PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10770977-1 2000 Heme oxygenase-1 (HO-1) is a microsomal enzyme involved in the degradation of heme, resulting in the generation of biliverdin, iron, and carbon monoxide. Carbon Monoxide 137-152 heme oxygenase 1 Mus musculus 0-16 11875494-4 2002 Additional experiments revealed the involvement of carbon monoxide, one of the products of HO-1-mediated heme degradation, in the anti-inflammatory effect of IL-10 in vitro. Carbon Monoxide 51-66 heme oxygenase 1 Mus musculus 91-95 11463724-1 2001 Heme oxygenase (HO)-1 degrades the pro-oxidant heme and generates carbon monoxide and antioxidant bilirubin. Carbon Monoxide 66-81 heme oxygenase 1 Mus musculus 0-21 11593363-1 2001 Heme oxygenase-1 (HO-1) is an inducible heat shock protein that regulates heme metabolism to form bilirubin, ferritin and carbon monoxide. Carbon Monoxide 122-137 heme oxygenase 1 Mus musculus 0-16 11593363-1 2001 Heme oxygenase-1 (HO-1) is an inducible heat shock protein that regulates heme metabolism to form bilirubin, ferritin and carbon monoxide. Carbon Monoxide 122-137 heme oxygenase 1 Mus musculus 18-22 11591199-3 2001 Heme oxygenase-1 (HO-1) protein, also called HSP32, is the rate-limiting enzyme in the catabolism of heme to biliverdin, free iron and CO. Carbon Monoxide 135-137 heme oxygenase 1 Mus musculus 0-16 11591199-3 2001 Heme oxygenase-1 (HO-1) protein, also called HSP32, is the rate-limiting enzyme in the catabolism of heme to biliverdin, free iron and CO. Carbon Monoxide 135-137 heme oxygenase 1 Mus musculus 18-22 11591199-3 2001 Heme oxygenase-1 (HO-1) protein, also called HSP32, is the rate-limiting enzyme in the catabolism of heme to biliverdin, free iron and CO. Carbon Monoxide 135-137 heme oxygenase 1 Mus musculus 45-50 11329062-2 2001 Ho-1-deficient (Hmox1-/-) mice exhibited lethal ischemic lung injury, but were rescued from death by inhaled CO. Carbon Monoxide 109-111 heme oxygenase 1 Mus musculus 16-21 11238670-0 2001 Carbon monoxide generated by heme oxygenase-1 suppresses the rejection of mouse-to-rat cardiac transplants. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 29-45 10961657-1 2000 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, carbon monoxide and iron, and its expression can be used as a marker for oxidative stress. Carbon Monoxide 127-142 heme oxygenase 1 Mus musculus 0-16 10961657-1 2000 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, carbon monoxide and iron, and its expression can be used as a marker for oxidative stress. Carbon Monoxide 127-142 heme oxygenase 1 Mus musculus 18-22 10807584-1 2000 Heme oxygenase-1 (HO-1) is a 32-kDa microsomal enzyme that catalyzes the conversion of heme to biliverdin, releasing iron and carbon monoxide. Carbon Monoxide 126-141 heme oxygenase 1 Mus musculus 0-16 10807584-1 2000 Heme oxygenase-1 (HO-1) is a 32-kDa microsomal enzyme that catalyzes the conversion of heme to biliverdin, releasing iron and carbon monoxide. Carbon Monoxide 126-141 heme oxygenase 1 Mus musculus 18-22 10770977-1 2000 Heme oxygenase-1 (HO-1) is a microsomal enzyme involved in the degradation of heme, resulting in the generation of biliverdin, iron, and carbon monoxide. Carbon Monoxide 137-152 heme oxygenase 1 Mus musculus 18-22 10666115-1 2000 Heme oxygenase (HO)-1 catalyzes the oxidative cleavage of heme to yield equimolar amounts of biliverdin, iron, and carbon monoxide. Carbon Monoxide 115-130 heme oxygenase 1 Mus musculus 0-21 10666115-8 2000 Inhibition of tumor necrosis factor-alpha-induced apoptosis by HO-1 overexpression was reversed by 1H-(1,2, 4)oxadiazolo(4,3-a)quinoxalin-1-one, an inhibitor of guanylate cyclase, which is a target enzyme for carbon monoxide. Carbon Monoxide 209-224 heme oxygenase 1 Mus musculus 63-67 10666115-9 2000 Taken together, our data suggest that the antiapoptotic effect of HO-1 may be mediated via carbon monoxide. Carbon Monoxide 91-106 heme oxygenase 1 Mus musculus 66-70 9572292-1 1998 Heme oxygenase isozymes, HO-1 (also known as hsp32) and HO-2, are the source for the formation of the putative messenger molecule carbon monoxide (CO), reactive iron, and the in vitro antioxidant bilirubin. Carbon Monoxide 130-145 heme oxygenase 1 Mus musculus 25-29 10037492-2 1999 HO-1 cleaves the heme molecule and produces carbon monoxide (CO) and biliverdin (an antioxidant) and is essential for iron homeostasis. Carbon Monoxide 44-59 heme oxygenase 1 Mus musculus 0-4 10037492-2 1999 HO-1 cleaves the heme molecule and produces carbon monoxide (CO) and biliverdin (an antioxidant) and is essential for iron homeostasis. Carbon Monoxide 61-63 heme oxygenase 1 Mus musculus 0-4 10728783-1 1999 Heme oxygenase (HO)-1 catalyzes the conversion of heme to biliverdin, iron and carbon monoxide. Carbon Monoxide 79-94 heme oxygenase 1 Mus musculus 0-21 9795173-4 1998 These results suggest that carbon monoxide, one product of HO-1 activity, interferes in the development of spatial navigation memory, and may play a role in normal memory function. Carbon Monoxide 27-42 heme oxygenase 1 Mus musculus 59-63 9572292-1 1998 Heme oxygenase isozymes, HO-1 (also known as hsp32) and HO-2, are the source for the formation of the putative messenger molecule carbon monoxide (CO), reactive iron, and the in vitro antioxidant bilirubin. Carbon Monoxide 130-145 heme oxygenase 1 Mus musculus 45-50 9572292-1 1998 Heme oxygenase isozymes, HO-1 (also known as hsp32) and HO-2, are the source for the formation of the putative messenger molecule carbon monoxide (CO), reactive iron, and the in vitro antioxidant bilirubin. Carbon Monoxide 147-149 heme oxygenase 1 Mus musculus 25-29 9572292-1 1998 Heme oxygenase isozymes, HO-1 (also known as hsp32) and HO-2, are the source for the formation of the putative messenger molecule carbon monoxide (CO), reactive iron, and the in vitro antioxidant bilirubin. Carbon Monoxide 147-149 heme oxygenase 1 Mus musculus 45-50 34359970-3 2021 Labile heme is scavenged by hemopexin (Hx) and processed by heme oxygenase-1 (HO-1, Hmox1), resulting in its removal and the generation of biliverdin/bilirubin, carbon monoxide (CO) and iron. Carbon Monoxide 161-176 heme oxygenase 1 Mus musculus 60-76 9380735-2 1997 Here, we generated mice lacking functional heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron, to assess its participation in iron homeostasis. Carbon Monoxide 121-136 heme oxygenase 1 Mus musculus 43-59 9380735-2 1997 Here, we generated mice lacking functional heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron, to assess its participation in iron homeostasis. Carbon Monoxide 121-136 heme oxygenase 1 Mus musculus 61-66 9271271-2 1997 Heme oxygenase-1 (HO-1), a heat shock protein, has been shown to increase intracellular cGMP levels by formation of carbon monoxide (CO). Carbon Monoxide 116-131 heme oxygenase 1 Mus musculus 0-16 9271271-2 1997 Heme oxygenase-1 (HO-1), a heat shock protein, has been shown to increase intracellular cGMP levels by formation of carbon monoxide (CO). Carbon Monoxide 116-131 heme oxygenase 1 Mus musculus 18-22 9271271-2 1997 Heme oxygenase-1 (HO-1), a heat shock protein, has been shown to increase intracellular cGMP levels by formation of carbon monoxide (CO). Carbon Monoxide 133-135 heme oxygenase 1 Mus musculus 0-16 9271271-2 1997 Heme oxygenase-1 (HO-1), a heat shock protein, has been shown to increase intracellular cGMP levels by formation of carbon monoxide (CO). Carbon Monoxide 133-135 heme oxygenase 1 Mus musculus 18-22 34943953-0 2021 Carbon Monoxide Regulates Macrophage Differentiation and Polarization toward the M2 Phenotype through Upregulation of Heme Oxygenase 1. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 118-134 34943953-1 2021 Carbon monoxide (CO) is generated by heme oxygenase (HO), and HO-1 is highly induced in monocytes and macrophages upon stimulation. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 62-66 34943953-1 2021 Carbon monoxide (CO) is generated by heme oxygenase (HO), and HO-1 is highly induced in monocytes and macrophages upon stimulation. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 62-66 34359970-3 2021 Labile heme is scavenged by hemopexin (Hx) and processed by heme oxygenase-1 (HO-1, Hmox1), resulting in its removal and the generation of biliverdin/bilirubin, carbon monoxide (CO) and iron. Carbon Monoxide 161-176 heme oxygenase 1 Mus musculus 78-82 34359970-3 2021 Labile heme is scavenged by hemopexin (Hx) and processed by heme oxygenase-1 (HO-1, Hmox1), resulting in its removal and the generation of biliverdin/bilirubin, carbon monoxide (CO) and iron. Carbon Monoxide 161-176 heme oxygenase 1 Mus musculus 84-89 34359970-3 2021 Labile heme is scavenged by hemopexin (Hx) and processed by heme oxygenase-1 (HO-1, Hmox1), resulting in its removal and the generation of biliverdin/bilirubin, carbon monoxide (CO) and iron. Carbon Monoxide 178-180 heme oxygenase 1 Mus musculus 60-76 34359970-3 2021 Labile heme is scavenged by hemopexin (Hx) and processed by heme oxygenase-1 (HO-1, Hmox1), resulting in its removal and the generation of biliverdin/bilirubin, carbon monoxide (CO) and iron. Carbon Monoxide 178-180 heme oxygenase 1 Mus musculus 78-82 34359970-3 2021 Labile heme is scavenged by hemopexin (Hx) and processed by heme oxygenase-1 (HO-1, Hmox1), resulting in its removal and the generation of biliverdin/bilirubin, carbon monoxide (CO) and iron. Carbon Monoxide 178-180 heme oxygenase 1 Mus musculus 84-89 33383563-2 2021 In our previous studies, we demonstrated that the nuclear factor erythroid 2-like-2 (Nrf-2)/heme oxygenase-1 (HO-1)/carbon monoxide (CO) axis protects lens epithelial cells (LECs) against oxidants and ER stress. Carbon Monoxide 116-131 heme oxygenase 1 Mus musculus 92-108 33853347-2 2021 HO-1 (heme oxygenase 1, Hmox1) and carbon monoxide (CO), a product of heme degradation by HO-1, ameliorate neointima formation by inhibiting proliferation of smooth muscle cells. Carbon Monoxide 35-50 heme oxygenase 1 Mus musculus 90-94 33853347-2 2021 HO-1 (heme oxygenase 1, Hmox1) and carbon monoxide (CO), a product of heme degradation by HO-1, ameliorate neointima formation by inhibiting proliferation of smooth muscle cells. Carbon Monoxide 52-54 heme oxygenase 1 Mus musculus 90-94 33408127-3 2021 The primary function of heme oxygenase-1 (HO1) is to catalyze the degradation of heme into biliverdin, ferrous iron, and carbon monoxide. Carbon Monoxide 121-136 heme oxygenase 1 Mus musculus 24-40 33408127-3 2021 The primary function of heme oxygenase-1 (HO1) is to catalyze the degradation of heme into biliverdin, ferrous iron, and carbon monoxide. Carbon Monoxide 121-136 heme oxygenase 1 Mus musculus 42-45 35619717-1 2022 The enzyme heme oxygenase-1 (HO-1) has cytoprotective effects by catalyzing the degradation of heme to produce carbon monoxide, iron and biliverdin. Carbon Monoxide 111-126 heme oxygenase 1 Mus musculus 11-27 35619717-1 2022 The enzyme heme oxygenase-1 (HO-1) has cytoprotective effects by catalyzing the degradation of heme to produce carbon monoxide, iron and biliverdin. Carbon Monoxide 111-126 heme oxygenase 1 Mus musculus 29-33 35581352-2 2022 The heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway mediates the resolution of inflammation and is defective in CF-affected macrophages (MPhis). Carbon Monoxide 28-43 heme oxygenase 1 Mus musculus 22-26 35581352-2 2022 The heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway mediates the resolution of inflammation and is defective in CF-affected macrophages (MPhis). Carbon Monoxide 45-47 heme oxygenase 1 Mus musculus 22-26 33207934-1 2021 OBJECTIVE: Hmox1 (heme oxygenase-1) is a stress-induced enzyme that catalyzes the degradation of heme to carbon monoxide, iron, and biliverdin. Carbon Monoxide 105-120 heme oxygenase 1 Mus musculus 11-16 33207934-1 2021 OBJECTIVE: Hmox1 (heme oxygenase-1) is a stress-induced enzyme that catalyzes the degradation of heme to carbon monoxide, iron, and biliverdin. Carbon Monoxide 105-120 heme oxygenase 1 Mus musculus 18-34 33207934-12 2021 Mechanistic studies showed that carbon monoxide stabilized HIF-1alpha in Hmox1-/- fibroblasts in response to hypoxia. Carbon Monoxide 32-47 heme oxygenase 1 Mus musculus 73-78 33383563-2 2021 In our previous studies, we demonstrated that the nuclear factor erythroid 2-like-2 (Nrf-2)/heme oxygenase-1 (HO-1)/carbon monoxide (CO) axis protects lens epithelial cells (LECs) against oxidants and ER stress. Carbon Monoxide 116-131 heme oxygenase 1 Mus musculus 110-114 33383563-2 2021 In our previous studies, we demonstrated that the nuclear factor erythroid 2-like-2 (Nrf-2)/heme oxygenase-1 (HO-1)/carbon monoxide (CO) axis protects lens epithelial cells (LECs) against oxidants and ER stress. Carbon Monoxide 133-135 heme oxygenase 1 Mus musculus 92-108 33383563-2 2021 In our previous studies, we demonstrated that the nuclear factor erythroid 2-like-2 (Nrf-2)/heme oxygenase-1 (HO-1)/carbon monoxide (CO) axis protects lens epithelial cells (LECs) against oxidants and ER stress. Carbon Monoxide 133-135 heme oxygenase 1 Mus musculus 110-114 32335359-1 2020 Carbon monoxide (CO) produced by heme oxygenase-1 (HO-1) or delivered by CO-releasing molecules (CO-RMs) exerts anti-inflammatory action, a feature also exhibited by the nuclear factor erythroid 2-related factor 2 (Nrf2), a master regulator of the stress response. