PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	18-22	
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	
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	
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	
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	
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	
20704548-4	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	
20704549-6	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	
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	
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	
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	
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	
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	
20732302-4	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
19457084-3	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	
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	
19039664-2	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.	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	
19039664-10	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	
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	
19526463-7	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	
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	
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	
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	
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.	Heme	111-115	heme oxygenase 1	Homo sapiens	72-77	
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	
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	
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	
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	
19162549-3	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	
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	
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	
18957281-3	2008	HO-1 is a key enzyme in physiological heme degradation.	Heme	38-42	heme oxygenase 1	Homo sapiens	0-4	
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	
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	
18799798-1	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	
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	
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	
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.	Heme	201-205	heme oxygenase 1	Homo sapiens	0-16	
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	
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	
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	
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	
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	
18786476-3	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	
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	
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	
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	
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	
18550526-8	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	
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	
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	
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	
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.	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.	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	
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	
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	
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	
18048804-1	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	
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	
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	
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	
18174022-7	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	
18178725-10	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	
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	
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	
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	
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	
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	
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	
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.	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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.	Heme	91-95	heme oxygenase 1	Homo sapiens	11-15	
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	
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	
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	
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	
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	
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	
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	
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	0-16	
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	
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	
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	
17275847-8	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
17018578-7	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
16495208-7	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	
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	
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	
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	
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	
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	
16329999-13	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
16181102-8	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	
16181102-11	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	
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	
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	
15649645-4	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	
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	
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	
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	
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	
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	
15516695-4	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	
15516695-10	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	
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	
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	
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	
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	
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	
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	
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	
15465821-7	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	
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	
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	
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	
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	
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	
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	
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.	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	
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	
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	
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	
15297453-10	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	
15339982-8	2004	Heme catabolism is regulated by (inducible) heme oxygenase-1 (HO-1).	Heme	0-4	heme oxygenase 1	Homo sapiens	44-60	
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	
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	
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	
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	
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	
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	
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	
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	
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	
15339982-8	2004	Heme catabolism is regulated by (inducible) heme oxygenase-1 (HO-1).	Heme	0-4	heme oxygenase 1	Homo sapiens	62-66	
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	
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	
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	
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	
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	
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	
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.	Heme	70-74	heme oxygenase 1	Homo sapiens	19-23	
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	
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	
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	
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.	Heme	159-163	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	159-163	heme oxygenase 1	Homo sapiens	30-34	
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	
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).	Heme	33-37	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.	Heme	54-58	heme oxygenase 1	Homo sapiens	0-16	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
12933701-1	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	
12933701-3	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<0.001).	Heme	117-121	heme oxygenase 1	Homo sapiens	18-22	
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	
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	
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	
12783778-4	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	
12783778-7	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	
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	
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	
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	
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	
12909459-0	2003	Heme oxygenase-1: unleashing the protective properties of heme.	Heme	58-62	heme oxygenase 1	Homo sapiens	0-16	
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	87-91	
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	
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	
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	
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	
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	
12704646-3	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	
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	
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	
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	
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	
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.	Heme	168-172	heme oxygenase 1	Homo sapiens	22-26	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
12699247-1	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	
12699247-4	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	
12699247-8	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	
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	
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	
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	
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	
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	
12964953-5	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	
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	
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	
12376366-4	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	
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	
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	
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	
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.	Heme	61-65	heme oxygenase 1	Homo sapiens	0-16	
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	
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	
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	
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.	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.	Heme	186-190	heme oxygenase 1	Homo sapiens	234-238	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
11668058-9	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.	Heme	60-64	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.	Heme	79-83	heme oxygenase 1	Homo sapiens	35-39	
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	
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	
11768235-12	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
10409239-6	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	
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	
10218639-5	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	
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	
10101013-11	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
8816811-11	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	
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	
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	
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	
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	
8679227-11	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	
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	
8650873-8	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	
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	
8547275-7	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
34874275-10	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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.	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
33845576-8	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
33868304-4	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	
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	
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	
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	
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	
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	
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	
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.	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	
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	
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	
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	
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	
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	
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	
33228260-4	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
32971746-8	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
33016915-6	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
31344980-5	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
30883732-6	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.	Heme	163-167	heme oxygenase 1	Homo sapiens	82-87	
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	
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	
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	
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	
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	
30009872-4	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	
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	
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	
30583467-5	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	
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	
30354231-11	2018	Surgery and heme arginate infusion significantly increased HO-1 mRNA concentration in peripheral blood mononuclear cells ( P<0.001).	Heme	12-16	heme oxygenase 1	Homo sapiens	59-63	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
28756878-2	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	
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	
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	
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	3-7	heme oxygenase 1	Homo sapiens	36-39	
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	
28655775-8	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	
28655775-8	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	
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	
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	
28655775-1	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	
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	
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	
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	
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	
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	
28347842-3	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	
28347842-5	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.	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	
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	
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	
28978042-7	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	
28978042-11	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
27244263-7	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	
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	
27795400-13	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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).	Heme	134-138	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	
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	
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	
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	
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	
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).	Heme	18-22	heme oxygenase 1	Homo sapiens	0-4	
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	
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	
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	
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	
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	
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	
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	
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	
25885228-2	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	
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	
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	
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	
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	
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	
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.	Heme	14-18	heme oxygenase 1	Homo sapiens	0-4	
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	
25744452-3	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
24954650-7	2014	HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO).	Heme	17-21	heme oxygenase 1	Homo sapiens	0-4	
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	
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	
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	
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	
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	
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	
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	
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	
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.	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
24847330-3	2014	HO-1 degrades heme but increases in experimental models of AKI.	Heme	14-18	heme oxygenase 1	Homo sapiens	0-4	
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	
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	
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	
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	
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	
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	
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	
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	
24179613-5	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
23720344-10	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
23068042-0	2013	Development of a heme sensor using fluorescently labeled heme oxygenase-1.	Heme	17-21	heme oxygenase 1	Homo sapiens	57-73	
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.	Heme	188-192	heme oxygenase 1	Homo sapiens	202-206	
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	
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	
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	
23092328-11	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	
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	
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	
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	
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	
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	
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	
23874015-6	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
22503972-10	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
21079975-13	2011	In a high heme-Fe condition, HO1 is found near the plasma membrane.	Heme	10-14	heme oxygenase 1	Homo sapiens	29-32	
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	
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	
21622183-4	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	
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	
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	
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	
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	
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	
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	
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