PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
29788294-0	2018	Epigallocatechin-3-gallate protected vanadium-induced eggshell depigmentation via P38MAPK-Nrf2/HO-1 signaling pathway in laying hens.	epigallocatechin gallate	0-26	heme oxygenase 1	Gallus gallus	95-99
30014460-6	2019	Compared with the HS group, taurine supplementation significantly decreased the levels of reactive oxygen species and malonaldehyde and increased the messenger RNA expressions of nuclear factor erythroid 2-related factor 2 (Nrf2), NAD(P)H quinone dehydrogenase 1 and heme oxygenase 1 in the HS + T group.	Taurine	28-35	heme oxygenase 1	Gallus gallus	267-283
29788294-0	2018	Epigallocatechin-3-gallate protected vanadium-induced eggshell depigmentation via P38MAPK-Nrf2/HO-1 signaling pathway in laying hens.	Vanadium	37-45	heme oxygenase 1	Gallus gallus	95-99
29788294-2	2018	In this study, 360 hens were randomly assigned to the 3 groups to study whether the potential mechanism P38MAPK-Nrf2/HO-1 signaling pathway is involved in the protective effect of EGCG on eggshell pigmentation in vanadium challenged laying hens.	epigallocatechin gallate	180-184	heme oxygenase 1	Gallus gallus	117-121
29788294-6	2018	Dietary vanadium reduced ferrochelatase, NF-E2-related factor 2 (Nrf2), and heme oxygenase (HO-1) mRNA expression, while EGCG up-regulated Nrf2 and HO-1 expression (P < 0.05).	epigallocatechin gallate	121-125	heme oxygenase 1	Gallus gallus	148-152
29788294-7	2018	Protein levels of Nrf2, HO-1 and phospho-p38 (P-P38) MAPK were reduced in V10 group, while dietary supplementation with 130 mg/kg EGCG markedly increased Nrf2, HO-1 and P-P38 MAPK protein levels in the uterus compared with the V10 group (P < 0.01).	epigallocatechin gallate	130-134	heme oxygenase 1	Gallus gallus	24-28
29788294-7	2018	Protein levels of Nrf2, HO-1 and phospho-p38 (P-P38) MAPK were reduced in V10 group, while dietary supplementation with 130 mg/kg EGCG markedly increased Nrf2, HO-1 and P-P38 MAPK protein levels in the uterus compared with the V10 group (P < 0.01).	epigallocatechin gallate	130-134	heme oxygenase 1	Gallus gallus	160-164
29788294-8	2018	In conclusion, EGCG improved eggshell color and antioxidant system in V10-challenged hens, which seems to be associated with P38MAPK-Nrf2/HO-1 signaling pathway.	epigallocatechin gallate	15-19	heme oxygenase 1	Gallus gallus	138-142
29089332-6	2018	Evaluation of the molecular mechanisms underlying the chemopreventive and antitumor effects of curcumin revealed that NF-kappaB and STAT3 signaling pathways were significantly inhibited but that the nuclear factor erythroid 2/heme oxygenase 1 antioxidant pathway was induced by curcumin intake in a dose-dependent manner in ovarian tissues (P < 0.05).	Curcumin	95-103	heme oxygenase 1	Gallus gallus	226-242
30115814-0	2018	Lycopene ameliorates oxidative stress in the aging chicken ovary via activation of Nrf2/HO-1 pathway.	Lycopene	0-8	heme oxygenase 1	Gallus gallus	88-92
30115814-7	2018	Lycopene rescued the decreased antioxidant capacity by increasing the activities of antioxidases and activating the Nrf2/HO-1 pathway in both D-gal-induced and naturally aged ovaries.	Lycopene	0-8	heme oxygenase 1	Gallus gallus	121-125
30115814-10	2018	In conclusion, lycopene can effectively ameliorate the oxidative stress in aging hen ovaries via the activation of the Nrf2/HO-1 pathway.	Lycopene	15-23	heme oxygenase 1	Gallus gallus	124-128
29438543-11	2018	Curcumin significantly increased (P < 0.05) the expression of Nrf2, HO-1, and gamma-GCLc in the liver as compared to the CON diet.	Curcumin	0-8	heme oxygenase 1	Gallus gallus	71-75
