PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30044956-4 2018 Reactive oxygen species (ROS) such as singlet oxygen [O2-] and hydroxyl radicals result in nonspecific reactivity, thus involved in several pathological conditions such as inflammation and reperfusion injury leading to damage of different biological molecules due to the production of enzyme myeloperoxidase because of activation of neutrophils in these diseases. Hydroxyl Radical 63-80 myeloperoxidase Homo sapiens 292-307 7748188-0 1995 Effect of anti-inflammatory drugs on myeloperoxidase-dependent hydroxyl radical generation by human neutrophils. Hydroxyl Radical 63-79 myeloperoxidase Homo sapiens 37-52 15689384-6 2005 The initial product of the MPO-H2O2-chloride system is hypochlorous acid, and subsequent formation of chlorine, chloramines, hydroxyl radicals, singlet oxygen, and ozone has been proposed. Hydroxyl Radical 125-142 myeloperoxidase Homo sapiens 27-30 12515618-1 2002 OBJECTIVE: To examine the relationship between susceptibility to lung cancer among Chinese and genetic polymorphism at nucleotide -463 (G/A) in myeloperoxidase (MPO), an enzyme found in lysosomes of phagocytes and involved in the formation of hydroxyl radicals and activation of various smoking-related carcinogens. Hydroxyl Radical 243-260 myeloperoxidase Homo sapiens 144-159 12515618-1 2002 OBJECTIVE: To examine the relationship between susceptibility to lung cancer among Chinese and genetic polymorphism at nucleotide -463 (G/A) in myeloperoxidase (MPO), an enzyme found in lysosomes of phagocytes and involved in the formation of hydroxyl radicals and activation of various smoking-related carcinogens. Hydroxyl Radical 243-260 myeloperoxidase Homo sapiens 161-164 12014661-3 2002 Myeloperoxidase converts hydrogen peroxide into the selective apoptosis mediator HOCl, which interacts with transformed target cell-derived superoxide anions and generates apoptosis-inducing hydroxyl radicals. Hydroxyl Radical 191-208 myeloperoxidase Homo sapiens 0-15 7748188-7 1995 In this study, we explored this possibility by investigating the role of different classes of anti-inflammatory drugs to ameliorate hydroxyl radical generation via the myeloperoxidase-dependent pathway. Hydroxyl Radical 132-148 myeloperoxidase Homo sapiens 168-183 7748188-8 1995 In this paper, we report that meclofenamic acid inhibited myeloperoxidase-dependent hydroxyl radical generation through scavenging of hypochlorous acid and not by direct inhibition of myeloperoxidase. Hydroxyl Radical 84-100 myeloperoxidase Homo sapiens 58-73 8406685-10 1993 In contrast to what has been reported earlier, HOCl/MPO only depolymerizes purified umbilical cord HA (in a hydroxyl radical-dependent manner) but does not depolymerize HA in SF. Hydroxyl Radical 108-124 myeloperoxidase Homo sapiens 52-55 8406685-11 1993 As a matter of fact, HOCl/MPO has a scavenging action on SF HA by consuming H2O2 and thus preventing the formation of reactive hydroxyl radicals. Hydroxyl Radical 127-144 myeloperoxidase Homo sapiens 26-29 1314821-6 1992 Detection of hydroxyl radical from stimulated monocyte-derived macrophages, which lack myeloperoxidase, required the addition of supplemental iron. Hydroxyl Radical 13-29 myeloperoxidase Homo sapiens 87-102 8395934-0 1993 Formation of a hydroxyl radical by the myeloperoxidase-NADH-oxygen system. Hydroxyl Radical 15-31 myeloperoxidase Homo sapiens 39-54 8395934-4 1993 The tyrosine formation by the MPO-NADH system was greatly reduced under anaerobic conditions, and significantly inhibited by hydroxyl radical scavengers. Hydroxyl Radical 125-141 myeloperoxidase Homo sapiens 30-33 8390261-5 1993 Using spin trapping/ESR spectroscopy, NPC 15669 was found to inhibit myeloperoxidase (MPO)-dependent hydroxyl radical primarily by scavenging hypochlorous acid, and secondarily by inhibiting agonist-stimulated degranulation as assessed by MPO and elastase release. Hydroxyl Radical 101-117 myeloperoxidase Homo sapiens 69-84 8390261-5 1993 Using spin trapping/ESR spectroscopy, NPC 15669 was found to inhibit myeloperoxidase (MPO)-dependent hydroxyl radical primarily by scavenging hypochlorous acid, and secondarily by inhibiting agonist-stimulated degranulation as assessed by MPO and elastase release. Hydroxyl Radical 101-117 myeloperoxidase Homo sapiens 86-89 1314821-0 1992 Spin trapping evidence for myeloperoxidase-dependent hydroxyl radical formation by human neutrophils and monocytes. Hydroxyl Radical 53-69 myeloperoxidase Homo sapiens 27-42 1314821-7 1992 The addition of purified myeloperoxidase to an