PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19577554-1 2009 The binding of the heme enzyme myeloperoxidase to phosphatidylserine epitopes on the surface of non-vital polymorphonuclear leukocytes and other cells at inflammatory sites favours modifications of this phospholipid by myeloperoxidase products. Phospholipids 203-215 myeloperoxidase Homo sapiens 31-46 20400181-1 2010 The close association of the heme enzyme myeloperoxidase to phosphatidylserine epitopes on the surface of non-vital polymorphonuclear leukocytes (PMNs) and other apoptotic cells at inflammatory sites favours modifications of this phospholipid by myeloperoxidase products. Phospholipids 230-242 myeloperoxidase Homo sapiens 41-56 20400181-1 2010 The close association of the heme enzyme myeloperoxidase to phosphatidylserine epitopes on the surface of non-vital polymorphonuclear leukocytes (PMNs) and other apoptotic cells at inflammatory sites favours modifications of this phospholipid by myeloperoxidase products. Phospholipids 230-242 myeloperoxidase Homo sapiens 246-261 23438648-13 2013 These results suggest that halogenated phospholipids formed in MPO-dependent reactions can be considered as a new class of biologically active compounds potentially capable of regulating sPLA2-IIA activity in the areas of inflammation and producing the effects opposite to those of oxidized phospholipids. Phospholipids 39-52 myeloperoxidase Homo sapiens 63-66 23438648-13 2013 These results suggest that halogenated phospholipids formed in MPO-dependent reactions can be considered as a new class of biologically active compounds potentially capable of regulating sPLA2-IIA activity in the areas of inflammation and producing the effects opposite to those of oxidized phospholipids. Phospholipids 291-304 myeloperoxidase Homo sapiens 63-66 20828647-8 2010 The odds ratio of CAD events associated with the highest tertiles of oxidized phospholipids on apolipoprotein B-100 particles or Lp(a) was significantly potentiated (approximately doubled) by the highest tertiles of secretory phospholipase A(2) activity and mass but less so for myeloperoxidase and lipoprotein-associated phospholipase A(2) activity. Phospholipids 78-91 myeloperoxidase Homo sapiens 279-294 19577554-1 2009 The binding of the heme enzyme myeloperoxidase to phosphatidylserine epitopes on the surface of non-vital polymorphonuclear leukocytes and other cells at inflammatory sites favours modifications of this phospholipid by myeloperoxidase products. Phospholipids 203-215 myeloperoxidase Homo sapiens 219-234 12737551-4 2003 Free radical-induced oxidative cleavage of DHA-PC promoted by myeloperoxidase or copper ions generates similar mixtures of these phospholipids. Phospholipids 129-142 myeloperoxidase Homo sapiens 62-77 17604010-11 2007 The results indicate that at physiological levels of chloride and bromide, chloride promotes MPO-mediated formation of bromohydrins and lyso-PC in unsaturated phospholipids. Phospholipids 159-172 myeloperoxidase Homo sapiens 93-96 15060092-3 2004 These oxidized phospholipids are largely generated by potent oxidants produced by the lipoxygenase and myeloperoxidase pathways. Phospholipids 15-28 myeloperoxidase Homo sapiens 103-118 10744670-0 2000 p-hydroxyphenylacetaldehyde, an aldehyde generated by myeloperoxidase, modifies phospholipid amino groups of low density lipoprotein in human atherosclerotic intima. Phospholipids 80-92 myeloperoxidase Homo sapiens 54-69 11677044-8 2001 Mono-chlorohydrins of 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine were detected after the incubation of the latter phospholipid with the myeloperoxidase-hydrogen peroxide-chloride system at pH 6.0. Phospholipids 119-131 myeloperoxidase Homo sapiens 141-156 10744670-6 2000 Activated human neutrophils generated pHA-ethanolamine, the reduced adduct of pHA with the amino group of phosphatidylethanolamine, on LDL phospholipids by a reaction that required myeloperoxidase, H(2)O(2), and L-tyrosine. Phospholipids 139-152 myeloperoxidase Homo sapiens 181-196 10744670-11 2000 Collectively, these results demonstrate a novel, myeloperoxidase-based mechanism for modifying