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 33-49 32335359-1 2020 Carbon monoxide (CO) produced by heme oxygenase-1 (HO-1) or delivered by CO-releasing molecules (CO-RMs) exerts anti-inflammatory action, a feature also exhibited by the nuclear factor erythroid 2-related factor 2 (Nrf2), a master regulator of the stress response. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 51-55 32335359-1 2020 Carbon monoxide (CO) produced by heme oxygenase-1 (HO-1) or delivered by CO-releasing molecules (CO-RMs) exerts anti-inflammatory action, a feature also exhibited by the nuclear factor erythroid 2-related factor 2 (Nrf2), a master regulator of the stress response. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 33-49 32335359-1 2020 Carbon monoxide (CO) produced by heme oxygenase-1 (HO-1) or delivered by CO-releasing molecules (CO-RMs) exerts anti-inflammatory action, a feature also exhibited by the nuclear factor erythroid 2-related factor 2 (Nrf2), a master regulator of the stress response. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 51-55 32035059-2 2020 In this study, we hypothesized that heme oxygenase-1 (HO-1), an enzyme responsible for degradation of heme to carbon monoxide (CO), bilirubin, and iron is an important regulator of inflammation and epithelial responses in the prostate. Carbon Monoxide 110-125 heme oxygenase 1 Mus musculus 36-52 32035059-2 2020 In this study, we hypothesized that heme oxygenase-1 (HO-1), an enzyme responsible for degradation of heme to carbon monoxide (CO), bilirubin, and iron is an important regulator of inflammation and epithelial responses in the prostate. Carbon Monoxide 110-125 heme oxygenase 1 Mus musculus 54-58 32035059-2 2020 In this study, we hypothesized that heme oxygenase-1 (HO-1), an enzyme responsible for degradation of heme to carbon monoxide (CO), bilirubin, and iron is an important regulator of inflammation and epithelial responses in the prostate. Carbon Monoxide 127-129 heme oxygenase 1 Mus musculus 36-52 32035059-2 2020 In this study, we hypothesized that heme oxygenase-1 (HO-1), an enzyme responsible for degradation of heme to carbon monoxide (CO), bilirubin, and iron is an important regulator of inflammation and epithelial responses in the prostate. Carbon Monoxide 127-129 heme oxygenase 1 Mus musculus 54-58 31848666-7 2020 HO-1 silence in Hepa 1-6 cells inhibited activation of autophagy and accelerated occurrence of apoptosis, and these could be recovered by CO pre-treatment. Carbon Monoxide 138-140 heme oxygenase 1 Mus musculus 0-4 31121086-2 2020 Carbon monoxide (CO)-releasing compounds were shown to exert an anti-inflammatory effect in murine POI partially through induction of heme oxygenase-1 (HO-1). Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 134-150 31121086-2 2020 Carbon monoxide (CO)-releasing compounds were shown to exert an anti-inflammatory effect in murine POI partially through induction of heme oxygenase-1 (HO-1). Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 152-156 32033079-5 2020 Also, MA, DMF and MF exert anti-inflammatory effects through the expression of heme oxygenase (HO) -1, a stress-inducing enzyme that converts heme to carbon monoxide (CO), iron and biliberdine. Carbon Monoxide 150-165 heme oxygenase 1 Mus musculus 79-101 32033079-5 2020 Also, MA, DMF and MF exert anti-inflammatory effects through the expression of heme oxygenase (HO) -1, a stress-inducing enzyme that converts heme to carbon monoxide (CO), iron and biliberdine. Carbon Monoxide 167-169 heme oxygenase 1 Mus musculus 79-101 32568195-2 2020 Heme oxygenase 1 (HO-1) is a stress protein that catalyzes the degradation of heme into free iron, biliverdin, and carbon monoxide. Carbon Monoxide 115-130 heme oxygenase 1 Mus musculus 0-16 31664855-5 2020 The production of cleaved IL-1B and the activation of caspase-1 in LPS- and ATP-primed macrophages were inhibited by hemin, an HO-1 inducer, and two HO-1 enzymatic products [bilirubin and carbon monoxide (CO)]. Carbon Monoxide 188-203 heme oxygenase 1 Mus musculus 149-153 31664855-5 2020 The production of cleaved IL-1B and the activation of caspase-1 in LPS- and ATP-primed macrophages were inhibited by hemin, an HO-1 inducer, and two HO-1 enzymatic products [bilirubin and carbon monoxide (CO)]. Carbon Monoxide 205-207 heme oxygenase 1 Mus musculus 149-153 32568195-2 2020 Heme oxygenase 1 (HO-1) is a stress protein that catalyzes the degradation of heme into free iron, biliverdin, and carbon monoxide. Carbon Monoxide 115-130 heme oxygenase 1 Mus musculus 18-22 31295319-5 2019 Because CO is physiologically generated during heme degradation by heme oxygenase 1 (HO-1), an IL-6-inducible enzyme with anti-inflammatory properties, we hypothesized that hepatocellular HO-1 may operate as a physiological feedback regulator of hepcidin that resolves inflammatory signaling. Carbon Monoxide 8-10 heme oxygenase 1 Mus musculus 67-83 31295319-5 2019 Because CO is physiologically generated during heme degradation by heme oxygenase 1 (HO-1), an IL-6-inducible enzyme with anti-inflammatory properties, we hypothesized that hepatocellular HO-1 may operate as a physiological feedback regulator of hepcidin that resolves inflammatory signaling. Carbon Monoxide 8-10 heme oxygenase 1 Mus musculus 188-192 31645120-0 2019 Carbon monoxide ameliorates acetaminophen-induced liver injury by increasing hepatic HO-1 and Parkin expression. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 85-89 31645120-3 2019 Carbon monoxide (CO), an end-product of heme oxygenase (HO)-1 activity, can confer anti-inflammatory and antiapoptotic properties in cellular models of toxicity via regulation of mitochondrial function. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 40-61 31645120-3 2019 Carbon monoxide (CO), an end-product of heme oxygenase (HO)-1 activity, can confer anti-inflammatory and antiapoptotic properties in cellular models of toxicity via regulation of mitochondrial function. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 40-61 31645120-7 2019 Additionally, CO gas inhalation significantly alleviated APAP-induced liver damage in vivo and correspondingly reduced serum alanine aminotransferase and aspartate aminotransferase levels as well as proinflammatory cytokines and reduced the expression of CHOP in liver tissues while dramatically increasing hepatic HO-1 and Parkin expression. Carbon Monoxide 14-16 heme oxygenase 1 Mus musculus 315-319 31645120-8 2019 We found that the protective effects of CO on APAP-induced liver damage were mediated by down-regulation of CHOP at a transcriptional and post-translational level via induction of HO-1 and Parkin, respectively, and associated with decreases in reactive oxygen species production and JNK phosphorylation. Carbon Monoxide 40-42 heme oxygenase 1 Mus musculus 180-184 31645120-9 2019 We conclude that CO may represent a promising therapeutic agent for APAP-induced liver injury.-Chen, Y., Park, H.-J., Park, J., Song, H.-C., Ryter, S. W., Surh, Y.-J., Kim, U.-H., Joe, Y., Chung, H. T. Carbon monoxide ameliorates acetaminophen-induced liver injury by increasing hepatic HO-1 and Parkin expression. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 287-291 31295319-5 2019 Because CO is physiologically generated during heme degradation by heme oxygenase 1 (HO-1), an IL-6-inducible enzyme with anti-inflammatory properties, we hypothesized that hepatocellular HO-1 may operate as a physiological feedback regulator of hepcidin that resolves inflammatory signaling. Carbon Monoxide 8-10 heme oxygenase 1 Mus musculus 85-89 30333233-9 2018 Critically, the HO-1 products carbon monoxide and bilirubin suppressed the NLRP3-RXR axis in pAECs. Carbon Monoxide 30-45 heme oxygenase 1 Mus musculus 16-20 31026585-1 2019 Heme oxygenase (HO)-1, a stress-inducible enzyme that converts heme into carbon monoxide (CO), iron and biliverdin, exerts important anti-inflammatory effects in activated macrophages. Carbon Monoxide 73-88 heme oxygenase 1 Mus musculus 0-21 31026585-1 2019 Heme oxygenase (HO)-1, a stress-inducible enzyme that converts heme into carbon monoxide (CO), iron and biliverdin, exerts important anti-inflammatory effects in activated macrophages. Carbon Monoxide 90-92 heme oxygenase 1 Mus musculus 0-21 30411846-4 2019 Previous studies indicated that carbon monoxide (CO), a product of heme oxygenase (HO)-1, protects against Abeta-induced toxicity and promotes neuroprotection. Carbon Monoxide 32-47 heme oxygenase 1 Mus musculus 67-88 30411846-4 2019 Previous studies indicated that carbon monoxide (CO), a product of heme oxygenase (HO)-1, protects against Abeta-induced toxicity and promotes neuroprotection. Carbon Monoxide 49-51 heme oxygenase 1 Mus musculus 67-88 29065700-4 2018 Heme oxygenase-1 (HO-1, encoded by the Hmox1 gene), an enzyme converting heme to biliverdin, carbon monoxide, and Fe2+, is cytoprotective and can affect stem cell performance. Carbon Monoxide 93-108 heme oxygenase 1 Mus musculus 0-22 30487665-1 2018 Heme oxygenases (HOs) are rate-limiting enzymes catabolizing heme to biliverdin, ferrous iron, and carbon monoxide, and of the three HO isoforms identified, HO-1 plays a protective role against inflammatory processes. Carbon Monoxide 99-114 heme oxygenase 1 Mus musculus 157-161 30425781-10 2018 Pharmacological application of the HO-1 reaction product carbon monoxide (CO), but not biliverdin or iron, conferred protection in Hmox-1-deficient macrophages. Carbon Monoxide 57-72 heme oxygenase 1 Mus musculus 35-39 30425781-10 2018 Pharmacological application of the HO-1 reaction product carbon monoxide (CO), but not biliverdin or iron, conferred protection in Hmox-1-deficient macrophages. Carbon Monoxide 57-72 heme oxygenase 1 Mus musculus 131-137 30425781-10 2018 Pharmacological application of the HO-1 reaction product carbon monoxide (CO), but not biliverdin or iron, conferred protection in Hmox-1-deficient macrophages. Carbon Monoxide 74-76 heme oxygenase 1 Mus musculus 35-39 30425781-10 2018 Pharmacological application of the HO-1 reaction product carbon monoxide (CO), but not biliverdin or iron, conferred protection in Hmox-1-deficient macrophages. Carbon Monoxide 74-76 heme oxygenase 1 Mus musculus 131-137 30068325-11 2018 Further in vitro studies showed that 1) silica-induced HO-1 was significantly attenuated by inhibiting ERK activation, and 2) carbon monoxide and bilirubin as final byproducts of HO-1 could inhibit ERK activation. Carbon Monoxide 126-141 heme oxygenase 1 Mus musculus 55-59 30068325-11 2018 Further in vitro studies showed that 1) silica-induced HO-1 was significantly attenuated by inhibiting ERK activation, and 2) carbon monoxide and bilirubin as final byproducts of HO-1 could inhibit ERK activation. Carbon Monoxide 126-141 heme oxygenase 1 Mus musculus 179-183 30068325-12 2018 Taken together, silica-induced HO-1 upregulation was mediated by ERK activation, and HO-1 further regulates ERK activation via its final byproducts, carbon monoxide and bilirubin. Carbon Monoxide 149-164 heme oxygenase 1 Mus musculus 85-89 30337301-1 2018 Heme oxygenase 1 (HMOX1), the inducible enzyme that catabolizes the degradation of heme into biliverdin, iron, and carbon monoxide, plays an essential role in the clearance of senescent and damaged red blood cells, systemic iron homeostasis, erythropoiesis, vascular hemostasis, and oxidative and inflammatory stress responses. Carbon Monoxide 115-130 heme oxygenase 1 Mus musculus 0-16 30337301-1 2018 Heme oxygenase 1 (HMOX1), the inducible enzyme that catabolizes the degradation of heme into biliverdin, iron, and carbon monoxide, plays an essential role in the clearance of senescent and damaged red blood cells, systemic iron homeostasis, erythropoiesis, vascular hemostasis, and oxidative and inflammatory stress responses. Carbon Monoxide 115-130 heme oxygenase 1 Mus musculus 18-23 29065700-4 2018 Heme oxygenase-1 (HO-1, encoded by the Hmox1 gene), an enzyme converting heme to biliverdin, carbon monoxide, and Fe2+, is cytoprotective and can affect stem cell performance. Carbon Monoxide 93-108 heme oxygenase 1 Mus musculus 39-44 29868517-6 2018 Additionally, mice were protected against MA-ALI/ARDS after treatment with carbon monoxide- releasing molecules or with carbon monoxide, which is also released by the HO-1 activity. Carbon Monoxide 75-90 heme oxygenase 1 Mus musculus 167-171 29868517-6 2018 Additionally, mice were protected against MA-ALI/ARDS after treatment with carbon monoxide- releasing molecules or with carbon monoxide, which is also released by the HO-1 activity. Carbon Monoxide 120-135 heme oxygenase 1 Mus musculus 167-171 