PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30190273-0 2018 Myeloperoxidase oxidation of methionine associates with early cystic fibrosis lung disease. Methionine 29-39 myeloperoxidase Homo sapiens 0-15 30190273-6 2018 The most significant annotated feature was methionine sulfoxide (MetO), a product of methionine oxidation by MPO-derived oxidants. Methionine 43-53 myeloperoxidase Homo sapiens 109-112 29174286-3 2018 In MPO, an additional sulfonium ion linkage was present between 2-vinyl group of pyrrole ring A of the heme moiety and a methionine residue of the protein. Methionine 121-131 myeloperoxidase Homo sapiens 3-6 25759391-0 2015 Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I. Methionine 25-35 myeloperoxidase Homo sapiens 0-15 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. Methionine 68-78 myeloperoxidase Homo sapiens 127-130 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. Methionine 80-83 myeloperoxidase Homo sapiens 127-130 22846601-9 2012 In both oxidation systems, an adduct with methionine was formed and it was a major product with MPO and SOD. Methionine 42-52 myeloperoxidase Homo sapiens 96-99 22609005-4 2012 Thus high SCN(-) levels protect against HOCl- and MPO-mediated damage to methionine, tryptophan, lysine, histidine, and tyrosine residues on proteins. Methionine 73-83 myeloperoxidase Homo sapiens 50-53 19775156-13 2009 Purified myeloperoxidase used hydrogen peroxide and chloride to catalyze the oxidation of N-terminal methionines to dehydromethionine. Methionine 101-112 myeloperoxidase Homo sapiens 9-24 21565256-7 2011 Furthermore, methionine, a hypochlorous acid (HOCl) scavenger, also significantly attenuated the cytotoxicity in HL-60 cells, but not in Jurkat cells, indicating the involvement of myeloperoxidase (MPO)-dependent hypohalous acid formation during the photocytotoxicity. Methionine 13-23 myeloperoxidase Homo sapiens 181-196 21565256-7 2011 Furthermore, methionine, a hypochlorous acid (HOCl) scavenger, also significantly attenuated the cytotoxicity in HL-60 cells, but not in Jurkat cells, indicating the involvement of myeloperoxidase (MPO)-dependent hypohalous acid formation during the photocytotoxicity. Methionine 13-23 myeloperoxidase Homo sapiens 198-201 19345674-5 2009 The formation of atheronals by the MPO-H(2)O(2)-Cl(-) system was inhibited by an inhibitor of MPO and scavengers of reactive oxygen species such as sodium azide, methionine, beta-carotene, and vinylbenzoic acid. Methionine 162-172 myeloperoxidase Homo sapiens 35-38 19056332-2 2009 Here we investigated the effects of methionine on tyrosyl nitration and oxidation induced by myeloperoxidase (MPO), H2O2 and NO2(-) and peroxynitrite (ONOO(-)) or ONOO(-) and bicarbonate (HCO3(-)) in model peptides, tyrosylmethionine (YM), tyrosylphenylalanine (YF) and tyrosine. Methionine 36-46 myeloperoxidase Homo sapiens 93-108 19056332-2 2009 Here we investigated the effects of methionine on tyrosyl nitration and oxidation induced by myeloperoxidase (MPO), H2O2 and NO2(-) and peroxynitrite (ONOO(-)) or ONOO(-) and bicarbonate (HCO3(-)) in model peptides, tyrosylmethionine (YM), tyrosylphenylalanine (YF) and tyrosine. Methionine 36-46 myeloperoxidase Homo sapiens 110-113 17726014-6 2007 Liquid chromatography-mass spectrometry and tandem mass spectrometry analyses demonstrated that methionine and N-terminal cysteine residues were rapidly oxidized by MPO-derived HOCl but only oxidation of the N-terminal cysteine of TIMP-1 correlated well with loss of inhibitory activity. Methionine 96-106 myeloperoxidase Homo sapiens 165-168 18688016-7 2008 Lysine methylation did not alter the sensitivity of apoAI to myeloperoxidase, whereas site-specific substitution of apoAI methionine to valine increased the sensitivity of apoAI to myeloperoxidase. Methionine 122-132 myeloperoxidase Homo sapiens 181-196 18331758-3 2008 To investigate these suggestions, we have used density functional theory to study the structure, spectra, and reduction potential of 25 models of myeloperoxidase in the reduced (Fe(II)) and oxidized (Fe(III)) states, as well as in the compound I (formally Fe(V)O) and II (Fe(IV)O or Fe(IV)OH) states, using appropriate models of the linkages to the Asp, Glu, and Met residues (including the back-bone connection between Glu-242 and Met-243) in