29629346-9	2018	Molecular analysis of the ovarian tumors revealed that lycopene reduced the expression of NF-kappaB while increasing the expression of nuclear factor erythroid 2 and its major target protein, heme oxygenase 1.	Lycopene	55-63	heme oxygenase 1	Gallus gallus	192-208
26825804-9	2016	Cu10 induced the expression of heme oxygenase-1, NAD(P)H quinone oxidoreductase 1, and gamma-glutamylcysteine synthetase, downstream proteins of Nrf2.	cu10	0-4	heme oxygenase 1	Gallus gallus	31-81
21406370-3	2011	Because the pigment is derived from oxidative degradation of heme catalyzed by heme oxygenase (HO), this study compared heme oxygenase (decycling) 1 (HMOX1), the gene encoding HO expression and HO activity, in the shell glands of the Dongxiang blue-shelled chicken (n = 12) and the Dongxiang brown-shelled chicken (n = 12).	Heme	61-65	heme oxygenase 1	Gallus gallus	79-94
23885212-1	2013	Blue egg coloring is attributed to biliverdin derived from the oxidative degradation of heme through catalysis by heme oxygenase (HO).	Biliverdine	35-45	heme oxygenase 1	Gallus gallus	114-129
23885212-1	2013	Blue egg coloring is attributed to biliverdin derived from the oxidative degradation of heme through catalysis by heme oxygenase (HO).	Heme	88-92	heme oxygenase 1	Gallus gallus	114-129
21406370-3	2011	Because the pigment is derived from oxidative degradation of heme catalyzed by heme oxygenase (HO), this study compared heme oxygenase (decycling) 1 (HMOX1), the gene encoding HO expression and HO activity, in the shell glands of the Dongxiang blue-shelled chicken (n = 12) and the Dongxiang brown-shelled chicken (n = 12).	Heme	61-65	heme oxygenase 1	Gallus gallus	150-155
10600159-0	1999	Effects of phenylarsine oxide on expression of heme oxygenase-1 reporter constructs in transiently transfected cultures of chick embryo liver cells.	oxophenylarsine	11-29	heme oxygenase 1	Gallus gallus	47-63
10933875-0	2000	Induction of the heme oxygenase-1 gene by metalloporphyrins.	Metalloporphyrins	42-59	heme oxygenase 1	Gallus gallus	17-33
10933875-7	2000	Deletional analysis showed that the key element(s) required for the metalloporphyrin-dependent induction of HO-1 is located between -3.6 and -5.6 kb upstream of the transcription starting point.	Metalloporphyrins	68-84	heme oxygenase 1	Gallus gallus	108-112
15297142-0	2004	Identification of key elements that are responsible for heme-mediated induction of the avian heme oxygenase-1 gene.	Heme	56-60	heme oxygenase 1	Gallus gallus	93-109
15297142-3	2004	In recent work, we had identified a metalloporphyrin-responsive element (MPRE) that localized at -3.7 kb upstream of the transcription start site of the chick HO-1 gene.	Metalloporphyrins	36-52	heme oxygenase 1	Gallus gallus	159-163
15297142-8	2004	CONCLUSIONS: The chick HO-1 promoter region contains "expanded" AP-1 sites that are important for up-regulation of the gene by heme and CoPP, but not other metalloporphyrins.	Heme	127-131	heme oxygenase 1	Gallus gallus	23-27
15297142-8	2004	CONCLUSIONS: The chick HO-1 promoter region contains "expanded" AP-1 sites that are important for up-regulation of the gene by heme and CoPP, but not other metalloporphyrins.	cobaltiprotoporphyrin	136-140	heme oxygenase 1	Gallus gallus	23-27
15297142-8	2004	CONCLUSIONS: The chick HO-1 promoter region contains "expanded" AP-1 sites that are important for up-regulation of the gene by heme and CoPP, but not other metalloporphyrins.	Metalloporphyrins	156-173	heme oxygenase 1	Gallus gallus	23-27
12788823-7	2003	(5) Overexpression of HO-1 protein elicited by VEGF in CAMs was significantly attenuated by the intracellular calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid-acetoxymethyl ester (BAPTA-AM).	Calcium	110-117	heme oxygenase 1	Gallus gallus	22-26
