo sapiens	339-345
10814519-2	2000	Unexpectedly, here we show that expression of HO-1 mRNA is repressed by hypoxia in primary cultures of human umbilical vein endothelial cells (HUVECs), but is increased by cobalt chloride (CoCl(2)) that is known to mimic hypoxia.	cobaltous chloride	172-187	heme oxygenase 1	Homo sapiens	46-50
10814519-2	2000	Unexpectedly, here we show that expression of HO-1 mRNA is repressed by hypoxia in primary cultures of human umbilical vein endothelial cells (HUVECs), but is increased by cobalt chloride (CoCl(2)) that is known to mimic hypoxia.	cobaltous chloride	189-196	heme oxygenase 1	Homo sapiens	46-50
10814519-4	2000	Therefore, hypoxia and cobalt showed opposing effects on HO-1 mRNA expression, despite activation of hypoxia-inducible factor 1.	Cobalt	23-29	heme oxygenase 1	Homo sapiens	57-61
10814519-5	2000	The half-life of HO-1 mRNA was not changed by hypoxia, but was significantly prolonged by CoCl(2).	cobaltous chloride	90-97	heme oxygenase 1	Homo sapiens	17-21
10839994-2	2000	In several circumstances, this cytoprotective effect has been attributed to increased generation of the antioxidant bilirubin during haem degradation by HO-1.	Bilirubin	116-125	heme oxygenase 1	Homo sapiens	153-157
10839994-3	2000	However, a direct implication for HO-1-derived bilirubin in protection against oxidative stress remains to be established.	Bilirubin	47-56	heme oxygenase 1	Homo sapiens	34-38
10839994-5	2000	We found that hemin-mediated increase in HO-1 protein expression and haem oxygenase activity is associated with augmented bilirubin levels.	Bilirubin	122-131	heme oxygenase 1	Homo sapiens	41-45
10839994-8	2000	Interestingly, this protective effect was manifest only when cells were actively producing bilirubin as a consequence of increased haem availability and utilization by HO-1.	Bilirubin	91-100	heme oxygenase 1	Homo sapiens	168-172
10839994-11	2000	Our findings provide direct evidence that bilirubin generated after up-regulation of the HO-1 pathway is cytoprotective against oxidative stress.	Bilirubin	42-51	heme oxygenase 1	Homo sapiens	89-93
10788478-2	2000	The stress protein heme oxygenase-1 (HO-1) is induced in endothelial cells exposed to nitric oxide (NO)-releasing agents, and this process is finely modulated by thiols (Foresti, R., Clark, J. E., Green, C. J., and Motterlini R. (1997) J. Biol.	Nitric Oxide	86-98	heme oxygenase 1	Homo sapiens	37-41
10788478-2	2000	The stress protein heme oxygenase-1 (HO-1) is induced in endothelial cells exposed to nitric oxide (NO)-releasing agents, and this process is finely modulated by thiols (Foresti, R., Clark, J. E., Green, C. J., and Motterlini R. (1997) J. Biol.	Sulfhydryl Compounds	162-168	heme oxygenase 1	Homo sapiens	19-35
10788478-2	2000	The stress protein heme oxygenase-1 (HO-1) is induced in endothelial cells exposed to nitric oxide (NO)-releasing agents, and this process is finely modulated by thiols (Foresti, R., Clark, J. E., Green, C. J., and Motterlini R. (1997) J. Biol.	Sulfhydryl Compounds	162-168	heme oxygenase 1	Homo sapiens	37-41
10788478-8	2000	A series of antioxidant agents did not prevent the elevation in heme oxygenase activity by hypoxia; however, the precursor of glutathione synthesis and thiol donor, N-acetylcysteine, completely abolished HO-1 induction.	Glutathione	126-137	heme oxygenase 1	Homo sapiens	204-208
10788478-8	2000	A series of antioxidant agents did not prevent the elevation in heme oxygenase activity by hypoxia; however, the precursor of glutathione synthesis and thiol donor, N-acetylcysteine, completely abolished HO-1 induction.	Sulfhydryl Compounds	152-157	heme oxygenase 1	Homo sapiens	204-208
10788478-8	2000	A series of antioxidant agents did not prevent the elevation in heme oxygenase activity by hypoxia; however, the precursor of glutathione synthesis and thiol donor, N-acetylcysteine, completely abolished HO-1 induction.	Acetylcysteine	165-181	heme oxygenase 1	Homo sapiens	204-208
10807584-6	2000	In vitro studies in human renal proximal tubule cells demonstrate that hemin, an inducer of HO-1, significantly attenuated cisplatin-induced apoptosis and necrosis, whereas inhibition of HO-1 enzyme activity reversed the cytoprotective effect.	Hemin	71-76	heme oxygenase 1	Homo sapiens	92-96
10788478-10	2000	These results indicate that intracellular interaction of thiols with NO is an important determinant in the mechanism leading to HO-1 induction by reduced oxygen levels.	Sulfhydryl Compounds	57-63	heme oxygenase 1	Homo sapiens	128-132
10807584-6	2000	In vitro studies in human renal proximal tubule cells demonstrate that hemin, an inducer of HO-1, significantly attenuated cisplatin-induced apoptosis and necrosis, whereas inhibition of HO-1 enzyme activity reversed the cytoprotective effect.	Cisplatin	123-132	heme oxygenase 1	Homo sapiens	92-96
10788478-10	2000	These results indicate that intracellular interaction of thiols with NO is an important determinant in the mechanism leading to HO-1 induction by reduced oxygen levels.	Oxygen	154-160	heme oxygenase 1	Homo sapiens	128-132
10788478-11	2000	We suggest that in addition to oxidative stress, HO-1 gene expression can be regulated by redox reactions involving NO and S-nitrosothiols (nitrosative stress), emphasizing a versatile role for the heme oxygenase pathway in the cellular adaptation to a variety of stressful conditions.	S-Nitrosothiols	123-138	heme oxygenase 1	Homo sapiens	49-53
10780998-5	2000	Incubation of cells with NO donors, spermine nonoate (SPNO) and S-nitroso-N-acetylpenicillamine (SNAP), induced a dose- and time-dependent expression of HO-1 protein.	spermine nitric oxide complex	36-52	heme oxygenase 1	Homo sapiens	153-157
10807735-0	2000	Heme oxygenase-1 is a cGMP-inducible endothelial protein and mediates the cytoprotective action of nitric oxide.	Cyclic GMP	22-26	heme oxygenase 1	Homo sapiens	0-16
10807735-0	2000	Heme oxygenase-1 is a cGMP-inducible endothelial protein and mediates the cytoprotective action of nitric oxide.	Nitric Oxide	99-111	heme oxygenase 1	Homo sapiens	0-16
10807735-2	2000	By use of Western blotting, cell viability analysis, and antisense technique, the present study investigates the involvement of HO-1 in endothelial protection induced by the clinically used nitric oxide (NO) donor molsidomine (specifically, its active metabolite 3-morpholinosydnonimine [SIN-1]) and the second messenger cGMP.	Nitric Oxide	190-202	heme oxygenase 1	Homo sapiens	128-132
10807735-2	2000	By use of Western blotting, cell viability analysis, and antisense technique, the present study investigates the involvement of HO-1 in endothelial protection induced by the clinically used nitric oxide (NO) donor molsidomine (specifically, its active metabolite 3-morpholinosydnonimine [SIN-1]) and the second messenger cGMP.	Molsidomine	214-225	heme oxygenase 1	Homo sapiens	128-132
10807735-4	2000	HO-1 induction by SIN-1 was inhibited in the presence of the NO scavenger phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide and the soluble guanylyl cyclase inhibitor 1H-[1,2,4]oxadiazole[4, 3-a]quinoxalin-1-one.	phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide	74-127	heme oxygenase 1	Homo sapiens	0-4
10780998-0	2000	Enhanced expression of haem oxygenase-1 by nitric oxide and antiinflammatory drugs in NIH 3T3 fibroblasts.	Nitric Oxide	43-55	heme oxygenase 1	Homo sapiens	23-39
10807735-4	2000	HO-1 induction by SIN-1 was inhibited in the presence of the NO scavenger phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide and the soluble guanylyl cyclase inhibitor 1H-[1,2,4]oxadiazole[4, 3-a]quinoxalin-1-one.	1h-[1,2,4]oxadiazole[4, 3-a]quinoxalin-1-one	171-215	heme oxygenase 1	Homo sapiens	0-4
10807735-8	2000	Pretreatment of cells with a phosphorothioate-linked HO-1 antisense oligonucleotide prevented protection by SIN-1 or 8-bromo-cGMP against tumor necrosis factor-alpha cytotoxicity, whereas sense and scrambled HO-1 were without effect under these conditions.	Parathion	29-45	heme oxygenase 1	Homo sapiens	53-57
10807735-8	2000	Pretreatment of cells with a phosphorothioate-linked HO-1 antisense oligonucleotide prevented protection by SIN-1 or 8-bromo-cGMP against tumor necrosis factor-alpha cytotoxicity, whereas sense and scrambled HO-1 were without effect under these conditions.	Parathion	29-45	heme oxygenase 1	Homo sapiens	208-212
10807735-8	2000	Pretreatment of cells with a phosphorothioate-linked HO-1 antisense oligonucleotide prevented protection by SIN-1 or 8-bromo-cGMP against tumor necrosis factor-alpha cytotoxicity, whereas sense and scrambled HO-1 were without effect under these conditions.	Oligonucleotides	68-83	heme oxygenase 1	Homo sapiens	53-57
10807735-8	2000	Pretreatment of cells with a phosphorothioate-linked HO-1 antisense oligonucleotide prevented protection by SIN-1 or 8-bromo-cGMP against tumor necrosis factor-alpha cytotoxicity, whereas sense and scrambled HO-1 were without effect under these conditions.	Oligonucleotides	68-83	heme oxygenase 1	Homo sapiens	208-212
10807735-9	2000	Our results show for the first time that HO-1 is a cGMP-sensitive endothelial gene and establish conclusively a causal relationship between HO-1 induction and endothelial protection by the NO/cGMP system.	Cyclic GMP	51-55	heme oxygenase 1	Homo sapiens	41-45
10807735-9	2000	Our results show for the first time that HO-1 is a cGMP-sensitive endothelial gene and establish conclusively a causal relationship between HO-1 induction and endothelial protection by the NO/cGMP system.	Cyclic GMP	51-55	heme oxygenase 1	Homo sapiens	140-144
10807735-9	2000	Our results show for the first time that HO-1 is a cGMP-sensitive endothelial gene and establish conclusively a causal relationship between HO-1 induction and endothelial protection by the NO/cGMP system.	Cyclic GMP	192-196	heme oxygenase 1	Homo sapiens	41-45
10807735-9	2000	Our results show for the first time that HO-1 is a cGMP-sensitive endothelial gene and establish conclusively a causal relationship between HO-1 induction and endothelial protection by the NO/cGMP system.	Cyclic GMP	192-196	heme oxygenase 1	Homo sapiens	140-144
10780998-5	2000	Incubation of cells with NO donors, spermine nonoate (SPNO) and S-nitroso-N-acetylpenicillamine (SNAP), induced a dose- and time-dependent expression of HO-1 protein.	spermine nitric oxide complex	54-58	heme oxygenase 1	Homo sapiens	153-157
10780998-5	2000	Incubation of cells with NO donors, spermine nonoate (SPNO) and S-nitroso-N-acetylpenicillamine (SNAP), induced a dose- and time-dependent expression of HO-1 protein.	S-Nitroso-N-Acetylpenicillamine	64-95	heme oxygenase 1	Homo sapiens	153-157
10780998-5	2000	Incubation of cells with NO donors, spermine nonoate (SPNO) and S-nitroso-N-acetylpenicillamine (SNAP), induced a dose- and time-dependent expression of HO-1 protein.	S-Nitroso-N-Acetylpenicillamine	97-101	heme oxygenase 1	Homo sapiens	153-157
10780998-8	2000	COX-2 protein was weakly induced by SPNO in basal conditions and in the presence of LPS a synergy for HO-1 and COX-2 protein expression was observed.	spermine nitric oxide complex	36-40	heme oxygenase 1	Homo sapiens	102-106
10780998-10	2000	Our results indicate that reactive oxygen species participate in the inductive effect of NO donors or LPS on HO-1 expression, whereas endogenous NO production may play a role in the mechanism of the synergy exhibited by SPNO and LPS on HO-1 and COX-2 expression.	Reactive Oxygen Species	26-49	heme oxygenase 1	Homo sapiens	109-113
10780998-10	2000	Our results indicate that reactive oxygen species participate in the inductive effect of NO donors or LPS on HO-1 expression, whereas endogenous NO production may play a role in the mechanism of the synergy exhibited by SPNO and LPS on HO-1 and COX-2 expression.	spermine nitric oxide complex	220-224	heme oxygenase 1	Homo sapiens	236-240
10780998-13	2000	The selective COX-2 inhibitors SC58125 and NS398 as well as the non-selective COX inhibitor, indomethacin, strongly reduced PGE(2) synthesis and showed a synergy with NO donors in HO-1 and COX-2 induction.	1-((4-methylsulfonyl)phenyl)-3-trifluoromethyl-5-(4-fluorophenyl)pyrazole	31-38	heme oxygenase 1	Homo sapiens	180-184
10872747-5	2000	Pre-treatment of the cells with PD98059, a selective ERK pathway inhibitor, and SB203580, a p38 MAPK inhibitor, blocked the induction of HO-1 by the NO donor in a dose-dependent manner.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	32-39	heme oxygenase 1	Homo sapiens	137-141
10872745-5	2000	We had previously shown that inhibitors of HO-1 and the mitochondrial permeability transition pore (MTP) block the uptake of mitochondrial iron in astrocytes exposed to the pro-oxidant effects of dopamine and several pro-inflammatory cytokines.	Iron	139-143	heme oxygenase 1	Homo sapiens	43-47
10872745-5	2000	We had previously shown that inhibitors of HO-1 and the mitochondrial permeability transition pore (MTP) block the uptake of mitochondrial iron in astrocytes exposed to the pro-oxidant effects of dopamine and several pro-inflammatory cytokines.	Dopamine	196-204	heme oxygenase 1	Homo sapiens	43-47
10872747-5	2000	Pre-treatment of the cells with PD98059, a selective ERK pathway inhibitor, and SB203580, a p38 MAPK inhibitor, blocked the induction of HO-1 by the NO donor in a dose-dependent manner.	SB 203580	80-88	heme oxygenase 1	Homo sapiens	137-141
10780998-13	2000	The selective COX-2 inhibitors SC58125 and NS398 as well as the non-selective COX inhibitor, indomethacin, strongly reduced PGE(2) synthesis and showed a synergy with NO donors in HO-1 and COX-2 induction.	N-(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide	43-48	heme oxygenase 1	Homo sapiens	180-184
10872747-12	2000	ERK and p38 inhibitors also suppressed induction of HO-1 by SNAP and GSNO.	snap	60-64	heme oxygenase 1	Homo sapiens	52-56
10872745-7	2000	Thus, the marked enhancement of HO-1 expression previously demonstrated in AD-affected neurons and astroglia may transduce amyloid (oxidative) stress into the abnormal patterns of iron deposition and mitochondrial insufficiency characteristic of this disease.	Iron	180-184	heme oxygenase 1	Homo sapiens	32-36
10872745-8	2000	Finally, in experiments employing cytotoxic concentrations of A40, we provide evidence that inhibition of HO-1 transcription and related mitochondrial iron deposition may be an important mechanism by which DEX protects tissues subjected to amyloid stress.	Dexamethasone	206-209	heme oxygenase 1	Homo sapiens	106-110
10780998-13	2000	The selective COX-2 inhibitors SC58125 and NS398 as well as the non-selective COX inhibitor, indomethacin, strongly reduced PGE(2) synthesis and showed a synergy with NO donors in HO-1 and COX-2 induction.	Indomethacin	93-105	heme oxygenase 1	Homo sapiens	180-184
10872747-0	2000	Nitric oxide induces heme oxygenase-1 via mitogen-activated protein kinases ERK and p38.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	21-37
10872747-12	2000	ERK and p38 inhibitors also suppressed induction of HO-1 by SNAP and GSNO.	S-Nitrosoglutathione	69-73	heme oxygenase 1	Homo sapiens	52-56