varying combinations. Methionine 363-366 myeloperoxidase Homo sapiens 146-161 18296711-6 2008 Reduction of HDL-associated chloramines with methionine strongly impaired binding affinity of MPO towards HOCl-HDL. Methionine 45-55 myeloperoxidase Homo sapiens 94-97 18819272-4 2008 The inhibitor of myeloperoxidase NaN3, the HOCl scavengers taurine and methionine, and guaiacol, a substrate for peroxidation cycle of myeloperoxidase, prevented luminescence. Methionine 71-81 myeloperoxidase Homo sapiens 17-32 18642140-3 2008 In addition, in myeloperoxidase, a methionine forms a sulfonium link to a heme vinyl group. Methionine 35-45 myeloperoxidase Homo sapiens 16-31 16732739-5 2006 The formation of lysophospholipids as well as of bromohydrins was not observed when the enzyme or one of its substrates (H2O2 or Br-) was absent from the incubation medium, or if an inhibitor of MPO (sodium azide) or hypobromite scavengers (taurine or methionine) were added. Methionine 252-262 myeloperoxidase Homo sapiens 195-198 10994870-7 2000 In stopped-flow investigations, the MPO/HOCl system has some advantage since: (i) in contrast to H2O2, HOCl cannot function as a one-electron donor of compound I; and (ii) MPO can easily be prevented from cycling by addition of methionine as HOCl scavenger. Methionine 228-238 myeloperoxidase Homo sapiens 36-39 15584761-2 2004 To duplicate the sulfonium link in myeloperoxidase and to obtain information on its mechanism of formation, we have engineered a methionine residue close to the 2-vinyl group in recombinant pea cytosolic ascorbate peroxidase (rpAPX) by replacement of Ser160 by Met (S160M variant). Methionine 129-139 myeloperoxidase Homo sapiens 35-50 11485572-7 2001 We found that when eosinophil peroxidase or myeloperoxidase oxidized thiocyanate, another product besides hypothiocyanite was formed; it also converted methionine into methionine sulphoxide. Methionine 152-162 myeloperoxidase Homo sapiens 44-59 11004581-5 2000 The efficiency of MPO inhibitors to prevent LDL damage increased in the series benzohydroxamic acid < salicylhydroxamic acid < 3-amino-1,2,4-triazole < sodium azide < potassium cyanide < p-hydroxy-benzoic acid hydrazide, while for the HOCl traps the protective efficiency increased in the series glycine < taurine < methionine. Methionine 337-347 myeloperoxidase Homo sapiens 18-21 16497665-0 2006 Myeloperoxidase impairs ABCA1-dependent cholesterol efflux through methionine oxidation and site-specific tyrosine chlorination of apolipoprotein A-I. Methionine 67-77 myeloperoxidase Homo sapiens 0-15 10994870-7 2000 In stopped-flow investigations, the MPO/HOCl system has some advantage since: (i) in contrast to H2O2, HOCl cannot function as a one-electron donor of compound I; and (ii) MPO can easily be prevented from cycling by addition of methionine as HOCl scavenger. Methionine 228-238 myeloperoxidase Homo sapiens 172-175 8387748-7 1993 The reaction with myeloperoxidase required chloride and was inhibited by catalase and methionine, indicating the involvement of hypochlorite. Methionine 86-96 myeloperoxidase Homo sapiens 18-33 7952625-2 1994 Stimulated neutrophils at sites of inflammation can inactivate SLPI by myeloperoxidase-mediated oxidation of the methionine residue in the active site of SLPI. Methionine 113-123 myeloperoxidase Homo sapiens 71-86 1846732-7 1991 All changes observed with the myeloperoxidase system were inhibited by azide or methionine, and were dependent upon the presence of chloride, indicating that they are mediated by HOCl. Methionine 80-90 myeloperoxidase Homo sapiens 30-45 3013850-2 1986 The processing of myeloperoxidase in human HL-60 promyelocytic leukemia cells was studied by pulse-labeling cells in culture with [35S]methionine followed by immunoprecipitation and identification of myeloperoxidase polypeptides from cell fractions after various chase intervals. Methionine 135-145 myeloperoxidase Homo sapiens 18-33 2173627-4 1990 Peroxidation was enhanced by catalase and methionine, especially when stimulants that release myeloperoxidase were used. Methionine 42-52 myeloperoxidase Homo sapiens 94-109 2824562-7 1987 Red cells efficiently inhibited deoxyribose oxidation by hydroxyl radicals generated from H2O2, O2- and Fe(EDTA), and myeloperoxidase-dependent oxidation of methionine to methionine