12788823-7	2003	(5) Overexpression of HO-1 protein elicited by VEGF in CAMs was significantly attenuated by the intracellular calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid-acetoxymethyl ester (BAPTA-AM).	1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester	127-203	heme oxygenase 1	Gallus gallus	22-26
12788823-7	2003	(5) Overexpression of HO-1 protein elicited by VEGF in CAMs was significantly attenuated by the intracellular calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid-acetoxymethyl ester (BAPTA-AM).	1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester	205-213	heme oxygenase 1	Gallus gallus	22-26
12788823-9	2003	(6) In addition, the protein kinase C inhibitor staurosporine significantly attenuated, in a dose-dependent manner, the VEGF-stimulated HO-1 induction observed in CAMs.	Staurosporine	48-61	heme oxygenase 1	Gallus gallus	136-140
12788823-10	2003	(7) These results demonstrate, for the first time, that VEGF upregulates HO-1 protein expression in vivo in CAMs by a mechanism dependent on an increase in cytosolic calcium levels and activation of protein kinase C. Our findings also suggest that HO-1 activity is necessary for VEGF-induced angiogenesis in CAMs.	Calcium	166-173	heme oxygenase 1	Gallus gallus	73-77
11888201-0	2002	Mapping of the chick heme oxygenase-1 proximal promoter for responsiveness to metalloporphyrins.	Metalloporphyrins	78-95	heme oxygenase 1	Gallus gallus	21-37
11888201-6	2002	This new metalloporphyrin-responsive element (MPRE) was localized to a 200-bp region 3.8 to 3.6 kb upstream of the transcription starting point of the chick HO-1 gene.	Metalloporphyrins	9-25	heme oxygenase 1	Gallus gallus	157-161
11888201-8	2002	In contrast, sodium arsenite, a prototypical stress-type inducer of HO-1, led to down-regulation of the reporter gene down stream of MPRE.	sodium arsenite	13-28	heme oxygenase 1	Gallus gallus	68-72
11888201-12	2002	We conclude that the chick HO-1 promoter region contains a unique sequence that subserves up-regulation of the gene by metalloporphyrins and propose the name "metalloporphyrin-responsive element" for this sequence.	Metalloporphyrins	119-136	heme oxygenase 1	Gallus gallus	27-31
11888201-12	2002	We conclude that the chick HO-1 promoter region contains a unique sequence that subserves up-regulation of the gene by metalloporphyrins and propose the name "metalloporphyrin-responsive element" for this sequence.	Metalloporphyrins	119-135	heme oxygenase 1	Gallus gallus	27-31
11080622-0	2000	Chimeric constructs containing the SH4/Unique domains of cYes can restrict the ability of Src(527F) to upregulate heme oxygenase-1 expression efficiently.	cyes	57-61	heme oxygenase 1	Gallus gallus	114-130
11080622-9	2000	We hypothesize that activated cSrc can direct upregulation of HO-1 while activated cYes may be less efficient in stimulating signal transduction pathways that direct expression of HO-1.	cyes	83-87	heme oxygenase 1	Gallus gallus	180-184
10942197-1	2000	Previously, chick heme oxygenase-1 (cHO-1) gene was cloned by us and two regions important for induction by sodium arsenite were identified.	sodium arsenite	108-123	heme oxygenase 1	Gallus gallus	18-34
10600159-11	1999	These findings support the hypothesis that the PAO-mediated induction of heme oxygenase-1 is caused by activation of AP-1 and MRE/cMyc elements and may involve nuclear proteins whose states of phosphorylation determine binding to regulatory elements, and thus the level of expression of heme oxygenase-1.	oxophenylarsine	47-50	heme oxygenase 1	Gallus gallus	287-303
