PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9038241-0 1997 Activation of CGS 12094 (prinomide metabolite) to 1,4-benzoquinone by myeloperoxidase: implications for human idiosyncratic agranulocytosis. quinone 50-66 myeloperoxidase Homo sapiens 70-85 27856348-5 2016 When glyceraldehyde 3-phosphate dehydrogenase was exposed to the myeloperoxidase system with 5HIAA, quinone adducts were formed on the protein molecule. quinone 100-107 myeloperoxidase Homo sapiens 65-80 9118926-4 1996 A combination of metabolites (hydroquinone and phenol, for example) may be necessary to duplicate the hematotoxic effect of benzene, perhaps due in part to the synergistic effect of phenol on myeloperoxidase-mediated oxidation of hydroquinone to the reactive metabolite benzoquinone. quinone 270-282 myeloperoxidase Homo sapiens 192-207 8571360-3 1995 A combination of metabolites (hydroquinone and phenol for example) is apparently necessary to duplicate the hematotoxic effect of benzene, perhaps due in part to the synergistic effect of phenol on myeloperoxidase-mediated oxidation of hydroquinone to the reactive metabolite benzoquinone. quinone 276-288 myeloperoxidase Homo sapiens 198-213 1654782-1 1991 Hydroquinone, a metabolite of benzene, is converted by human myeloperoxidase to 1,4-benzoquinone, a highly toxic species. quinone 80-96 myeloperoxidase Homo sapiens 61-76 3022817-7 1986 Although the myeloperoxidase-catalyzed oxidation of DMA at pH 7 in the presence of Cl- gave only the cation radical of DMA, a fairly large amount of p-benzoquinone was obtained as a product. quinone 149-163 myeloperoxidase Homo sapiens 13-28 8643080-12 1996 Addition of human myeloperoxidase to the HQ/Cu/Zn-SOD synergistically enhanced the formation of BQ from HQ. quinone 96-98 myeloperoxidase Homo sapiens 18-33 8643080-17 1996 The H202 generated from the Cu/Zn-SOD-accelerated oxidation of HQ can also be utilized by myeloperoxidase resulting in additional conversion of HQ to BQ. quinone 150-152 myeloperoxidase Homo sapiens 90-105 8288159-7 1993 It is postulated that both iodoacetamide and a thyroxine-derived oxidation product (presumably a quinone) alkylate sulphydryl groups near the active centre of myeloperoxidase making it more accessible for its substrate. quinone 97-104 myeloperoxidase Homo sapiens 159-174 1314822-9 1992 Both compound III and ferro-MPO reacted with benzoquinone to regenerate ferric-MPO. quinone 45-57 myeloperoxidase Homo sapiens 28-31 1314822-9 1992 Both compound III and ferro-MPO reacted with benzoquinone to regenerate ferric-MPO. quinone 45-57 myeloperoxidase Homo sapiens 79-82 1314822-12 1992 However, as benzoquinone accumulates, it oxidizes ferro-MPO and compound III to ferric-MPO, thereby increasing the rate of peroxidation. quinone 12-24 myeloperoxidase Homo sapiens 56-59 1314822-12 1992 However, as benzoquinone accumulates, it oxidizes ferro-MPO and compound III to ferric-MPO, thereby increasing the rate of peroxidation. quinone 12-24 myeloperoxidase Homo sapiens 87-90 1314822-13 1992 There is a minimal lag phase under an atmosphere of N2 because ferro-MPO would be rapidly oxidized by benzoquinone, without formation of compound III. quinone 102-114 myeloperoxidase Homo sapiens 69-72 2154673-11 1990 High performance liquid chromatographic analysis of incubations containing purified myeloperoxidase, hydroquinone, and hydrogen peroxide showed that greater than 90% of hydroquinone was removed and could be detected stoichometrically as 1,4-benzoquinone. quinone 237-253 myeloperoxidase Homo sapiens 84-99 2551665-2 1989 Studies employing horseradish peroxidase and human myeloperoxidase have shown that in the presence of hydrogen peroxide phenol is converted to 4,4"-diphenoquinone and other covalent binding metabolites, whereas hydroquinone is converted solely to 1,4-benzoquinone. quinone 247-263 myeloperoxidase Homo sapiens 51-66 2562421-3 1989 Myeloperoxidase, isolated and purified from human PMNs, catalyzed the oxidation of eugenol to a reactive intermediate which is likely to be a quinone methide. quinone 142-149 myeloperoxidase Homo sapiens 0-15 19828014-9 2009 This toxic quinone was produced by stimulated neutrophils in a reaction that required myeloperoxidase. quinone 11-18 myeloperoxidase Homo sapiens 86-101 17166200-6 2005 In the bone marrow, hydroquinone is oxidized into p-benzoquinone because of the high myeloperoxidase activity. quinone 50-64 myeloperoxidase Homo sapiens 85-100 19212761-8 2009 If an oxidized benzene metabolite such as p-BQ was actually the precursor for the ultimate carcinogenic benzene metabolite and further activation proceeds via MPO mediated reactions, it should be possible to activate p-BQ to a genotoxic compound in vitro. quinone 42-46 myeloperoxidase Homo sapiens 159-162 19212761-8 2009 If an oxidized benzene metabolite such as p-BQ was actually the precursor for the ultimate carcinogenic benzene metabolite and further activation proceeds via MPO mediated reactions, it should be possible to activate p-BQ to a genotoxic compound in vitro. quinone 217-221 myeloperoxidase Homo sapiens 159-162 16841962-0 2006 Myeloperoxidase-catalyzed metabolism of etoposide to its quinone and glutathione adduct forms in HL60 cells. quinone 57-64 myeloperoxidase Homo sapiens 0-15 11543641-1 2001 The benzene metabolite hydroquinone (HQ) is postulated to exert its myelotoxicity by bioactivation to reactive quinone derivatives in myeloperoxidase (MPO)-containing cells. quinone 28-35 myeloperoxidase Homo sapiens 134-149 11543641-1 2001 The benzene metabolite hydroquinone (HQ) is postulated to exert its myelotoxicity by bioactivation to reactive quinone derivatives in myeloperoxidase (MPO)-containing cells. quinone 28-35 myeloperoxidase Homo sapiens 151-154