PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30689356-3 2019 Their kinetics were determined by monitoring the consumption of H2O2 with a nitrogen-doped carbon nanotubes (N-CNT) electrode, which could detect 0.50 muM H2O2 at -0.20 V. The unique design of internally calibrated electrochemical continuous enzyme assay (ICECEA) and electrode stability allowed use of one N-CNT electrode for over half a year to reliably determine MPO. Carbon 91-97 myeloperoxidase Homo sapiens 366-369 31445206-9 2019 NMR studies revealed that there are two exchangeable hydrogens, one of which is on the alpha-carbon, justifying the carbon-centred edaravone radical produced from MPO. Carbon 93-99 myeloperoxidase Homo sapiens 163-166 31445206-9 2019 NMR studies revealed that there are two exchangeable hydrogens, one of which is on the alpha-carbon, justifying the carbon-centred edaravone radical produced from MPO. Carbon 116-122 myeloperoxidase Homo sapiens 163-166 28440832-0 2017 Nanoemitters and innate immunity: the role of surfactants and bio-coronas in myeloperoxidase-catalyzed oxidation of pristine single-walled carbon nanotubes. Carbon 139-145 myeloperoxidase Homo sapiens 77-92 29271441-1 2018 Neutrophils were previously shown to digest oxidized carbon nanotubes through a myeloperoxidase (MPO)-dependent mechanism, and graphene oxide (GO) was found to undergo degradation when incubated with purified MPO, but there are no studies to date showing degradation of GO by neutrophils. Carbon 53-59 myeloperoxidase Homo sapiens 97-100 28042968-1 2017 Neutrophil myeloperoxidase (MPO) and peroxynitrite (ONOO-) can oxidatively biodegrade carboxylated single-walled carbon nanotubes (SWCNTs). Carbon 113-119 myeloperoxidase Homo sapiens 11-26 28042968-1 2017 Neutrophil myeloperoxidase (MPO) and peroxynitrite (ONOO-) can oxidatively biodegrade carboxylated single-walled carbon nanotubes (SWCNTs). Carbon 113-119 myeloperoxidase Homo sapiens 28-31 27614147-0 2016 Binding of human IgG to single-walled carbon nanotubes accelerated myeloperoxidase-mediated degradation in activated neutrophils. Carbon 38-44 myeloperoxidase Homo sapiens 67-82 27885574-1 2017 Previous studies have shown that carboxylated single-walled carbon nanotubes (SWCNTs) could be oxidatively biodegraded by neutrophil myeloperoxidase (MPO) and peroxynitrite (ONOO-). Carbon 60-66 myeloperoxidase Homo sapiens 133-148 27885574-1 2017 Previous studies have shown that carboxylated single-walled carbon nanotubes (SWCNTs) could be oxidatively biodegraded by neutrophil myeloperoxidase (MPO) and peroxynitrite (ONOO-). Carbon 60-66 myeloperoxidase Homo sapiens 150-153 27126478-11 2016 Stronger positive associations of black carbon and sulfate with myeloperoxidase were observed among participants with diabetes than in those without. Carbon 40-46 myeloperoxidase Homo sapiens 64-79 24673477-9 2014 KEY FINDINGS: 3-(aminoalkyl)-5-fluoroindole derivative with 5 carbons on the side chain and paroxetine showed the best activity on both MPO and SERT at the nanomolar range. Carbon 62-69 myeloperoxidase Homo sapiens 136-139 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(+). Carbon 193-199 myeloperoxidase Homo sapiens 0-3 24994664-0 2014 Carbon nanotube wiring for signal amplification of electrochemical magneto immunosensors: application to myeloperoxidase detection. Carbon 0-6 myeloperoxidase Homo sapiens 105-120 24994664-1 2014 In this work, chronoamperometric myelo-peroxidase (MPO) detection was accomplished using immunofunctionalized magnetic microparticles (MPs), disposable carbon screen-printed electrodes (C-SPEs), and a ready-to-use commercially available tetramethylbenzidine (TMB)-based enzymatic substrate. Carbon 152-158 myeloperoxidase Homo sapiens 33-49 24994664-1 2014 In this work, chronoamperometric myelo-peroxidase (MPO) detection was accomplished using immunofunctionalized magnetic microparticles (MPs), disposable carbon screen-printed electrodes (C-SPEs), and a ready-to-use commercially available tetramethylbenzidine (TMB)-based enzymatic substrate. Carbon 152-158 myeloperoxidase Homo sapiens 51-54 24995502-7 2014 Myeloperoxidase release was inhibited by urolithins A and C (at 20 microM by 46.7 +- 16.1 and 63.8 +- 8.6%, respectively). Carbon 58-59 myeloperoxidase Homo sapiens 0-15 24870066-1 2014 Previous studies have shown that carboxylated single-walled carbon nanotubes (SWCNTs) can be catalytically biodegraded by hypochlorite (OCl-) and reactive radical intermediates of the human neutrophil enzyme myeloperoxidase (MPO). Carbon 60-66 myeloperoxidase Homo sapiens 225-228 24870066-7 2014 Our findings suggest that the binding of HSA may be an important determinant for MPO-mediated SWCNT biodegradation in human inflammatory cells and therefore shed light on the biomedical and biotechnological applications of safe carbon nanotubes by comprehensive preconsideration of their interactions with human serum proteins. Carbon 228-234 myeloperoxidase Homo sapiens 81-84 23626907-4 2013 While reactive intermediates generated by MPO efficiently degrade oxidized single-walled carbon nanotubes (o-SWCNTs); the exact mechanism of enzyme-catalysed biodegradation