10600159-11	1999	These findings support the hypothesis that the PAO-mediated induction of heme oxygenase-1 is caused by activation of AP-1 and MRE/cMyc elements and may involve nuclear proteins whose states of phosphorylation determine binding to regulatory elements, and thus the level of expression of heme oxygenase-1.	oxophenylarsine	47-50	heme oxygenase 1	Gallus gallus	73-89
10600159-2	1999	Induction of heme oxygenase-1 can be caused by numerous factors, including heme, other metalloporphyrins, transition metal ions, heat shock, ultraviolet light, phorbol esters, sodium arsenite, and phenylarsine oxide (PAO).	Metalloporphyrins	87-104	heme oxygenase 1	Gallus gallus	13-29
10600159-2	1999	Induction of heme oxygenase-1 can be caused by numerous factors, including heme, other metalloporphyrins, transition metal ions, heat shock, ultraviolet light, phorbol esters, sodium arsenite, and phenylarsine oxide (PAO).	Metals	87-92	heme oxygenase 1	Gallus gallus	13-29
10600159-2	1999	Induction of heme oxygenase-1 can be caused by numerous factors, including heme, other metalloporphyrins, transition metal ions, heat shock, ultraviolet light, phorbol esters, sodium arsenite, and phenylarsine oxide (PAO).	Phorbol Esters	160-174	heme oxygenase 1	Gallus gallus	13-29
10600159-2	1999	Induction of heme oxygenase-1 can be caused by numerous factors, including heme, other metalloporphyrins, transition metal ions, heat shock, ultraviolet light, phorbol esters, sodium arsenite, and phenylarsine oxide (PAO).	sodium arsenite	176-191	heme oxygenase 1	Gallus gallus	13-29
10600159-2	1999	Induction of heme oxygenase-1 can be caused by numerous factors, including heme, other metalloporphyrins, transition metal ions, heat shock, ultraviolet light, phorbol esters, sodium arsenite, and phenylarsine oxide (PAO).	oxophenylarsine	197-215	heme oxygenase 1	Gallus gallus	13-29
10600159-2	1999	Induction of heme oxygenase-1 can be caused by numerous factors, including heme, other metalloporphyrins, transition metal ions, heat shock, ultraviolet light, phorbol esters, sodium arsenite, and phenylarsine oxide (PAO).	oxophenylarsine	217-220	heme oxygenase 1	Gallus gallus	13-29
10600159-4	1999	Using heme oxygenase-1 promoter/reporter gene constructs, we have previously reported that the sodium arsenite-mediated induction of heme oxygenase-1 in chick embryo liver cells and chicken hepatoma (LMH) cells involves an AP-1 element.	sodium arsenite	95-110	heme oxygenase 1	Gallus gallus	6-22
10600159-4	1999	Using heme oxygenase-1 promoter/reporter gene constructs, we have previously reported that the sodium arsenite-mediated induction of heme oxygenase-1 in chick embryo liver cells and chicken hepatoma (LMH) cells involves an AP-1 element.	sodium arsenite	95-110	heme oxygenase 1	Gallus gallus	133-149
10600159-5	1999	We have now investigated whether the PAO-mediated induction of heme oxygenase-1 also involves an AP-1 element.	oxophenylarsine	37-40	heme oxygenase 1	Gallus gallus	63-79
10600159-9	1999	Studies with mutated constructs showed that both an AP-1 element and a metal responsive element are involved in the PAO-mediated induction of the heme oxygenase-1 reporter construct.	Metals	71-76	heme oxygenase 1	Gallus gallus	146-162
10600159-9	1999	Studies with mutated constructs showed that both an AP-1 element and a metal responsive element are involved in the PAO-mediated induction of the heme oxygenase-1 reporter construct.	oxophenylarsine	116-119	heme oxygenase 1	Gallus gallus	146-162
9224953-7	1997	We conclude that, in chick liver cell cultures, induction of the HO-1 gene by heme is fundamentally different from that produced by transition metals or sodium arsenite.	Heme	78-82	heme oxygenase 1	Gallus gallus	65-69
