PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19705807-3 2009 In the oral cavity, salivary peroxidase and MPO catalyze the oxidation of the pseudohalide thiocyanate (SCN(-)) by hydrogen peroxide to produce the antimicrobial hypothiocyanite (OSCN(-)). thiocyanate 91-102 myeloperoxidase Homo sapiens 44-47 19705807-3 2009 In the oral cavity, salivary peroxidase and MPO catalyze the oxidation of the pseudohalide thiocyanate (SCN(-)) by hydrogen peroxide to produce the antimicrobial hypothiocyanite (OSCN(-)). thiocyanate 104-107 myeloperoxidase Homo sapiens 44-47 18851713-1 2009 MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. thiocyanate 71-82 myeloperoxidase Homo sapiens 0-3 18851713-1 2009 MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. thiocyanate 71-82 myeloperoxidase Homo sapiens 5-20 18521543-3 2008 Au(CN) (2) (-) is generated from the therapeutic gold complexes by small amounts of hydrogen cyanide, HCN, produced from thiocyanate, SCN(-), by myeloperoxidase (MPO) an enzyme in neutrophils which normally produces hypochlorite, OCl(-). thiocyanate 121-132 myeloperoxidase Homo sapiens 145-160 18521543-3 2008 Au(CN) (2) (-) is generated from the therapeutic gold complexes by small amounts of hydrogen cyanide, HCN, produced from thiocyanate, SCN(-), by myeloperoxidase (MPO) an enzyme in neutrophils which normally produces hypochlorite, OCl(-). thiocyanate 121-132 myeloperoxidase Homo sapiens 162-165 18521543-3 2008 Au(CN) (2) (-) is generated from the therapeutic gold complexes by small amounts of hydrogen cyanide, HCN, produced from thiocyanate, SCN(-), by myeloperoxidase (MPO) an enzyme in neutrophils which normally produces hypochlorite, OCl(-). thiocyanate 134-137 myeloperoxidase Homo sapiens 145-160 18521543-3 2008 Au(CN) (2) (-) is generated from the therapeutic gold complexes by small amounts of hydrogen cyanide, HCN, produced from thiocyanate, SCN(-), by myeloperoxidase (MPO) an enzyme in neutrophils which normally produces hypochlorite, OCl(-). thiocyanate 134-137 myeloperoxidase Homo sapiens 162-165 17359937-0 2007 The vinyl-sulfonium bond in human myeloperoxidase: impact on compound I formation and reduction by halides and thiocyanate. thiocyanate 111-122 myeloperoxidase Homo sapiens 34-49 16111647-3 2006 In human saliva the major function of hSPO and hMPO is to catalyze the oxidation of thiocyanate (SCN(-)) in the presence of hydrogen peroxide (H(2)O(2)) resulting in end products of wide antimicrobial potential. thiocyanate 84-95 myeloperoxidase Homo sapiens 47-51 16430221-0 2006 Myeloperoxidase metabolizes thiocyanate in a reaction driven by nitric oxide. thiocyanate 28-39 myeloperoxidase Homo sapiens 0-15 16430221-1 2006 We examined the potential physiological relevance of myeloperoxidase (MPO)-nitric oxide (NO) interactions as they may relate to the cosubstrate, pseudo halide thiocyanate (SCN(-)), and substrate switching. thiocyanate 159-170 myeloperoxidase Homo sapiens 53-68 16430221-1 2006 We examined the potential physiological relevance of myeloperoxidase (MPO)-nitric oxide (NO) interactions as they may relate to the cosubstrate, pseudo halide thiocyanate (SCN(-)), and substrate switching. thiocyanate 159-170 myeloperoxidase Homo sapiens 70-73 16430221-1 2006 We examined the potential physiological relevance of myeloperoxidase (MPO)-nitric oxide (NO) interactions as they may relate to the cosubstrate, pseudo halide thiocyanate (SCN(-)), and substrate switching. thiocyanate 172-175 myeloperoxidase Homo sapiens 53-68 16430221-1 2006 We examined the potential physiological relevance of myeloperoxidase (MPO)-nitric oxide (NO) interactions as they may relate to the cosubstrate, pseudo halide thiocyanate (SCN(-)), and substrate switching. thiocyanate 172-175 myeloperoxidase Homo sapiens 70-73 16288970-4 2006 Based on the published crystal structures of free MPO and its complexes with cyanide, bromide and thiocyanate as well as on sequence analysis and modeling, we critically discuss structure-function