sulfoxide by stimulated neutrophils. Methionine 157-167 myeloperoxidase Homo sapiens 118-133 2822016-3 1987 This was inhibited by azide and methionine, indicating that inactivation was due to myeloperoxidase-derived oxidants. Methionine 32-42 myeloperoxidase Homo sapiens 84-99 2157659-8 1990 The hypochlorite, which is known to be generated during the reaction of MPO with H2O2 and chloride, exhibited a similar inactivating effect on C1q, which was prevented by an external source of methionine. Methionine 193-203 myeloperoxidase Homo sapiens 72-75 2542279-7 1989 In pulse-chase experiments on HL-60 cells with [35S]methionine, pulse-labeled myeloperoxidase precursors were shown to be processed to a light chain and a heavy chain of cellular enzyme. Methionine 52-62 myeloperoxidase Homo sapiens 78-93 2833080-0 1987 Prevention of tissue damage: inhibition of myeloperoxidase mediated inactivation of alpha 1-proteinase inhibitor by N-acetyl cysteine, glutathione, and methionine. Methionine 152-162 myeloperoxidase Homo sapiens 43-58 2833080-1 1987 The ability of the sulphur compounds, N-acetyl cysteine, Methionine, and Glutathione to prevent inactivation of alpha 1-proteinase inhibitor by Myeloperoxidase-H2O2-Cl--system was investigated in vitro with purified components. Methionine 57-67 myeloperoxidase Homo sapiens 144-159 3006833-5 1986 In HL-60 cells labeled with [35S]-methionine, the labeled MPO isolated by immunoprecipitation had a mol wt of 89,000. Methionine 34-44 myeloperoxidase Homo sapiens 58-61 2981591-12 1985 Six-hour 35S-methionine labeling experiments showed that the relative rate of MPO synthesis compared with total TCA precipitable radioactivity was 0.5% in HL-60 blasts and almost negligible in HL-60 macrophages and granulocytes, normal human granulocytes, and B-lymphocytes. Methionine 13-23 myeloperoxidase Homo sapiens 78-81 6307386-2 1983 The process of inactivation is impeded by the addition of inhibitors of myeloperoxidase (KCN, NaN3), of catalase, of methionine but not by the addition of superoxide dismutase, indicating that the mechanism of inactivation is the oxidation of methionine residue by myeloperoxidase-H2O2-halide system. Methionine 117-127 myeloperoxidase Homo sapiens 72-87 6307386-2 1983 The process of inactivation is impeded by the addition of inhibitors of myeloperoxidase (KCN, NaN3), of catalase, of methionine but not by the addition of superoxide dismutase, indicating that the mechanism of inactivation is the oxidation of methionine residue by myeloperoxidase-H2O2-halide system. Methionine 117-127 myeloperoxidase Homo sapiens 265-280 6307386-2 1983 The process of inactivation is impeded by the addition of inhibitors of myeloperoxidase (KCN, NaN3), of catalase, of methionine but not by the addition of superoxide dismutase, indicating that the mechanism of inactivation is the oxidation of methionine residue by myeloperoxidase-H2O2-halide system. Methionine 243-253 myeloperoxidase Homo sapiens 72-87 6301583-1 1983 Methionine-containing chemotactic peptides, such as formyl-methionyl-leucyl-phenylalanine (FMLP), are inactivated via a neutrophil-derived, myeloperoxidase-mediated oxidation of the methionine residue. Methionine 0-10 myeloperoxidase Homo sapiens 140-155 6301583-12 1983 These studies show that intact PMN inactivate methionine-containing chemotactic peptides by a pathway that is sensitive to myeloperoxidase inhibitors and is absent in myeloperoxidase-deficient PMN. Methionine 46-56 myeloperoxidase Homo sapiens 123-138 6301583-12 1983 These studies show that intact PMN inactivate methionine-containing chemotactic peptides by a pathway that is sensitive to myeloperoxidase inhibitors and is absent in myeloperoxidase-deficient PMN. Methionine 46-56 myeloperoxidase Homo sapiens 167-182 6301583-1 1983 Methionine-containing chemotactic peptides, such as formyl-methionyl-leucyl-phenylalanine (FMLP), are inactivated via a neutrophil-derived, myeloperoxidase-mediated oxidation of the methionine residue. Methionine 182-192 myeloperoxidase Homo sapiens 140-155 6301583-2 1983 We report that extracellular inactivation of FMLP by myeloperoxidase modulates the apparent binding of methionine-containing chemotactic peptides to their surface receptors. Methionine 103-113 myeloperoxidase Homo sapiens 53-68 6298110-1 1982 We have previously