PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17166480-6 2007 However, this thiol compound was efficiently oxidized by the apocynin radical during the MPO-catalyzed oxidation. Sulfhydryl Compounds 14-19 myeloperoxidase Homo sapiens 89-92 16171780-0 2005 Thiol-containing molecules interact with the myeloperoxidase/H2O2/chloride system to inhibit LDL oxidation. Sulfhydryl Compounds 0-5 myeloperoxidase Homo sapiens 45-60 10569638-0 1999 Myeloperoxidase-catalyzed redox-cycling of phenol promotes lipid peroxidation and thiol oxidation in HL-60 cells. Sulfhydryl Compounds 82-87 myeloperoxidase Homo sapiens 0-15 15292529-11 2004 BASDAI was positively correlated with VAS, ESR and CRP; but MPO was negatively correlated with thiol/albumin ratio, both in total and active AS patients. Sulfhydryl Compounds 95-100 myeloperoxidase Homo sapiens 60-63 9355763-0 1997 Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Sulfhydryl Compounds 48-54 myeloperoxidase Homo sapiens 58-73 10556685-1 1999 Ambroxol (100 microM and 1 mM) and the thiols (all 1 mM), glutathione, tiopronin and cysteine, significantly attenuated the myeloperoxidase, H(2)O(2) and Cl(-) system-caused destruction of alpha(1)-antiproteinase and the HOCl-induced destruction of collagen, whereas they did not affect the elastase-induced destruction of collagen. Sulfhydryl Compounds 39-45 myeloperoxidase Homo sapiens 124-139 10462537-10 1999 2) Intracellular reductants, GSH and protein sulfhydryls (but not phospholipids), are involved in myeloperoxidase-catalyzed etoposide redox-cycling that oxidizes endogenous thiols; pretreatment of HL60 cells with a maleimide thiol reagent, ThioGlo1, prevents redox-cycling of etoposide-O(.) Sulfhydryl Compounds 173-179 myeloperoxidase Homo sapiens 98-113 10025950-0 1999 Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. Sulfhydryl Compounds 48-54 myeloperoxidase Homo sapiens 58-73 10025950-2 1999 Because most of the non-steroidal anti-inflammatory drugs and other drugs contain a thiol group, it is necessary to understand how these substrates are oxidized by MPO. Sulfhydryl Compounds 84-89 myeloperoxidase Homo sapiens 164-167 25841785-3 2015 Low molecular mass thiol compounds, including glutathione (GSH) and methionine (Met), have demonstrated efficacy in scavenging MPO-derived oxidants, which prevents oxidative damage in vitro and ex vivo. Sulfhydryl Compounds 19-24 myeloperoxidase Homo sapiens 127-130 7767941-0 1995 Influence of thiols on the chlorinating effect of a myeloperoxidase system. Sulfhydryl Compounds 13-19 myeloperoxidase Homo sapiens 52-67 7767941-1 1995 The structure-activity relationships for the interactions of a number of sulfhydryl compounds on the transformation of (Z)-3-(4-bromophenyl)-3-(3-pyridyl)allylamine (CPP 200) by an MPO-H2O2-Cl-(-)system at pH 5.25 have been studied. Sulfhydryl Compounds 73-93 myeloperoxidase Homo sapiens 181-184 2833080-4 1987 These results indicate that the sulphydryl compounds work as scavengers of the products of the Myeloperoxidase system, and might be useful in inflammatory disorders, to prevent tissue damage inflicted by this system. Sulfhydryl Compounds 32-42 myeloperoxidase Homo sapiens 95-110 32570189-4 2020 Unlike HOCl, HOSCN can be detoxified by thioredoxin reductase, and reacts selectively with thiols to result in reversible modifications, which could potentially reduce the extent of MPO-induced damage during chronic inflammation. Sulfhydryl Compounds 91-97 myeloperoxidase Homo sapiens 182-185 2852003-0 1988 Myeloperoxidase oxidation states involved in myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds 82-88 myeloperoxidase Homo sapiens 0-15 2852003-0 1988 Myeloperoxidase oxidation states involved in myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds 82-88 myeloperoxidase Homo sapiens 45-60 2852003-1 1988 The changes in the oxidation state of the leucocyte enzyme myeloperoxidase, induced by buffer and thiols, were studied with visible-light-absorption spectroscopy. Sulfhydryl Compounds 98-104 myeloperoxidase Homo sapiens 59-74 2852003-3 1988 These minute amounts of reduced oxygen species are suggested to account for the initiation of myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds 131-137 myeloperoxidase Homo sapiens 94-109 2852003-4 1988 Myeloperoxidase was found to be in its Compound III oxidation state during myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds 112-118 myeloperoxidase Homo sapiens 0-15 2852003-4 1988 Myeloperoxidase was found to be in its Compound III oxidation state during myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds 112-118 myeloperoxidase Homo sapiens 75-90 2852003-5 1988 However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. Sulfhydryl Compounds 47-53 myeloperoxidase Homo sapiens 9-24 2852003-5 1988 However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. Sulfhydryl Compounds 47-53 myeloperoxidase Homo sapiens 106-121 2852003-6 1988 These studies indicate that the ferro and Compound III oxidation states may not be essential intermediates in myeloperoxidase-oxidase oxidation of thiols, but rather that the formation of the Compound III oxidation state retards the reaction. Sulfhydryl Compounds 147-153 myeloperoxidase Homo sapiens 110-125 2998407-0 1985 Antiarthritic drugs containing thiol groups scavenge hypochlorite and inhibit its formation