relationships. thiocyanate 98-109 myeloperoxidase Homo sapiens 50-53 16125131-1 2006 Myeloperoxidase and eosinophil peroxidase use hydrogen peroxide to oxidize halides and thiocyanate to their respective hypohalous acids. thiocyanate 87-98 myeloperoxidase Homo sapiens 0-15 16277530-2 2005 The mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thiocyanate to the antimicrobial agents hypothiocyanous acid (HOSCN) and (SCN)2 and are part of a defense system that protects the host from infections. thiocyanate 100-111 myeloperoxidase Homo sapiens 76-91 15203186-4 2004 The pseudo-halide thiocyanate (SCN-) has been shown to be a suitable substrate for MPO, forming reactive HOSCN/SCN*. thiocyanate 18-29 myeloperoxidase Homo sapiens 83-86 15894800-1 2005 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). thiocyanate 56-67 myeloperoxidase Homo sapiens 116-131 15894800-1 2005 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). thiocyanate 56-67 myeloperoxidase Homo sapiens 133-136 15894800-1 2005 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). thiocyanate 69-72 myeloperoxidase Homo sapiens 116-131 15894800-1 2005 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). thiocyanate 69-72 myeloperoxidase Homo sapiens 133-136 15203186-4 2004 The pseudo-halide thiocyanate (SCN-) has been shown to be a suitable substrate for MPO, forming reactive HOSCN/SCN*. thiocyanate 31-34 myeloperoxidase Homo sapiens 83-86 15203186-6 2004 Measurement of conjugated diene and lipid hydroperoxide formation in LDL preparations exposed to MPO/H2O2 revealed that SCN- catalyzed lipid oxidation in LDL. thiocyanate 120-123 myeloperoxidase Homo sapiens 97-100 15203186-13 2004 When LDL oxidation was performed with activated human neutrophils, which employ the MPO pathway, SCN- catalyzed the cell-mediated LDL oxidation. thiocyanate 97-100 myeloperoxidase Homo sapiens 84-87 12071050-4 2002 Myeloperoxidase easily oxidizes thiocyanate to hypothiocyanate and Br- to HOBr, which are involved in protective reactions. thiocyanate 32-43 myeloperoxidase Homo sapiens 0-15 12612415-0 2003 Modification by fluoride, bromide, iodide, thiocyanate and nitrite anions of reaction of a myeloperoxidase-H2O2-Cl- system with nucleosides. thiocyanate 43-54 myeloperoxidase Homo sapiens 91-106 14993514-2 2004 Recent studies examining the myeloperoxidase(MPO)/thiocyanate system have suggested a link between thiocyanate and atherosclerosis. thiocyanate 99-110 myeloperoxidase Homo sapiens 29-44 14993514-2 2004 Recent studies examining the myeloperoxidase(MPO)/thiocyanate system have suggested a link between thiocyanate and atherosclerosis. thiocyanate 99-110 myeloperoxidase Homo sapiens 45-48 14993514-13 2004 Because thiocyanate is a preferred substrate for MPO, it may play a role in uraemic complications including cardiovascular events. thiocyanate 8-19 myeloperoxidase Homo sapiens 49-52 9922160-0 1998 Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. thiocyanate 75-86 myeloperoxidase Homo sapiens 12-27 11705390-0 2001 Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. thiocyanate 91-102 myeloperoxidase Homo sapiens 6-21 11705390-5 2001 The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. thiocyanate 89-100 myeloperoxidase Homo sapiens 158-173 11705390-5 2001 The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. thiocyanate 306-317 myeloperoxidase Homo sapiens 158-173 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. thiocyanate 79-90 myeloperoxidase Homo sapiens 174-189 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. thiocyanate 69-80 myeloperoxidase Homo sapiens 44-59 11425491-11 2001 MPO also utilized the pseudohalide thiocyanate to oxidize apoB cysteine residues. thiocyanate 35-46 myeloperoxidase Homo sapiens 0-3 9922160-3 1998 This study for the first time presents transient kinetic measurements of the oxidation of these halides and thiocyanate by the myeloperoxidase intermediate compound I, using the sequential mixing stopped-flow