PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26867495-3 2016 The role of neutrophil myeloperoxidase (MPO) in INH-NAD(+) adduct formation has never been explored; this is important, as neutrophils are recruited at the site of tuberculosis infection (granuloma) through infected macrophages" cell death signals. NAD 52-58 myeloperoxidase Homo sapiens 40-43 26867495-5 2016 MPO or activated human neutrophils (by phorbol myristate acetate) catalyzed the oxidation of INH and formed several free radical intermediates; the inclusion of superoxide dismutase revealed a carbon-centered radical which is considered to be the reactive metabolite that binds with NAD(+). NAD 283-289 myeloperoxidase Homo sapiens 0-3 26867495-8 2016 Furthermore, only INH oxidation by MPO led to a new product (lambdamax=326nm) in the presence of NAD(+). NAD 97-103 myeloperoxidase Homo sapiens 35-38 26867495-0 2016 Metabolism of isoniazid by neutrophil myeloperoxidase leads to isoniazid-NAD(+) adduct formation: A comparison of the reactivity of isoniazid with its known human metabolites. NAD 73-79 myeloperoxidase Homo sapiens 38-53 16385446-8 2006 In an application to asthma case-control data from the Children"s Health Study, FITF identified a significant multilocus effect between the nicotinamide adenine dinucleotide (phosphate) reduced:quinone oxidoreductase gene (NQO1), myeloperoxidase gene (MPO), and catalase gene (CAT) (unadjusted P = .00026), three genes that are involved in the oxidative stress pathway. NAD 140-173 myeloperoxidase Homo sapiens 230-245 16385446-8 2006 In an application to asthma case-control data from the Children"s Health Study, FITF identified a significant multilocus effect between the nicotinamide adenine dinucleotide (phosphate) reduced:quinone oxidoreductase gene (NQO1), myeloperoxidase gene (MPO), and catalase gene (CAT) (unadjusted P = .00026), three genes that are involved in the oxidative stress pathway. NAD 140-173 myeloperoxidase Homo sapiens 252-255 15531583-10 2005 MPO potentiation was inhibited by NADH, but not azide, suggesting oxidative nitrosylation with NO(2)(.) NAD 34-38 myeloperoxidase Homo sapiens 0-3 9706251-9 1998 The MPO/NADH/halide systems, where NADH replaced H2O2, also inactivated LADH. NAD 8-12 myeloperoxidase Homo sapiens 4-7 9706251-9 1998 The MPO/NADH/halide systems, where NADH replaced H2O2, also inactivated LADH. NAD 35-39 myeloperoxidase Homo sapiens 4-7 9706251-10 1998 Native (not denatured) catalase completely prevented the MPO/NADH/Kl system effect (Table 1), in close agreement with H2O2 production by the LADH-catalysed NADH oxidation and the role of H2O2 in LADH inactivation. NAD 61-65 myeloperoxidase Homo sapiens 57-60 9706251-10 1998 Native (not denatured) catalase completely prevented the MPO/NADH/Kl system effect (Table 1), in close agreement with H2O2 production by the LADH-catalysed NADH oxidation and the role of H2O2 in LADH inactivation. NAD 156-160 myeloperoxidase Homo sapiens 57-60 8288159-1 1993 Thyroxine and other iodothyronines (concentrations in the nanomolar range) stimulated the oxidation of NADH in the myeloperoxidase-H2O2-Cl- system. NAD 103-107 myeloperoxidase Homo sapiens 115-130 8288159-5 1993 Pre-incubation of thyroxine in the myeloperoxidase system showed that thyroxine was oxidized to a product capable of stimulating NADH oxidation. NAD 129-133 myeloperoxidase Homo sapiens 35-50 2841217-0 1988 The effect of thyroxine and related compounds on the aerobic myeloperoxidase--catalysed oxidation of NADH. NAD 101-105 myeloperoxidase Homo sapiens 61-76 2841217-1 1988 Thyroxine concentrations as low as 1 microM significantly stimulate compound III formation during aerobic oxidation of NADH by highly purified myeloperoxidase. NAD 119-123 myeloperoxidase Homo sapiens 143-158 2986713-1 1985 The reactivities of myeloperoxidase-H2O2-Cl- and sodium hypochlorite with amino acids, uric acid, NADH, ascorbic acid, ADP, albumin, haemoglobin, alpha 1-antitrypsin and some hydroxyl radical scavengers have been compared. NAD 98-102 myeloperoxidase Homo sapiens 20-35 15464726-1 2004 We have studied the peroxidase-oxidase reaction catalyzed by human myeloperoxidase in an open system where both substrates-molecular oxygen and NADH-are supplied continuously to the reaction mixture. NAD 144-148 myeloperoxidase Homo sapiens 67-82 8395934-0 1993 Formation of a hydroxyl radical by the myeloperoxidase-NADH-oxygen system. NAD 55-59 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. NAD 34-38 myeloperoxidase Homo sapiens 30-33 8395934-6 1993 Even though the superoxide radical (O2-)-producing ability of the MPO-NADH system was about 29% of that of the hypoxanthine-xanthine oxidase system, under the experimental conditions employed, the rate of tyrosine formation from phenylalanine by two systems was found to be a similar. NAD 70-74 myeloperoxidase Homo sapiens 66-69 8395934-8 1993 may occur in the MPO-NADH system under aerobic conditions and a superoxide radical may be involved in the OH. NAD 21-25 myeloperoxidase Homo sapiens 17-20 1650217-4 1991 Chloride stimulated the oxidation of NADH in the MPO-H2O2 system in a concentration-dependent manner (50-fold at 150 mM NaCl). NAD 37-41 myeloperoxidase Homo sapiens 49-52 1650217-6 1991 Observations demonstrating the effect of the drugs on the MPO system, are: (1) Inhibition of Cl(-)-stimulated oxidation of NADH. NAD 123-127 myeloperoxidase Homo sapiens 58-61 6243364-0 1980 Chlorination or reduced nicotinamide adenine dinucleotides by myeloperoxidase: a novel bactericidal mechanism. NAD 24-58 myeloperoxidase Homo sapiens 62-77 32766477-11 2020 NAD+ concentration was inversely related to serum bilirubin concentration (r 2 = -0.127; P = 0.04) and positively correlated with myeloperoxidase activity (r 2 = 0.31; P = 0.003). NAD 0-4 myeloperoxidase Homo sapiens 130-145