by myeloperoxidase from human leukocytes. Sulfhydryl Compounds 31-36 myeloperoxidase Homo sapiens 95-110 25460734-2 2014 As a substrate of myeloperoxidase in vitro, serotonin is oxidized to tryptamine-4,5-dione (TD), which is highly reactive with thiols. Sulfhydryl Compounds 126-132 myeloperoxidase Homo sapiens 18-33 24389598-6 2014 Unlike S100A9, S100A8 effectively scavenges oxidants generated by the myeloperoxidase system in vivo, forming novel thiol modifications. Sulfhydryl Compounds 116-121 myeloperoxidase Homo sapiens 70-85 25050609-0 2014 High plasma thiocyanate levels are associated with enhanced myeloperoxidase-induced thiol oxidation and long-term survival in subjects following a first myocardial infarction. Sulfhydryl Compounds 84-89 myeloperoxidase Homo sapiens 60-75 25050609-6 2014 In this retrospective study, we examined whether elevated plasma MPO and SCN(-) levels increased thiol oxidation as a result of increased HOSCN formation, and impacted on long-term survival in 176 subjects (74 non-smokers, 46 smokers, and 56 previous smokers) hospitalized after a first myocardial infarction. Sulfhydryl Compounds 97-102 myeloperoxidase Homo sapiens 65-68 25050609-8 2014 However, significant positive correlations were detected between SCN(-) levels and MPO-induced thiol loss in the total population (r = 0.19, P = 0.020) and smokers alone (r = 0.58, P < 0.0001). Sulfhydryl Compounds 95-100 myeloperoxidase Homo sapiens 83-86 23009681-0 2012 Myeloperoxidase catalyzes the conjugation of serotonin to thiols via free radicals and tryptamine-4,5-dione. Sulfhydryl Compounds 58-64 myeloperoxidase Homo sapiens 0-15 23009681-11 2012 Our results indicate that myeloperoxidase can oxidize serotonin to species that form adducts with low molecular weight thiols and cysteine residues in proteins. Sulfhydryl Compounds 119-125 myeloperoxidase Homo sapiens 26-41 21884783-0 2011 High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase. Sulfhydryl Compounds 67-72 myeloperoxidase Homo sapiens 94-109 22609005-2 2012 In previous studies we have demonstrated that smokers have elevated levels of thiocyanate ions (SCN(-)), relative to nonsmokers, and increased thiol oxidation, as SCN(-) is a favored substrate for MPO, and the resulting hypothiocyanous acid (HOSCN) targets thiol groups rapidly and selectively. Sulfhydryl Compounds 143-148 myeloperoxidase Homo sapiens 197-200 22609005-2 2012 In previous studies we have demonstrated that smokers have elevated levels of thiocyanate ions (SCN(-)), relative to nonsmokers, and increased thiol oxidation, as SCN(-) is a favored substrate for MPO, and the resulting hypothiocyanous acid (HOSCN) targets thiol groups rapidly and selectively. Sulfhydryl Compounds 257-262 myeloperoxidase Homo sapiens 197-200 22214747-3 2012 We have shown previously that the myeloperoxidase (MPO)-derived oxidants HOCl and HOSCN target thiols and mediate cellular dysfunction. Sulfhydryl Compounds 95-101 myeloperoxidase Homo sapiens 34-49 22214747-3 2012 We have shown previously that the myeloperoxidase (MPO)-derived oxidants HOCl and HOSCN target thiols and mediate cellular dysfunction. Sulfhydryl Compounds 95-101 myeloperoxidase Homo sapiens 51-54 21884783-2 2011 We hypothesized that smokers would have a high level of thiocyanate (SCN(-)), a preferred substrate for MPO, which in turn would predispose to thiol oxidation, an established independent risk factor for atherosclerosis. Sulfhydryl Compounds 143-148 myeloperoxidase Homo sapiens 104-107 21884783-3 2011 In this study it is shown that on exposure to MPO/H(2)O(2), thiols on plasma proteins from nonsmokers were increasingly oxidized with increasing added SCN(-) concentrations. Sulfhydryl Compounds 60-66 myeloperoxidase Homo sapiens 46-49 21884783-5 2011 When plasma from smokers and nonsmokers was exposed to MPO/H(2)O(2)-stimulated oxidation, a strong positive correlation (r=0.8139, P<0.0001) between the extent of thiol oxidation and the plasma SCN(-) concentrations was observed. Sulfhydryl Compounds 166-171 myeloperoxidase Homo sapiens 55-58 21884783-7 2011 These data indicate that plasma SCN(-) levels are a key determinant of the extent of thiol oxidation on plasma proteins induced by MPO, and implicate HOSCN as an important mediator of inflammation-induced oxidative damage to proteins in smokers. Sulfhydryl Compounds 85-90 myeloperoxidase Homo sapiens 131-134 20954832-9 2011 The findings reveal that MPO activity and its reactive products represent useful predictors of the doses of inhaled thiol antioxidants required to ameliorate airway oxidative stress and inflammation in CF patients and provide mechanistic insight into the antioxidative/anti-inflammatory mechanisms of action of GSH and NAC when administered into the CF lung. Sulfhydryl Compounds 116-121 myeloperoxidase Homo sapiens 25-28 21097707-6 2011 Formation of etoposide radicals resulted in the oxidation of endogenous thiols, thus providing evidence for etoposide-mediated MPO-catalyzed redox cycling that may play a role in enhanced etoposide genotoxicity. Sulfhydryl Compounds 72-78 myeloperoxidase Homo sapiens 127-130 18698849-8 2008 A similar selectivity of reaction and extent of thiol oxidation were also observed with myeloperoxidase in the presence of hydrogen peroxide and chloride ions. Sulfhydryl Compounds 48-53 myeloperoxidase Homo sapiens 88-103