shown that deuterium oxide (D2O) enhances the oxidation of methionine, a myeloperoxidase (MPO) -mediated reaction, by human neutrophils during phagocytosis. Methionine 78-88 myeloperoxidase Homo sapiens 92-107 6298110-1 1982 We have previously shown that deuterium oxide (D2O) enhances the oxidation of methionine, a myeloperoxidase (MPO) -mediated reaction, by human neutrophils during phagocytosis. Methionine 78-88 myeloperoxidase Homo sapiens 109-112 7142703-6 1982 Thus, chemotactic peptides can trigger neutrophils to secrete myeloperoxidase and hydrogen peroxide, which together with a halide destroy the biologic activity of the peptide, probably by oxidizing a methionine residue. Methionine 200-210 myeloperoxidase Homo sapiens 62-77 6278020-0 1982 Chemotactic factor inactivation by stimulated human neutrophils mediated by myeloperoxidase-catalyzed methionine oxidation. Methionine 102-112 myeloperoxidase Homo sapiens 76-91 6278020-6 1982 Paper chromatography demonstrated that exposure of a formyl-methionyl peptide chemotactic factor to either the cellfree myeloperoxidase system or stimulated neutrophils resulted in its conversion to a molecular species whose location in the chromatographs was identical to that of the peptide containing oxidized methionine. Methionine 313-323 myeloperoxidase Homo sapiens 120-135 6278020-7 1982 Thus, stimulated human neutrophils inactivate peptide chemoattractants by secretion of myeloperoxidase and H2O2, which combine with halides to form oxidants that react with a critical methionine residue. Methionine 184-194 myeloperoxidase Homo sapiens 87-102 6276480-8 1982 The MPO-mediated oxidation of met5-enkephalin was inhibited by methionine but not by methionine sulfoxide, tyrosine, glycine, or phenylalanine, confirming that it was the methionine moiety of met5-enkephalin which was oxidized. Methionine 63-73 myeloperoxidase Homo sapiens 4-7 6276480-8 1982 The MPO-mediated oxidation of met5-enkephalin was inhibited by methionine but not by methionine sulfoxide, tyrosine, glycine, or phenylalanine, confirming that it was the methionine moiety of met5-enkephalin which was oxidized. Methionine 85-95 myeloperoxidase Homo sapiens 4-7 6276298-5 1981 Human neutrophils and the MPO system were about 10 times more efficient in decarboxylating alanine than methionine. Methionine 104-114 myeloperoxidase Homo sapiens 26-29 6276298-7 1981 The fraction of methionine decarboxylated by human neutrophils or the MPO system was small compared to the fraction which was oxidized to methionine sulfoxide. Methionine 16-26 myeloperoxidase Homo sapiens 70-73 6276298-8 1981 Thus methionine was preferentially oxidized to methionine sulfoxide by the MPO system. Methionine 5-15 myeloperoxidase Homo sapiens 75-78 6276298-9 1981 However, once methionine was oxidized to methionine sulfoxide, it was readily decarboxylated by the MPO system. Methionine 14-24 myeloperoxidase Homo sapiens 100-103 6245104-5 1980 The oxidation of methionine by phagocytosing normal PMN was inhibited by (1)O(2) quenchers, (1.4-diazabicyclo-[2,2,2]-octane, tryptophan, NaN(3)), myeloperoxidase (MPO) inhibitors (NaN(3), KCN) and catalase. Methionine 17-27 myeloperoxidase Homo sapiens 147-162 6245104-5 1980 The oxidation of methionine by phagocytosing normal PMN was inhibited by (1)O(2) quenchers, (1.4-diazabicyclo-[2,2,2]-octane, tryptophan, NaN(3)), myeloperoxidase (MPO) inhibitors (NaN(3), KCN) and catalase. Methionine 17-27 myeloperoxidase Homo sapiens 164-167 6245104-12 1980 The oxidation of methionine by the combination of H(2)O(2) and granular fractions was inhibited by (1)O(2) quenchers and MPO inhibitors, but it was stimulated by deuterium oxide. Methionine 17-27 myeloperoxidase Homo sapiens 121-124 6245104-14 1980 Our results suggest that the oxidation of methionine by phagocytosing PMN is dependent on the MPO-mediated antimicrobial system (MPO-H(2)O(2)-Cl(-)). Methionine 42-52 myeloperoxidase Homo sapiens 94-97 6245104-14 1980 Our results suggest that the oxidation of methionine by phagocytosing PMN is dependent on the MPO-mediated antimicrobial system (MPO-H(2)O(2)-Cl(-)). Methionine 42-52 myeloperoxidase Homo sapiens 129-132 6245132-0 1980 Chemotactic factor inactivation by myeloperoxidase-mediated oxidation of methionine. Methionine 73-83 myeloperoxidase Homo sapiens 35-50