29247123-0 2018 Taurine chloramine potentiates phagocytic activity of peritoneal macrophages through up-regulation of dectin-1 mediated by heme oxygenase-1-derived carbon monoxide. Carbon Monoxide 148-163 heme oxygenase 1 Mus musculus 123-139 29694434-11 2018 The HO-1 reaction product carbon monoxide, fully restored the protection, in part by inhibiting Weibel-Palade body mobilization of P-selectin and von Willebrand factor to endothelial cell surfaces. Carbon Monoxide 26-41 heme oxygenase 1 Mus musculus 4-8 29247614-0 2018 Mechanism implicated in the anti-allodynic and anti-hyperalgesic effects induced by the activation of heme oxygenase 1/carbon monoxide signaling pathway in the central nervous system of mice with neuropathic pain. Carbon Monoxide 119-134 heme oxygenase 1 Mus musculus 102-118 30039753-5 2018 Since heme oxygenase, via its products bilirubin and carbon monoxide, functions as a physiological inhibitor of various isoforms of NADPH oxidase, phase 2-inducing nutraceuticals with blood brain-barrier permeability such as lipoic acid, an effective inducer of heme oxygenase-1, may have potential for prevention of morphine tolerance; indeed, this has been demonstrated in a mouse study. Carbon Monoxide 53-68 heme oxygenase 1 Mus musculus 262-278 28747460-3 2017 We moreover predict that heme oxygenase-1 (HO-1/Hmox1) and its product carbon monoxide (CO) contribute to the restoration of rhythm and neuroprotection. Carbon Monoxide 71-86 heme oxygenase 1 Mus musculus 25-41 28747460-3 2017 We moreover predict that heme oxygenase-1 (HO-1/Hmox1) and its product carbon monoxide (CO) contribute to the restoration of rhythm and neuroprotection. Carbon Monoxide 71-86 heme oxygenase 1 Mus musculus 48-53 28747460-3 2017 We moreover predict that heme oxygenase-1 (HO-1/Hmox1) and its product carbon monoxide (CO) contribute to the restoration of rhythm and neuroprotection. Carbon Monoxide 88-90 heme oxygenase 1 Mus musculus 25-41 28747460-3 2017 We moreover predict that heme oxygenase-1 (HO-1/Hmox1) and its product carbon monoxide (CO) contribute to the restoration of rhythm and neuroprotection. Carbon Monoxide 88-90 heme oxygenase 1 Mus musculus 48-53 28763300-1 2017 Background Hmox1 plays an important role in the regulation of mitochondrial bioenergetics and function by regulating cellular heme-derived CO and bilirubin. Carbon Monoxide 139-141 heme oxygenase 1 Mus musculus 11-16 28560357-4 2017 Furthermore, free heme induces expression of heme oxygenase-1 to increase production of CO, biliverdin and bilirubin. Carbon Monoxide 88-90 heme oxygenase 1 Mus musculus 45-61 27554679-1 2017 AIMS: The heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway induced in astrocytes after ischemic brain injury promotes vascular endothelial growth factor (VEGF) expression to maintain and repair neurovascular function. Carbon Monoxide 34-49 heme oxygenase 1 Mus musculus 10-26 27554679-1 2017 AIMS: The heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway induced in astrocytes after ischemic brain injury promotes vascular endothelial growth factor (VEGF) expression to maintain and repair neurovascular function. Carbon Monoxide 34-49 heme oxygenase 1 Mus musculus 28-32 27554679-1 2017 AIMS: The heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway induced in astrocytes after ischemic brain injury promotes vascular endothelial growth factor (VEGF) expression to maintain and repair neurovascular function. Carbon Monoxide 51-53 heme oxygenase 1 Mus musculus 10-26 27554679-1 2017 AIMS: The heme oxygenase-1 (HO-1)/carbon monoxide (CO) pathway induced in astrocytes after ischemic brain injury promotes vascular endothelial growth factor (VEGF) expression to maintain and repair neurovascular function. Carbon Monoxide 51-53 heme oxygenase 1 Mus musculus 28-32 28576353-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 0-16 28576353-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 18-22 28576353-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 0-16 28576353-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 18-22 27057920-9 2016 The met-Hb readily releases free hemin that directly induces HO-1 in the liver, which metabolizes the hemin into iron, biliverdin, and CO. Carbon Monoxide 135-137 heme oxygenase 1 Mus musculus 61-65 27867098-9 2017 However, silencing HO-1 expression abrogated the protective action of ammonia and this was reversed by the administration of carbon monoxide but not bilirubin or iron. Carbon Monoxide 125-140 heme oxygenase 1 Mus musculus 19-23 27867098-10 2017 In conclusion, this study demonstrates that ammonia stimulates the expression of HO-1 in endothelial cells via the ROS-Nrf2 pathway, and that the induction of HO-1 contributes to the cytoprotective action of ammonia by generating carbon monoxide. Carbon Monoxide 230-245 heme oxygenase 1 Mus musculus 159-163 26866925-2 2016 Heme oxygenase 1 (HO-1, hmox) is the first and rate limiting enzyme in the breakdown of heme originating from degraded senescent erythrocytes and heme-proteins, yielding equal amounts of iron, carbon monoxide and biliverdin. Carbon Monoxide 193-208 heme oxygenase 1 Mus musculus 18-22 26866925-2 2016 Heme oxygenase 1 (HO-1, hmox) is the first and rate limiting enzyme in the breakdown of heme originating from degraded senescent erythrocytes and heme-proteins, yielding equal amounts of iron, carbon monoxide and biliverdin. Carbon Monoxide 193-208 heme oxygenase 1 Mus musculus 24-28 26385576-3 2016 Heme oxygenase isoform 1 (HO-1) is crucial for the response to oxidative stress via the catabolism of heme to carbon monoxide, bilirubin, and iron. Carbon Monoxide 110-125 heme oxygenase 1 Mus musculus 0-24 26385576-3 2016 Heme oxygenase isoform 1 (HO-1) is crucial for the response to oxidative stress via the catabolism of heme to carbon monoxide, bilirubin, and iron. Carbon Monoxide 110-125 heme oxygenase 1 Mus musculus 26-30 27817989-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 0-16 27817989-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 18-22 27817989-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 0-16 27817989-1 2017 Heme oxygenase-1 (HO-1) is stress-inducible, cytoprotective enzyme degrading heme to carbon monoxide (CO), biliverdin and Fe2+. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 18-22 27867098-0 2017 Ammonia promotes endothelial cell survival via the heme oxygenase-1-mediated release of carbon monoxide. Carbon Monoxide 88-103 heme oxygenase 1 Mus musculus 51-67 27906108-8 2016 Mechanistically, HO-1 degrades heme into biliverdin, releasing in the process ferrous iron and carbon monoxide (CO). Carbon Monoxide 95-110 heme oxygenase 1 Mus musculus 17-21 27906108-8 2016 Mechanistically, HO-1 degrades heme into biliverdin, releasing in the process ferrous iron and carbon monoxide (CO). Carbon Monoxide 112-114 heme oxygenase 1 Mus musculus 17-21 27020787-1 2016 RATIONALE: The activation of cannabinoid 2 receptors (CB2R) attenuates chronic pain, but the role played by carbon monoxide synthesized by the inducible heme oxygenase 1 (HO-1) on the anti-nociceptive effects produced by a selective CB2R agonist, JWH-015, during painful diabetic neuropathy remains unknown. Carbon Monoxide 108-123 heme oxygenase 1 Mus musculus 153-169 27020787-1 2016 RATIONALE: The activation of cannabinoid 2 receptors (CB2R) attenuates chronic pain, but the role played by carbon monoxide synthesized by the inducible heme oxygenase 1 (HO-1) on the anti-nociceptive effects produced by a selective CB2R agonist, JWH-015, during painful diabetic neuropathy remains unknown. Carbon Monoxide 108-123 heme oxygenase 1 Mus musculus 171-175 27057920-7 2016 Thus, a homeostatic feedback model for the CO/HO-1 system was proposed as follows: HemoCD primarily removes CO from cell-free CO-Hb. Carbon Monoxide 43-45 heme oxygenase 1 Mus musculus 46-50 25816687-10 2015 Pharmacologic inhibition of HO-1 activity or knockdown of HO-1 gene in RAW264.7 cells abolished the TauCl-induced efferocytosis, whereas both overexpression of HO-1 and treatment with carbon monoxide (CO), the product of HO, potentiated the efferocytic activity of macrophages. Carbon Monoxide 201-203 heme oxygenase 1 Mus musculus 58-62 25640654-3 2016 The cytoprotective protein heme oxygenase-1 (HO-1), which generates endogenous carbon monoxide (CO), is expressed in the lung during Lipopolysaccharide (LPS) tolerance and cross tolerance. Carbon Monoxide 79-94 heme oxygenase 1 Mus musculus 27-43 25640654-3 2016 The cytoprotective protein heme oxygenase-1 (HO-1), which generates endogenous carbon monoxide (CO), is expressed in the lung during Lipopolysaccharide (LPS) tolerance and cross tolerance. Carbon Monoxide 79-94 heme oxygenase 1 Mus musculus 45-49 25640654-3 2016 The cytoprotective protein heme oxygenase-1 (HO-1), which generates endogenous carbon monoxide (CO), is expressed in the lung during Lipopolysaccharide (LPS) tolerance and cross tolerance. Carbon Monoxide 96-98 heme oxygenase 1 Mus musculus 27-43 25640654-3 2016 The cytoprotective protein heme oxygenase-1 (HO-1), which generates endogenous carbon monoxide (CO), is expressed in the lung during Lipopolysaccharide (LPS) tolerance and cross tolerance. Carbon Monoxide 96-98 heme oxygenase 1 Mus musculus 45-49 27110594-1 2016 The cardioprotective inducible enzyme heme oxygenase-1 (HO-1) degrades prooxidant heme into equimolar quantities of carbon monoxide, biliverdin, and iron. Carbon Monoxide 116-131 heme oxygenase 1 Mus musculus 38-54 27110594-1 2016 The cardioprotective inducible enzyme heme oxygenase-1 (HO-1) degrades prooxidant heme into equimolar quantities of carbon monoxide, biliverdin, and iron. Carbon Monoxide 116-131 heme oxygenase 1 Mus musculus 56-60 26445592-8 2015 The HO-1 inducer hemin and the HO-1 byproduct carbon monoxide (CO) also enhanced hepatic oxidative metabolism in HFD-fed obese mice. Carbon Monoxide 46-61 heme oxygenase 1 Mus musculus 31-35 26445592-8 2015 The HO-1 inducer hemin and the HO-1 byproduct carbon monoxide (CO) also enhanced hepatic oxidative metabolism in HFD-fed obese mice. Carbon Monoxide 63-65 heme oxygenase 1 Mus musculus 4-8 26445592-8 2015 The HO-1 inducer hemin and the HO-1 byproduct carbon monoxide (CO) also enhanced hepatic oxidative metabolism in HFD-fed obese mice. Carbon Monoxide 63-65 heme oxygenase 1 Mus musculus 31-35 26160631-1 2015 BACKGROUND: Heme oxygenase-1 (HO-1) is an inducible stress-responsive enzyme converting heme to bilirubin, carbon monoxide, and free iron, which exerts anti-inflammatory and antiapoptotic effects. Carbon Monoxide 107-122 heme oxygenase 1 Mus musculus 12-28 26160631-1 2015 BACKGROUND: Heme oxygenase-1 (HO-1) is an inducible stress-responsive enzyme converting heme to bilirubin, carbon monoxide, and free iron, which exerts anti-inflammatory and antiapoptotic effects. Carbon Monoxide 107-122 heme oxygenase 1 Mus musculus 30-34 26672618-1 2016 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that catalyzes the breakdown of heme to biliverdin, carbon monoxide, and iron. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 0-16 26672618-1 2016 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that catalyzes the breakdown of heme to biliverdin, carbon monoxide, and iron. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 18-22 26879758-4 2016 These effects of HO-1 were mimicked by exogenous carbon monoxide, which is one of the catalytic products of HO-1. Carbon Monoxide 49-64 heme oxygenase 1 Mus musculus 17-21 26879758-4 2016 These effects of HO-1 were mimicked by exogenous carbon monoxide, which is one of the catalytic products of HO-1. Carbon Monoxide 49-64 heme oxygenase 1 Mus musculus 108-112 26133060-2 2015 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme that catalyzes the degradation of heme to yield biliverdin, CO and free iron. Carbon Monoxide 110-112 heme oxygenase 1 Mus musculus 0-16 26133060-2 2015 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme that catalyzes the degradation of heme to yield biliverdin, CO and free iron. Carbon Monoxide 110-112 heme oxygenase 1 Mus musculus 18-22 25816687-10 2015 Pharmacologic inhibition of HO-1 activity or knockdown of HO-1 gene in RAW264.7 cells abolished the TauCl-induced efferocytosis, whereas both overexpression of HO-1 and treatment with carbon monoxide (CO), the product of HO, potentiated the efferocytic activity of macrophages. Carbon Monoxide 201-203 heme oxygenase 1 Mus musculus 58-62 25455753-2 2015 Heme oxygenase (HO)-1 cleaves heme to form biliverdin, carbon monoxide (CO) and iron (Fe(2+)). Carbon Monoxide 55-70 heme oxygenase 1 Mus musculus 0-21 25179131-1 2015 Carbon monoxide (CO) has been recently reported as the main anti-inflammatory mediator of the haem-degrading enzyme haem-oxygenase 1 (HO-1). Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 116-132 25179131-1 2015 Carbon monoxide (CO) has been recently reported as the main anti-inflammatory mediator of the haem-degrading enzyme haem-oxygenase 1 (HO-1). Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 134-138 25179131-1 2015 Carbon monoxide (CO) has been recently reported as the main anti-inflammatory mediator of the haem-degrading enzyme haem-oxygenase 1 (HO-1). Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 116-132 25179131-1 2015 Carbon monoxide (CO) has been recently reported as the main anti-inflammatory mediator of the haem-degrading enzyme haem-oxygenase 1 (HO-1). Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 134-138 25455753-2 2015 Heme oxygenase (HO)-1 cleaves heme to form biliverdin, carbon monoxide (CO) and iron (Fe(2+)). Carbon Monoxide 72-74 heme oxygenase 1 Mus musculus 0-21 25628565-9 2014 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of heme catalyzed by HO-1. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 15-19 25628565-9 2014 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of heme catalyzed by HO-1. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 165-169 25628565-9 2014 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of heme catalyzed by HO-1. Carbon Monoxide 129-131 heme oxygenase 1 Mus musculus 15-19 25628565-9 2014 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of heme catalyzed by HO-1. Carbon Monoxide 129-131 heme oxygenase 1 Mus musculus 165-169 26217498-2 2014 However, the specific role of the heme oxygenase-1 metabolite, carbon monoxide (CO), in this response has yet to be established. Carbon Monoxide 63-78 heme oxygenase 1 Mus musculus 34-50 25111043-1 2014 Heme oxygenase-1 (HO-1) encoded by the HMOX1 gene is a 32-kDa stress protein that catabolizes heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 129-144 heme oxygenase 1 Mus musculus 0-16 25111043-1 2014 Heme oxygenase-1 (HO-1) encoded by the HMOX1 gene is a 32-kDa stress protein that catabolizes heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 129-144 heme oxygenase 1 Mus musculus 18-22 25111043-1 2014 Heme oxygenase-1 (HO-1) encoded by the HMOX1 gene is a 32-kDa stress protein that catabolizes heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 129-144 heme oxygenase 1 Mus musculus 39-44 25111043-1 2014 Heme oxygenase-1 (HO-1) encoded by the HMOX1 gene is a 32-kDa stress protein that catabolizes heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 146-148 heme oxygenase 1 Mus musculus 0-16 25111043-1 2014 Heme oxygenase-1 (HO-1) encoded by the HMOX1 gene is a 32-kDa stress protein that catabolizes heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 146-148 heme oxygenase 1 Mus musculus 18-22 25111043-1 2014 Heme oxygenase-1 (HO-1) encoded by the HMOX1 gene is a 32-kDa stress protein that catabolizes heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 146-148 heme oxygenase 1 Mus musculus 39-44 25295542-2 2014 The gasotransmitter carbon monoxide (CO) is generated by the stress-responsive enzyme heme oxygenase-1 (HO-1, encoded by Hmox1), which is highly induced in macrophages in response to bacterial infection. Carbon Monoxide 20-35 heme oxygenase 1 Mus musculus 86-108 25295542-2 2014 The gasotransmitter carbon monoxide (CO) is generated by the stress-responsive enzyme heme oxygenase-1 (HO-1, encoded by Hmox1), which is highly induced in macrophages in response to bacterial infection. Carbon Monoxide 20-35 heme oxygenase 1 Mus musculus 121-126 25295542-2 2014 The gasotransmitter carbon monoxide (CO) is generated by the stress-responsive enzyme heme oxygenase-1 (HO-1, encoded by Hmox1), which is highly induced in macrophages in response to bacterial infection. Carbon Monoxide 37-39 heme oxygenase 1 Mus musculus 86-108 25295542-2 2014 The gasotransmitter carbon monoxide (CO) is generated by the stress-responsive enzyme heme oxygenase-1 (HO-1, encoded by Hmox1), which is highly induced in macrophages in response to bacterial infection. Carbon Monoxide 37-39 heme oxygenase 1 Mus musculus 121-126 25734151-7 2014 Breath CO/CO2 values correlated with systemic inflammation biomarkers in serum and heme oxygenase-1 gene expression in blood. Carbon Monoxide 7-9 heme oxygenase 1 Mus musculus 83-99 24530569-3 2014 Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the rate-limiting step in the oxidative degradation of heme to free iron, biliverdin and carbon monoxide. Carbon Monoxide 149-164 heme oxygenase 1 Mus musculus 0-21 24532288-0 2014 Suppression of inflammatory cell trafficking and alveolar simplification by the heme oxygenase-1 product carbon monoxide. Carbon Monoxide 105-120 heme oxygenase 1 Mus musculus 80-96 26217498-2 2014 However, the specific role of the heme oxygenase-1 metabolite, carbon monoxide (CO), in this response has yet to be established. Carbon Monoxide 80-82 heme oxygenase 1 Mus musculus 34-50 24334457-1 2014 The protective role of hemeoxygenase-1 (HO-1) in various inflammatory conditions is mediated in part by its products, carbon monoxide (CO) and biliverdin. Carbon Monoxide 118-133 heme oxygenase 1 Mus musculus 23-44 24366077-0 2014 Carbon monoxide promotes proliferation of uterine natural killer cells and remodeling of spiral arteries in pregnant hypertensive heme oxygenase-1 mutant mice. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 130-146 24366077-1 2014 Heme Oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO) promote implantation and placentation. Carbon Monoxide 43-58 heme oxygenase 1 Mus musculus 0-16 24366077-1 2014 Heme Oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO) promote implantation and placentation. Carbon Monoxide 60-62 heme oxygenase 1 Mus musculus 0-16 24366077-6 2014 Application of CO at low dose during early to midgestation prevented intrauterine growth restriction in Hmox1(+/-) mothers, this being associated with enhanced in situ proliferation of uNK cells and normalization of angiogenic parameters. Carbon Monoxide 15-17 heme oxygenase 1 Mus musculus 104-109 24114430-1 2014 RATIONALE: Carbon monoxide synthetized by inducible heme oxygenase (HO-1) exerts potent anti-inflammatory and antinociceptive effects during acute and neuropathic pain, but its role in the modulation of chronic inflammatory pain and the possible involvement of nitric oxide in this action remain unknown. Carbon Monoxide 11-26 heme oxygenase 1 Mus musculus 68-72 24114430-8 2014 An interaction between HO-1/carbon monoxide and NOS1/nitric oxide systems was also demonstrated. Carbon Monoxide 28-43 heme oxygenase 1 Mus musculus 23-27 24334457-1 2014 The protective role of hemeoxygenase-1 (HO-1) in various inflammatory conditions is mediated in part by its products, carbon monoxide (CO) and biliverdin. Carbon Monoxide 135-137 heme oxygenase 1 Mus musculus 23-44 24349609-1 2013 Endogenous carbon monoxide (CO) is produced by heme oxygenase-1 (HO)-1 which mediates the degradation of heme into CO, iron, and biliverdin. Carbon Monoxide 11-26 heme oxygenase 1 Mus musculus 47-63 24771904-7 2013 HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO). Carbon Monoxide 46-61 heme oxygenase 1 Mus musculus 0-4 24771904-7 2013 HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO). Carbon Monoxide 63-65 heme oxygenase 1 Mus musculus 0-4 24255121-2 2013 We previously demonstrated that M. tuberculosis induces an enzyme, heme oxygenase (HO1), that produces carbon monoxide (CO) gas and that M. tuberculosis adapts its transcriptome during CO exposure. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 83-86 24255121-2 2013 We previously demonstrated that M. tuberculosis induces an enzyme, heme oxygenase (HO1), that produces carbon monoxide (CO) gas and that M. tuberculosis adapts its transcriptome during CO exposure. Carbon Monoxide 120-122 heme oxygenase 1 Mus musculus 83-86 24255121-9 2013 In addition to these molecules, human and mouse macrophages also produce carbon monoxide (CO) gas by the heme oxygenase (HO1) enzyme. Carbon Monoxide 73-88 heme oxygenase 1 Mus musculus 121-124 24255121-9 2013 In addition to these molecules, human and mouse macrophages also produce carbon monoxide (CO) gas by the heme oxygenase (HO1) enzyme. Carbon Monoxide 90-92 heme oxygenase 1 Mus musculus 121-124 23691924-3 2013 Here we propose that a new potential target for therapy is haem oxygenase-1 (HO-1), an enzyme that catalyses the degradation of the haem group into biliverdin, carbon monoxide (CO) and Fe(2+) . Carbon Monoxide 160-175 heme oxygenase 1 Mus musculus 59-75 23691924-3 2013 Here we propose that a new potential target for therapy is haem oxygenase-1 (HO-1), an enzyme that catalyses the degradation of the haem group into biliverdin, carbon monoxide (CO) and Fe(2+) . Carbon Monoxide 160-175 heme oxygenase 1 Mus musculus 77-81 23691924-3 2013 Here we propose that a new potential target for therapy is haem oxygenase-1 (HO-1), an enzyme that catalyses the degradation of the haem group into biliverdin, carbon monoxide (CO) and Fe(2+) . Carbon Monoxide 177-179 heme oxygenase 1 Mus musculus 59-75 23691924-3 2013 Here we propose that a new potential target for therapy is haem oxygenase-1 (HO-1), an enzyme that catalyses the degradation of the haem group into biliverdin, carbon monoxide (CO) and Fe(2+) . Carbon Monoxide 177-179 heme oxygenase 1 Mus musculus 77-81 23650615-0 2013 Inhaled carbon monoxide accelerates resolution of inflammation via unique proresolving mediator-heme oxygenase-1 circuits. Carbon Monoxide 8-23 heme oxygenase 1 Mus musculus 96-112 23578787-3 2013 Heme oxygenase-1 (HO-1) mediates intestinal protection due to anti-inflammatory, antioxidative, and antiapoptotic effects of its products carbon monoxide, biliverdin, and bilirubin. Carbon Monoxide 138-153 heme oxygenase 1 Mus musculus 0-16 23578787-3 2013 Heme oxygenase-1 (HO-1) mediates intestinal protection due to anti-inflammatory, antioxidative, and antiapoptotic effects of its products carbon monoxide, biliverdin, and bilirubin. Carbon Monoxide 138-153 heme oxygenase 1 Mus musculus 18-22 23393395-2 2013 Previous studies have shown that heme oxygenase-1 and its reaction byproduct, carbon monoxide (CO), induce SDF-1alpha expression in ischemic heart. Carbon Monoxide 78-93 heme oxygenase 1 Mus musculus 33-49 23393395-2 2013 Previous studies have shown that heme oxygenase-1 and its reaction byproduct, carbon monoxide (CO), induce SDF-1alpha expression in ischemic heart. Carbon Monoxide 95-97 heme oxygenase 1 Mus musculus 33-49 23087099-1 2013 AIMS: Haem oxygenase-1 (HO-1) is a haem-degrading enzyme that generates carbon monoxide, bilirubin, and iron ions. Carbon Monoxide 72-87 heme oxygenase 1 Mus musculus 6-28 24308158-1 2013 Heme oxygenase-1 [HO-1, also called heat shot protein 32 (HSP32)] can specifically metabolize heme to carbon monoxide, biliverdin, and ferrous iron and plays an important role in the processes of anti-inflammation, tissue protection, and antioxidative stress reaction. Carbon Monoxide 102-117 heme oxygenase 1 Mus musculus 0-16 24308158-1 2013 Heme oxygenase-1 [HO-1, also called heat shot protein 32 (HSP32)] can specifically metabolize heme to carbon monoxide, biliverdin, and ferrous iron and plays an important role in the processes of anti-inflammation, tissue protection, and antioxidative stress reaction. Carbon Monoxide 102-117 heme oxygenase 1 Mus musculus 18-22 24308158-1 2013 Heme oxygenase-1 [HO-1, also called heat shot protein 32 (HSP32)] can specifically metabolize heme to carbon monoxide, biliverdin, and ferrous iron and plays an important role in the processes of anti-inflammation, tissue protection, and antioxidative stress reaction. Carbon Monoxide 102-117 heme oxygenase 1 Mus musculus 36-56 24308158-1 2013 Heme oxygenase-1 [HO-1, also called heat shot protein 32 (HSP32)] can specifically metabolize heme to carbon monoxide, biliverdin, and ferrous iron and plays an important role in the processes of anti-inflammation, tissue protection, and antioxidative stress reaction. Carbon Monoxide 102-117 heme oxygenase 1 Mus musculus 58-63 23904222-3 2013 Heme oxygenase (HO)-1 cleaves heme to form biliverdin, carbon monoxide (CO), and iron (Fe(2+)), which is used with 5-ALA. Carbon Monoxide 55-70 heme oxygenase 1 Mus musculus 0-21 23904222-3 2013 Heme oxygenase (HO)-1 cleaves heme to form biliverdin, carbon monoxide (CO), and iron (Fe(2+)), which is used with 5-ALA. Carbon Monoxide 72-74 heme oxygenase 1 Mus musculus 0-21 23266559-1 2013 BACKGROUND & AIMS: Heme oxygenase-1 (HO-1) and its metabolic by-product, carbon monoxide (CO), protect against intestinal inflammation in experimental models of colitis, but little is known about their intestinal immune mechanisms. Carbon Monoxide 77-92 heme oxygenase 1 Mus musculus 23-39 23266559-1 2013 BACKGROUND & AIMS: Heme oxygenase-1 (HO-1) and its metabolic by-product, carbon monoxide (CO), protect against intestinal inflammation in experimental models of colitis, but little is known about their intestinal immune mechanisms. Carbon Monoxide 77-92 heme oxygenase 1 Mus musculus 41-45 23266559-1 2013 BACKGROUND & AIMS: Heme oxygenase-1 (HO-1) and its metabolic by-product, carbon monoxide (CO), protect against intestinal inflammation in experimental models of colitis, but