9535875-0	1998	Mechanism of sodium arsenite-mediated induction of heme oxygenase-1 in hepatoma cells.	sodium arsenite	13-28	heme oxygenase 1	Gallus gallus	51-67
9535875-4	1998	We identified a heme oxygenase-1 promoter-driven luciferase reporter construct that was highly and reproducibly expressed in response to sodium arsenite treatment.	sodium arsenite	137-152	heme oxygenase 1	Gallus gallus	16-32
9535875-5	1998	This construct was used to investigate the role of mitogen-activated protein (MAP) kinases in arsenite-mediated heme oxygenase-1 gene expression.	arsenite	94-102	heme oxygenase 1	Gallus gallus	112-128
9535875-8	1998	Involvement of an AP-1 site in arsenite induction of heme oxygenase-1 gene expression was studied.	arsenite	31-39	heme oxygenase 1	Gallus gallus	53-69
8645700-3	1996	Two forms of this enzyme, heme oxygenase-1 and -2, have been identified; only heme oxygenase-1 is subject to induction by heme, metal ions, and other chemical and physical perturbations (e.g. drugs, oxidants, and heat shock).	Metals	128-133	heme oxygenase 1	Gallus gallus	26-49
9089626-2	1997	One of the two forms of heme oxygenase (heme oxygenase-1) has been shown to be increased by heme, metals, and in some systems, by certain environmental stresses.	Heme	24-28	heme oxygenase 1	Gallus gallus	40-56
9089626-3	1997	However, it remains uncertain whether heme induces hepatic heme oxygenase-1 by a general stress response, or a specific heme-dependent cellular response.	Heme	38-42	heme oxygenase 1	Gallus gallus	59-75
9089626-4	1997	The work communicated here explores this issue by examining possible mechanisms whereby heme and other metalloporphyrins induce heme oxygenase-1 in normal liver cells.	Heme	88-92	heme oxygenase 1	Gallus gallus	128-144
9089626-4	1997	The work communicated here explores this issue by examining possible mechanisms whereby heme and other metalloporphyrins induce heme oxygenase-1 in normal liver cells.	Metalloporphyrins	103-120	heme oxygenase 1	Gallus gallus	128-144
9089626-6	1997	The ability of antioxidants to decrease metalloporphyrin-mediated induction of heme oxygenase-1 mRNA was also tested.	Metalloporphyrins	40-56	heme oxygenase 1	Gallus gallus	79-95
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Heme	46-50	heme oxygenase 1	Gallus gallus	347-363
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Metalloporphyrins	94-111	heme oxygenase 1	Gallus gallus	46-62
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Metalloporphyrins	94-111	heme oxygenase 1	Gallus gallus	347-363
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Heme	80-84	heme oxygenase 1	Gallus gallus	46-62
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Heme	80-84	heme oxygenase 1	Gallus gallus	347-363
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Heme	80-84	heme oxygenase 1	Gallus gallus	46-62
9089626-7	1997	Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1.	Heme	80-84	heme oxygenase 1	Gallus gallus	347-363
9089626-8	1997	We conclude that heme and other non-heme metalloporphyrins induce heme oxygenase-1 through a mechanism requiring protein synthesis, not because metalloporphyrins increase cellular oxidative or other stress.	Heme	17-21	heme oxygenase 1	Gallus gallus	66-82
9089626-8	1997	We conclude that heme and other non-heme metalloporphyrins induce heme oxygenase-1 through a mechanism requiring protein synthesis, not because metalloporphyrins increase cellular oxidative or other stress.	Metalloporphyrins	41-58	heme oxygenase 1	Gallus gallus	66-82
8645700-3	1996	Two forms of this enzyme, heme oxygenase-1 and -2, have been identified; only heme oxygenase-1 is subject to induction by heme, metal ions, and other chemical and physical perturbations (e.g. drugs, oxidants, and heat shock).	Metals	128-133	heme oxygenase 1	Gallus gallus	26-42