10773020-10	2000	The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes.	Bilirubin	264-273	heme oxygenase 1	Homo sapiens	16-20
10872747-13	2000	The increase in HO-1 mRNA was inhibited by actinomycin D and cycloheximide, but not by NAC, and was not mimicked by the lipophilic cGMP analogue, 8-bromo-cGMP, suggesting that NO-mediated induction required de novo RNA and protein synthesis and was unrelated to cGMP and redox signaling.	Dactinomycin	43-56	heme oxygenase 1	Homo sapiens	16-20
10872747-13	2000	The increase in HO-1 mRNA was inhibited by actinomycin D and cycloheximide, but not by NAC, and was not mimicked by the lipophilic cGMP analogue, 8-bromo-cGMP, suggesting that NO-mediated induction required de novo RNA and protein synthesis and was unrelated to cGMP and redox signaling.	Cycloheximide	61-74	heme oxygenase 1	Homo sapiens	16-20
10872747-13	2000	The increase in HO-1 mRNA was inhibited by actinomycin D and cycloheximide, but not by NAC, and was not mimicked by the lipophilic cGMP analogue, 8-bromo-cGMP, suggesting that NO-mediated induction required de novo RNA and protein synthesis and was unrelated to cGMP and redox signaling.	Cyclic GMP	154-158	heme oxygenase 1	Homo sapiens	16-20
10872748-7	2000	Analysis of MT-1, MT-2 and HO-1 expression, through Western and Northern blotting, indicates that there is a variable pattern of induction and suppression of these two genes following hypoxia preconditioning alone as well as after kainic acid-induced seizures compared to non-preconditioned animals.	Kainic Acid	231-242	heme oxygenase 1	Homo sapiens	27-31
10773020-7	2000	In addition, we investigated the possibility that the human HO-1 gene altered the expression of the endogenous rat enzyme after administration of cobalt chloride s.c. Cobalt chloride administration resulted in increased HO activity in all tissues examined in rats transduced with the human HO-1 gene to the same degree as in nontransduced rats.	cobaltous chloride	146-161	heme oxygenase 1	Homo sapiens	60-64
10773020-7	2000	In addition, we investigated the possibility that the human HO-1 gene altered the expression of the endogenous rat enzyme after administration of cobalt chloride s.c. Cobalt chloride administration resulted in increased HO activity in all tissues examined in rats transduced with the human HO-1 gene to the same degree as in nontransduced rats.	cobaltous chloride	167-182	heme oxygenase 1	Homo sapiens	60-64
10773020-7	2000	In addition, we investigated the possibility that the human HO-1 gene altered the expression of the endogenous rat enzyme after administration of cobalt chloride s.c. Cobalt chloride administration resulted in increased HO activity in all tissues examined in rats transduced with the human HO-1 gene to the same degree as in nontransduced rats.	cobaltous chloride	167-182	heme oxygenase 1	Homo sapiens	290-294
10773020-9	2000	The increase in HO activity after adenoviral-mediated human HO-1 transfer was associated with a decrease in microsomal heme-CYP and CYP activity.	Heme	119-123	heme oxygenase 1	Homo sapiens	60-64
10773020-10	2000	The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes.	Carbon Monoxide	244-259	heme oxygenase 1	Homo sapiens	16-20
10773020-10	2000	The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes.	Carbon Monoxide	244-259	heme oxygenase 1	Homo sapiens	62-66
10872747-2	2000	Nitric oxide (NO) is among the extensive array of stimuli that induce HO-1.	Nitric Oxide	0-12	heme oxygenase 1	Homo sapiens	70-74
10872747-4	2000	In the present study, we have demonstrated that exposure of HeLa cells to the NO donor, sodium nitroprusside (SNP), results in concentration and time-dependent increase in HO-1 mRNA and activation of MAPKs: ERK (ERK1 and ERK2) and p38 pathways, but not SAPK/JNK pathway.	Nitroprusside	88-108	heme oxygenase 1	Homo sapiens	172-176
10773020-10	2000	The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes.	Carbon Monoxide	244-259	heme oxygenase 1	Homo sapiens	62-66
10773020-10	2000	The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes.	Bilirubin	264-273	heme oxygenase 1	Homo sapiens	62-66
10773020-10	2000	The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes.	Bilirubin	264-273	heme oxygenase 1	Homo sapiens	62-66
10766788-7	2000	Based on sequence identity with the mammalian enzymes the proximal ligand in HO-1 (His-25) and HO-2 (His-45) is conserved (His-20) in the bacterial enzyme.	Histidine	83-86	heme oxygenase 1	Homo sapiens	77-81
10766788-7	2000	Based on sequence identity with the mammalian enzymes the proximal ligand in HO-1 (His-25) and HO-2 (His-45) is conserved (His-20) in the bacterial enzyme.	Histidine	101-104	heme oxygenase 1	Homo sapiens	77-81
10766788-7	2000	Based on sequence identity with the mammalian enzymes the proximal ligand in HO-1 (His-25) and HO-2 (His-45) is conserved (His-20) in the bacterial enzyme.	Histidine	101-104	heme oxygenase 1	Homo sapiens	77-81
10746601-1	2000	BACKGROUND: Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that catalyzes the degradation of heme to biliverdin.	Heme	97-101	heme oxygenase 1	Homo sapiens	12-28
10733947-1	2000	Heme oxygenase-1 is the heme catabolic enzyme induced in human dermal fibroblasts by environmental stress.	Heme	24-28	heme oxygenase 1	Homo sapiens	0-16
10733947-4	2000	The relationship between heme oxygenase-1 activation and iron metabolism was investigated by measurement of activities of both cytosolic and mitochondrial cis-aconitase enzymes.	Iron	57-61	heme oxygenase 1	Homo sapiens	25-41
10733947-6	2000	We propose that modulation of cis-aconitase activity at the translational level by an increase of cellular iron is an important consequence of heme oxygenase-1 activation.	Iron	107-111	heme oxygenase 1	Homo sapiens	143-159
11232594-2	2000	The precipitating cause of such oxidative stress may be misregulated iron homeostasis because there are profound alterations in heme oxygenase-1 (HO-1), redox-active iron, and iron regulatory proteins.	Iron	69-73	heme oxygenase 1	Homo sapiens	128-144
11232594-2	2000	The precipitating cause of such oxidative stress may be misregulated iron homeostasis because there are profound alterations in heme oxygenase-1 (HO-1), redox-active iron, and iron regulatory proteins.	Iron	69-73	heme oxygenase 1	Homo sapiens	146-150
10746601-1	2000	BACKGROUND: Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that catalyzes the degradation of heme to biliverdin.	Heme	97-101	heme oxygenase 1	Homo sapiens	30-34
10746601-1	2000	BACKGROUND: Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that catalyzes the degradation of heme to biliverdin.	Biliverdine	105-115	heme oxygenase 1	Homo sapiens	12-28
10746601-1	2000	BACKGROUND: Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that catalyzes the degradation of heme to biliverdin.	Biliverdine	105-115	heme oxygenase 1	Homo sapiens	30-34
10746601-7	2000	The AACD group exhibited plasma HO-1 concentrations (1.06 +/- 0.33 microg/mL) intermediate between, but not different from, those of the AD patients and NEC.	aacd	4-8	heme oxygenase 1	Homo sapiens	32-36
10631150-3	2000	A (GT)n dinucleotide repeat in the 5"-flanking region of human HO-1 gene shows length polymorphism and could modulate the level of gene transcription.	n dinucleotide	6-20	heme oxygenase 1	Homo sapiens	63-67
10681502-0	2000	Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1.	Heme	79-83	heme oxygenase 1	Homo sapiens	93-109
10681514-4	2000	In transfected cells overexpressing HO-1, the activity of heme oxygenase was increased, and conversely, the level of tau protein was dramatically decreased when compared with antisense HO-1 or CEP transfected cells.	Heme	58-62	heme oxygenase 1	Homo sapiens	36-40
10653390-9	2000	To explore the hypothesis that these peptides exert their immunosuppressive effect by altering HO-1 activity, animals were treated with iron protoporphyrin, an inducer of HO-1 activity, or tin protoporphyrin, an inhibitor of HO-1.	Heme	136-155	heme oxygenase 1	Homo sapiens	171-175
10653390-9	2000	To explore the hypothesis that these peptides exert their immunosuppressive effect by altering HO-1 activity, animals were treated with iron protoporphyrin, an inducer of HO-1 activity, or tin protoporphyrin, an inhibitor of HO-1.	Heme	136-155	heme oxygenase 1	Homo sapiens	171-175
10733587-7	2000	Activation of the heme oxygenase 1 promoter by arsenite or cadmium and activation of the cadmium-inducible metallothionein promoter also were unaffected by the expression of mutant SWI-SNF components.	Cadmium	59-66	heme oxygenase 1	Homo sapiens	18-34
10672026-3	2000	We report here that the known antioxidant pyrrolidinedithiocarbamate (PDTC) leads to time and dose dependent activation of heat-shock protein 70 (Hsp70) as well as Hsp32 in EC.	pyrrolidine dithiocarbamic acid	42-68	heme oxygenase 1	Homo sapiens	164-169
10672026-3	2000	We report here that the known antioxidant pyrrolidinedithiocarbamate (PDTC) leads to time and dose dependent activation of heat-shock protein 70 (Hsp70) as well as Hsp32 in EC.	pyrrolidine dithiocarbamic acid	70-74	heme oxygenase 1	Homo sapiens	164-169
10631150-8	2000	H2O2 exposure up-regulated the transcriptional activity of the HO-1 promoter/luciferase fusion genes with (GT)16 or (GT)20 but did not do so with (GT)29 or (GT)38.	Hydrogen Peroxide	0-4	heme oxygenase 1	Homo sapiens	63-67
10631150-9	2000	These findings suggest that the large size of a (GT)n repeat in the HO-1 gene promoter may reduce HO-1 inducibility by reactive oxygen species in cigarette smoke, thereby resulting in the development of CPE.	Reactive Oxygen Species	119-142	heme oxygenase 1	Homo sapiens	68-72
10644516-0	2000	Induction of heme oxygenase-1 by hypoxia and free radicals in human dermal fibroblasts.	Free Radicals	45-58	heme oxygenase 1	Homo sapiens	13-29
10644516-1	2000	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme catabolism and presumably is involved in cellular iron homeostasis.	Iron	115-119	heme oxygenase 1	Homo sapiens	0-16
10644516-1	2000	Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme catabolism and presumably is involved in cellular iron homeostasis.	Iron	115-119	heme oxygenase 1	Homo sapiens	18-22
10863530-8	2000	Mammalian cells also sense and respond to sub-toxic levels of nitric oxide, activating expression of heme oxygenase 1 through stabilization of its mRNA.	Nitric Oxide	62-74	heme oxygenase 1	Homo sapiens	101-117
10644516-6	2000	In contrast, HO-1 induction by the oxidants, H(2)O(2) and carbonyl cyanide m-chlorophenylhydrazone (CCCP) was significantly attenuated in the presence of free radical scavengers.	Hydrogen Peroxide	45-53	heme oxygenase 1	Homo sapiens	13-17
10644516-6	2000	In contrast, HO-1 induction by the oxidants, H(2)O(2) and carbonyl cyanide m-chlorophenylhydrazone (CCCP) was significantly attenuated in the presence of free radical scavengers.	Carbonyl Cyanide m-Chlorophenyl Hydrazone	58-98	heme oxygenase 1	Homo sapiens	13-17
10644516-6	2000	In contrast, HO-1 induction by the oxidants, H(2)O(2) and carbonyl cyanide m-chlorophenylhydrazone (CCCP) was significantly attenuated in the presence of free radical scavengers.	Carbonyl Cyanide m-Chlorophenyl Hydrazone	100-104	heme oxygenase 1	Homo sapiens	13-17
10644516-8	2000	Iron depletion by desferrioxamine mesylate, a specific iron complexon, completely inhibited hypoxic stimulation of HO-1 but did not attenuate the effect of H(2)O(2) and CCCP on HO-1 mRNA.	Iron	0-4	heme oxygenase 1	Homo sapiens	115-119
10644516-8	2000	Iron depletion by desferrioxamine mesylate, a specific iron complexon, completely inhibited hypoxic stimulation of HO-1 but did not attenuate the effect of H(2)O(2) and CCCP on HO-1 mRNA.	Deferoxamine	18-42	heme oxygenase 1	Homo sapiens	115-119
10644516-8	2000	Iron depletion by desferrioxamine mesylate, a specific iron complexon, completely inhibited hypoxic stimulation of HO-1 but did not attenuate the effect of H(2)O(2) and CCCP on HO-1 mRNA.	Iron	55-59	heme oxygenase 1	Homo sapiens	115-119
10644516-9	2000	Addition of Fe(2+), Fe(3+), or holo-transferrin to fibroblasts increased levels of HO-1 mRNA.	ammonium ferrous sulfate	12-18	heme oxygenase 1	Homo sapiens	83-87
10644516-9	2000	Addition of Fe(2+), Fe(3+), or holo-transferrin to fibroblasts increased levels of HO-1 mRNA.	ferric sulfate	20-26	heme oxygenase 1	Homo sapiens	83-87
15693275-6	2000	Our results show that Homocysteine (Hcy) and oxidized LDL (oxLDL) enhance the activity and expression of oxidative stress markers, such as NFkB and heme oxygenase 1.	Homocysteine	22-34	heme oxygenase 1	Homo sapiens	148-164
15693275-6	2000	Our results show that Homocysteine (Hcy) and oxidized LDL (oxLDL) enhance the activity and expression of oxidative stress markers, such as NFkB and heme oxygenase 1.	Homocysteine	36-39	heme oxygenase 1	Homo sapiens	148-164
10631150-9	2000	These findings suggest that the large size of a (GT)n repeat in the HO-1 gene promoter may reduce HO-1 inducibility by reactive oxygen species in cigarette smoke, thereby resulting in the development of CPE.	Reactive Oxygen Species	119-142	heme oxygenase 1	Homo sapiens	98-102
10842752-4	2000	In fact, in oxidative stress in vitro, HO-1 is protective (91-94) but within a narrow threshold of overexpression (93,94) in some models, since iron released in the HO reaction may obviate any cytoprotective effect (Fig.	Iron	144-148	heme oxygenase 1	Homo sapiens	39-43
10564189-2	1999	Our results show that especially Zn(2+) and Cd(2+) are inducers of 70-kDa (HSP70), 60-kDa (HSP60), 32-kDa (HSP32), and 27-kDa (HSP27) HSPs.	Zinc	33-35	heme oxygenase 1	Homo sapiens	107-112
10627295-8	2000	HO-1 immunostaining was low in the placenta but intense on the CTB within the placental bed.	ctb	63-66	heme oxygenase 1	Homo sapiens	0-4
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Biliverdine	83-93	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Biliverdine	83-93	heme oxygenase 1	Homo sapiens	60-64
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Carbon Monoxide	95-110	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Carbon Monoxide	95-110	heme oxygenase 1	Homo sapiens	60-64
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Carbon Monoxide	112-114	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Carbon Monoxide	112-114	heme oxygenase 1	Homo sapiens	60-64
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Iron	121-125	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Iron	121-125	heme oxygenase 1	Homo sapiens	60-64
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Iron	127-129	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Iron	127-129	heme oxygenase 1	Homo sapiens	60-64
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Carbon Monoxide	165-167	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Carbon Monoxide	165-167	heme oxygenase 1	Homo sapiens	60-64
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Iron	172-174	heme oxygenase 1	Homo sapiens	42-58
