PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8679227-8 1996 Since the identification of HO-1 in 1968, many of the studies involving this enzyme were understandably focused on the regulation and function of HO-1 in heme metabolism. Heme 154-158 heme oxygenase 1 Homo sapiens 28-32 8679227-8 1996 Since the identification of HO-1 in 1968, many of the studies involving this enzyme were understandably focused on the regulation and function of HO-1 in heme metabolism. Heme 154-158 heme oxygenase 1 Homo sapiens 146-150 8679227-9 1996 This emphasis is self-evident as HO-1 catalyzes the first and rate-limiting step in heme degradation. Heme 84-88 heme oxygenase 1 Homo sapiens 33-37 8679227-10 1996 Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins. Heme 128-132 heme oxygenase 1 Homo sapiens 86-90 8679227-10 1996 Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins. Heme 162-166 heme oxygenase 1 Homo sapiens 86-90 8679227-10 1996 Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins. Prostaglandins 249-263 heme oxygenase 1 Homo sapiens 86-90 8679227-11 1996 The chemical diversity of HO-1 inducers led to the speculation that HO-1, besides its role in heme degradation, may also play a vital function in maintaining cellular homeostasis. Heme 94-98 heme oxygenase 1 Homo sapiens 26-30 8679227-11 1996 The chemical diversity of HO-1 inducers led to the speculation that HO-1, besides its role in heme degradation, may also play a vital function in maintaining cellular homeostasis. Heme 94-98 heme oxygenase 1 Homo sapiens 68-72 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Carbon Monoxide 195-210 heme oxygenase 1 Homo sapiens 17-21 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Carbon Monoxide 195-210 heme oxygenase 1 Homo sapiens 239-243 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Iron 212-216 heme oxygenase 1 Homo sapiens 17-21 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Iron 212-216 heme oxygenase 1 Homo sapiens 239-243 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Bilirubin 222-231 heme oxygenase 1 Homo sapiens 17-21 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Bilirubin 222-231 heme oxygenase 1 Homo sapiens 239-243