enzymatic superoxide generating system resulted in the detection of hydroxyl radical that was dependent upon the presence of chloride and was inhibited by superoxide dismutase, catalase, and azide. Hydroxyl Radical 115-131 myeloperoxidase Homo sapiens 25-40 1314821-9 1992 4-POBN-CH(CH3)OH was not observed upon stimulation of myeloperoxidase-deficient neutrophils, whereas addition of myeloperoxidase to the reaction mixture resulted in the detection of hydroxyl radical. Hydroxyl Radical 182-198 myeloperoxidase Homo sapiens 113-128 1314821-10 1992 These results support the ability of human neutrophils and monocytes to generate hydroxyl radical through a myeloperoxidase-dependent mechanism. Hydroxyl Radical 81-97 myeloperoxidase Homo sapiens 108-123 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Hydroxyl Radical 284-300 myeloperoxidase Homo sapiens 38-53 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Hydroxyl Radical 284-300 myeloperoxidase Homo sapiens 55-58 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Hydroxyl Radical 284-300 myeloperoxidase Homo sapiens 98-101 2171513-10 1990 Our results support the ability of myeloperoxidase derived HOCl to act as a direct oxidative activator of HNC and further suggest the existence of a new/alternative oxidative activation pathway of HNC involving hydroxyl radical. Hydroxyl Radical 211-227 myeloperoxidase Homo sapiens 35-50 1665882-2 1991 Today there are four major arguments for such a role in IBD: Infiltration of the inflamed intestinal mucosa with myeloperoxidase containing activated neutrophils able to produce superoxide, hydroxyl and hypochlorite, increased chemoluminescence response of peripheral and mucosal phagocytic cells to various stimuli, decreased inflammation following specific scavenger treatment in animal models of colitis and defined radical scavenger and inhibitory properties of drugs, especially aminosalicylates used in the therapy of IBD. Hydroxyl Radical 190-198 myeloperoxidase Homo sapiens 113-128 1649085-4 1991 Furthermore, neutrophil lactoferrin and myeloperoxidase limit the magnitude (and in the case of lactoferrin the duration) of hydroxyl radical formed by neutrophils in an iron catalyzed system. Hydroxyl Radical 125-141 myeloperoxidase Homo sapiens 40-55 2560462-7 1989 Inhibition by sodium azide and sodium benzoate indicated that these oxygen metabolites could be derived from the MPO-halide system but also from hydroxyl radical production. Hydroxyl Radical 145-161 myeloperoxidase Homo sapiens 113-116 3016031-8 1986 It is concluded that under conditions where neutrophils release myeloperoxidase as well as superoxide and hydrogen peroxide, breakdown of hydrogen peroxide by myeloperoxidase would make conditions unfavorable for hydroxyl radical production. Hydroxyl Radical 213-229 myeloperoxidase Homo sapiens 159-174 2825313-6 1986 MPO-independent oxidant generation in neutrophils and macrophages involves the generation of highly toxic species derived from the interaction of O2- and H2O2, such as hydroxyl radical and singlet oxygen. Hydroxyl Radical 168-184 myeloperoxidase Homo sapiens 0-3 6282074-17 1982 Although our data suggests the production of superoxide anion and hydroxyl radical from the MPO-H2O2-Cl- reaction, the actual presence or involvement of these free radical species is not confirmed herein. Hydroxyl Radical 66-82 myeloperoxidase Homo sapiens 92-95 16337888-5 2006 These results demonstrate that vanadium in the +2, +3, and +4 valence states interacts prooxidatively with human neutrophils, competing effectively with MPO for hydrogen peroxide to promote formation of the highly toxic hydroxyl radical. Hydroxyl Radical 220-236 myeloperoxidase Homo sapiens 153-156 2849797-4 1988 By consuming hydrogen peroxide, the release of myeloperoxidase limits the magnitude of hydroxyl radical production. Hydroxyl Radical 87-103 myeloperoxidase Homo sapiens 47-62 3016031-0 1986 Myeloperoxidase as an effective inhibitor of hydroxyl radical production. Hydroxyl Radical 45-61 myeloperoxidase Homo sapiens 0-15 3016031-3 1986 Purified myeloperoxidase, and neutrophils stimulated with fMet-Leu-Phe and cytochalasin B, strongly inhibited this hydroxyl radical production in a concentration-dependent manner. Hydroxyl Radical 115-131 myeloperoxidase Homo sapiens 9-24 3016031-7 1986 With neutrophils stimulated with phorbol myristate acetate, which release very little myeloperoxidase, hydroxyl radical production was enhanced due to the additional superoxide produced by the cells. Hydroxyl Radical 103-119 myeloperoxidase Homo sapiens 86-101