10589693-4	1999	Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression.	Iron	172-174	heme oxygenase 1	Homo sapiens	60-64
10589693-6	1999	Glomerular HO-1 expression in nephritic animals was upregulated by treatment with hemin (30 micromol/kg body wt).	Hemin	82-87	heme oxygenase 1	Homo sapiens	11-15
10589693-12	1999	Hemin treatment of nephritic animals resulted in upregulation of glomerular HO-1 levels and a two- to threefold reduction in glomerular iNOS mRNA levels.	Hemin	0-5	heme oxygenase 1	Homo sapiens	76-80
10589693-15	1999	These studies demonstrate that in glomerular immune injury, hemin treatment upregulates glomerular HO-1 with an attendant downregulation of iNOS expression, and thus points to regulatory interaction between the two systems.	Hemin	60-65	heme oxygenase 1	Homo sapiens	99-103
10629191-4	2000	The product of the hemO gene is homologous to enzymes that degrade heme; 21% of its amino acid residues are identical, and 44% are similar, to those of the human heme oxygenase-1.	Heme	67-71	heme oxygenase 1	Homo sapiens	162-178
10630670-3	1999	However, as attempts are made to unravel the mechanisms by which HO-1 is induced and as we discover that CO, iron and bilirubin may be important effector molecules, we are learning to appreciate that heme oxygenases may be central to the regulation of many physiological and pathophysiological processes besides their established function in heme catabolism.	Heme	200-204	heme oxygenase 1	Homo sapiens	65-69
10581397-0	1999	Regulation of heme oxygenase-1 expression by dopamine in cultured C6 glioma and primary astrocytes.	Dopamine	45-53	heme oxygenase 1	Homo sapiens	14-30
10581397-1	1999	Heme oxygenase-1 (HO-1) is an inducible enzyme involved in heme catabolism, tissue iron homeostasis and the cellular response to oxidative stress.	Iron	83-87	heme oxygenase 1	Homo sapiens	0-16
10581397-1	1999	Heme oxygenase-1 (HO-1) is an inducible enzyme involved in heme catabolism, tissue iron homeostasis and the cellular response to oxidative stress.	Iron	83-87	heme oxygenase 1	Homo sapiens	18-22
10581397-2	1999	Elevated HO-1 expression in astrocytes has been observed in association with abnormal iron deposition and increased oxidative stress in Parkinson"s disease (PD).	Iron	86-90	heme oxygenase 1	Homo sapiens	9-13
10581397-4	1999	Here we report that dopamine is a potent inducer of HO-1.	Dopamine	20-28	heme oxygenase 1	Homo sapiens	52-56
10581397-6	1999	When the time-course of HO-1 expression was compared between dopamine and hemin, the latter induced the gene immediately while the former did so with a lag.	Dopamine	61-69	heme oxygenase 1	Homo sapiens	24-28
10581397-6	1999	When the time-course of HO-1 expression was compared between dopamine and hemin, the latter induced the gene immediately while the former did so with a lag.	Hemin	74-79	heme oxygenase 1	Homo sapiens	24-28
10581397-8	1999	However, cycloheximide blocked both hemin- and dopamine-induced HO-1 expression, suggesting that both pathways may involve proteins with short half-lives.	Cycloheximide	9-22	heme oxygenase 1	Homo sapiens	64-68
10581397-8	1999	However, cycloheximide blocked both hemin- and dopamine-induced HO-1 expression, suggesting that both pathways may involve proteins with short half-lives.	Dopamine	47-55	heme oxygenase 1	Homo sapiens	64-68
10581397-9	1999	Ascorbic acid blocked dopamine induction of HO-1 but had no effect on hemin-induced expression.	Ascorbic Acid	0-13	heme oxygenase 1	Homo sapiens	44-48
10581397-9	1999	Ascorbic acid blocked dopamine induction of HO-1 but had no effect on hemin-induced expression.	Dopamine	22-30	heme oxygenase 1	Homo sapiens	44-48
10581397-12	1999	These results suggest that dopamine, released or secreted from affected neurons, may trigger HO-1 expression in neighboring astrocytes.	Dopamine	27-35	heme oxygenase 1	Homo sapiens	93-97
10581397-13	1999	HO-1 and its metabolites could then contribute to the oxidative stress and iron deposition associated with PD.	Iron	75-79	heme oxygenase 1	Homo sapiens	0-4
10564189-2	1999	Our results show that especially Zn(2+) and Cd(2+) are inducers of 70-kDa (HSP70), 60-kDa (HSP60), 32-kDa (HSP32), and 27-kDa (HSP27) HSPs.	Cadmium	44-46	heme oxygenase 1	Homo sapiens	107-112
10490932-4	1999	Additionally, we studied HO-1 expression in experimental models of adhesion molecule expression produced by heme in endothelial cells, and the relationship of HO-1 expression to the induced adhesion molecules.	Heme	108-112	heme oxygenase 1	Homo sapiens	25-29
10547244-1	1999	OBJECTIVES: Oxidative stress and inflammation induce the expression of heme oxygenase-1, which produces carbon monoxide (CO), and nitric oxide synthase, which produces nitric oxide (NO).	Carbon Monoxide	104-119	heme oxygenase 1	Homo sapiens	71-87
10547244-1	1999	OBJECTIVES: Oxidative stress and inflammation induce the expression of heme oxygenase-1, which produces carbon monoxide (CO), and nitric oxide synthase, which produces nitric oxide (NO).	Carbon Monoxide	121-123	heme oxygenase 1	Homo sapiens	71-87
10564544-2	1999	We have shown that the inflammatory cytokines, interleukin-6 (IL-6) and heme-induced HO-1 gene expression, were suppressed by dexamethasone (Dex) in a sustained manner.	Dexamethasone	126-139	heme oxygenase 1	Homo sapiens	85-89
10564544-2	1999	We have shown that the inflammatory cytokines, interleukin-6 (IL-6) and heme-induced HO-1 gene expression, were suppressed by dexamethasone (Dex) in a sustained manner.	Dexamethasone	141-144	heme oxygenase 1	Homo sapiens	85-89
10564544-4	1999	Endothelial cells treated with heme (10 microM) and IL-6 (25 ng/ml), increased HO-1 mRNA 15- and 60-fold, respectively.	Heme	31-35	heme oxygenase 1	Homo sapiens	79-83
10564544-7	1999	Several human HO-1 promoter-drive chloramphenicol acetyltransferase (CAT) constructs were examined to analyze IL-6 and Dex-mediated modulation of the HO-1 gene in endothelial cells.	Dexamethasone	119-122	heme oxygenase 1	Homo sapiens	150-154
10517538-2	1999	The expression of several genes (including heme oxygenase-1, HO-1; collagenase; the CL100 phosphatase and the nuclear oncogenes, c-fos and c-jun) is induced following physiological doses of UVA to cells and this effect can be strongly enhanced by removing intracellular glutathione or enhancing singlet oxygen lifetime.	Glutathione	270-281	heme oxygenase 1	Homo sapiens	43-59
10517538-2	1999	The expression of several genes (including heme oxygenase-1, HO-1; collagenase; the CL100 phosphatase and the nuclear oncogenes, c-fos and c-jun) is induced following physiological doses of UVA to cells and this effect can be strongly enhanced by removing intracellular glutathione or enhancing singlet oxygen lifetime.	Glutathione	270-281	heme oxygenase 1	Homo sapiens	61-65
10517538-2	1999	The expression of several genes (including heme oxygenase-1, HO-1; collagenase; the CL100 phosphatase and the nuclear oncogenes, c-fos and c-jun) is induced following physiological doses of UVA to cells and this effect can be strongly enhanced by removing intracellular glutathione or enhancing singlet oxygen lifetime.	Singlet Oxygen	295-309	heme oxygenase 1	Homo sapiens	43-59
10517538-2	1999	The expression of several genes (including heme oxygenase-1, HO-1; collagenase; the CL100 phosphatase and the nuclear oncogenes, c-fos and c-jun) is induced following physiological doses of UVA to cells and this effect can be strongly enhanced by removing intracellular glutathione or enhancing singlet oxygen lifetime.	Singlet Oxygen	295-309	heme oxygenase 1	Homo sapiens	61-65
10517538-3	1999	We have observed that heme is released from microsomal heme-containing proteins by UVA and other oxidants and that activation of HO-1 expression by UVA correlates with levels of heme release.	Heme	22-26	heme oxygenase 1	Homo sapiens	129-133
10517538-4	1999	UVA radiation also leads to an increase in labile iron pools (either directly or via HO-1) and eventual increases in ferritin levels.	Iron	50-54	heme oxygenase 1	Homo sapiens	85-89
10490932-17	1999	It is possible that amelioration of the heme-induced oxidative stress and expression of ICAM-I is due, in part, to the induction of HO-1 activity.	Heme	40-44	heme oxygenase 1	Homo sapiens	132-136
10490932-9	1999	Endothelial cells exposed to heme elicited increased HO activity, which was prevented (70%) by HO-1 antisense ODNs.	Heme	29-33	heme oxygenase 1	Homo sapiens	95-99
10490932-11	1999	Addition of HO-1 antisense ODNs prevented heme degradation and resulted in elevation of microsomal heme.	Heme	42-46	heme oxygenase 1	Homo sapiens	12-16
10490932-11	1999	Addition of HO-1 antisense ODNs prevented heme degradation and resulted in elevation of microsomal heme.	Heme	99-103	heme oxygenase 1	Homo sapiens	12-16
10490624-6	1999	5"-AMP and to a lesser extent 5"-ADP inhibit c-Src when combined with either HSP-27 or HSP-32.	Adenosine Monophosphate	0-6	heme oxygenase 1	Homo sapiens	87-93
10490932-13	1999	Incubation of endothelial cells with HO-1 antisense enhanced heme-dependent increase of ICAM-1.	Heme	61-65	heme oxygenase 1	Homo sapiens	37-41
10491455-3	1999	Exhaled carbon monoxide (CO), a product of heme degradation by heme oxygenase 1 (HO-1) which is induced by inflammatory cytokines and oxidants, was therefore tested as a non-invasive marker of airway inflammation and oxidative stress.	Carbon Monoxide	8-23	heme oxygenase 1	Homo sapiens	63-79
10491455-3	1999	Exhaled carbon monoxide (CO), a product of heme degradation by heme oxygenase 1 (HO-1) which is induced by inflammatory cytokines and oxidants, was therefore tested as a non-invasive marker of airway inflammation and oxidative stress.	Carbon Monoxide	8-23	heme oxygenase 1	Homo sapiens	81-85
10491455-3	1999	Exhaled carbon monoxide (CO), a product of heme degradation by heme oxygenase 1 (HO-1) which is induced by inflammatory cytokines and oxidants, was therefore tested as a non-invasive marker of airway inflammation and oxidative stress.	Carbon Monoxide	25-27	heme oxygenase 1	Homo sapiens	63-79
10491455-3	1999	Exhaled carbon monoxide (CO), a product of heme degradation by heme oxygenase 1 (HO-1) which is induced by inflammatory cytokines and oxidants, was therefore tested as a non-invasive marker of airway inflammation and oxidative stress.	Carbon Monoxide	25-27	heme oxygenase 1	Homo sapiens	81-85
10491455-3	1999	Exhaled carbon monoxide (CO), a product of heme degradation by heme oxygenase 1 (HO-1) which is induced by inflammatory cytokines and oxidants, was therefore tested as a non-invasive marker of airway inflammation and oxidative stress.	Heme	43-47	heme oxygenase 1	Homo sapiens	81-85
10491455-10	1999	CONCLUSIONS: High exhaled CO concentrations in patients with cystic fibrosis may reflect induction of HO-1.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	102-106
10460761-5	1999	Tin protoporphyrin IX (50 micrometer) and zinc protoporphyrin IX (10 microM), inhibitors of HO-1, reduced hemin-induced and IL-1beta-induced inhibitory effects.	tin protoporphyrin IX	0-21	heme oxygenase 1	Homo sapiens	92-96
10460761-5	1999	Tin protoporphyrin IX (50 micrometer) and zinc protoporphyrin IX (10 microM), inhibitors of HO-1, reduced hemin-induced and IL-1beta-induced inhibitory effects.	zinc protoporphyrin	42-64	heme oxygenase 1	Homo sapiens	92-96
10460761-9	1999	These findings suggest that HO-1 induction provides protection against H(2)O(2)-induced injury of the cultured human airway epithelial cells in part via the HO-bilirubin pathway.	Hydrogen Peroxide	71-79	heme oxygenase 1	Homo sapiens	28-32
10460761-9	1999	These findings suggest that HO-1 induction provides protection against H(2)O(2)-induced injury of the cultured human airway epithelial cells in part via the HO-bilirubin pathway.	Bilirubin	160-169	heme oxygenase 1	Homo sapiens	28-32
12835114-3	1999	The effects of dopamine on HO-1 expression were inhibited by ascorbate implicating a free radical mechanism of action.	Dopamine	15-23	heme oxygenase 1	Homo sapiens	27-31
12835114-3	1999	The effects of dopamine on HO-1 expression were inhibited by ascorbate implicating a free radical mechanism of action.	Ascorbic Acid	61-70	heme oxygenase 1	Homo sapiens	27-31
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	Dopamine	0-8	heme oxygenase 1	Homo sapiens	175-179
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	Iron	31-35	heme oxygenase 1	Homo sapiens	175-179
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	tin mesoporphyrin	111-128	heme oxygenase 1	Homo sapiens	175-179
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	tin mesoporphyrin	130-134	heme oxygenase 1	Homo sapiens	175-179
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	Dexamethasone	139-152	heme oxygenase 1	Homo sapiens	175-179
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	Dexamethasone	154-157	heme oxygenase 1	Homo sapiens	175-179
12835114-4	1999	Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells.	Iron	235-239	heme oxygenase 1	Homo sapiens	175-179
12835114-5	1999	Overexpression of the human HO-1 gene in cultured rat astroglia by transient transfection also stimulated mitochondrial (55)Fe deposition, an effect that was again preventible by SnMP or DEX administration.	Iron	124-126	heme oxygenase 1	Homo sapiens	28-32
12835114-5	1999	Overexpression of the human HO-1 gene in cultured rat astroglia by transient transfection also stimulated mitochondrial (55)Fe deposition, an effect that was again preventible by SnMP or DEX administration.	tin mesoporphyrin	179-183	heme oxygenase 1	Homo sapiens	28-32
12835114-5	1999	Overexpression of the human HO-1 gene in cultured rat astroglia by transient transfection also stimulated mitochondrial (55)Fe deposition, an effect that was again preventible by SnMP or DEX administration.	Dexamethasone	187-190	heme oxygenase 1	Homo sapiens	28-32
12835114-6	1999	We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle.	ammonium ferrous sulfate	25-32	heme oxygenase 1	Homo sapiens	71-75
12835114-6	1999	We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle.	Iron	33-37	heme oxygenase 1	Homo sapiens	71-75
12835114-6	1999	We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle.	Carbon Monoxide	42-57	heme oxygenase 1	Homo sapiens	71-75
12835114-6	1999	We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle.	Heme	85-89	heme oxygenase 1	Homo sapiens	71-75
12835114-6	1999	We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle.	Iron	175-179	heme oxygenase 1	Homo sapiens	71-75
12835114-8	1999	Stress-induced up-regulation of HO-1 in astroglia may be responsible for the abnormal patterns of brain iron deposition and mitochondrial insufficiency documented in various human neurodegenerative disorders.	Iron	104-108	heme oxygenase 1	Homo sapiens	32-36
10423162-0	1999	Induction of heme oxygenase-1 as a response in sensing the signals evoked by distinct nitric oxide donors.	Nitric Oxide	86-98	heme oxygenase 1	Homo sapiens	13-29
10423162-1	1999	To gain insights into the cellular responses evoked by nitric oxide (NO), we have studied the effects of NO donors with distinct chemistries on the expression of heme oxygenase-1 mRNA by northern blot analysis.	Nitric Oxide	55-67	heme oxygenase 1	Homo sapiens	162-178