little is known about their intestinal immune mechanisms. Carbon Monoxide 94-96 heme oxygenase 1 Mus musculus 23-39 23266559-1 2013 BACKGROUND & AIMS: Heme oxygenase-1 (HO-1) and its metabolic by-product, carbon monoxide (CO), protect against intestinal inflammation in experimental models of colitis, but little is known about their intestinal immune mechanisms. Carbon Monoxide 94-96 heme oxygenase 1 Mus musculus 41-45 24349609-1 2013 Endogenous carbon monoxide (CO) is produced by heme oxygenase-1 (HO)-1 which mediates the degradation of heme into CO, iron, and biliverdin. Carbon Monoxide 28-30 heme oxygenase 1 Mus musculus 47-63 24349609-1 2013 Endogenous carbon monoxide (CO) is produced by heme oxygenase-1 (HO)-1 which mediates the degradation of heme into CO, iron, and biliverdin. Carbon Monoxide 115-117 heme oxygenase 1 Mus musculus 47-63 22391129-0 2012 Sensing endoplasmic reticulum stress by protein kinase RNA-like endoplasmic reticulum kinase promotes adaptive mitochondrial DNA biogenesis and cell survival via heme oxygenase-1/carbon monoxide activity. Carbon Monoxide 179-194 heme oxygenase 1 Mus musculus 162-178 22670665-1 2012 Heme oxygenase-1 (HO-1) is an antioxidant, antiapoptotic and cytoprotective enzyme, catalysing the degradation of heme to carbon monoxide, biliverdin and ferrous iron. Carbon Monoxide 122-137 heme oxygenase 1 Mus musculus 0-16 22670665-1 2012 Heme oxygenase-1 (HO-1) is an antioxidant, antiapoptotic and cytoprotective enzyme, catalysing the degradation of heme to carbon monoxide, biliverdin and ferrous iron. Carbon Monoxide 122-137 heme oxygenase 1 Mus musculus 18-22 22495295-1 2012 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, producing equimolar amounts of carbon monoxide, iron, and biliverdin. Carbon Monoxide 109-124 heme oxygenase 1 Mus musculus 0-16 22495295-1 2012 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, producing equimolar amounts of carbon monoxide, iron, and biliverdin. Carbon Monoxide 109-124 heme oxygenase 1 Mus musculus 18-22 22391129-9 2012 Carbon monoxide (CO), an enzymatic by-product of HO-1 activity is responsible for the function of HO-1. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 49-53 22391129-9 2012 Carbon monoxide (CO), an enzymatic by-product of HO-1 activity is responsible for the function of HO-1. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 98-102 22391129-9 2012 Carbon monoxide (CO), an enzymatic by-product of HO-1 activity is responsible for the function of HO-1. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 49-53 22391129-9 2012 Carbon monoxide (CO), an enzymatic by-product of HO-1 activity is responsible for the function of HO-1. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 98-102 22348450-2 2012 Carbon monoxide (CO) has been found to mimic the protective effects of HO-1 activity, rescuing HO-1-deficient fetuses. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 71-75 22342655-2 2012 Its efficacy in the latter has been linked to increased expression and activity of heme oxygenase (HO)-1, suggesting that it facilitates heme degradation and subsequent release of cytoprotective biliverdin and carbon monoxide. Carbon Monoxide 210-225 heme oxygenase 1 Mus musculus 83-104 22145952-0 2012 Carbon monoxide, generated by heme oxygenase-1, mediates the enhanced permeability and retention effect in solid tumors. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 30-46 22456182-12 2012 In vivo treatment with hemin, an inducer of HO-1, blocked the vascular hypertrophy induced by Nox4 deletion in the angiotensin II infusion model and carbon monoxide, the product of HO-1, blocked the Nox4-deletion-induced apoptosis in LECs. Carbon Monoxide 149-164 heme oxygenase 1 Mus musculus 181-185 22450026-1 2012 BACKGROUND: The purpose of this study was to determine if inhaled carbon monoxide (CO) can ameliorate skeletal muscle injury, modulate endogenous heme oxygenase-1 expression, and improve indexes of tissue integrity and inflammation after hind limb ischemia reperfusion. Carbon Monoxide 66-81 heme oxygenase 1 Mus musculus 146-162 22450026-1 2012 BACKGROUND: The purpose of this study was to determine if inhaled carbon monoxide (CO) can ameliorate skeletal muscle injury, modulate endogenous heme oxygenase-1 expression, and improve indexes of tissue integrity and inflammation after hind limb ischemia reperfusion. Carbon Monoxide 83-85 heme oxygenase 1 Mus musculus 146-162 22348450-2 2012 Carbon monoxide (CO) has been found to mimic the protective effects of HO-1 activity, rescuing HO-1-deficient fetuses. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 95-99 22348450-2 2012 Carbon monoxide (CO) has been found to mimic the protective effects of HO-1 activity, rescuing HO-1-deficient fetuses. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 71-75 22348450-2 2012 Carbon monoxide (CO) has been found to mimic the protective effects of HO-1 activity, rescuing HO-1-deficient fetuses. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 95-99 22325451-1 2012 OBJECTIVES: Heme oxygenase-1 (HO-1) which degrades Heme to free iron, biliverdin and carbon monoxide (CO) plays an important role in inflammation. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 12-28 22325451-0 2012 Heme oxygenase-1 end-products carbon monoxide and biliverdin ameliorate murine collagen induced arthritis. Carbon Monoxide 30-45 heme oxygenase 1 Mus musculus 0-16 21827279-1 2012 AIMS: Heme oxygenase-1 (HMOX1) is a cytoprotective enzyme degrading heme to biliverdin, iron ions, and carbon monoxide, whose expression is induced in response to oxidative stress. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 6-22 21827279-1 2012 AIMS: Heme oxygenase-1 (HMOX1) is a cytoprotective enzyme degrading heme to biliverdin, iron ions, and carbon monoxide, whose expression is induced in response to oxidative stress. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 24-29 22325451-1 2012 OBJECTIVES: Heme oxygenase-1 (HO-1) which degrades Heme to free iron, biliverdin and carbon monoxide (CO) plays an important role in inflammation. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 30-34 22325451-1 2012 OBJECTIVES: Heme oxygenase-1 (HO-1) which degrades Heme to free iron, biliverdin and carbon monoxide (CO) plays an important role in inflammation. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 12-28 22325451-1 2012 OBJECTIVES: Heme oxygenase-1 (HO-1) which degrades Heme to free iron, biliverdin and carbon monoxide (CO) plays an important role in inflammation. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 30-34 21744344-0 2011 Haem oxygenase-1 dictates intrauterine fetal survival in mice via carbon monoxide. Carbon Monoxide 66-81 heme oxygenase 1 Mus musculus 0-16 22928017-1 2012 BACKGROUND: Carbon monoxide (CO) synthesized by heme oxygenase 1 (HO-1) exerts antinociceptive effects during inflammation but its role during neuropathic pain remains unknown. Carbon Monoxide 12-27 heme oxygenase 1 Mus musculus 48-64 22928017-1 2012 BACKGROUND: Carbon monoxide (CO) synthesized by heme oxygenase 1 (HO-1) exerts antinociceptive effects during inflammation but its role during neuropathic pain remains unknown. Carbon Monoxide 12-27 heme oxygenase 1 Mus musculus 66-70 22928017-1 2012 BACKGROUND: Carbon monoxide (CO) synthesized by heme oxygenase 1 (HO-1) exerts antinociceptive effects during inflammation but its role during neuropathic pain remains unknown. Carbon Monoxide 29-31 heme oxygenase 1 Mus musculus 48-64 22928017-1 2012 BACKGROUND: Carbon monoxide (CO) synthesized by heme oxygenase 1 (HO-1) exerts antinociceptive effects during inflammation but its role during neuropathic pain remains unknown. Carbon Monoxide 29-31 heme oxygenase 1 Mus musculus 66-70 22761690-8 2012 Further experiments demonstrated that carbon monoxide and bilirubin, the byproducts derived from heme degradation by HO-1, enhanced macrophage migration by increasing phosphorylation of p38 and FAK, respectively. Carbon Monoxide 38-53 heme oxygenase 1 Mus musculus 117-121 21744344-7 2011 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of haem catabolism by HO-1 that restores placentation and fetal growth. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 15-19 21744344-7 2011 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of haem catabolism by HO-1 that restores placentation and fetal growth. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 166-170 21744344-7 2011 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of haem catabolism by HO-1 that restores placentation and fetal growth. Carbon Monoxide 129-131 heme oxygenase 1 Mus musculus 15-19 21744344-7 2011 The protective HO-1 effects on placentation and fetal growth can be mimicked by the exogenous administration of carbon monoxide (CO), a product of haem catabolism by HO-1 that restores placentation and fetal growth. Carbon Monoxide 129-131 heme oxygenase 1 Mus musculus 166-170 21433045-2 2011 Carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) strongly influences cellular proliferation and both HO-1 and CO are accepted hepatoprotective molecules. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 34-50 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 13-28 heme oxygenase 1 Mus musculus 0-4 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 13-28 heme oxygenase 1 Mus musculus 66-70 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 13-28 heme oxygenase 1 Mus musculus 66-70 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 13-28 heme oxygenase 1 Mus musculus 66-70 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 30-32 heme oxygenase 1 Mus musculus 0-4 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 30-32 heme oxygenase 1 Mus musculus 66-70 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 30-32 heme oxygenase 1 Mus musculus 66-70 20716121-6 2011 HO-1 related carbon monoxide (CO) production was detected in NTg, HO-1 Tg and HO-1 Tg + SnPPIX treated groups, and a substantial increase in CO production was observed in the HO-1 Tg hearts subjected to ischemia/reperfusion. Carbon Monoxide 30-32 heme oxygenase 1 Mus musculus 66-70 21741361-1 2011 Heme oxygenase-1 (HO-1), which catalyzes the degradation of free heme to biliverdin, carbon monoxide (CO), and free iron (Fe(2+)), is up-regulated by several cellular stress and cell injuries, including inflammation, ischemia and hypoxia. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 0-16 21741361-1 2011 Heme oxygenase-1 (HO-1), which catalyzes the degradation of free heme to biliverdin, carbon monoxide (CO), and free iron (Fe(2+)), is up-regulated by several cellular stress and cell injuries, including inflammation, ischemia and hypoxia. Carbon Monoxide 85-100 heme oxygenase 1 Mus musculus 18-22 21741361-1 2011 Heme oxygenase-1 (HO-1), which catalyzes the degradation of free heme to biliverdin, carbon monoxide (CO), and free iron (Fe(2+)), is up-regulated by several cellular stress and cell injuries, including inflammation, ischemia and hypoxia. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 0-16 21741361-1 2011 Heme oxygenase-1 (HO-1), which catalyzes the degradation of free heme to biliverdin, carbon monoxide (CO), and free iron (Fe(2+)), is up-regulated by several cellular stress and cell injuries, including inflammation, ischemia and hypoxia. Carbon Monoxide 102-104 heme oxygenase 1 Mus musculus 18-22 21677132-1 2011 Heme oxygenase (HO)-1 is the inducible isoform of the rate-limiting enzyme of heme degradation and provides cytoprotection against oxidative stress by its products carbon monoxide and biliverdin. Carbon Monoxide 164-179 heme oxygenase 1 Mus musculus 0-21 21086163-1 2011 BACKGROUND: Endogenous carbon monoxide (CO) is one of the three products of heme degradation by heme oxygenase-1 (HO-1) and exerts novel anti-inflammatory and anti-apoptotic effects as a gaseous second messenger. Carbon Monoxide 23-38 heme oxygenase 1 Mus musculus 96-112 21086163-1 2011 BACKGROUND: Endogenous carbon monoxide (CO) is one of the three products of heme degradation by heme oxygenase-1 (HO-1) and exerts novel anti-inflammatory and anti-apoptotic effects as a gaseous second messenger. Carbon Monoxide 40-42 heme oxygenase 1 Mus musculus 96-112 21433045-2 2011 Carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) strongly influences cellular proliferation and both HO-1 and CO are accepted hepatoprotective molecules. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 110-121 21433045-2 2011 Carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) strongly influences cellular proliferation and both HO-1 and CO are accepted hepatoprotective molecules. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 34-50 21433045-2 2011 Carbon monoxide (CO) generated by heme oxygenase-1 (HO-1) strongly influences cellular proliferation and both HO-1 and CO are accepted hepatoprotective molecules. Carbon Monoxide 17-19 heme oxygenase 1 Mus musculus 110-121 22146483-3 2011 Carbon monoxide, an enzymatic product of heme oxygenase-1, exerts antiapoptotic effects at low concentration in vitro and in vivo. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 41-57 21518986-9 2011 Supernatants from hypoxic M2 macrophages promoted the proliferation of pulmonary artery smooth muscle cells, whereas treatment with carbon monoxide, a heme oxygenase-1 enzymatic product, abrogated this effect. Carbon Monoxide 132-147 heme oxygenase 1 Mus musculus 151-167 21345995-2 2011 The heme oxygenase system (HO-1 and HO-2) represents an intrinsic cytoprotective and anti-inflammatory pathway based on its ability to modulate leukocyte migration and to inhibit the expression of inflammatory cytokines and proteins by its products biliverdin/bilirubin and carbon monoxide. Carbon Monoxide 274-289 heme oxygenase 1 Mus musculus 27-31 20378827-3 2010 HO1 catalyzes the breakdown of heme into iron, biliverdin and, carbon monoxide (CO). Carbon Monoxide 63-78 heme oxygenase 1 Mus musculus 0-3 21842368-4 2011 HO-1 is a microsomal enzyme that catalyses the degradation of heme to iron, carbon monoxide and bilirubin. Carbon Monoxide 76-91 heme oxygenase 1 Mus musculus 0-4 21441618-1 2011 The aim of this study was to assess the interaction between the heme oxygenase-1/ biliverdin/carbon monoxide (HO-1/BVD/CO) and cyclooxygenase-2 (COX-2) pathways in the writhing test. Carbon Monoxide 93-108 heme oxygenase 1 Mus musculus 64-80 21441618-1 2011 The aim of this study was to assess the interaction between the heme oxygenase-1/ biliverdin/carbon monoxide (HO-1/BVD/CO) and cyclooxygenase-2 (COX-2) pathways in the writhing test. Carbon Monoxide 93-108 heme oxygenase 1 Mus musculus 110-121 21157922-1 2011 Heme oxygenase-1 (HO-1), which catalyzes the degradation of heme to iron, carbon monoxide, and biliverdin, performs a cytoprotective function. Carbon Monoxide 74-89 heme oxygenase 1 Mus musculus 0-16 21157922-1 2011 Heme oxygenase-1 (HO-1), which catalyzes the degradation of heme to iron, carbon monoxide, and biliverdin, performs a cytoprotective function. Carbon Monoxide 74-89 heme oxygenase 1 Mus musculus 18-22 20638948-1 2010 Our objective was to evaluate the role of heme-oxygenase 1 (HO-1)/biliverdin/CO pathway in gastric defense against ethanol-induced gastric damage in mice. Carbon Monoxide 77-79 heme oxygenase 1 Mus musculus 42-58 20638948-15 2010 Our results suggest that HO-1/biliverdin/CO pathway plays a protective role against ethanol-induced gastric damage through mechanisms that can be dependent (CO) or independent (biliverdin) of sGC activation. Carbon Monoxide 41-43 heme oxygenase 1 Mus musculus 25-29 20378827-3 2010 HO1 catalyzes the breakdown of heme into iron, biliverdin and, carbon monoxide (CO). Carbon Monoxide 80-82 heme oxygenase 1 Mus musculus 0-3 20378827-4 2010 The aim of this study was to determine whether inhalation of CO can mimic the protective effects of HO1. Carbon Monoxide 61-63 heme oxygenase 1 Mus musculus 100-103 19366789-1 2009 We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group box 1 (HMGB1) in RAW264.7 cells activated with lipopolysaccharide (LPS) in vitro and in LPS- or cecal ligation and puncture (CLP)-induced septic mice in vivo, so that HO-1 induction or CO improves survival of sepsis in rodents. Carbon Monoxide 64-79 heme oxygenase 1 Mus musculus 32-48 19426286-0 2009 After vascular injury, heme oxygenase-1/carbon monoxide enhances re-endothelialization via promoting mobilization of circulating endothelial progenitor cells. Carbon Monoxide 40-55 heme oxygenase 1 Mus musculus 23-39 19426286-8 2009 The effect of carbon monoxide (CO), a byproduct from heme degradation by HO-1, was assessed by exposing mice to 250 p.p.m. Carbon Monoxide 14-29 heme oxygenase 1 Mus musculus 73-77 19426286-8 2009 The effect of carbon monoxide (CO), a byproduct from heme degradation by HO-1, was assessed by exposing mice to 250 p.p.m. Carbon Monoxide 31-33 heme oxygenase 1 Mus musculus 73-77 19498004-0 2009 Carbon monoxide rescues heme oxygenase-1-deficient mice from arterial thrombosis in allogeneic aortic transplantation. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 24-40 19498004-1 2009 Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin. Carbon Monoxide 62-77 heme oxygenase 1 Mus musculus 0-16 19498004-1 2009 Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin. Carbon Monoxide 62-77 heme oxygenase 1 Mus musculus 18-22 19498004-1 2009 Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin. Carbon Monoxide 79-81 heme oxygenase 1 Mus musculus 0-16 19498004-1 2009 Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin. Carbon Monoxide 79-81 heme oxygenase 1 Mus musculus 18-22 20338478-5 2010 RESULTS: Both tumor cells and macrophages displayed a coherent picture of iNOS induction at transcriptional/translational levels and NO/nitrite production, whereas macrophages showed also co-induction of the inducible heme oxygenase-1, which is associated with carbon monoxide (CO) and bilirubin production. Carbon Monoxide 261-276 heme oxygenase 1 Mus musculus 218-234 20338478-5 2010 RESULTS: Both tumor cells and macrophages displayed a coherent picture of iNOS induction at transcriptional/translational levels and NO/nitrite production, whereas macrophages showed also co-induction of the inducible heme oxygenase-1, which is associated with carbon monoxide (CO) and bilirubin production. Carbon Monoxide 278-280 heme oxygenase 1 Mus musculus 218-234 19759334-1 2009 Induction of heme oxygenase-1 (HO-1) in the renal medulla increases carbon monoxide and bilirubin production and decreases ANG II-mediated superoxide production. Carbon Monoxide 68-83 heme oxygenase 1 Mus musculus 13-29 19759334-1 2009 Induction of heme oxygenase-1 (HO-1) in the renal medulla increases carbon monoxide and bilirubin production and decreases ANG II-mediated superoxide production. Carbon Monoxide 68-83 heme oxygenase 1 Mus musculus 31-35 19097991-9 2009 HO-1(-/-) mice treated with a carbon monoxide-releasing molecule or biliverdin showed a reduction in plasma HMGB1, which was associated with a marked improvement in survival. Carbon Monoxide 30-45 heme oxygenase 1 Mus musculus 0-4 19366789-1 2009 We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group box 1 (HMGB1) in RAW264.7 cells activated with lipopolysaccharide (LPS) in vitro and in LPS- or cecal ligation and puncture (CLP)-induced septic mice in vivo, so that HO-1 induction or CO improves survival of sepsis in rodents. Carbon Monoxide 64-79 heme oxygenase 1 Mus musculus 296-300 19366789-1 2009 We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group box 1 (HMGB1) in RAW264.7 cells activated with lipopolysaccharide (LPS) in vitro and in LPS- or cecal ligation and puncture (CLP)-induced septic mice in vivo, so that HO-1 induction or CO improves survival of sepsis in rodents. Carbon Monoxide 81-83 heme oxygenase 1 Mus musculus 32-48 19366789-1 2009 We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group box 1 (HMGB1) in RAW264.7 cells activated with lipopolysaccharide (LPS) in vitro and in LPS- or cecal ligation and puncture (CLP)-induced septic mice in vivo, so that HO-1 induction or CO improves survival of sepsis in rodents. Carbon Monoxide 81-83 heme oxygenase 1 Mus musculus 50-54 19366789-1 2009 We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group box 1 (HMGB1) in RAW264.7 cells activated with lipopolysaccharide (LPS) in vitro and in LPS- or cecal ligation and puncture (CLP)-induced septic mice in vivo, so that HO-1 induction or CO improves survival of sepsis in rodents. Carbon Monoxide 81-83 heme oxygenase 1 Mus musculus 296-300 19366789-1 2009 We examined our hypothesis that heme-oxygenase-1 (HO-1)-derived carbon monoxide (CO) inhibits the release of high-mobility group box 1 (HMGB1) in RAW264.7 cells activated with lipopolysaccharide (LPS) in vitro and in LPS- or cecal ligation and puncture (CLP)-induced septic mice in vivo, so that HO-1 induction or CO improves survival of sepsis in rodents. Carbon Monoxide 64-79 heme oxygenase 1 Mus musculus 50-54 19265160-0 2009 The heme oxygenase-1/carbon monoxide pathway suppresses TLR4 signaling by regulating the interaction of TLR4 with caveolin-1. Carbon Monoxide 21-36 heme oxygenase 1 Mus musculus 4-20 19168058-1 2009 Heme oxygenase-1 (HO) metabolizes heme to form the vasodilator carbon monoxide and antioxidant biliverdin. Carbon Monoxide 63-78 heme oxygenase 1 Mus musculus 0-16 19265160-4 2009 Cav-1 was required for the anti-inflammatory effects of carbon monoxide (CO), a product of heme oxygenase-1 (HO-1) activity. Carbon Monoxide 56-71 heme oxygenase 1 Mus musculus 91-107 19265160-4 2009 Cav-1 was required for the anti-inflammatory effects of carbon monoxide (CO), a product of heme oxygenase-1 (HO-1) activity. Carbon Monoxide 56-71 heme oxygenase 1 Mus musculus 109-113 19265160-4 2009 Cav-1 was required for the anti-inflammatory effects of carbon monoxide (CO), a product of heme oxygenase-1 (HO-1) activity. Carbon Monoxide 73-75 heme oxygenase 1 Mus musculus 91-107 19265160-4 2009 Cav-1 was required for the anti-inflammatory effects of carbon monoxide (CO), a product of heme oxygenase-1 (HO-1) activity. Carbon Monoxide 73-75 heme oxygenase 1 Mus musculus 109-113 19201840-1 2009 Heme oxygenase-1 (HO-1) exerts its functions via the catabolism of heme into carbon monoxide (CO), Fe(2+), and biliverdin, as well as by depletion of free heme. Carbon Monoxide 77-92 heme oxygenase 1 Mus musculus 0-16 19282658-3 2009 HO-1 degrades heme into carbon monoxide (CO), biliverdin, and iron. Carbon Monoxide 24-39 heme oxygenase 1 Mus musculus 0-4 19282658-3 2009 HO-1 degrades heme into carbon monoxide (CO), biliverdin, and iron. Carbon Monoxide 41-43 heme oxygenase 1 Mus musculus 0-4 19201840-1 2009 Heme oxygenase-1 (HO-1) exerts its functions via the catabolism of heme into carbon monoxide (CO), Fe(2+), and biliverdin, as well as by depletion of free heme. Carbon Monoxide 77-92 heme oxygenase 1 Mus musculus 18-22 19201840-1 2009 Heme oxygenase-1 (HO-1) exerts its functions via the catabolism of heme into carbon monoxide (CO), Fe(2+), and biliverdin, as well as by depletion of free heme. Carbon Monoxide 94-97 heme oxygenase 1 Mus musculus 0-16 19201840-1 2009 Heme oxygenase-1 (HO-1) exerts its functions via the catabolism of heme into carbon monoxide (CO), Fe(2+), and biliverdin, as well as by depletion of free heme. Carbon Monoxide 94-97 heme oxygenase 1 Mus musculus 18-22 18845810-4 2008 Mechanistically, in cardiomyocytes, endogenous carbon monoxide (CO) generated by HO-1 overexpression stimulates superoxide dismutase-2 upregulation and mitochondrial H(2)O(2) production, which activates Akt/PKB. Carbon Monoxide 47-62 heme oxygenase 1 Mus musculus 81-85 19239176-3 2009 Heme oxygenase-1 (HO-1), a stress inducible enzyme, degrades heme to biliverdin, free iron and carbon monoxide (CO), which are involved in the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 95-110 heme oxygenase 1 Mus musculus 0-16 19239176-3 2009 Heme oxygenase-1 (HO-1), a stress inducible enzyme, degrades heme to biliverdin, free iron and carbon monoxide (CO), which are involved in the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 95-110 heme oxygenase 1 Mus musculus 18-22 19239176-3 2009 Heme oxygenase-1 (HO-1), a stress inducible enzyme, degrades heme to biliverdin, free iron and carbon monoxide (CO), which are involved in the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 95-110 heme oxygenase 1 Mus musculus 188-192 19239176-3 2009 Heme oxygenase-1 (HO-1), a stress inducible enzyme, degrades heme to biliverdin, free iron and carbon monoxide (CO), which are involved in the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 112-114 heme oxygenase 1 Mus musculus 0-16 19239176-3 2009 Heme oxygenase-1 (HO-1), a stress inducible enzyme, degrades heme to biliverdin, free iron and carbon monoxide (CO), which are involved in the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 112-114 heme oxygenase 1 Mus musculus 18-22 19239176-3 2009 Heme oxygenase-1 (HO-1), a stress inducible enzyme, degrades heme to biliverdin, free iron and carbon monoxide (CO), which are involved in the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 112-114 heme oxygenase 1 Mus musculus 188-192 19119918-1 2009 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades heme to iron, carbon monoxide (CO), and biliverdin, the latter two of which are thought to mediate the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 88-103 heme oxygenase 1 Mus musculus 0-21 19119918-1 2009 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades heme to iron, carbon monoxide (CO), and biliverdin, the latter two of which are thought to mediate the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 88-103 heme oxygenase 1 Mus musculus 222-226 19119918-1 2009 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades heme to iron, carbon monoxide (CO), and biliverdin, the latter two of which are thought to mediate the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 