the amino group of LDL phospholipids. Phospholipids 118-131 myeloperoxidase Homo sapiens 49-64 10754262-5 2000 This study provides the first direct evidence that lipid chlorohydrins rather than peroxides are the major products of HOCl- or myeloperoxidase-treated LDL phospholipids. Phospholipids 156-169 myeloperoxidase Homo sapiens 128-143 2852626-0 1988 Peroxidation of phospholipids promoted by myeloperoxidase. Phospholipids 16-29 myeloperoxidase Homo sapiens 42-57 9894014-6 1999 When phospholipid model systems and cell membranes were exposed to physiological levels of L-tyrosine and the myeloperoxidase/hydrogen peroxide/chloride system followed by treatment with NaBH3CN, reduced Schiff base adducts of pHA with ethanolamine glycerophospholipid and serine glycerophospholipid (pHA-PE and pHA-PS, respectively) were produced. Phospholipids 5-17 myeloperoxidase Homo sapiens 110-125 34568331-7 2021 On the other hand, NE, which was previously reported to be released from granules to cytosol by MPO during NET formation, is not required for either the peroxidation of phospholipids or the execution of NETosis, but contributes to chromatin decondensation and nuclear swelling independently of MPO-mediated oxidized phospholipids. Phospholipids 316-329 myeloperoxidase Homo sapiens 294-297 2852626-1 1988 Myeloperoxidase was found to promote peroxidation of phospholipids under acidic conditions in the presence of hydrogen peroxide and iodide ions. Phospholipids 53-66 myeloperoxidase Homo sapiens 0-15 33915354-4 2021 We have previously shown that MPO, a highly cationic protein, regulates coagulation through heteromolecular interactions with various negatively charged structures, including membrane phospholipids and low-molecular-weight heparin. Phospholipids 184-197 myeloperoxidase Homo sapiens 30-33 29378164-1 2018 Myeloperoxidase produces the two-electron oxidant HOCl, which targets plasmalogen phospholipids liberating 2-chlorofatty aldehyde. Phospholipids 82-95 myeloperoxidase Homo sapiens 0-15 32457656-4 2020 2-Chlorofatty aldehyde (2-ClFALD) is the direct oxidation product of MPO-derived hypochlorous acid (HOCl) targeting plasmalogen phospholipids. Phospholipids 128-141 myeloperoxidase Homo sapiens 69-72 29149817-5 2018 Mainly, in proteome, Apolipoprotein A1 (Apo-A1), Myeloperoxidase (MPO), Paroxonase (PON) are affected by inflammation or glycation-related factors; and especially esterification or unesterification of lipids, changes in phospholipid or unsaturated lipid content change the HDL function. Phospholipids 220-232 myeloperoxidase Homo sapiens 49-64 29149817-5 2018 Mainly, in proteome, Apolipoprotein A1 (Apo-A1), Myeloperoxidase (MPO), Paroxonase (PON) are affected by inflammation or glycation-related factors; and especially esterification or unesterification of lipids, changes in phospholipid or unsaturated lipid content change the HDL function. Phospholipids 220-232 myeloperoxidase Homo sapiens 66-69 29167411-4 2018 2-Chlorofatty acids (2-ClFAs) are produced as a result of MPO-derived HOCl targeting plasmalogen phospholipids. Phospholipids 97-110 myeloperoxidase Homo sapiens 58-61 29212118-0 2017 Myeloperoxidase Is a Negative Regulator of Phospholipid-Dependent Coagulation. Phospholipids 43-55 myeloperoxidase Homo sapiens 0-15 29212118-6 2017 MPO and MPO/H2O2 also inhibited the PCA of activated platelets and purified phospholipids (PLs), suggesting that modulation of negatively charged PLs, i.e., phosphatidylserine, rather than direct interference with the TF/FVIIa initiation complex was involved. Phospholipids 76-89 myeloperoxidase Homo sapiens 0-3 29212118-6 2017 MPO and MPO/H2O2 also inhibited the PCA of activated platelets and purified phospholipids (PLs), suggesting that modulation of negatively charged PLs, i.e., phosphatidylserine, rather than direct interference with the TF/FVIIa initiation complex was involved. Phospholipids 76-89 myeloperoxidase Homo sapiens 8-11 28138552-5 2017 Aligning with changes in TLR signals, oxidized phospholipids, which function as TLR4 antagonists, were increased in monocytes in the presence of MPO-ANCA. Phospholipids 47-60 myeloperoxidase Homo sapiens 145-148