10423162-2	1999	The expression levels of heme oxygenase-1 mRNA were increased significantly in DLD-1 human colorectal adenocarcinoma cells by treatment with each of three NO donors: sodium nitroprusside (SNP), S-nitroso-L-glutathione (GSNO), and 3-morpholinosydnonimine (SIN-1).	Nitroprusside	166-186	heme oxygenase 1	Homo sapiens	25-41
10423162-2	1999	The expression levels of heme oxygenase-1 mRNA were increased significantly in DLD-1 human colorectal adenocarcinoma cells by treatment with each of three NO donors: sodium nitroprusside (SNP), S-nitroso-L-glutathione (GSNO), and 3-morpholinosydnonimine (SIN-1).	S-Nitrosoglutathione	194-217	heme oxygenase 1	Homo sapiens	25-41
10423162-2	1999	The expression levels of heme oxygenase-1 mRNA were increased significantly in DLD-1 human colorectal adenocarcinoma cells by treatment with each of three NO donors: sodium nitroprusside (SNP), S-nitroso-L-glutathione (GSNO), and 3-morpholinosydnonimine (SIN-1).	S-Nitrosoglutathione	219-223	heme oxygenase 1	Homo sapiens	25-41
10423162-2	1999	The expression levels of heme oxygenase-1 mRNA were increased significantly in DLD-1 human colorectal adenocarcinoma cells by treatment with each of three NO donors: sodium nitroprusside (SNP), S-nitroso-L-glutathione (GSNO), and 3-morpholinosydnonimine (SIN-1).	linsidomine	230-253	heme oxygenase 1	Homo sapiens	25-41
10423162-3	1999	A combination of SIN-1 plus SNP or GSNO additively increased heme oxygenase-1 mRNA expression, whereas synergistic induction was seen with SNP plus GSNO.	S-Nitrosoglutathione	35-39	heme oxygenase 1	Homo sapiens	61-77
10423162-6	1999	Transient transfection assays suggested that treatment with SNP, but not with GSNO or SIN-1, increased the expression of a reporter gene through a cis-acting element, including the cadmium-responsive element, of the human heme oxygenase-1 gene.	Cadmium	181-188	heme oxygenase 1	Homo sapiens	222-238
10409239-2	1999	Overexpression of HO-1 in cells might, therefore, protect against oxidative stress produced by certain agents, specifically heme, by catalyzing its degradation to bilirubin, which by itself has antioxidant properties.	Heme	124-128	heme oxygenase 1	Homo sapiens	18-22
10409239-2	1999	Overexpression of HO-1 in cells might, therefore, protect against oxidative stress produced by certain agents, specifically heme, by catalyzing its degradation to bilirubin, which by itself has antioxidant properties.	Bilirubin	163-172	heme oxygenase 1	Homo sapiens	18-22
10409239-6	1999	Moreover, human HO-1 gene-transduced endothelial cells acquired substantial resistance to toxicity produced by exposure to heme and H(2)O(2) compared with that in nontransduced cells.	Heme	123-127	heme oxygenase 1	Homo sapiens	16-20
10409239-7	1999	The protective effect of enhancement of HO-1 activity against heme and H(2)O(2) was reversed by pretreatment with stannic mesoporphyrin, a competitive inhibitor of HO.	Heme	62-66	heme oxygenase 1	Homo sapiens	40-44
10409239-7	1999	The protective effect of enhancement of HO-1 activity against heme and H(2)O(2) was reversed by pretreatment with stannic mesoporphyrin, a competitive inhibitor of HO.	Hydrogen Peroxide	71-79	heme oxygenase 1	Homo sapiens	40-44
10409239-7	1999	The protective effect of enhancement of HO-1 activity against heme and H(2)O(2) was reversed by pretreatment with stannic mesoporphyrin, a competitive inhibitor of HO.	stannic mesoporphyrin	114-135	heme oxygenase 1	Homo sapiens	40-44
10403520-5	1999	The treatment of the two cell lines with 50 microM CdCl2 induced hsp72, hsp32 and metallothionein (MT-II) mRNAs, and the induction level of each mRNA did not differ in the two cell lines.	Cadmium Chloride	51-56	heme oxygenase 1	Homo sapiens	72-77
10403520-6	1999	However, the treatment with 20 microM CdCl2 induced the hsp72 and hsp32 mRNAs in A2780CP cells less than in A2780 cells, while the MT-II mRNA was induced to similar levels in the two cell lines.	Cadmium Chloride	38-43	heme oxygenase 1	Homo sapiens	66-71
10373419-1	1999	Whether or not reducing equivalents are indispensable for the conversion of ferric alpha-hydroxyheme bound to heme oxygenase-1 to verdoheme remains controversial (Matera, K. M., Takahashi, S., Fujii, H., Zhou, H., Ishikawa, K., Yoshimura, T., Rousseau, D. L., Yoshida, T., and Ikeda-Saito, M. (1996) J. Biol.	ferric alpha-hydroxyheme	76-100	heme oxygenase 1	Homo sapiens	110-126
10513606-10	1999	Strain treatment, similar to H2O2 exposure, induced HO-1 expression in a time-dependent manner.	Hydrogen Peroxide	29-33	heme oxygenase 1	Homo sapiens	52-56
10513606-12	1999	ECs treated with N-acetyl-cysteine abolished HO-1 gene induction.	Acetylcysteine	17-34	heme oxygenase 1	Homo sapiens	45-49
10513606-13	1999	Our results suggest that cyclic strain-induced ROS cause a transient increase of glutathione peroxidase activity that results in a decrease of GSH level in ECs and that this decrease is crucial to HO-1 induction.	Reactive Oxygen Species	47-50	heme oxygenase 1	Homo sapiens	197-201
10373419-1	1999	Whether or not reducing equivalents are indispensable for the conversion of ferric alpha-hydroxyheme bound to heme oxygenase-1 to verdoheme remains controversial (Matera, K. M., Takahashi, S., Fujii, H., Zhou, H., Ishikawa, K., Yoshimura, T., Rousseau, D. L., Yoshida, T., and Ikeda-Saito, M. (1996) J. Biol.	verdoheme	130-139	heme oxygenase 1	Homo sapiens	110-126
10373419-6	1999	To resolve this controversy, we have prepared a ferric alpha-hydroxyheme-heme oxygenase-1 complex and titrated the complex with O2 under strictly anaerobic conditions.	Oxygen	128-130	heme oxygenase 1	Homo sapiens	73-89
10373419-11	1999	The verdoheme formed from alpha-hydroxyheme was shown to be in the ferrous oxidation state by the addition of CO or potassium ferricyanide to the resultant verdoheme-heme oxygenase-1 complex.	verdoheme	4-13	heme oxygenase 1	Homo sapiens	166-182
10373419-11	1999	The verdoheme formed from alpha-hydroxyheme was shown to be in the ferrous oxidation state by the addition of CO or potassium ferricyanide to the resultant verdoheme-heme oxygenase-1 complex.	alpha-hydroxyheme	26-43	heme oxygenase 1	Homo sapiens	166-182
10373419-11	1999	The verdoheme formed from alpha-hydroxyheme was shown to be in the ferrous oxidation state by the addition of CO or potassium ferricyanide to the resultant verdoheme-heme oxygenase-1 complex.	Carbon Monoxide	110-112	heme oxygenase 1	Homo sapiens	166-182
10373419-11	1999	The verdoheme formed from alpha-hydroxyheme was shown to be in the ferrous oxidation state by the addition of CO or potassium ferricyanide to the resultant verdoheme-heme oxygenase-1 complex.	potassium ferricyanide	116-138	heme oxygenase 1	Homo sapiens	166-182
10330231-4	1999	Acute exposure to the PKC activator phorbol 12-myristate 13-acetate (PMA) stimulated HO-1 mRNA.	Tetradecanoylphorbol Acetate	36-67	heme oxygenase 1	Homo sapiens	85-89
10349844-8	1999	Moreover, pretreatment with interferon-gamma partially suppressed the induction of heme oxygenase-1 mRNA expression caused by either sodium nitroprusside, cadmium, or hemin.	Nitroprusside	133-153	heme oxygenase 1	Homo sapiens	83-99
10349844-8	1999	Moreover, pretreatment with interferon-gamma partially suppressed the induction of heme oxygenase-1 mRNA expression caused by either sodium nitroprusside, cadmium, or hemin.	Cadmium	155-162	heme oxygenase 1	Homo sapiens	83-99
10349844-8	1999	Moreover, pretreatment with interferon-gamma partially suppressed the induction of heme oxygenase-1 mRNA expression caused by either sodium nitroprusside, cadmium, or hemin.	Hemin	167-172	heme oxygenase 1	Homo sapiens	83-99
10330231-4	1999	Acute exposure to the PKC activator phorbol 12-myristate 13-acetate (PMA) stimulated HO-1 mRNA.	Tetradecanoylphorbol Acetate	69-72	heme oxygenase 1	Homo sapiens	85-89
10330231-6	1999	Additionally, the phosphatase inhibitors okadaic acid and calyculin enhanced cytokine induction of HO-1.	Okadaic Acid	41-53	heme oxygenase 1	Homo sapiens	99-103
10330231-7	1999	Mepacrine, a PLA2 inhibitor, prevented HO-1 induction by cytokine, suggesting a role for arachidonate, the product of PLA2 hydrolysis of phospholipids, in HO-1 expression.	Quinacrine	0-9	heme oxygenase 1	Homo sapiens	39-43
10330231-7	1999	Mepacrine, a PLA2 inhibitor, prevented HO-1 induction by cytokine, suggesting a role for arachidonate, the product of PLA2 hydrolysis of phospholipids, in HO-1 expression.	Quinacrine	0-9	heme oxygenase 1	Homo sapiens	155-159
10330231-7	1999	Mepacrine, a PLA2 inhibitor, prevented HO-1 induction by cytokine, suggesting a role for arachidonate, the product of PLA2 hydrolysis of phospholipids, in HO-1 expression.	Arachidonic Acid	89-101	heme oxygenase 1	Homo sapiens	39-43
10330231-7	1999	Mepacrine, a PLA2 inhibitor, prevented HO-1 induction by cytokine, suggesting a role for arachidonate, the product of PLA2 hydrolysis of phospholipids, in HO-1 expression.	Arachidonic Acid	89-101	heme oxygenase 1	Homo sapiens	155-159
10330231-7	1999	Mepacrine, a PLA2 inhibitor, prevented HO-1 induction by cytokine, suggesting a role for arachidonate, the product of PLA2 hydrolysis of phospholipids, in HO-1 expression.	Phospholipids	137-150	heme oxygenase 1	Homo sapiens	39-43
10330231-7	1999	Mepacrine, a PLA2 inhibitor, prevented HO-1 induction by cytokine, suggesting a role for arachidonate, the product of PLA2 hydrolysis of phospholipids, in HO-1 expression.	Phospholipids	137-150	heme oxygenase 1	Homo sapiens	155-159
10330231-8	1999	The intracellular calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid acetoxymethyl ester (BAPTA-AM) blocked cytokine induction of HO-1.	Calcium	18-25	heme oxygenase 1	Homo sapiens	153-157
10330231-8	1999	The intracellular calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid acetoxymethyl ester (BAPTA-AM) blocked cytokine induction of HO-1.	1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester	35-111	heme oxygenase 1	Homo sapiens	153-157
10330231-8	1999	The intracellular calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid acetoxymethyl ester (BAPTA-AM) blocked cytokine induction of HO-1.	1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester	113-121	heme oxygenase 1	Homo sapiens	153-157
10330231-9	1999	Paradoxically, the calcium ionophore A-23187 prevented HO-1 induction by cytokine but not by PMA.	Calcium	19-26	heme oxygenase 1	Homo sapiens	55-59
10330231-10	1999	Finally, the oxidant scavenger N-acetylcysteine inhibited HO-1 induction by cytokines.	Acetylcysteine	31-47	heme oxygenase 1	Homo sapiens	58-62
10217256-3	1999	We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia.	Dopamine	158-166	heme oxygenase 1	Homo sapiens	66-82
10425949-2	1999	Synthesis of the enzyme heme oxygenase-1 (HO-1) is increased after exposure of eukaryotic cells to conditions of oxidative stress (including H2O2) as a defense against the damaging effects of free radicals.	Hydrogen Peroxide	141-145	heme oxygenase 1	Homo sapiens	24-40
10217256-3	1999	We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia.	Iron	141-145	heme oxygenase 1	Homo sapiens	66-82
10101013-0	1999	Iron regulates hyperoxia-dependent human heme oxygenase 1 gene expression in pulmonary endothelial cells.	Iron	0-4	heme oxygenase 1	Homo sapiens	41-57
10101013-3	1999	Recently, heme oxygenase 1 (HO-1), the rate-limiting enzyme in the metabolism of heme, has been found to have a protective role in oxidant injury.	Heme	10-14	heme oxygenase 1	Homo sapiens	28-32
10101013-8	1999	We also found that HO-1 expression depended on chelatable iron.	Iron	58-62	heme oxygenase 1	Homo sapiens	19-23
10101013-9	1999	The iron chelator desferrioxamine not only inhibited the iron- dependent potentiation of HO-1 in response to hyperoxia but also inhibited both hyperoxia and basal expression.	Iron	4-8	heme oxygenase 1	Homo sapiens	89-93
10101013-9	1999	The iron chelator desferrioxamine not only inhibited the iron- dependent potentiation of HO-1 in response to hyperoxia but also inhibited both hyperoxia and basal expression.	Deferoxamine	18-33	heme oxygenase 1	Homo sapiens	89-93
10101013-9	1999	The iron chelator desferrioxamine not only inhibited the iron- dependent potentiation of HO-1 in response to hyperoxia but also inhibited both hyperoxia and basal expression.	Iron	57-61	heme oxygenase 1	Homo sapiens	89-93
10101013-11	1999	We also evaluated 4.5 kb of the human HO-1 promoter region and demonstrated that this region has promoter activity to the stimulus heme; however, there was no evidence of promoter activity to either iron or hyperoxia.	Heme	131-135	heme oxygenase 1	Homo sapiens	38-42
10101013-12	1999	This diversity of promoter activity to heme, heavy metals, and hyperoxia is unique to the human HO-1 gene.	Heme	39-43	heme oxygenase 1	Homo sapiens	96-100
10425949-2	1999	Synthesis of the enzyme heme oxygenase-1 (HO-1) is increased after exposure of eukaryotic cells to conditions of oxidative stress (including H2O2) as a defense against the damaging effects of free radicals.	Hydrogen Peroxide	141-145	heme oxygenase 1	Homo sapiens	42-46
10425949-3	1999	Dental pulps were evaluated for HO-1 (aka Heat Shock Protein 32) presence in teeth treated with 10% carbamide peroxide.	Carbamide Peroxide	100-118	heme oxygenase 1	Homo sapiens	32-36
10090762-1	1999	The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized.	Iron	83-87	heme oxygenase 1	Homo sapiens	35-51
10090762-1	1999	The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized.	Iron	83-87	heme oxygenase 1	Homo sapiens	53-58
10090762-1	1999	The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized.	Cysteine	112-120	heme oxygenase 1	Homo sapiens	35-51
10090762-1	1999	The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized.	Cysteine	112-120	heme oxygenase 1	Homo sapiens	53-58
10090762-1	1999	The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized.	Tyrosine	124-132	heme oxygenase 1	Homo sapiens	35-51
10090762-1	1999	The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized.	Tyrosine	124-132	heme oxygenase 1	Homo sapiens	53-58
10218639-4	1999	We also demonstrate a high degree of correlation between the amount of heme released and the degree of subsequent induction of heme oxygenase 1 transcription following UVA and hydrogen peroxide treatment.	Heme	71-75	heme oxygenase 1	Homo sapiens	127-143
10218639-0	1999	Cyclooxygenase dependent release of heme from microsomal hemeproteins correlates with induction of heme oxygenase 1 transcription in human fibroblasts.	Heme	36-40	heme oxygenase 1	Homo sapiens	99-115
10218639-4	1999	We also demonstrate a high degree of correlation between the amount of heme released and the degree of subsequent induction of heme oxygenase 1 transcription following UVA and hydrogen peroxide treatment.	Hydrogen Peroxide	176-193	heme oxygenase 1	Homo sapiens	127-143
10218639-1	1999	Induction of heme oxygenase 1 transcription and enzymatic activity is a common response after exposure of cells to various forms of oxidative stress including ultraviolet A radiation (UVA) and hydrogen peroxide.	Hydrogen Peroxide	193-210	heme oxygenase 1	Homo sapiens	13-29