8645700-8	1996	The induction of heme oxygenase-1 was assessed by measuring changes in mRNA levels or enzyme activities in response to several treatments, including heme, heavy metals, sodium arsenite, and heat shock, which have been shown to increase the expression of heme oxygenase.	sodium arsenite	169-184	heme oxygenase 1	Gallus gallus	17-33
8874798-6	1996	Nevertheless, the heme-dependent induction of endogenous heme oxygenase-1 in these cells was normal.	Heme	18-22	heme oxygenase 1	Gallus gallus	57-73
8504830-9	1993	Instead, the results suggest a down-regulation of the intracellular machinery required for heme-dependent induction of heme oxygenase-1.	Heme	91-95	heme oxygenase 1	Gallus gallus	119-135
35453433-7	2022	Our in vitro results showed exogenous melatonin supplementation inhibited B-lymphocyte apoptosis, decreased IL-6, TNF-alpha, IFN-gamma and ROS production, down-regulated RORalpha, RORgamma mRNA level and p-ikappab and p-p65 protein expression, whereas it improved the IL-10 level and Nrf2 and the HO-1 protein expression in bursal B lymphocyte.	Melatonin	38-47	heme oxygenase 1	Gallus gallus	297-301
35550135-8	2022	Excessive glutamine and glutamate cooperated with PS-MPs to inhibit the Nrf2-Keap1-HO-1/NQO1 signaling pathway and triggered autophagy-dependent ferroptosis and apoptosis.	Glutamine	10-19	heme oxygenase 1	Gallus gallus	83-87
35550135-8	2022	Excessive glutamine and glutamate cooperated with PS-MPs to inhibit the Nrf2-Keap1-HO-1/NQO1 signaling pathway and triggered autophagy-dependent ferroptosis and apoptosis.	Glutamic Acid	24-33	heme oxygenase 1	Gallus gallus	83-87
8504830-2	1993	The effects of heme on the induction of mRNA and protein synthesis for heme oxygenase-1 have been studied in primary cultures of chick embryo liver cells.	Heme	15-19	heme oxygenase 1	Gallus gallus	71-87
8504830-3	1993	Heme increased the amount of mRNA and the rate of heme oxygenase-1-gene transcription in a dose-dependent fashion, with a maximal 20-fold increase occurring at 20 microM heme.	Heme	0-4	heme oxygenase 1	Gallus gallus	50-66
8504830-6	1993	In contrast, addition of cycloheximide markedly increased the stability of the message (half-life = 18 h), suggesting that a short-lived protein plays a key role in modulating heme oxygenase-1 mRNA levels.	Cycloheximide	25-38	heme oxygenase 1	Gallus gallus	176-192
34363818-5	2021	Moreover, 1/10 NOAEL dose of BPA undermined the redox homeostasis of the ovary through activating Keap1 and suppressing the Nrf2-signaling pathway (Nrf2, NQO1, and HO-1).	bisphenol A	29-32	heme oxygenase 1	Gallus gallus	164-168
35196587-5	2022	PCR analysis showed that MAG increased the levels of NF-E2-related factor 2 (Nrf2), NAD(P)H/quinone oxidoreductase 1 (NQO1), heme oxygenase-1 (HO-1), glutathione-S transferase (GST), glutamate-cysteine ligase catalytic subunit (GCLC), glutamate-cysteine ligase modifier subunit (GCLM), and SOD expressions (P < 0.05).	magnolol	25-28	heme oxygenase 1	Gallus gallus	125-141
35196587-5	2022	PCR analysis showed that MAG increased the levels of NF-E2-related factor 2 (Nrf2), NAD(P)H/quinone oxidoreductase 1 (NQO1), heme oxygenase-1 (HO-1), glutathione-S transferase (GST), glutamate-cysteine ligase catalytic subunit (GCLC), glutamate-cysteine ligase modifier subunit (GCLM), and SOD expressions (P < 0.05).	magnolol	25-28	heme oxygenase 1	Gallus gallus	143-147
33488931-5	2020	The protective effect of EGCG in oxidative damage in lymphocytes was accompanied by mRNA expression of SOD, Heme oxygenase-1 (HO-1), Catalase (CAT), GSH-PX, nuclear factor erythroid 2-related factor 2 (Nrf2), and thioredoxin-1 (Trx-1).	epigallocatechin gallate	25-29	heme oxygenase 1	Gallus gallus	108-124