remains ambiguous. Carbon 89-95 myeloperoxidase Homo sapiens 42-45 23581551-5 2013 The fluoroindole compound with three carbons in the side chain and one amide group exhibited a selectivity index of 35 (Ki/IC50) with high inhibition of MPO activity (IC50 = 18 nM), whereas its effect on SERT was in the micromolar range. Carbon 37-44 myeloperoxidase Homo sapiens 153-156 23626907-3 2013 In particular, myeloperoxidase (MPO), an enzyme expressed by inflammatory cells of animals including humans, catalyse the degradation of oxidized carbon nanomaterials. Carbon 146-152 myeloperoxidase Homo sapiens 15-30 23626907-3 2013 In particular, myeloperoxidase (MPO), an enzyme expressed by inflammatory cells of animals including humans, catalyse the degradation of oxidized carbon nanomaterials. Carbon 146-152 myeloperoxidase Homo sapiens 32-35 23086900-3 2012 To develop a molecule that binds MPO, salicylhydroxamic acid (SHA), a substrate analog inhibitor of MPO with a KD=2 muM, was conjugated to a designed set of 42-residue polypeptide scaffolds via 9- and 11-carbon atom aliphatic spacers to form 20 different protein binder candidates, and their interactions with MPO were evaluated by surface plasmon resonance analysis. Carbon 204-210 myeloperoxidase Homo sapiens 33-36 17359937-1 2007 In human myeloperoxidase (MPO) the heme is covalently attached to the protein via two ester linkages and a unique sulfonium ion linkage between the sulfur atom of Met243 and the beta-carbon of the vinyl ring on pyrrole ring A. Carbon 183-189 myeloperoxidase Homo sapiens 9-24 22096994-0 2011 [Myeloperoxidase-induced biodegradation of single-walled carbon nanotubes is mediated by hypochlorite]. Carbon 57-63 myeloperoxidase Homo sapiens 1-16 22096994-4 2011 The comparison of the ability of various peroxidases to degrade SWNTs in vitro revealed that myeloperoxidase, due to its ability to produce hypochlorite, and lactoperoxidase, due to its ability to produce hypobromite, are extremely efficient in the degradation of carbon nanotubes. Carbon 264-270 myeloperoxidase Homo sapiens 93-108 20364135-0 2010 Carbon nanotubes degraded by neutrophil myeloperoxidase induce less pulmonary inflammation. Carbon 0-6 myeloperoxidase Homo sapiens 40-55 20364135-3 2010 Here, we show that hypochlorite and reactive radical intermediates of the human neutrophil enzyme myeloperoxidase catalyse the biodegradation of single-walled carbon nanotubes in vitro, in neutrophils and to a lesser degree in macrophages. Carbon 159-165 myeloperoxidase Homo sapiens 98-113 17359937-1 2007 In human myeloperoxidase (MPO) the heme is covalently attached to the protein via two ester linkages and a unique sulfonium ion linkage between the sulfur atom of Met243 and the beta-carbon of the vinyl ring on pyrrole ring A. Carbon 183-189 myeloperoxidase Homo sapiens 26-29 9337863-5 1997 In support of this, we find: (i) CNO- inhibits both peroxidative and halogenating activities of MPO and also inhibits the enzyme within intact human neutrophils; (ii) the inhibition is H2O2-dependent, irreversible, accompanied by covalent addition of [14C]CNO- (or a carbon-containing fragment thereof) to the enzyme; (iii) CNO- also inhibits Cl-/H2O2/MPO-mediated bacterial killing. Carbon 267-273 myeloperoxidase Homo sapiens 96-99 11705390-6 2001 These results support a model for a single common binding site for halides and thiocyanate as substrates or as inhibitors near the delta-meso carbon of the porphyrin ring in myeloperoxidase. Carbon 142-148 myeloperoxidase Homo sapiens 174-189 32803946-1 2020 Myeloperoxidase (MPO), a key enzyme released by neutrophils during inflammation, has been shown to catalyze the biodegradation of carbon nanomaterials. Carbon 130-136 myeloperoxidase Homo sapiens 0-15 8982278-1 1996 Unsaturated fatty acids of odd carbons, 13:1(12), 17:1(10trans), 19:1(7) and 19:1(10) inhibited release of myeloperoxidase (MPO) from fMet-Leu-Phe-cytochalasin B-treated neutrophils. Carbon 31-38 myeloperoxidase Homo sapiens 107-122 8982278-1 1996 Unsaturated fatty acids of odd carbons, 13:1(12), 17:1(10trans), 19:1(7) and 19:1(10) inhibited release of myeloperoxidase (MPO) from fMet-Leu-Phe-cytochalasin B-treated neutrophils. Carbon 31-38 myeloperoxidase Homo sapiens 124-127 32803946-1 2020 Myeloperoxidase (MPO), a key enzyme released by neutrophils during inflammation, has been shown to catalyze the biodegradation of carbon nanomaterials. Carbon 130-136 myeloperoxidase Homo sapiens 17-20 32803946-2 2020 In this work, we perform photoluminescence studies on the MPO-catalyzed oxidation of graphene oxide (GO) and surfactant-coated pristine (6,5) single-walled carbon nanotubes (SWCNTs). Carbon 156-162 myeloperoxidase Homo sapiens 58-61 32803946-9 2020 Our sensors show linear response to MPO oxidative machinery, and hold the promise to be used as self-calibrating carbon nanomaterial-based MPO activity indicators. Carbon 113-119 myeloperoxidase Homo sapiens 36-39 32803946-9 2020 Our sensors show linear response to MPO oxidative machinery, and hold the promise to be used as self-calibrating carbon nanomaterial-based MPO activity indicators. Carbon 113-119 myeloperoxidase Homo sapiens 139-142