10218639-5	1999	We propose that release of heme from microsomal hemeproteins determines the degree of induction of heme oxygenase 1 transcription in human fibroblasts after oxidative stress.	Heme	27-31	heme oxygenase 1	Homo sapiens	99-115
9920842-5	1999	Because HO-1 lysed peptide-loaded Fas-deficient target cells derived from a patient with a homozygous Fas gene mutation, its cytotoxicity appeared to be mediated by a Fas-independent pathway.	ammonium ferrous sulfate	34-37	heme oxygenase 1	Homo sapiens	8-12
9920842-5	1999	Because HO-1 lysed peptide-loaded Fas-deficient target cells derived from a patient with a homozygous Fas gene mutation, its cytotoxicity appeared to be mediated by a Fas-independent pathway.	ammonium ferrous sulfate	102-105	heme oxygenase 1	Homo sapiens	8-12
9920842-8	1999	HO-1 expressed mRNA for apoptosis-inducing mediators, including perforin, granzyme B, Fas ligand, TNF-alpha, and lymphotoxin; however, no DNA fragmentation was detected in target cells incubated with HO-1 by 5-[125I]Iodo-2"-deoxyuridine release assay and agarose gel electrophoresis of DNA.	5-[125i]iodo-2"-deoxyuridine	208-236	heme oxygenase 1	Homo sapiens	0-4
9920842-8	1999	HO-1 expressed mRNA for apoptosis-inducing mediators, including perforin, granzyme B, Fas ligand, TNF-alpha, and lymphotoxin; however, no DNA fragmentation was detected in target cells incubated with HO-1 by 5-[125I]Iodo-2"-deoxyuridine release assay and agarose gel electrophoresis of DNA.	Sepharose	255-262	heme oxygenase 1	Homo sapiens	0-4
9920842-9	1999	Although it has been suggested that the Fas/Fas ligand system is the main pathway by which CD4(+) CTL-mediated cytotoxicity is exerted in murine systems, HO-1 produced peptide-specific and HLA-restricted cytotoxicity via a Fas-independent and nonapoptotic pathway.	ammonium ferrous sulfate	40-43	heme oxygenase 1	Homo sapiens	154-158
9920842-9	1999	Although it has been suggested that the Fas/Fas ligand system is the main pathway by which CD4(+) CTL-mediated cytotoxicity is exerted in murine systems, HO-1 produced peptide-specific and HLA-restricted cytotoxicity via a Fas-independent and nonapoptotic pathway.	ammonium ferrous sulfate	44-47	heme oxygenase 1	Homo sapiens	154-158
11089885-11	1999	The expression of heme oxygenase (HO-1), a stress-response protein, has been used to monitor effects of hyperthermia, 12-O-tetradecanoly phorbol 13-acetate (TPA) and 4-HNE.	12-o-tetradecanoly phorbol 13-acetate	118-155	heme oxygenase 1	Homo sapiens	34-38
10083452-0	1999	Glutamine-induced heme oxygenase-1 protects intestines and hearts from warm ischemic injury.	Glutamine	0-9	heme oxygenase 1	Homo sapiens	18-34
10943654-1	1999	Oxidative stress and hypoxia, which may occur in cystic fibrosis patients (CF) at rest and may be worsened by exercise, induce the expression of heme oxygenase (HO)-1, resulting in increased carbon monoxide (CO) formation.	Carbon Monoxide	191-206	heme oxygenase 1	Homo sapiens	145-166
10943654-1	1999	Oxidative stress and hypoxia, which may occur in cystic fibrosis patients (CF) at rest and may be worsened by exercise, induce the expression of heme oxygenase (HO)-1, resulting in increased carbon monoxide (CO) formation.	Carbon Monoxide	208-210	heme oxygenase 1	Homo sapiens	145-166
11089885-11	1999	The expression of heme oxygenase (HO-1), a stress-response protein, has been used to monitor effects of hyperthermia, 12-O-tetradecanoly phorbol 13-acetate (TPA) and 4-HNE.	Tetradecanoylphorbol Acetate	157-160	heme oxygenase 1	Homo sapiens	34-38
11089885-11	1999	The expression of heme oxygenase (HO-1), a stress-response protein, has been used to monitor effects of hyperthermia, 12-O-tetradecanoly phorbol 13-acetate (TPA) and 4-HNE.	4-hydroxy-2-nonenal	166-171	heme oxygenase 1	Homo sapiens	34-38
9808084-0	1998	Linoleyl hydroperoxide transcriptionally upregulates heme oxygenase-1 gene expression in human renal epithelial and aortic endothelial cells.	linoleyl hydroperoxide	0-22	heme oxygenase 1	Homo sapiens	53-69
9890653-1	1999	Inducible heme oxygenase (HO-1) is an antioxidant stress protein, that is mainly induced by reactive oxygen species (ROS), cytokines and hyperthermia.	Reactive Oxygen Species	92-115	heme oxygenase 1	Homo sapiens	26-30
9890653-1	1999	Inducible heme oxygenase (HO-1) is an antioxidant stress protein, that is mainly induced by reactive oxygen species (ROS), cytokines and hyperthermia.	Reactive Oxygen Species	117-120	heme oxygenase 1	Homo sapiens	26-30
9884071-1	1998	The contribution of haeme oxygenase-derived carbon monoxide (CO) to the regulation of vascular tone in thoracic aorta was investigated following induction of the inducible isoform of haeme oxygenase (HO-1).	Carbon Monoxide	61-63	heme oxygenase 1	Homo sapiens	200-204
9884071-6	1998	Induction of HO-1 in SNAP-treated rings was associated with a higher 14CO release compared to control, as measured by scintillation counting after incubation of aortas with [2-14C]-L-glycine, the precursor of haeme.	14co	69-73	heme oxygenase 1	Homo sapiens	13-17
9884071-6	1998	Induction of HO-1 in SNAP-treated rings was associated with a higher 14CO release compared to control, as measured by scintillation counting after incubation of aortas with [2-14C]-L-glycine, the precursor of haeme.	[2-14c]-l-glycine	173-190	heme oxygenase 1	Homo sapiens	13-17
9884071-7	1998	Guanosine 3",5"-monophosphate (cyclic GMP) content was also greatly enhanced in aortas expressing high levels of HO-1.	Cyclic GMP	0-29	heme oxygenase 1	Homo sapiens	113-117
9863766-8	1998	Concurrent with these changes, mercuric chloride treatment activates transcription of the heme oxygenase-1 (HO-1) gene in a dose dependent manner, further indicating an oxidative stress response.	Mercuric Chloride	31-48	heme oxygenase 1	Homo sapiens	90-106
9863766-8	1998	Concurrent with these changes, mercuric chloride treatment activates transcription of the heme oxygenase-1 (HO-1) gene in a dose dependent manner, further indicating an oxidative stress response.	Mercuric Chloride	31-48	heme oxygenase 1	Homo sapiens	108-112
9808084-3	1998	Oxidized LDL has been shown to induce heme oxygenase-1 (HO-1), a microsomal enzyme that is involved in heme detoxification and is a major endogenous source of carbon monoxide.	Carbon Monoxide	159-174	heme oxygenase 1	Homo sapiens	38-54
9808084-3	1998	Oxidized LDL has been shown to induce heme oxygenase-1 (HO-1), a microsomal enzyme that is involved in heme detoxification and is a major endogenous source of carbon monoxide.	Carbon Monoxide	159-174	heme oxygenase 1	Homo sapiens	56-60
9808084-6	1998	Exposure to LAox (25 microM) showed an approximately 16-fold induction of HO-1 mRNA, whereas exposure to lyso-PC (25 microM) showed only an approximate 2.6-fold increase.	laox	12-16	heme oxygenase 1	Homo sapiens	74-78
9808084-7	1998	Treatment with actinomycin-D (4 microM), a transcriptional inhibitor, as well as nuclear run-on assays, demonstrated that LAox-mediated HO-1 gene induction is dependent on de novo transcription.	Dactinomycin	15-28	heme oxygenase 1	Homo sapiens	136-140
9808084-7	1998	Treatment with actinomycin-D (4 microM), a transcriptional inhibitor, as well as nuclear run-on assays, demonstrated that LAox-mediated HO-1 gene induction is dependent on de novo transcription.	laox	122-126	heme oxygenase 1	Homo sapiens	136-140
9808084-10	1998	These studies are the first demonstration that LAox induces HO-1 by transcriptional mechanisms and may have implications in the pathogenesis of cell injury in atherosclerosis and progressive renal disease.	laox	47-51	heme oxygenase 1	Homo sapiens	60-64
10193374-2	1998	Induction of heme oxygenase (HO-1) by reactive oxygen species is a general cytoprotective mechanism against oxidative stress.	Reactive Oxygen Species	38-61	heme oxygenase 1	Homo sapiens	29-33
10193374-3	1998	HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO).	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4
10193374-3	1998	HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO).	Bilirubin	25-34	heme oxygenase 1	Homo sapiens	0-4
10193374-3	1998	HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO).	Iron	41-45	heme oxygenase 1	Homo sapiens	0-4
10193374-3	1998	HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO).	Carbon Monoxide	50-65	heme oxygenase 1	Homo sapiens	0-4
10193374-3	1998	HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO).	Carbon Monoxide	67-69	heme oxygenase 1	Homo sapiens	0-4
9784401-0	1998	Human lymphocyte heme oxygenase 1 as a response biomarker to inorganic arsenic.	Arsenic	71-78	heme oxygenase 1	Homo sapiens	17-33
9784401-2	1998	We report the induction of HO1 in human lymphoblastoid cells (LBs) by arsenite in a dose-related manner.	arsenite	70-78	heme oxygenase 1	Homo sapiens	27-30
9784401-1	1998	We propose the use of human lymphocyte heme oxygenase 1 (HO1) as a biomarker of response to environmental arsenic exposure.	Arsenic	106-113	heme oxygenase 1	Homo sapiens	39-55
9784401-3	1998	HO1 was identified by SDS-PAGE from its molecular weight and from its detection by Western blotting with anti-HO1.	Sodium Dodecyl Sulfate	22-25	heme oxygenase 1	Homo sapiens	0-3
9784401-1	1998	We propose the use of human lymphocyte heme oxygenase 1 (HO1) as a biomarker of response to environmental arsenic exposure.	Arsenic	106-113	heme oxygenase 1	Homo sapiens	57-60
9784401-4	1998	HO1 levels in LBs treated with arsenite increased by de novo synthesis as demonstrated by incorporation of 35S-methionine and by inhibition of HO1 synthesis by actinomycin D.	arsenite	31-39	heme oxygenase 1	Homo sapiens	0-3
9784401-4	1998	HO1 levels in LBs treated with arsenite increased by de novo synthesis as demonstrated by incorporation of 35S-methionine and by inhibition of HO1 synthesis by actinomycin D.	arsenite	31-39	heme oxygenase 1	Homo sapiens	143-146
9722676-0	1998	Involvement of the tyrosine phosphorylation pathway in induction of human heme oxygenase-1 by hemin, sodium arsenite, and cadmium chloride.	Tyrosine	19-27	heme oxygenase 1	Homo sapiens	74-90
9784401-4	1998	HO1 levels in LBs treated with arsenite increased by de novo synthesis as demonstrated by incorporation of 35S-methionine and by inhibition of HO1 synthesis by actinomycin D.	35s-methionine	107-121	heme oxygenase 1	Homo sapiens	0-3
9784401-4	1998	HO1 levels in LBs treated with arsenite increased by de novo synthesis as demonstrated by incorporation of 35S-methionine and by inhibition of HO1 synthesis by actinomycin D.	Dactinomycin	160-173	heme oxygenase 1	Homo sapiens	0-3
9784401-4	1998	HO1 levels in LBs treated with arsenite increased by de novo synthesis as demonstrated by incorporation of 35S-methionine and by inhibition of HO1 synthesis by actinomycin D.	Dactinomycin	160-173	heme oxygenase 1	Homo sapiens	143-146
9784401-6	1998	HO1 was also induced by 10 microM cadmium or mercuric chloride.	Cadmium	34-41	heme oxygenase 1	Homo sapiens	0-3
9784401-6	1998	HO1 was also induced by 10 microM cadmium or mercuric chloride.	Mercuric Chloride	45-62	heme oxygenase 1	Homo sapiens	0-3
9784401-7	1998	We suggest that circulating lymphocyte HO1 levels may be useful in assessing the biological activity of arsenic exposure in vivo under properly controlled conditions of simultaneous urinalysis for arsenic, cadmium, and mercury.	Arsenic	104-111	heme oxygenase 1	Homo sapiens	39-42
9784401-7	1998	We suggest that circulating lymphocyte HO1 levels may be useful in assessing the biological activity of arsenic exposure in vivo under properly controlled conditions of simultaneous urinalysis for arsenic, cadmium, and mercury.	Arsenic	197-204	heme oxygenase 1	Homo sapiens	39-42
9784401-7	1998	We suggest that circulating lymphocyte HO1 levels may be useful in assessing the biological activity of arsenic exposure in vivo under properly controlled conditions of simultaneous urinalysis for arsenic, cadmium, and mercury.	Cadmium	206-213	heme oxygenase 1	Homo sapiens	39-42
9784401-7	1998	We suggest that circulating lymphocyte HO1 levels may be useful in assessing the biological activity of arsenic exposure in vivo under properly controlled conditions of simultaneous urinalysis for arsenic, cadmium, and mercury.	Mercury	219-226	heme oxygenase 1	Homo sapiens	39-42
9722676-4	1998	Genistein (50 microM), another tyrosine kinase inhibitor, also inhibited the induction of HO-1 mRNA by hemin, arsenite, and cadmium.	Hemin	103-108	heme oxygenase 1	Homo sapiens	90-94
9722676-4	1998	Genistein (50 microM), another tyrosine kinase inhibitor, also inhibited the induction of HO-1 mRNA by hemin, arsenite, and cadmium.	arsenite	110-118	heme oxygenase 1	Homo sapiens	90-94
9722676-4	1998	Genistein (50 microM), another tyrosine kinase inhibitor, also inhibited the induction of HO-1 mRNA by hemin, arsenite, and cadmium.	Cadmium	124-131	heme oxygenase 1	Homo sapiens	90-94
9747510-0	1998	Oxygen tension regulates heme oxygenase-1 gene expression in mammalian cell lines.	Oxygen	0-6	heme oxygenase 1	Homo sapiens	25-41
9747510-5	1998	Cycloheximide and actinomycin D inhibited the increases in the HO-1 mRNA level produced by hyperoxia, indicating that response to hyperoxia is dependent on de novo protein synthesis and mRNA transcription.	Cycloheximide	0-13	heme oxygenase 1	Homo sapiens	63-67
9747510-5	1998	Cycloheximide and actinomycin D inhibited the increases in the HO-1 mRNA level produced by hyperoxia, indicating that response to hyperoxia is dependent on de novo protein synthesis and mRNA transcription.	Dactinomycin	18-31	heme oxygenase 1	Homo sapiens	63-67
9747510-6	1998	Antioxidants, desferrioxamine (DES) and o-phenanthroline (OP) partially inhibited the HO-1 mRNA elevation by hyperoxia.	Deferoxamine	14-29	heme oxygenase 1	Homo sapiens	86-90
9747510-6	1998	Antioxidants, desferrioxamine (DES) and o-phenanthroline (OP) partially inhibited the HO-1 mRNA elevation by hyperoxia.	Deferoxamine	31-34	heme oxygenase 1	Homo sapiens	86-90
9747510-6	1998	Antioxidants, desferrioxamine (DES) and o-phenanthroline (OP) partially inhibited the HO-1 mRNA elevation by hyperoxia.	1,10-phenanthroline	40-56	heme oxygenase 1	Homo sapiens	86-90
9747510-7	1998	In addition to hyperoxia, sodium arsenite (NaAsO2), cadmium chloride (CdCl(2)) and hydrogen peroxide (H2O2), which are reactive oxygen intermediates (ROI) generators, increased the HO-1 mRNA level by 11-, 22- and 2.5-fold, respectively.	sodium arsenite	26-41	heme oxygenase 1	Homo sapiens	181-185
9747510-7	1998	In addition to hyperoxia, sodium arsenite (NaAsO2), cadmium chloride (CdCl(2)) and hydrogen peroxide (H2O2), which are reactive oxygen intermediates (ROI) generators, increased the HO-1 mRNA level by 11-, 22- and 2.5-fold, respectively.	sodium arsenite	43-49	heme oxygenase 1	Homo sapiens	181-185
9747510-7	1998	In addition to hyperoxia, sodium arsenite (NaAsO2), cadmium chloride (CdCl(2)) and hydrogen peroxide (H2O2), which are reactive oxygen intermediates (ROI) generators, increased the HO-1 mRNA level by 11-, 22- and 2.5-fold, respectively.	Cadmium Chloride	52-68	heme oxygenase 1	Homo sapiens	181-185