35303923-0	2022	Oral administration of Lactobacillus brevis 23017 combined with ellagic acid attenuates intestinal inflammatory injury caused by Eimeria infection by activating the Nrf2/HO-1 antioxidant pathway.	Ellagic Acid	64-76	heme oxygenase 1	Gallus gallus	170-174
35303923-1	2022	The aim of this study was to investigate whether oral administration of Lactobacillus brevis 23017 (LB) alone and in combination with ellagic acid inhibits ChTLR15/ChNLRP3/ChIL-1beta by activating the Nrf2/HO-1 pathway to attenuate intestinal inflammatory injury.	Ellagic Acid	134-146	heme oxygenase 1	Gallus gallus	206-210
35303923-8	2022	The results showed that the levels of the genes in the Nrf2/HO-1 pathway in the chickens in the LB(+) groups were higher than those in the LB(-) groups (p < 0.001); those in the H/LB(+) group were higher than those in the M/LB(+) and L/LB(+) groups (p < 0.001); and those in the H/EA + H/LB(+) group showed the highest expression levels compared with the other groups (p < 0.001).	lb	96-98	heme oxygenase 1	Gallus gallus	60-64
33518145-11	2021	With the content of H2O2 increased, the H2O2 groups linearly downregulated the mRNA expressions of GPX, CAT, HMOX1, NQO1, and Nrf2 and its downstream target genes.	Hydrogen Peroxide	20-24	heme oxygenase 1	Gallus gallus	109-114
33518145-11	2021	With the content of H2O2 increased, the H2O2 groups linearly downregulated the mRNA expressions of GPX, CAT, HMOX1, NQO1, and Nrf2 and its downstream target genes.	Hydrogen Peroxide	40-44	heme oxygenase 1	Gallus gallus	109-114
33440766-7	2021	The assessment of selected antioxidant gene expression showed that the 5% FL group significantly elevated heme oxygenase-1 and nuclear factor erythroid 2-related factor 2 expression, compared to the control and WB groups (p < 0.05).	Fluorides	74-76	heme oxygenase 1	Gallus gallus	106-122
3575228-5	1987	True metabolizable energy (TME) and nitrogen-corrected TME (TMEn) values of HO1 corn were determined using adult roosters.	Nitrogen	36-44	heme oxygenase 1	Gallus gallus	76-79
34016350-7	2021	In addition, NAC treatment regulated the expression of HO-1, GSH, SOD2 and PRDX3 by regulating the activity of Nrf2 at different time points to resist oxidative stress caused by heat exposure.	Acetylcysteine	13-16	heme oxygenase 1	Gallus gallus	55-59
33488931-5	2020	The protective effect of EGCG in oxidative damage in lymphocytes was accompanied by mRNA expression of SOD, Heme oxygenase-1 (HO-1), Catalase (CAT), GSH-PX, nuclear factor erythroid 2-related factor 2 (Nrf2), and thioredoxin-1 (Trx-1).	epigallocatechin gallate	25-29	heme oxygenase 1	Gallus gallus	126-130
33142488-5	2020	Taurine supplementation increased the antioxidant enzyme activities and decreased (linear, P < 0.001) the content of malondialdehyde in both serum and the liver of broilers and alleviated oxidative damage through enhancing (P < 0.05) the hepatic genes expression of nuclear factor erythroid-2-related factor 2 (NRF2), glutathione peroxidase (GPX), and heme oxygenase-1 (HO-1).	Taurine	0-7	heme oxygenase 1	Gallus gallus	352-368
33248609-5	2020	Dietary Arg level had a linear (P < 0.05) or quadratic (P < 0.05) effect on the gene expression of glutathione peroxidase 1, heme oxygenase 1, nuclear factor erythroid 2-related factor 2, and the activities of glutathione peroxidase and total antioxidative capacity in the jejunum and ileum.	Arginine	8-11	heme oxygenase 1	Gallus gallus	125-141