105-107 heme oxygenase 1 Mus musculus 0-21 19119918-1 2009 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades heme to iron, carbon monoxide (CO), and biliverdin, the latter two of which are thought to mediate the anti-inflammatory and antioxidant actions of HO-1. Carbon Monoxide 105-107 heme oxygenase 1 Mus musculus 222-226 18845810-4 2008 Mechanistically, in cardiomyocytes, endogenous carbon monoxide (CO) generated by HO-1 overexpression stimulates superoxide dismutase-2 upregulation and mitochondrial H(2)O(2) production, which activates Akt/PKB. Carbon Monoxide 64-66 heme oxygenase 1 Mus musculus 81-85 18094356-1 2008 Heme oxygenase (HMOX) regulates vascular tone and blood pressure through the production of carbon monoxide (CO), a vasodilator derived from the heme degradation pathway. Carbon Monoxide 91-106 heme oxygenase 1 Mus musculus 0-14 18474360-3 2008 HO-1 overexpression in the liver leads to a proportional increase in parasite liver load, and treatment of mice with carbon monoxide and with biliverdin, each an enzymatic product of HO-1, also increases parasite liver load. Carbon Monoxide 117-132 heme oxygenase 1 Mus musculus 183-187 18094356-1 2008 Heme oxygenase (HMOX) regulates vascular tone and blood pressure through the production of carbon monoxide (CO), a vasodilator derived from the heme degradation pathway. Carbon Monoxide 91-106 heme oxygenase 1 Mus musculus 16-20 18094356-1 2008 Heme oxygenase (HMOX) regulates vascular tone and blood pressure through the production of carbon monoxide (CO), a vasodilator derived from the heme degradation pathway. Carbon Monoxide 108-110 heme oxygenase 1 Mus musculus 0-14 18094356-1 2008 Heme oxygenase (HMOX) regulates vascular tone and blood pressure through the production of carbon monoxide (CO), a vasodilator derived from the heme degradation pathway. Carbon Monoxide 108-110 heme oxygenase 1 Mus musculus 16-20 18025230-1 2007 Heme oxygenase-1 (HO-1; encoded by the Hmox1 gene) catalyzes the degradation of free heme into biliverdin, via a reaction that releases iron (Fe) and carbon monoxide. Carbon Monoxide 150-165 heme oxygenase 1 Mus musculus 0-22 18060048-0 2008 Heme oxygenase-1-derived carbon monoxide enhances the host defense response to microbial sepsis in mice. Carbon Monoxide 25-40 heme oxygenase 1 Mus musculus 0-16 18554543-0 2008 Interactive relations between nitric oxide (NO) and carbon monoxide (CO): heme oxygenase-1/CO pathway is a key modulator in NO-mediated antiapoptosis and anti-inflammation. Carbon Monoxide 52-67 heme oxygenase 1 Mus musculus 74-90 18554543-0 2008 Interactive relations between nitric oxide (NO) and carbon monoxide (CO): heme oxygenase-1/CO pathway is a key modulator in NO-mediated antiapoptosis and anti-inflammation. Carbon Monoxide 69-71 heme oxygenase 1 Mus musculus 74-90 18154739-1 2008 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme and forms antioxidant bile pigments as well as the signaling molecule carbon monoxide. Carbon Monoxide 128-143 heme oxygenase 1 Mus musculus 0-16 18154739-1 2008 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme and forms antioxidant bile pigments as well as the signaling molecule carbon monoxide. Carbon Monoxide 128-143 heme oxygenase 1 Mus musculus 18-22 18242889-1 2008 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, carbon monoxide and iron. Carbon Monoxide 127-142 heme oxygenase 1 Mus musculus 0-16 18242889-1 2008 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, carbon monoxide and iron. Carbon Monoxide 127-142 heme oxygenase 1 Mus musculus 18-22 18025230-1 2007 Heme oxygenase-1 (HO-1; encoded by the Hmox1 gene) catalyzes the degradation of free heme into biliverdin, via a reaction that releases iron (Fe) and carbon monoxide. Carbon Monoxide 150-165 heme oxygenase 1 Mus musculus 39-44 17885218-0 2007 Heme oxygenase-1 deficiency accelerates formation of arterial thrombosis through oxidative damage to the endothelium, which is rescued by inhaled carbon monoxide. Carbon Monoxide 146-161 heme oxygenase 1 Mus musculus 0-16 17440721-2 2007 The UVA protection was mediated via the UVA induction of the stress protein heme oxygenase-1, and its enzymatic product carbon monoxide (CO). Carbon Monoxide 120-135 heme oxygenase 1 Mus musculus 76-92 17440721-2 2007 The UVA protection was mediated via the UVA induction of the stress protein heme oxygenase-1, and its enzymatic product carbon monoxide (CO). Carbon Monoxide 137-139 heme oxygenase 1 Mus musculus 76-92 17885218-1 2007 Heme oxygenase (HO)-1 (encoded by Hmox1) catalyzes the oxidative degradation of heme to biliverdin and carbon monoxide. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 0-21 17885218-1 2007 Heme oxygenase (HO)-1 (encoded by Hmox1) catalyzes the oxidative degradation of heme to biliverdin and carbon monoxide. Carbon Monoxide 103-118 heme oxygenase 1 Mus musculus 34-39 17885218-9 2007 Fourth, inhaled carbon monoxide and biliverdin administration rescued the prothrombotic phenotype in Hmox1-/- mice. Carbon Monoxide 16-31 heme oxygenase 1 Mus musculus 101-106 17632083-8 2007 Additional experiments revealed the involvement of carbon monoxide (CO) and iron, products of HO-1-mediated heme degradation, in the cytoprotective effect of LPS. Carbon Monoxide 51-66 heme oxygenase 1 Mus musculus 94-98 17560646-1 2007 Haem oxygenase-1 (HO-1) is an inducible enzyme that catalyses the rate-limiting step in the degradation of haem to biliverdin, carbon monoxide and iron. Carbon Monoxide 127-142 heme oxygenase 1 Mus musculus 0-16 17560646-1 2007 Haem oxygenase-1 (HO-1) is an inducible enzyme that catalyses the rate-limiting step in the degradation of haem to biliverdin, carbon monoxide and iron. Carbon Monoxide 127-142 heme oxygenase 1 Mus musculus 18-22 17495224-1 2007 Heme oxygenase (HO-1) is the rate-limiting enzyme in the catabolism of heme, which leads to the generation of biliverdin, iron, and carbon monoxide. Carbon Monoxide 132-147 heme oxygenase 1 Mus musculus 16-20 17496899-6 2007 Pharmacological induction of HO-1 and exposure to the end-product of HO-1 activity, carbon monoxide (CO), reduced ECM incidence in C57BL/6 mice to 10% and 0%, respectively. Carbon Monoxide 84-99 heme oxygenase 1 Mus musculus 69-73 17496899-6 2007 Pharmacological induction of HO-1 and exposure to the end-product of HO-1 activity, carbon monoxide (CO), reduced ECM incidence in C57BL/6 mice to 10% and 0%, respectively. Carbon Monoxide 101-103 heme oxygenase 1 Mus musculus 69-73 16783602-0 2006 Carbon monoxide-induced early thrombolysis contributes to heme oxygenase-1-mediated inhibition of neointimal growth after vascular injury in hypercholesterolemic mice. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 58-74 17242398-2 2007 The products of heme catabolism by HO-1 are ferrous iron, biliverdin (subsequently converted to bilirubin), and carbon monoxide. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 35-39 17389265-3 2007 Heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO) exert protective effects against oxidative stimuli. Carbon Monoxide 43-58 heme oxygenase 1 Mus musculus 0-16 17389265-3 2007 Heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO) exert protective effects against oxidative stimuli. Carbon Monoxide 43-58 heme oxygenase 1 Mus musculus 18-22 17389265-3 2007 Heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO) exert protective effects against oxidative stimuli. Carbon Monoxide 60-62 heme oxygenase 1 Mus musculus 0-16 17389265-3 2007 Heme oxygenase-1 (HO-1) and its metabolite carbon monoxide (CO) exert protective effects against oxidative stimuli. Carbon Monoxide 60-62 heme oxygenase 1 Mus musculus 18-22 16943204-3 2006 We found that overexpression of HO-1 and [Ru(CO)(3)Cl(2)](2), a carbon monoxide (CO)-releasing compound, increased not only ERK5 kinase activity, but also its transcriptional activity measured by luciferase assay with the transfection of the Gal4-ERK5 reporter gene. Carbon Monoxide 64-79 heme oxygenase 1 Mus musculus 32-36 17442976-5 2007 HO-1 overexpression or exposure to carbon monoxide (CO), a product of HO-1 enzymatic activity, resulted in augmented A2aR mRNA and protein levels in RAW264.7 cells and primary macrophages. Carbon Monoxide 35-50 heme oxygenase 1 Mus musculus 70-74 17442976-5 2007 HO-1 overexpression or exposure to carbon monoxide (CO), a product of HO-1 enzymatic activity, resulted in augmented A2aR mRNA and protein levels in RAW264.7 cells and primary macrophages. Carbon Monoxide 52-54 heme oxygenase 1 Mus musculus 70-74 17256058-1 2007 Heme oxygenase-1 (HO-1, encoded by HMOX1) dampens inflammatory reactions via the catabolism of heme into CO, Fe, and biliverdin. Carbon Monoxide 105-107 heme oxygenase 1 Mus musculus 0-22 17256058-1 2007 Heme oxygenase-1 (HO-1, encoded by HMOX1) dampens inflammatory reactions via the catabolism of heme into CO, Fe, and biliverdin. Carbon Monoxide 105-107 heme oxygenase 1 Mus musculus 35-40 17135272-10 2007 We also show that carbon monoxide promoted an interaction of heme oxygenase-1 with Bax. Carbon Monoxide 18-33 heme oxygenase 1 Mus musculus 61-77 17169158-2 2006 The stress protein heme oxygenase-1 (HO-1) catalyzes heme degradation producing biliverdin, iron and CO. Carbon Monoxide 101-103 heme oxygenase 1 Mus musculus 19-35 16971418-8 2006 However, HO-1 and its reaction product carbon monoxide (CO) lose their protective effects in the presence of STAT3 siRNA in MLEC or in endothelial-specific, STAT3-deficient mice. Carbon Monoxide 39-54 heme oxygenase 1 Mus musculus 9-13 16971418-8 2006 However, HO-1 and its reaction product carbon monoxide (CO) lose their protective effects in the presence of STAT3 siRNA in MLEC or in endothelial-specific, STAT3-deficient mice. Carbon Monoxide 56-58 heme oxygenase 1 Mus musculus 9-13 16625420-0 2006 Carbon monoxide and bilirubin from heme oxygenase-1 suppresses reactive oxygen species generation and plasminogen activator inhibitor-1 induction. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 35-51 16625420-8 2006 Interestingly, these increases in HO-1 deficient cells were significantly lowered by BR, CO, GSH and DPI while DFO had little effect. Carbon Monoxide 89-91 heme oxygenase 1 Mus musculus 34-38 16783602-6 2006 The thrombolytic effect was also observed by exposing animals with existing arterial thrombosis to carbon monoxide (CO) (250 ppm, 2 h), a byproduct derived from heme degradation by HO-1. Carbon Monoxide 99-114 heme oxygenase 1 Mus musculus 181-185 16783602-6 2006 The thrombolytic effect was also observed by exposing animals with existing arterial thrombosis to carbon monoxide (CO) (250 ppm, 2 h), a byproduct derived from heme degradation by HO-1. Carbon Monoxide 116-118 heme oxygenase 1 Mus musculus 181-185 16824198-2 2006 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades pro-oxidant heme to carbon monoxide (CO) and biliverdin/bilirubin, which are thought to mediate anti-inflammatory and anti-oxidant actions of HO-1. Carbon Monoxide 94-109 heme oxygenase 1 Mus musculus 0-21 16824198-2 2006 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades pro-oxidant heme to carbon monoxide (CO) and biliverdin/bilirubin, which are thought to mediate anti-inflammatory and anti-oxidant actions of HO-1. Carbon Monoxide 94-109 heme oxygenase 1 Mus musculus 216-220 16824198-2 2006 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades pro-oxidant heme to carbon monoxide (CO) and biliverdin/bilirubin, which are thought to mediate anti-inflammatory and anti-oxidant actions of HO-1. Carbon Monoxide 111-113 heme oxygenase 1 Mus musculus 0-21 16824198-2 2006 Heme oxygenase (HO)-1 is an inducible cytoprotective enzyme that degrades pro-oxidant heme to carbon monoxide (CO) and biliverdin/bilirubin, which are thought to mediate anti-inflammatory and anti-oxidant actions of HO-1. Carbon Monoxide 111-113 heme oxygenase 1 Mus musculus 216-220 16563347-1 2006 Heme oxygenase-1 (HO-1) plays a central role in antioxidant and anti-inflammatory actions, which may be mediated through its formation of biliverdin/bilirubin and carbon monoxide. Carbon Monoxide 163-178 heme oxygenase 1 Mus musculus 0-16 16563347-1 2006 Heme oxygenase-1 (HO-1) plays a central role in antioxidant and anti-inflammatory actions, which may be mediated through its formation of biliverdin/bilirubin and carbon monoxide. Carbon Monoxide 163-178 heme oxygenase 1 Mus musculus 18-22 16417236-5 2006 We previously reported that UVA photoimmunoprotection depends on the induction of cutaneous heme oxygenase-1, particularly its enzymatic product, carbon monoxide (CO). Carbon Monoxide 146-161 heme oxygenase 1 Mus musculus 92-108 16242122-0 2006 Carbon monoxide and nitric oxide protect against tumor necrosis factor-alpha-induced apoptosis in osteoblasts: HO-1 is necessary to mediate the protection. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 111-115 16242122-7 2006 RESULTS: The increased expression of HO-1 is required for the protective effect of NO and a single treatment of CO can increase the expression of HO-1, and this is also important for the protective effect of CO in MC3T3E1 osteoblasts. Carbon Monoxide 112-114 heme oxygenase 1 Mus musculus 37-41 16242122-7 2006 RESULTS: The increased expression of HO-1 is required for the protective effect of NO and a single treatment of CO can increase the expression of HO-1, and this is also important for the protective effect of CO in MC3T3E1 osteoblasts. Carbon Monoxide 112-114 heme oxygenase 1 Mus musculus 146-150 16242122-12 2006 CONCLUSIONS: There is a need for HO-1 expression to mediate the protection provided by exogenous CO or NO in osteoblasts. Carbon Monoxide 0-2 heme oxygenase 1 Mus musculus 33-37 16417236-5 2006 We previously reported that UVA photoimmunoprotection depends on the induction of cutaneous heme oxygenase-1, particularly its enzymatic product, carbon monoxide (CO). Carbon Monoxide 163-165 heme oxygenase 1 Mus musculus 92-108 16137650-1 2005 Heme oxygenase cleaves heme to form biliverdin, carbon monoxide (CO), and iron, and consists of two structurally related isozymes, HO-1 and HO-2. Carbon Monoxide 48-63 heme oxygenase 1 Mus musculus 131-144 16365149-0 2005 Carbon monoxide ameliorates chronic murine colitis through a heme oxygenase 1-dependent pathway. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 61-77 16365149-1 2005 Heme oxygenase (HO)-1 and its metabolic product carbon monoxide (CO) play regulatory roles in acute inflammatory states. Carbon Monoxide 48-63 heme oxygenase 1 Mus musculus 0-21 16365149-1 2005 Heme oxygenase (HO)-1 and its metabolic product carbon monoxide (CO) play regulatory roles in acute inflammatory states. Carbon Monoxide 65-67 heme oxygenase 1 Mus musculus 0-21 16327497-13 2005 The protection is caused by the increased arteriolar blood flow due to significant arteriolar dilation, which is mediated through the carbon monoxide-associated vasoactive properties of HSP-32. Carbon Monoxide 134-149 heme oxygenase 1 Mus musculus 186-192 16137650-1 2005 Heme oxygenase cleaves heme to form biliverdin, carbon monoxide (CO), and iron, and consists of two structurally related isozymes, HO-1 and HO-2. Carbon Monoxide 65-67 heme oxygenase 1 Mus musculus 131-144 15803024-2 2005 The products of heme catalysis, biliverdin/bilirubin, carbon monoxide (CO), and iron (that induces apoferritin) mediate the beneficial effects of HO-1. Carbon Monoxide 54-69 heme oxygenase 1 Mus musculus 146-150 15880142-1 2005 The enzyme heme oxygenase-1 (HO-1) is a cytoprotective and anti-inflammatory protein that degrades heme to produce biliverdin/bilirubin, ferrous iron and carbon monoxide (CO). Carbon Monoxide 154-169 heme oxygenase 1 Mus musculus 11-27 15880142-1 2005 The enzyme heme oxygenase-1 (HO-1) is a cytoprotective and anti-inflammatory protein that degrades heme to produce biliverdin/bilirubin, ferrous iron and carbon monoxide (CO). Carbon Monoxide 154-169 heme oxygenase 1 Mus musculus 29-33 15880142-1 2005 The enzyme heme oxygenase-1 (HO-1) is a cytoprotective and anti-inflammatory protein that degrades heme to produce biliverdin/bilirubin, ferrous iron and carbon monoxide (CO). Carbon Monoxide 171-173 heme oxygenase 1 Mus musculus 11-27 15880142-1 2005 The enzyme heme oxygenase-1 (HO-1) is a cytoprotective and anti-inflammatory protein that degrades heme to produce biliverdin/bilirubin, ferrous iron and carbon monoxide (CO). Carbon Monoxide 171-173 heme oxygenase 1 Mus musculus 29-33 16181103-1 2005 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 (CO), and induction of heme oxygenase-1 (HO-1) is potentially associated with cellular protection, especially against oxidative insults. Carbon Monoxide 157-172 heme oxygenase 1 Mus musculus 196-212 16389572-1 2005 OBJECTIVES: Heme oxygenase-1 (HO-1) is an enzyme that degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 100-115 heme oxygenase 1 Mus musculus 12-28 16389572-1 2005 OBJECTIVES: Heme oxygenase-1 (HO-1) is an enzyme that degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 100-115 heme oxygenase 1 Mus musculus 30-34 16389572-1 2005 OBJECTIVES: Heme oxygenase-1 (HO-1) is an enzyme that degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 117-119 heme oxygenase 1 Mus musculus 12-28 16389572-1 2005 OBJECTIVES: Heme oxygenase-1 (HO-1) is an enzyme that degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 117-119 heme oxygenase 1 Mus musculus 30-34 15803024-2 2005 The products of heme catalysis, biliverdin/bilirubin, carbon monoxide (CO), and iron (that induces apoferritin) mediate the beneficial effects of HO-1. Carbon Monoxide 71-73 heme oxygenase 1 Mus musculus 146-150 15640283-1 2005 Heme oxygenase-1 (HO-1), which degrades heme into three products (carbon monoxide, free iron, and biliverdin), plays a protective role in many models of disease via its anti-inflammatory, anti-apoptotic, and anti-proliferative actions. Carbon Monoxide 66-81 heme oxygenase 1 Mus musculus 0-16 15640283-1 2005 Heme oxygenase-1 (HO-1), which degrades heme into three products (carbon monoxide, free iron, and biliverdin), plays a protective role in many models of disease via its anti-inflammatory, anti-apoptotic, and anti-proliferative actions. Carbon Monoxide 66-81 heme oxygenase 1 Mus musculus 18-22 15737207-2 2005 In skin, UVA photoimmunoprotection is mediated by the inducible antioxidant stress enzyme, heme oxygenase-1 (HO-1), which degrades heme into carbon monoxide (CO), iron, and biliverdin (reduced to bilirubin), and is important for cell survival under conditions of oxidative stress. Carbon Monoxide 141-156 heme oxygenase 1 Mus musculus 91-107 15812227-1 2005 Heme oxygenase 1 (HO-1) is an inducible enzyme that catalyzes heme to generate bilirubin, ferritin, and carbon monoxide. Carbon Monoxide 104-119 heme oxygenase 1 Mus musculus 0-16 15812227-1 2005 Heme oxygenase 1 (HO-1) is an inducible enzyme that catalyzes heme to generate bilirubin, ferritin, and carbon monoxide. Carbon Monoxide 104-119 heme oxygenase 1 Mus musculus 18-22 15737207-2 2005 In skin, UVA photoimmunoprotection is mediated by the inducible antioxidant stress enzyme, heme oxygenase-1 (HO-1), which degrades heme into carbon monoxide (CO), iron, and biliverdin (reduced to bilirubin), and is important for cell survival under conditions of oxidative stress. Carbon Monoxide 158-160 heme oxygenase 1 Mus musculus 91-107 12133584-3 2002 In the present study, we examined the effect of PGG on the expression of neuronal heme oxygenase-1 (HO-1), an inducible stress protein that degrades heme to the neuroactive molecule, carbon monoxide and the anti-oxidant, biliverdin. Carbon Monoxide 183-198 heme oxygenase 1 Mus musculus 82-98 14739596-1 2004 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide (CO), and free iron. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 0-16 14739596-1 2004 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide (CO), and free iron. Carbon Monoxide 112-127 heme oxygenase 1 Mus musculus 18-22 14739596-1 2004 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide (CO), and free iron. Carbon Monoxide 129-131 heme oxygenase 1 Mus musculus 0-16 14739596-1 2004 Heme oxygenase-1 (HO-1) is an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide (CO), and free iron. Carbon Monoxide 129-131 heme oxygenase 1 Mus musculus 18-22 12918124-1 2003 AIM: Heme oxygenase (HO)-1 catalyzes the conversion of heme to biliverdin, iron and carbon monoxide. Carbon Monoxide 84-99 heme oxygenase 1 Mus musculus 5-26 12706494-8 2003 Additional experiments revealed the involvement of carbon monoxide in the cytoprotective effect of SNP/HO-1 in L929 cells. Carbon Monoxide 51-66 heme oxygenase 1 Mus musculus 103-107 12709566-2 2003 Although the mechanisms involved in this cytoprotection are largely unknown, HO-1 and its enzymatic products, carbon monoxide and bilirubin, downregulate the inflammatory response by either attenuating the expression of adhesion molecules and thus inhibiting leukocyte recruitment or by repressing the induction of cytokines and chemokines. Carbon Monoxide 110-125 heme oxygenase 1 Mus musculus 77-81 12449100-1 2002 Heme oxygenase 1 (HO-1) is an inducible enzyme that catalyzes heme to generate bilirubin, ferritin, and carbon monoxide. Carbon Monoxide 104-119 heme oxygenase 1 Mus musculus 0-16 12449100-1 2002 Heme oxygenase 1 (HO-1) is an inducible enzyme that catalyzes heme to generate bilirubin, ferritin, and carbon monoxide. Carbon Monoxide 104-119 heme oxygenase 1 Mus musculus 18-22 12124217-1 2002 Heme oxygenase (HO)-1 converts heme to bilirubin, carbon monoxide, and iron. Carbon Monoxide 50-65 heme oxygenase 1 Mus musculus 0-21 15217802-11 2004 Thus our data indicate that the delay-induced protection from tissue necrosis is mediated by HO-1, predominantly through its carbon monoxide-associated action of adequately maintaining nutritive capillary perfusion. Carbon Monoxide 125-140 heme oxygenase 1 Mus musculus 93-97 15240108-1 2004 Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron, and CO. Carbon Monoxide 65-67 heme oxygenase 1 Mus musculus 0-16 15240108-1 2004 Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron, and CO. Carbon Monoxide 65-67 heme oxygenase 1 Mus musculus 18-22 14657222-0 2003 Carbon monoxide protects against liver failure through nitric oxide-induced heme oxygenase 1. Carbon Monoxide 0-15 heme oxygenase 1 Mus musculus 76-92 12958158-0 2003 Heme oxygenase-1-related carbon monoxide production and ventricular fibrillation in isolated ischemic/reperfused mouse myocardium. Carbon Monoxide 25-40 heme oxygenase 1 Mus musculus 0-16 12958158-1 2003 Heme oxygenase-1 (HO-1)-dependent carbon monoxide (CO) production related to reperfusion-induced ventricular fibrillation (VF) was studied in HO-1 wild-type (+/+), heterozygous (+/-), and homozygous (-/-) isolated ischemic/reperfused mouse heart. Carbon Monoxide 34-49 heme oxygenase 1 Mus musculus 0-16 12958158-1 2003 Heme oxygenase-1 (HO-1)-dependent carbon monoxide (CO) production related to reperfusion-induced ventricular fibrillation (VF) was studied in HO-1 wild-type (+/+), heterozygous (+/-), and homozygous (-/-) isolated ischemic/reperfused mouse heart. Carbon Monoxide 34-49 heme oxygenase 1 Mus musculus 18-22 12958158-1 2003 Heme oxygenase-1 (HO-1)-dependent carbon monoxide (CO) production related to reperfusion-induced ventricular fibrillation (VF) was studied in HO-1 wild-type (+/+), heterozygous (+/-), and homozygous (-/-) isolated ischemic/reperfused mouse heart. Carbon Monoxide 51-53 heme oxygenase 1 Mus musculus 0-16 12958158-1 2003 Heme oxygenase-1 (HO-1)-dependent carbon monoxide (CO) production related to reperfusion-induced ventricular fibrillation (VF) was studied in HO-1 wild-type (+/+), heterozygous (+/-), and homozygous (-/-) isolated ischemic/reperfused mouse heart. Carbon Monoxide 51-53 heme oxygenase 1 Mus musculus 18-22 14512878-0 2003 Heme oxygenase-1 and its reaction product, carbon monoxide, prevent inflammation-related apoptotic liver damage in mice. Carbon Monoxide 43-58 heme oxygenase 1 Mus musculus 0-16 14512878-1 2003 Heme oxygenase-1 (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 injury and rejection. Carbon Monoxide 79-94 heme oxygenase 1 Mus musculus 0-16 14512878-1 2003 Heme oxygenase-1 (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 injury and rejection. Carbon Monoxide 79-94 heme oxygenase 1 Mus musculus 18-22 14512878-1 2003 Heme oxygenase-1 (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 injury and rejection. Carbon Monoxide 96-98 heme oxygenase 1 Mus musculus 0-16 14512878-1 2003 Heme oxygenase-1 (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 injury and rejection. Carbon Monoxide 96-98 heme oxygenase 1 Mus musculus 18-22 12857751-5 2003 The same effect was seen with increased endogenous CO production through overexpression of heme oxygenase-1. Carbon Monoxide 51-53 heme oxygenase 1 Mus musculus 91-107 12593855-4 2003 Heme oxygenase 1 (HO-1) is an enzyme which degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 89-104 heme oxygenase 1 Mus musculus 0-16 12593855-4 2003 Heme oxygenase 1 (HO-1) is an enzyme which degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 89-104 heme oxygenase 1 Mus musculus 18-22 12593855-4 2003 Heme oxygenase 1 (HO-1) is an enzyme which degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 106-108 heme oxygenase 1 Mus musculus 0-16 12593855-4 2003 Heme oxygenase 1 (HO-1) is an enzyme which degrades heme into biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 106-108 heme oxygenase 1 Mus musculus 18-22 12673348-1 2003 Heme oxygenase-1 (HO-1), an inducible enzyme degrading heme to biliverdin, iron and carbon monoxide, is involved in regulation of inflammation and angiogenesis. Carbon Monoxide 84-99 heme oxygenase 1 Mus musculus 0-16 12673348-1 2003 Heme oxygenase-1 (HO-1), an inducible enzyme degrading heme to biliverdin, iron and carbon monoxide, is involved in regulation of inflammation and angiogenesis. Carbon Monoxide 84-99 heme oxygenase 1 Mus musculus 18-22