9747510-7	1998	In addition to hyperoxia, sodium arsenite (NaAsO2), cadmium chloride (CdCl(2)) and hydrogen peroxide (H2O2), which are reactive oxygen intermediates (ROI) generators, increased the HO-1 mRNA level by 11-, 22- and 2.5-fold, respectively.	cdcl	70-74	heme oxygenase 1	Homo sapiens	181-185
9747510-7	1998	In addition to hyperoxia, sodium arsenite (NaAsO2), cadmium chloride (CdCl(2)) and hydrogen peroxide (H2O2), which are reactive oxygen intermediates (ROI) generators, increased the HO-1 mRNA level by 11-, 22- and 2.5-fold, respectively.	Hydrogen Peroxide	83-100	heme oxygenase 1	Homo sapiens	181-185
9747510-7	1998	In addition to hyperoxia, sodium arsenite (NaAsO2), cadmium chloride (CdCl(2)) and hydrogen peroxide (H2O2), which are reactive oxygen intermediates (ROI) generators, increased the HO-1 mRNA level by 11-, 22- and 2.5-fold, respectively.	Hydrogen Peroxide	102-106	heme oxygenase 1	Homo sapiens	181-185
9747510-9	1998	In contrast to OP, N-acetylcysteine (NAC), an antioxidant and membrane-permeable reducing reagent, enhanced the HO-1 mRNA elevation induced by hyperoxia, although NAC inhibited the mRNA elevation induced by NaAsO2, CdCl2 and H2O2.	Acetylcysteine	19-35	heme oxygenase 1	Homo sapiens	112-116
9747510-9	1998	In contrast to OP, N-acetylcysteine (NAC), an antioxidant and membrane-permeable reducing reagent, enhanced the HO-1 mRNA elevation induced by hyperoxia, although NAC inhibited the mRNA elevation induced by NaAsO2, CdCl2 and H2O2.	Acetylcysteine	37-40	heme oxygenase 1	Homo sapiens	112-116
9747510-10	1998	These results indicate that oxygen tension regulates HO-1 gene expression and suggest that hyperoxia-specific and redox-sensitive regulators may be involved in hyperoxia-mediated HO-1 gene expression.	Oxygen	28-34	heme oxygenase 1	Homo sapiens	53-57
9747510-10	1998	These results indicate that oxygen tension regulates HO-1 gene expression and suggest that hyperoxia-specific and redox-sensitive regulators may be involved in hyperoxia-mediated HO-1 gene expression.	Oxygen	28-34	heme oxygenase 1	Homo sapiens	179-183
9855696-5	1998	In contrast, the HO-1 isoform is strongly induced in vascular cells by various stress-associated agents and markedly increases CO synthesis during pathological conditions.	Carbon Monoxide	127-129	heme oxygenase 1	Homo sapiens	17-21
9722676-5	1998	Nuclear runoff assays revealed that herbimycin blocked the hemin-induced transcription of the HO-1 gene.	herbimycin	36-46	heme oxygenase 1	Homo sapiens	94-98
9722676-5	1998	Nuclear runoff assays revealed that herbimycin blocked the hemin-induced transcription of the HO-1 gene.	Hemin	59-64	heme oxygenase 1	Homo sapiens	94-98
9722676-6	1998	The induction of HO-1 mRNA by hemin in human peripheral blood mononuclear cells was inhibited by herbimycin.	herbimycin	97-107	heme oxygenase 1	Homo sapiens	17-21
9722676-8	1998	When HeLa cells were treated with a specific inhibitor of the mitogen-activated protein kinase (MAPK)/extracellular-signal regulated kinase cascade, PD58059 (100 microM), suppression of the cadmium-dependent HO-1 induction was not observed, but the hemin- or arsenite-dependent induction was slightly inhibited.	pd58059	149-156	heme oxygenase 1	Homo sapiens	208-212
9722676-8	1998	When HeLa cells were treated with a specific inhibitor of the mitogen-activated protein kinase (MAPK)/extracellular-signal regulated kinase cascade, PD58059 (100 microM), suppression of the cadmium-dependent HO-1 induction was not observed, but the hemin- or arsenite-dependent induction was slightly inhibited.	Cadmium	190-197	heme oxygenase 1	Homo sapiens	208-212
9722676-8	1998	When HeLa cells were treated with a specific inhibitor of the mitogen-activated protein kinase (MAPK)/extracellular-signal regulated kinase cascade, PD58059 (100 microM), suppression of the cadmium-dependent HO-1 induction was not observed, but the hemin- or arsenite-dependent induction was slightly inhibited.	Hemin	249-254	heme oxygenase 1	Homo sapiens	208-212
9722676-8	1998	When HeLa cells were treated with a specific inhibitor of the mitogen-activated protein kinase (MAPK)/extracellular-signal regulated kinase cascade, PD58059 (100 microM), suppression of the cadmium-dependent HO-1 induction was not observed, but the hemin- or arsenite-dependent induction was slightly inhibited.	arsenite	259-267	heme oxygenase 1	Homo sapiens	208-212
9722676-0	1998	Involvement of the tyrosine phosphorylation pathway in induction of human heme oxygenase-1 by hemin, sodium arsenite, and cadmium chloride.	Hemin	94-99	heme oxygenase 1	Homo sapiens	74-90
9722676-0	1998	Involvement of the tyrosine phosphorylation pathway in induction of human heme oxygenase-1 by hemin, sodium arsenite, and cadmium chloride.	sodium arsenite	101-116	heme oxygenase 1	Homo sapiens	74-90
9722676-0	1998	Involvement of the tyrosine phosphorylation pathway in induction of human heme oxygenase-1 by hemin, sodium arsenite, and cadmium chloride.	Cadmium Chloride	122-138	heme oxygenase 1	Homo sapiens	74-90
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	herbimycin	43-55	heme oxygenase 1	Homo sapiens	77-93
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	herbimycin	43-55	heme oxygenase 1	Homo sapiens	95-99
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	Hemin	137-142	heme oxygenase 1	Homo sapiens	77-93
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	Hemin	137-142	heme oxygenase 1	Homo sapiens	95-99
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	sodium arsenite	144-159	heme oxygenase 1	Homo sapiens	77-93
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	sodium arsenite	144-159	heme oxygenase 1	Homo sapiens	95-99
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	Cadmium Chloride	164-180	heme oxygenase 1	Homo sapiens	77-93
9722676-1	1998	The effect of a tyrosine kinase inhibitor, herbimycin A, on the induction of heme oxygenase-1 (HO-1) mRNA in HeLa cells upon exposure to hemin, sodium arsenite and cadmium chloride was examined.	Cadmium Chloride	164-180	heme oxygenase 1	Homo sapiens	95-99
9722676-2	1998	The induction of HO-1 mRNA by hemin was inhibited when the cells were pretreated with herbimycin A.	Hemin	30-35	heme oxygenase 1	Homo sapiens	17-21
9722676-2	1998	The induction of HO-1 mRNA by hemin was inhibited when the cells were pretreated with herbimycin A.	herbimycin	86-98	heme oxygenase 1	Homo sapiens	17-21
9722676-3	1998	Herbimycin also inhibited arsenite- and cadmium-dependent induction of HO-1 mRNA in a dose-dependent manner, but less inhibition was observed in cadmium-treated cells than in ones treated with hemin- or arsenite.	herbimycin	0-10	heme oxygenase 1	Homo sapiens	71-75
9722676-3	1998	Herbimycin also inhibited arsenite- and cadmium-dependent induction of HO-1 mRNA in a dose-dependent manner, but less inhibition was observed in cadmium-treated cells than in ones treated with hemin- or arsenite.	arsenite	26-34	heme oxygenase 1	Homo sapiens	71-75
9722676-3	1998	Herbimycin also inhibited arsenite- and cadmium-dependent induction of HO-1 mRNA in a dose-dependent manner, but less inhibition was observed in cadmium-treated cells than in ones treated with hemin- or arsenite.	Cadmium	40-47	heme oxygenase 1	Homo sapiens	71-75
9722676-4	1998	Genistein (50 microM), another tyrosine kinase inhibitor, also inhibited the induction of HO-1 mRNA by hemin, arsenite, and cadmium.	Genistein	0-9	heme oxygenase 1	Homo sapiens	90-94
9828853-0	1998	Raised levels of exhaled carbon monoxide are associated with an increased expression of heme oxygenase-1 in airway macrophages in asthma: a new marker of oxidative stress.	Carbon Monoxide	25-40	heme oxygenase 1	Homo sapiens	88-104
9766835-4	1998	NAC treatment raised nerve glutathione levels compared to untreated nerves, as indicated using hemeoxygenase-1 (hsp32) immunoreactivity as a marker of glutathione depletion.	Acetylcysteine	0-3	heme oxygenase 1	Homo sapiens	112-117
9828853-3	1998	HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO).	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4
9828853-3	1998	HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO).	Bilirubin	25-34	heme oxygenase 1	Homo sapiens	0-4
9828853-3	1998	HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO).	Iron	41-45	heme oxygenase 1	Homo sapiens	0-4
9828853-3	1998	HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO).	Carbon Monoxide	51-66	heme oxygenase 1	Homo sapiens	0-4
9828853-3	1998	HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO).	Carbon Monoxide	68-70	heme oxygenase 1	Homo sapiens	0-4
9828853-9	1998	CONCLUSIONS: Increased exhaled CO levels and HO-1 expression may reflect induction of HO-1 which may be inhibited by steroids.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	45-49
9828853-9	1998	CONCLUSIONS: Increased exhaled CO levels and HO-1 expression may reflect induction of HO-1 which may be inhibited by steroids.	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	86-90
9828853-9	1998	CONCLUSIONS: Increased exhaled CO levels and HO-1 expression may reflect induction of HO-1 which may be inhibited by steroids.	Steroids	117-125	heme oxygenase 1	Homo sapiens	45-49
9828853-9	1998	CONCLUSIONS: Increased exhaled CO levels and HO-1 expression may reflect induction of HO-1 which may be inhibited by steroids.	Steroids	117-125	heme oxygenase 1	Homo sapiens	86-90
9486963-0	1998	Hemeoxygenase-1 inhibits human myometrial contractility via carbon monoxide and is upregulated by progesterone during pregnancy.	Carbon Monoxide	60-75	heme oxygenase 1	Homo sapiens	0-15
9622162-5	1998	This upregulation of HO-1 was completely blocked by the antioxidant N-acetylcysteine (NAC, 20 mmol/L).	Acetylcysteine	68-84	heme oxygenase 1	Homo sapiens	21-25
9622162-5	1998	This upregulation of HO-1 was completely blocked by the antioxidant N-acetylcysteine (NAC, 20 mmol/L).	Acetylcysteine	86-89	heme oxygenase 1	Homo sapiens	21-25
9622162-6	1998	In contrast, steady laminar shear (5 dyne/cm2) induced NADH oxidase activity and NAC-sensitive HO-1 mRNA expression only at 1 and 5 hours, a transient response that returned toward baseline at 24 hours.	Acetylcysteine	81-84	heme oxygenase 1	Homo sapiens	95-99
9545559-9	1998	Furthermore, this low concentration of NAC also decreased the CdCl2-induced gene expression of HSP32 which represents a general response to oxidative stress.	Cadmium Chloride	62-67	heme oxygenase 1	Homo sapiens	95-100
9530200-8	1998	Inhibition of the AP-1 transcription factor with curcumin decreased the cytokine induction of HO-1 mRNA, suggesting the involvement of this transcription factor in cytokine signaling of HO-1.	Curcumin	49-57	heme oxygenase 1	Homo sapiens	94-98
9530200-8	1998	Inhibition of the AP-1 transcription factor with curcumin decreased the cytokine induction of HO-1 mRNA, suggesting the involvement of this transcription factor in cytokine signaling of HO-1.	Curcumin	49-57	heme oxygenase 1	Homo sapiens	186-190
9514830-3	1998	In the substantia nigra of both PD and control specimens, moderate HO-1 immunoreactivity was consistently observed in neuromelanin-containing (dopaminergic) neurons.	neuromelanin	118-130	heme oxygenase 1	Homo sapiens	67-71
9514830-9	1998	In addition, excessive cellular levels of heme-derived free iron and carbon monoxide resulting from HO-1 overactivity may contribute to the pathogenesis of PD.	Heme	42-46	heme oxygenase 1	Homo sapiens	100-104
9514830-9	1998	In addition, excessive cellular levels of heme-derived free iron and carbon monoxide resulting from HO-1 overactivity may contribute to the pathogenesis of PD.	Iron	60-64	heme oxygenase 1	Homo sapiens	100-104
9514830-9	1998	In addition, excessive cellular levels of heme-derived free iron and carbon monoxide resulting from HO-1 overactivity may contribute to the pathogenesis of PD.	Carbon Monoxide	69-84	heme oxygenase 1	Homo sapiens	100-104
9486963-0	1998	Hemeoxygenase-1 inhibits human myometrial contractility via carbon monoxide and is upregulated by progesterone during pregnancy.	Progesterone	98-110	heme oxygenase 1	Homo sapiens	0-15
9486963-6	1998	Reverse transcription-PCR analysis revealed that mRNA encoding HO-1 and HO-2 was undetected in explant cultures of nonlaboring pregnant myometrium under basal conditions, however, exposure to progesterone, but not estradiol-17beta, induced the expression of HO-1 and HO-2 mRNAs.	Progesterone	192-204	heme oxygenase 1	Homo sapiens	63-76
9486963-6	1998	Reverse transcription-PCR analysis revealed that mRNA encoding HO-1 and HO-2 was undetected in explant cultures of nonlaboring pregnant myometrium under basal conditions, however, exposure to progesterone, but not estradiol-17beta, induced the expression of HO-1 and HO-2 mRNAs.	Progesterone	192-204	heme oxygenase 1	Homo sapiens	258-271
9486963-7	1998	Progesterone also significantly induced HO-1 protein synthesis (n = 4, P &lt; 0.001) while estradiol-17beta had no effect (n = 4).	Progesterone	0-12	heme oxygenase 1	Homo sapiens	40-44
9337616-8	1997	Because either hemin alone or UVA radiation are able to lead to a refractoriness of the heme oxygenase-1 gene to reinduction by a second exposure to one or the other agent in human fibroblasts, we conclude that heme, or an as yet unidentified heme derivative, is involved in the refractoriness response.	Hemin	15-20	heme oxygenase 1	Homo sapiens	88-104
9425252-2	1997	We have examined the effect of the NO donor sodium nitroprusside (SNP) on heme oxygenase-1 (HO-1) expression in human epidermal keratinocytes and investigated the contribution of the heme oxygenase pathway in the control of keratinocyte proliferation.	Nitroprusside	44-64	heme oxygenase 1	Homo sapiens	74-90
9374724-0	1997	Regulation of heme oxygenase-1 gene expression in vascular smooth muscle cells by nitric oxide.	Nitric Oxide	82-94	heme oxygenase 1	Homo sapiens	14-30
9374724-4	1997	We demonstrate that the NO donor spermine NONOate (SNN) increases steady-state levels of HO-1 mRNA in aortic vascular smooth muscle cells (aSMC) in both a time- and dose-dependent manner.	spermine nitric oxide complex	33-49	heme oxygenase 1	Homo sapiens	89-93
9374724-4	1997	We demonstrate that the NO donor spermine NONOate (SNN) increases steady-state levels of HO-1 mRNA in aortic vascular smooth muscle cells (aSMC) in both a time- and dose-dependent manner.	spermine nitric oxide complex	51-54	heme oxygenase 1	Homo sapiens	89-93
9374724-4	1997	We demonstrate that the NO donor spermine NONOate (SNN) increases steady-state levels of HO-1 mRNA in aortic vascular smooth muscle cells (aSMC) in both a time- and dose-dependent manner.	asmc	139-143	heme oxygenase 1	Homo sapiens	89-93
9374724-6	1997	Inhibition of the NO-induced HO-1 mRNA expression by cycloheximide suggests that new protein synthesis is required for increased HO-1 gene expression.	Cycloheximide	53-66	heme oxygenase 1	Homo sapiens	29-33
9374724-6	1997	Inhibition of the NO-induced HO-1 mRNA expression by cycloheximide suggests that new protein synthesis is required for increased HO-1 gene expression.	Cycloheximide	53-66	heme oxygenase 1	Homo sapiens	129-133