33142488-5	2020	Taurine supplementation increased the antioxidant enzyme activities and decreased (linear, P < 0.001) the content of malondialdehyde in both serum and the liver of broilers and alleviated oxidative damage through enhancing (P < 0.05) the hepatic genes expression of nuclear factor erythroid-2-related factor 2 (NRF2), glutathione peroxidase (GPX), and heme oxygenase-1 (HO-1).	Taurine	0-7	heme oxygenase 1	Gallus gallus	370-374
32062552-8	2020	Over accumulation of Cd lead to oxidative stress and activated Nrf2 signal pathway through upregulating pivotal target genes (HO-1, NQO1, GCLC, GCLM and SOD).	Cadmium	21-23	heme oxygenase 1	Gallus gallus	126-130
32954422-9	2020	Taurine reduced the genes expression of IL-1beta, TNF-alpha, IL-6, cyclooxygenase-2 and inducible nitric oxide synthase, whereas it boosted the expression levels of antioxidant-related genes (nuclear factor erythroid 2-related factor 2, heme oxygenase-1, glutamate-cysteine ligase catalytic subunit, and GSH-Px) in the liver of LPS-induced broilers.	Taurine	0-7	heme oxygenase 1	Gallus gallus	237-253
31442540-6	2019	Furthermore, upregulation of HO-1, SOD-1, and TRX in the ATO groups were consistent with ATO-induced oxidative damage.	Arsenic Trioxide	57-60	heme oxygenase 1	Gallus gallus	29-33
32475452-8	2020	Pterostilbene also boosted the expression levels of nuclear factor erythroid 2-related factor 2 (P = 0.010), heme oxygenase 1 (P = 0.037), superoxide dismutase 1 (P = 0.014), and the glutamate-cysteine ligase catalytic subunit (P = 0.001), irrespective of DQ challenge.	pterostilbene	0-13	heme oxygenase 1	Gallus gallus	109-125
32110995-6	2020	Quercetin attenuated the LPS-induced inhibition of Nrf2 activation, translocation, and downstream gene expression, including heme oxygenase-1 (HO-1), NAD (P) H dehydrogenase quinone 1 (NQO1), and manganese superoxide dismutase (SOD2).	Quercetin	0-9	heme oxygenase 1	Gallus gallus	125-141
31845690-7	2020	Also, liver gene and protein expression of P-38MAPK, nuclear factor erythroid 2-related 2 (Nrf2) and hemeoxygenase 1 (HO-1) was up-regulated by EGCG.	epigallocatechin gallate	144-148	heme oxygenase 1	Gallus gallus	101-116
31442540-6	2019	Furthermore, upregulation of HO-1, SOD-1, and TRX in the ATO groups were consistent with ATO-induced oxidative damage.	Arsenic Trioxide	89-92	heme oxygenase 1	Gallus gallus	29-33
31703342-5	2019	Furthermore, RNA-seq analyses also revealed that nine genes including SIVA1, FAS, and HMOX1 were differentially expressed in HD11 cells infected with salmonella following Se treatment, and GO enrichment analysis showed that these DEGs were mainly enriched in an extrinsic apoptotic signaling pathway.	Selenium	171-173	heme oxygenase 1	Gallus gallus	86-91
31376349-0	2019	Baicalin ameliorates oxidative stress and apoptosis by restoring mitochondrial dynamics in the spleen of chickens via the opposite modulation of NF-kappaB and Nrf2/HO-1 signaling pathway during Mycoplasma gallisepticum infection.	baicalin	0-8	heme oxygenase 1	Gallus gallus	164-168
31376349-9	2019	Intriguingly, the protective effects of baicalin were associated with the upregulation of nuclear factor erythroid 2-related factor 2 (Nrf2)/Heme oxygenase-1 (HO-1) pathway and suppression of nuclear factor-kappa B (NF-kappaB) pathway in the spleen of chicken.	baicalin	40-48	heme oxygenase 1	Gallus gallus	141-157
31376349-9	2019	Intriguingly, the protective effects of baicalin were associated with the upregulation of nuclear factor erythroid 2-related factor 2 (Nrf2)/Heme oxygenase-1 (HO-1) pathway and suppression of nuclear factor-kappa B (NF-kappaB) pathway in the spleen of chicken.	baicalin	40-48	heme oxygenase 1	Gallus gallus	159-163
30925330-5	2019	Meanwhile, Nrf2/HO-1 pathway was depressed by AFB1 treatment.	Aflatoxin B1	46-50	heme oxygenase 1	Gallus gallus	16-20