9374724-8	1997	The antioxidant N-acetyl-L-cysteine markedly inhibited SNN-induced HO-1 mRNA expression, whereas peroxynitrite did not induce HO-1 expression in aSMC.	Acetylcysteine	16-35	heme oxygenase 1	Homo sapiens	67-71
9374724-8	1997	The antioxidant N-acetyl-L-cysteine markedly inhibited SNN-induced HO-1 mRNA expression, whereas peroxynitrite did not induce HO-1 expression in aSMC.	spermine nitric oxide complex	55-58	heme oxygenase 1	Homo sapiens	67-71
9407320-2	1998	Overexpression of HO-1 in endothelial cells (EC) might, therefore, protect against oxidative stress produced under these pathological conditions, by generation of CO, a vasodilator, and bilirubin, which has antioxidant properties that enhance blood vessel formation to counteract hypoxia-induced injury.	Bilirubin	186-195	heme oxygenase 1	Homo sapiens	18-22
9434639-2	1997	We investigated cellular events leading to the heme oxygenase-1 gene expression induced by sublethal concentrations of glutathione depletors, phorone and diethyl maleate, in human fibroblastic cells.	Glutathione	119-130	heme oxygenase 1	Homo sapiens	47-63
9434639-2	1997	We investigated cellular events leading to the heme oxygenase-1 gene expression induced by sublethal concentrations of glutathione depletors, phorone and diethyl maleate, in human fibroblastic cells.	phorone	142-149	heme oxygenase 1	Homo sapiens	47-63
9434639-2	1997	We investigated cellular events leading to the heme oxygenase-1 gene expression induced by sublethal concentrations of glutathione depletors, phorone and diethyl maleate, in human fibroblastic cells.	diethyl maleate	154-169	heme oxygenase 1	Homo sapiens	47-63
9434639-3	1997	Accumulation of heme oxygenase-1 mRNA by glutathione depletors was canceled by simultaneous treatment with cycloheximide, an inhibitor of protein synthesis; however, the inhibitory effect decreased when the inhibitor was added 30 min later.	Glutathione	41-52	heme oxygenase 1	Homo sapiens	16-32
9434639-3	1997	Accumulation of heme oxygenase-1 mRNA by glutathione depletors was canceled by simultaneous treatment with cycloheximide, an inhibitor of protein synthesis; however, the inhibitory effect decreased when the inhibitor was added 30 min later.	Cycloheximide	107-120	heme oxygenase 1	Homo sapiens	16-32
9434639-5	1997	Accumulation of heme oxygenase-1 and c-fos transcripts was abrogated in cells pretreated with 1,4-diazabicyclo[2.2.2]octane, an oxygen-free radical quencher.	triethylenediamine	94-123	heme oxygenase 1	Homo sapiens	16-32
9434639-7	1997	Pretreatment of cells with PD 98059, an inhibitor of the extracellular-signal regulated kinase cascade, or the c-fos antisense oligodeoxynucleotide inhibited the heme oxygenase-1 induction elicited by glutathione depletion.	Oligodeoxyribonucleotides	127-147	heme oxygenase 1	Homo sapiens	162-178
9434639-7	1997	Pretreatment of cells with PD 98059, an inhibitor of the extracellular-signal regulated kinase cascade, or the c-fos antisense oligodeoxynucleotide inhibited the heme oxygenase-1 induction elicited by glutathione depletion.	Glutathione	201-212	heme oxygenase 1	Homo sapiens	162-178
9434639-8	1997	These observations indicated that c-Fos protein plays a role in heme oxygenase-1 gene expression induced by glutathione depletion-mediated oxidative stress in human fibroblasts.	Glutathione	108-119	heme oxygenase 1	Homo sapiens	64-80
9402154-3	1997	Indirect immunofluorescence double labeling studies demonstrated a simultaneous increase of ICAM-1 and HO-1 after exposure of cells to heme for 24 hr.	Heme	135-139	heme oxygenase 1	Homo sapiens	103-107
9402154-9	1997	These results suggest that upregulation of ICAM-1, VCAM-1, and E selectin expression is associated with oxidative stress induced by hemoglobin/heme and that HO-1 may play a modulating role via its ability to degrade heme to a substance with antioxidant properties.	Heme	216-220	heme oxygenase 1	Homo sapiens	157-161
9337616-8	1997	Because either hemin alone or UVA radiation are able to lead to a refractoriness of the heme oxygenase-1 gene to reinduction by a second exposure to one or the other agent in human fibroblasts, we conclude that heme, or an as yet unidentified heme derivative, is involved in the refractoriness response.	Heme	211-215	heme oxygenase 1	Homo sapiens	88-104
9380735-0	1997	Heme oxygenase 1 is required for mammalian iron reutilization.	Iron	43-47	heme oxygenase 1	Homo sapiens	0-16
9276739-5	1997	Heme oxygenase-1 (HO-1), the inducible isoform of HO, was highly induced by mildly oxidized LDL, and augmented induction was observed with hemin pretreatment.	Hemin	139-144	heme oxygenase 1	Homo sapiens	0-16
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Heme	37-41	heme oxygenase 1	Homo sapiens	55-60
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Biliverdine	103-113	heme oxygenase 1	Homo sapiens	37-53
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Biliverdine	103-113	heme oxygenase 1	Homo sapiens	55-60
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Carbon Monoxide	115-130	heme oxygenase 1	Homo sapiens	37-53
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Carbon Monoxide	115-130	heme oxygenase 1	Homo sapiens	55-60
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Iron	141-145	heme oxygenase 1	Homo sapiens	37-53
9380736-1	1997	Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron.	Iron	141-145	heme oxygenase 1	Homo sapiens	55-60
9276739-5	1997	Heme oxygenase-1 (HO-1), the inducible isoform of HO, was highly induced by mildly oxidized LDL, and augmented induction was observed with hemin pretreatment.	Hemin	139-144	heme oxygenase 1	Homo sapiens	18-22
9276739-9	1997	Oxidized phospholipids in the mildly oxidized LDL appear to be responsible for HO-1 induction, since oxidized but not native arachidonic acid-containing phospholipids also induced HO-1.	Phospholipids	9-22	heme oxygenase 1	Homo sapiens	79-83
9276739-9	1997	Oxidized phospholipids in the mildly oxidized LDL appear to be responsible for HO-1 induction, since oxidized but not native arachidonic acid-containing phospholipids also induced HO-1.	Phospholipids	9-22	heme oxygenase 1	Homo sapiens	180-184
9276739-9	1997	Oxidized phospholipids in the mildly oxidized LDL appear to be responsible for HO-1 induction, since oxidized but not native arachidonic acid-containing phospholipids also induced HO-1.	Phospholipids	153-166	heme oxygenase 1	Homo sapiens	180-184
9276739-10	1997	These results suggest that HO-1 induced by mildly oxidized LDL may protect against the induction of inflammatory responses in artery wall cells through the production of the antioxidants biliverdin and bilirubin.	Biliverdine	187-197	heme oxygenase 1	Homo sapiens	27-31
9276739-10	1997	These results suggest that HO-1 induced by mildly oxidized LDL may protect against the induction of inflammatory responses in artery wall cells through the production of the antioxidants biliverdin and bilirubin.	Bilirubin	202-211	heme oxygenase 1	Homo sapiens	27-31
9054378-1	1997	Conversion of heme to verdoheme by heme oxygenase-1 (HO-1) is thought to involve alpha-meso-hydroxylation and elimination of the meso-carbon as CO, a reaction supported by both H2O2 and NADPH-cytochrome P450 reductase/O2.	Carbon	134-140	heme oxygenase 1	Homo sapiens	35-51
9295197-7	1997	Heme oxygenase-1 (HO-1) markedly reduced the activity of both the endogenous AD inhibitor and hemin, indicating that the endogenous inhibitor contains heme.	Heme	151-155	heme oxygenase 1	Homo sapiens	0-16
9295197-7	1997	Heme oxygenase-1 (HO-1) markedly reduced the activity of both the endogenous AD inhibitor and hemin, indicating that the endogenous inhibitor contains heme.	Heme	151-155	heme oxygenase 1	Homo sapiens	18-22
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Heme	130-134	heme oxygenase 1	Homo sapiens	88-92
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Heme	130-134	heme oxygenase 1	Homo sapiens	94-99
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Biliverdine	146-165	heme oxygenase 1	Homo sapiens	88-92
9266806-5	1997	In addition, at lower doses, acrolein caused induction of heme oxygenase 1 protein; however, stress protein 72 (SP72) was not induced.	Acrolein	29-37	heme oxygenase 1	Homo sapiens	58-74
9225984-2	1997	Heme oxygenase-1 (HO-1), a key enzyme in heme catabolism, also functions as an antioxidant enzyme.	Heme	41-45	heme oxygenase 1	Homo sapiens	0-16
9225984-2	1997	Heme oxygenase-1 (HO-1), a key enzyme in heme catabolism, also functions as an antioxidant enzyme.	Heme	41-45	heme oxygenase 1	Homo sapiens	18-22
9354392-0	1997	Possible implications of the induction of human heme oxygenase-1 by nitric oxide donors.	Nitric Oxide	68-80	heme oxygenase 1	Homo sapiens	48-64
9354392-1	1997	To explore the involvement of nitric oxide (NO) in the induction of heme oxygenase-1, an essential enzyme in heme catabolism, we studied the effects of NO donors on the expression of heme oxygenase-1 mRNA in HeLa human cervical cancer cells.	Nitric Oxide	30-42	heme oxygenase 1	Homo sapiens	68-84
9354392-4	1997	We showed that sodium nitroprusside also increased the levels of heme oxygenase-1 protein.	Nitroprusside	15-35	heme oxygenase 1	Homo sapiens	65-81
9354392-5	1997	The sodium nitroprusside-mediated increase in heme oxygenase-1 mRNA levels was abolished by treatment with actinomycin D.	Nitroprusside	4-24	heme oxygenase 1	Homo sapiens	46-62
9354392-5	1997	The sodium nitroprusside-mediated increase in heme oxygenase-1 mRNA levels was abolished by treatment with actinomycin D.	Dactinomycin	107-120	heme oxygenase 1	Homo sapiens	46-62
9190885-6	1997	Pretreatment with ebselen increased the expression of such stress proteins as heat shock protein 70 and heme oxygenase-1 (heat shock protein 32) in cardiac myocytes, as assessed by Western blotting.	ebselen	18-25	heme oxygenase 1	Homo sapiens	104-120
9190885-7	1997	Expression of heat shock protein 70 was increased only at a higher dose of ebselen (30 microM), whereas expression of heme oxygenase-1 was markedly increased at a lower dose of ebselen (3 microM).	ebselen	177-184	heme oxygenase 1	Homo sapiens	118-134
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Biliverdine	146-165	heme oxygenase 1	Homo sapiens	94-99
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Carbon Monoxide	167-169	heme oxygenase 1	Homo sapiens	88-92
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Carbon Monoxide	167-169	heme oxygenase 1	Homo sapiens	94-99
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Iron	174-176	heme oxygenase 1	Homo sapiens	88-92
9116047-1	1997	Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe.	Iron	174-176	heme oxygenase 1	Homo sapiens	94-99
9054378-1	1997	Conversion of heme to verdoheme by heme oxygenase-1 (HO-1) is thought to involve alpha-meso-hydroxylation and elimination of the meso-carbon as CO, a reaction supported by both H2O2 and NADPH-cytochrome P450 reductase/O2.	Hydrogen Peroxide	177-181	heme oxygenase 1	Homo sapiens	35-51
8816811-2	1996	Heme oxygenase-1 (HO-1) is inducible not only by its heme substrate, but also by a variety of agents causing oxidative stress.	Heme	53-57	heme oxygenase 1	Homo sapiens	0-16
9596945-1	1997	OBJECTIVE: The purification and identification of heme oxygenase isoforms (HO-1) and HO-2 from human liver were described and Sn-protoporphyrin (SnPP) was used to inhibit HO-1 activity in order to provide a new method for prevention and treatment of neonatal jaundice.	tin protoporphyrin IX	126-143	heme oxygenase 1	Homo sapiens	75-79
9596945-1	1997	OBJECTIVE: The purification and identification of heme oxygenase isoforms (HO-1) and HO-2 from human liver were described and Sn-protoporphyrin (SnPP) was used to inhibit HO-1 activity in order to provide a new method for prevention and treatment of neonatal jaundice.	tin protoporphyrin IX	126-143	heme oxygenase 1	Homo sapiens	171-175
9596945-1	1997	OBJECTIVE: The purification and identification of heme oxygenase isoforms (HO-1) and HO-2 from human liver were described and Sn-protoporphyrin (SnPP) was used to inhibit HO-1 activity in order to provide a new method for prevention and treatment of neonatal jaundice.	tin protoporphyrin IX	145-149	heme oxygenase 1	Homo sapiens	171-175
9596945-5	1997	The apparent molecular weight of HO-1 and HO-2 on SDS-PAGE was 30,000 and 36,000 under reducing conditions, respectively.	Sodium Dodecyl Sulfate	50-53	heme oxygenase 1	Homo sapiens	33-46
9012361-15	1997	Higher levels of HO-1 may be a contributing factor for the undetectable levels of cytochrome P450 arachidonic acid metabolites, 20-HETE, in the adenocarcinoma.	Arachidonic Acid	98-114	heme oxygenase 1	Homo sapiens	17-21
9073574-6	1997	As an example of such an approach, singlet oxygen has been implicated in the UVA radiation activation of HO-1 because the activation is enhanced by deuterium oxide (which enhances singlet oxygen lifetime) and suppressed by histidine (which scavenges the species).	Singlet Oxygen	35-49	heme oxygenase 1	Homo sapiens	105-109
9073574-6	1997	As an example of such an approach, singlet oxygen has been implicated in the UVA radiation activation of HO-1 because the activation is enhanced by deuterium oxide (which enhances singlet oxygen lifetime) and suppressed by histidine (which scavenges the species).	Deuterium Oxide	148-163	heme oxygenase 1	Homo sapiens	105-109
9073574-6	1997	As an example of such an approach, singlet oxygen has been implicated in the UVA radiation activation of HO-1 because the activation is enhanced by deuterium oxide (which enhances singlet oxygen lifetime) and suppressed by histidine (which scavenges the species).	Singlet Oxygen	180-194	heme oxygenase 1	Homo sapiens	105-109
9073574-6	1997	As an example of such an approach, singlet oxygen has been implicated in the UVA radiation activation of HO-1 because the activation is enhanced by deuterium oxide (which enhances singlet oxygen lifetime) and suppressed by histidine (which scavenges the species).	Histidine	223-232	heme oxygenase 1	Homo sapiens	105-109
8897897-3	1996	SNAP (300 microM) caused a transient increase in heme oxygenase-1 (HO-1) mRNA associated with a fivefold increase in HO activity that was completely blocked by the competitive HO inhibitor, tin protoporphyrin IX (SnPP).	protoporphyrin IX	194-211	heme oxygenase 1	Homo sapiens	49-65
8897897-3	1996	SNAP (300 microM) caused a transient increase in heme oxygenase-1 (HO-1) mRNA associated with a fivefold increase in HO activity that was completely blocked by the competitive HO inhibitor, tin protoporphyrin IX (SnPP).	S-Nitroso-N-propionyl-D,L-penicillamine	213-217	heme oxygenase 1	Homo sapiens	49-65
8816811-2	1996	Heme oxygenase-1 (HO-1) is inducible not only by its heme substrate, but also by a variety of agents causing oxidative stress.	Heme	53-57	heme oxygenase 1	Homo sapiens	18-22
8816811-10	1996	Tin protoporphyrin, a selective inhibitor of HO, reversed the growth arrest and ablated the increased survival against hyperoxia observed in the A549-A4 cells overexpressing HO-1.	tin protoporphyrin IX	0-18	heme oxygenase 1	Homo sapiens	174-178
8816811-11	1996	Taken together, our data suggest that overexpression of HO-1 results in cell growth arrest, which may facilitate cellular protection against non-heme-mediated oxidant insult such as hyperoxia.	Heme	145-149	heme oxygenase 1	Homo sapiens	56-60
8783636-2	1996	BSC-1 cells adapted by long-term exposure to H2O2 exhibited a twofold increase in basal HO activity and expression of HO-1 mRNA as compared with their wild-type counterparts.	Hydrogen Peroxide	45-49	heme oxygenase 1	Homo sapiens	118-122
8800205-3	1996	Among proteins induced after oxidative stress is a 32 kDa protein-probably corresponding to heme oxygenase-1 (HO-1)- and a 27 kDa protein, both known to be induced by reactive oxygen species.	Reactive Oxygen Species	167-190	heme oxygenase 1	Homo sapiens	92-108
8800205-3	1996	Among proteins induced after oxidative stress is a 32 kDa protein-probably corresponding to heme oxygenase-1 (HO-1)- and a 27 kDa protein, both known to be induced by reactive oxygen species.	Reactive Oxygen Species	167-190	heme oxygenase 1	Homo sapiens	110-114
8783636-3	1996	Exposure of both adapted and wild-type BSC-1 cells to H2O2 induced HO-1 mRNA.	Hydrogen Peroxide	54-58	heme oxygenase 1	Homo sapiens	67-71
8783636-8	1996	In conclusion, two interrelated stressors, H2O2 and hemin, produced a stimulation of HO-1, and this was associated with a reduction in the viability of BSC-1 cells.	Hydrogen Peroxide	43-47	heme oxygenase 1	Homo sapiens	85-89
8783636-8	1996	In conclusion, two interrelated stressors, H2O2 and hemin, produced a stimulation of HO-1, and this was associated with a reduction in the viability of BSC-1 cells.	Hemin	52-57	heme oxygenase 1	Homo sapiens	85-89
8769112-0	1996	A precursor of the nitric oxide donor SIN-1 modulates the stress protein heme oxygenase-1 in rat liver.	Nitric Oxide	19-31	heme oxygenase 1	Homo sapiens	73-89
8694803-1	1996	Heme oxygenase-1, a key enzyme in heme catabolism, and inducible nitric oxide synthase (iNOS) are responsible for production of carbon monoxide and nitric oxide (NO), respectively.	Carbon Monoxide	128-143	heme oxygenase 1	Homo sapiens	0-16
8764571-0	1996	Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors.	Nitric Oxide	99-111	heme oxygenase 1	Homo sapiens	79-95
8764571-4	1996	In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs.	Nitroprusside	89-109	heme oxygenase 1	Homo sapiens	212-228
8764571-4	1996	In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs.	linsidomine	111-134	heme oxygenase 1	Homo sapiens	212-228
8764571-4	1996	In a human glioblastoma cell line, T98G, treatment with any of three types of NO donors--sodium nitroprusside, 3-morpholinosydnonimine, and S-nitroso-L-glutathione--caused a significant increase in the levels of heme oxygenase-1 mRNA but not in the levels of heme oxygenase-2 and heat-shock protein 70 mRNAs.	S-Nitrosoglutathione	140-163	heme oxygenase 1	Homo sapiens	212-228
8764571-5	1996	Sodium nitroprusside increased the levels of heme oxygenase-1 protein but not the levels of heat-shock protein 70 in T98G cells.	Nitroprusside	0-20	heme oxygenase 1	Homo sapiens	45-61
8764571-6	1996	The increase in content of heme oxygenase-1 mRNA caused by sodium nitro-prusside was completely abolished by the treatment with actinomycin D.	Nitroprusside	59-80	heme oxygenase 1	Homo sapiens	27-43
8764571-6	1996	The increase in content of heme oxygenase-1 mRNA caused by sodium nitro-prusside was completely abolished by the treatment with actinomycin D.	Dactinomycin	128-141	heme oxygenase 1	Homo sapiens	27-43
8735643-2	1996	In the feline lower oesophageal sphincter (LOS), the distribution of the carbon monoxide (CO) producing enzymes haem oxygenase (HO)-1 and -2 was studied by immunohistochemistry and confocal microscopy, the HO activity was measured and the possible role for CO as a mediator of relaxation was investigated.	Carbon Monoxide	73-88	heme oxygenase 1	Homo sapiens	112-140
8679227-8	1996	Since the identification of HO-1 in 1968, many of the studies involving this enzyme were understandably focused on the regulation and function of HO-1 in heme metabolism.	Heme	154-158	heme oxygenase 1	Homo sapiens	28-32
8679227-8	1996	Since the identification of HO-1 in 1968, many of the studies involving this enzyme were understandably focused on the regulation and function of HO-1 in heme metabolism.	Heme	154-158	heme oxygenase 1	Homo sapiens	146-150
8679227-9	1996	This emphasis is self-evident as HO-1 catalyzes the first and rate-limiting step in heme degradation.	Heme	84-88	heme oxygenase 1	Homo sapiens	33-37
8679227-10	1996	Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins.	Heme	128-132	heme oxygenase 1	Homo sapiens	86-90
8679227-10	1996	Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins.	Heme	162-166	heme oxygenase 1	Homo sapiens	86-90
8679227-10	1996	Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins.	Prostaglandins	249-263	heme oxygenase 1	Homo sapiens	86-90
8679227-11	1996	The chemical diversity of HO-1 inducers led to the speculation that HO-1, besides its role in heme degradation, may also play a vital function in maintaining cellular homeostasis.	Heme	94-98	heme oxygenase 1	Homo sapiens	26-30
8679227-11	1996	The chemical diversity of HO-1 inducers led to the speculation that HO-1, besides its role in heme degradation, may also play a vital function in maintaining cellular homeostasis.	Heme	94-98	heme oxygenase 1	Homo sapiens	68-72
8679227-14	1996	The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury.	Carbon Monoxide	195-210	heme oxygenase 1	Homo sapiens	17-21
8679227-14	1996	The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury.	Carbon Monoxide	195-210	heme oxygenase 1	Homo sapiens	239-243
8679227-14	1996	The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury.	Iron	212-216	heme oxygenase 1	Homo sapiens	17-21
8679227-14	1996	The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury.	Iron	212-216	heme oxygenase 1	Homo sapiens	239-243
8679227-14	1996	The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury.	Bilirubin	222-231	heme oxygenase 1	Homo sapiens	17-21
8679227-14	1996	The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury.	Bilirubin	222-231	heme oxygenase 1	Homo sapiens	239-243
8652820-7	1996	Interestingly, heat shock abolished the remarkable increase in the levels of heme oxygenase-1 mRNA in YN-1-0-A cells treated with hemin or cadmium, in which HSP70 mRNA was noticeably induced.	Hemin	130-135	heme oxygenase 1	Homo sapiens	77-93
8652820-7	1996	Interestingly, heat shock abolished the remarkable increase in the levels of heme oxygenase-1 mRNA in YN-1-0-A cells treated with hemin or cadmium, in which HSP70 mRNA was noticeably induced.	Cadmium	139-146	heme oxygenase 1	Homo sapiens	77-93
8652820-8	1996	Furthermore, transient expression assays showed that heat shock inhibits the cadmium-mediated activation of the heme oxygenase-1 promoter, whereas the HSP70 gene promoter was activated upon heat shock.	Cadmium	77-84	heme oxygenase 1	Homo sapiens	112-128
8735643-2	1996	In the feline lower oesophageal sphincter (LOS), the distribution of the carbon monoxide (CO) producing enzymes haem oxygenase (HO)-1 and -2 was studied by immunohistochemistry and confocal microscopy, the HO activity was measured and the possible role for CO as a mediator of relaxation was investigated.	Carbon Monoxide	90-92	heme oxygenase 1	Homo sapiens	112-140
8675634-1	1995	CO is produced in vascular smooth muscle cells (VSMC) by heme oxygenase-1 (HO-1).	Carbon Monoxide	0-2	heme oxygenase 1	Homo sapiens	57-73
8650873-1	1996	OBJECTIVES: Heme oxygenase isozymes, HO-1 and HO-2, are members of the stress/heat shock (HSP) family of proteins, with the known function of cleaving the heme molecule to biliverdin, iron, and carbon monoxide.	Heme	155-159	heme oxygenase 1	Homo sapiens	37-50
8650873-1	1996	OBJECTIVES: Heme oxygenase isozymes, HO-1 and HO-2, are members of the stress/heat shock (HSP) family of proteins, with the known function of cleaving the heme molecule to biliverdin, iron, and carbon monoxide.	Biliverdine	172-182	heme oxygenase 1	Homo sapiens	37-50
8650873-1	1996	OBJECTIVES: Heme oxygenase isozymes, HO-1 and HO-2, are members of the stress/heat shock (HSP) family of proteins, with the known function of cleaving the heme molecule to biliverdin, iron, and carbon monoxide.	Iron	184-188	heme oxygenase 1	Homo sapiens	37-50
8650873-1	1996	OBJECTIVES: Heme oxygenase isozymes, HO-1 and HO-2, are members of the stress/heat shock (HSP) family of proteins, with the known function of cleaving the heme molecule to biliverdin, iron, and carbon monoxide.	Carbon Monoxide	194-209	heme oxygenase 1	Homo sapiens	37-50
8650873-8	1996	HO-1 in the prostate tissue was found catalytically active and oxidatively cleaved the heme molecule (Fe-protoporphyrin IX) to biliverdin.	Heme	87-91	heme oxygenase 1	Homo sapiens	0-4
8650873-8	1996	HO-1 in the prostate tissue was found catalytically active and oxidatively cleaved the heme molecule (Fe-protoporphyrin IX) to biliverdin.	ferriheme b(1-)	102-122	heme oxygenase 1	Homo sapiens	0-4
8650873-8	1996	HO-1 in the prostate tissue was found catalytically active and oxidatively cleaved the heme molecule (Fe-protoporphyrin IX) to biliverdin.	Biliverdine	127-137	heme oxygenase 1	Homo sapiens	0-4
8650873-12	1996	CONCLUSIONS: The finding that HO-1 expression is increased in BPH and malignant prostate tissue is consistent with a role for this stress protein in the pathogenesis of BPH and prostate cancer; in the context of iron metabolism, an argument is made in support of this possibility.	Iron	212-216	heme oxygenase 1	Homo sapiens	30-34
8547275-0	1996	Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.	Histidine	23-26	heme oxygenase 1	Homo sapiens	16-20
8547275-0	1996	Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.	Water	51-56	heme oxygenase 1	Homo sapiens	16-20
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Histidine	0-3	heme oxygenase 1	Homo sapiens	83-107
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Histidine	0-3	heme oxygenase 1	Homo sapiens	109-113
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Histidine	11-14	heme oxygenase 1	Homo sapiens	83-107
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Histidine	11-14	heme oxygenase 1	Homo sapiens	109-113
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Heme	63-67	heme oxygenase 1	Homo sapiens	83-107
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Heme	63-67	heme oxygenase 1	Homo sapiens	109-113
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Iron	68-72	heme oxygenase 1	Homo sapiens	83-107
8547275-1	1996	His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1).	Iron	68-72	heme oxygenase 1	Homo sapiens	109-113
8547275-7	1996	These results place His-132 close to the iron on the distal side of the heme pocket and indicate that His-132 facilitates, but is not absolutely required for, the catalytic turnover of HO-1.	Histidine	20-23	heme oxygenase 1	Homo sapiens	185-189
8547275-7	1996	These results place His-132 close to the iron on the distal side of the heme pocket and indicate that His-132 facilitates, but is not absolutely required for, the catalytic turnover of HO-1.	Heme	72-76	heme oxygenase 1	Homo sapiens	185-189
8547275-7	1996	These results place His-132 close to the iron on the distal side of the heme pocket and indicate that His-132 facilitates, but is not absolutely required for, the catalytic turnover of HO-1.	Histidine	102-105	heme oxygenase 1	Homo sapiens	185-189
8654390-1	1996	Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide.	Heme	43-47	heme oxygenase 1	Homo sapiens	0-16
8654390-1	1996	Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide.	Heme	72-76	heme oxygenase 1	Homo sapiens	0-16
8654390-1	1996	Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide.	Biliverdine	85-95	heme oxygenase 1	Homo sapiens	0-16
8654390-1	1996	Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide.	Iron	97-101	heme oxygenase 1	Homo sapiens	0-16
8654390-1	1996	Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide.	Carbon Monoxide	107-122	heme oxygenase 1	Homo sapiens	0-16
8654390-2	1996	The human heme-oxygenase-1 gene is transcriptionally activated through the cis-regulatory element (MTE), GTCATATGAC (positions -156 to -147), during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of myelomonocytic cell lines, such as THP-1, to macrophages.	Tetradecanoylphorbol Acetate	149-185	heme oxygenase 1	Homo sapiens	10-26
8654390-2	1996	The human heme-oxygenase-1 gene is transcriptionally activated through the cis-regulatory element (MTE), GTCATATGAC (positions -156 to -147), during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of myelomonocytic cell lines, such as THP-1, to macrophages.	Tetradecanoylphorbol Acetate	187-190	heme oxygenase 1	Homo sapiens	10-26
8743975-6	1996	These results indicate that peroxidation of internal membrane lipids, a decrease in the intracellular GSH levels and the integrity of the plasma membrane are all important for the UVA-induction of heme oxygenase-1.	Glutathione	102-105	heme oxygenase 1	Homo sapiens	197-213
8743975-8	1996	The nonenzymatic lipid peroxidation product 4-hydroxynonenal induces heme oxygenase-1 mRNA up to 40-fold and the phospholipase metabolites diacylglycerol and arachidonic acid induce this mRNA by three-to sixfold above basal levels.	4-hydroxy-2-nonenal	44-60	heme oxygenase 1	Homo sapiens	69-85
8743975-9	1996	We also demonstrate that the cyclooxygenase metabolites of arachidonic acid are important for the UVA-activation of the heme oxygenase-1 gene.	Arachidonic Acid	59-75	heme oxygenase 1	Homo sapiens	120-136
8600294-8	1995	Hyperthermia and treatment with Na arsenite both resulted in enhanced expression of HSP70 and HO-1.	na arsenite	32-43	heme oxygenase 1	Homo sapiens	94-98
8600294-9	1995	In addition, exposure to hydrogen peroxide (H2O2), cadmium (Cd), and lipopolysaccharide (LPS) stimulated a rise in HO-1 levels.	Hydrogen Peroxide	25-42	heme oxygenase 1	Homo sapiens	115-119
8600294-9	1995	In addition, exposure to hydrogen peroxide (H2O2), cadmium (Cd), and lipopolysaccharide (LPS) stimulated a rise in HO-1 levels.	Hydrogen Peroxide	44-48	heme oxygenase 1	Homo sapiens	115-119
8600294-9	1995	In addition, exposure to hydrogen peroxide (H2O2), cadmium (Cd), and lipopolysaccharide (LPS) stimulated a rise in HO-1 levels.	Cadmium	51-58	heme oxygenase 1	Homo sapiens	115-119
8600294-9	1995	In addition, exposure to hydrogen peroxide (H2O2), cadmium (Cd), and lipopolysaccharide (LPS) stimulated a rise in HO-1 levels.	Cadmium	60-62	heme oxygenase 1	Homo sapiens	115-119
7476027-3	1995	In the present study, we determined that CSH treatment resulted in an increase in HSP 27, HSP 90 and heme oxygenase (HO-1) at both the protein and mRNA level.	csh	41-44	heme oxygenase 1	Homo sapiens	117-121
7545388-8	1995	Induction of heme oxygenase-1 and its inhibition by Sn protoporphyrin IX had no effect on cGMP levels.	Tin	52-54	heme oxygenase 1	Homo sapiens	13-29