technique. thiocyanate 108-119 myeloperoxidase Homo sapiens 127-142 9922160-11 1998 Our results show that thiocyanate is an important substrate of myeloperoxidase in most environments and that hypothiocyanate is likely to contribute to leukocyte antimicrobial activity. thiocyanate 22-33 myeloperoxidase Homo sapiens 63-78 9337863-4 1997 We hypothesized that CNO- (which resembles the "pseudohalide" thiocyanate, an alternative substrate for MPO) might somehow interfere with the activity of MPO. thiocyanate 62-73 myeloperoxidase Homo sapiens 104-107 9359420-0 1997 Thiocyanate and chloride as competing substrates for myeloperoxidase. thiocyanate 0-11 myeloperoxidase Homo sapiens 53-68 9359420-1 1997 The neutrophil enzyme myeloperoxidase uses H2O2 to oxidize chloride, bromide, iodide and thiocyanate to their respective hypohalous acids. thiocyanate 89-100 myeloperoxidase Homo sapiens 22-37 9359420-4 1997 Our aim was to establish whether myeloperoxidase oxidizes thiocyanate in the presence of chloride at physiological concentrations of these substrates. thiocyanate 58-69 myeloperoxidase Homo sapiens 33-48 9359420-6 1997 The relative specificity constants for chloride, bromide and thiocyanate were 1:60:730 respectively, indicating that thiocyanate is by far the most favoured substrate for myeloperoxidase. thiocyanate 61-72 myeloperoxidase Homo sapiens 171-186 9359420-6 1997 The relative specificity constants for chloride, bromide and thiocyanate were 1:60:730 respectively, indicating that thiocyanate is by far the most favoured substrate for myeloperoxidase. thiocyanate 117-128 myeloperoxidase Homo sapiens 171-186 9359420-7 1997 In the presence of 100 mM chloride, myeloperoxidase catalysed the production of hypothiocyanite at concentrations of thiocyanate as low as 25 microM. thiocyanate 117-128 myeloperoxidase Homo sapiens 36-51 9359420-9 1997 The rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubled when 100 microM thiocyanate was added, and was maximal with 1mM thiocyanate. thiocyanate 110-121 myeloperoxidase Homo sapiens 35-50 9359420-9 1997 The rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubled when 100 microM thiocyanate was added, and was maximal with 1mM thiocyanate. thiocyanate 158-169 myeloperoxidase Homo sapiens 35-50 9359420-10 1997 This indicates that at plasma concentrations of thiocyanate and chloride, myeloperoxidase is far from saturated. thiocyanate 48-59 myeloperoxidase Homo sapiens 74-89 9359420-11 1997 We conclude that thiocyanate is a major physiological substrate of myeloperoxidase, regardless of where the enzyme acts. thiocyanate 17-28 myeloperoxidase Homo sapiens 67-82 9337863-4 1997 We hypothesized that CNO- (which resembles the "pseudohalide" thiocyanate, an alternative substrate for MPO) might somehow interfere with the activity of MPO. thiocyanate 62-73 myeloperoxidase Homo sapiens 154-157 1964765-4 1990 Regression equations have been determined which can be used to calculate concentrations of bovine lactoperoxidase (LPO), human salivary peroxidase (SPO), and human myeloperoxidase (MPO) from activities measured with the following donors: pyrogallol, guaiacol, 2,2"-azinobis(3-ethylbenzylthiazoline-6-sulfonic acid), and thiocyanate (SCN-). thiocyanate 320-331 myeloperoxidase Homo sapiens 181-184 1964765-4 1990 Regression equations have been determined which can be used to calculate concentrations of bovine lactoperoxidase (LPO), human salivary peroxidase (SPO), and human myeloperoxidase (MPO) from activities measured with the following donors: pyrogallol, guaiacol, 2,2"-azinobis(3-ethylbenzylthiazoline-6-sulfonic acid), and thiocyanate (SCN-). thiocyanate 333-337 myeloperoxidase Homo sapiens 181-184 2154520-9 1990 Both MPO and EPO catalyze thiocyanate oxidation, but the product (HOSCN) was a poor oxidant for TMB, and thiocyanate inhibited the measured activities. thiocyanate 26-37 myeloperoxidase Homo sapiens 5-8 2154520-9 1990 Both MPO and EPO catalyze thiocyanate oxidation, but the product (HOSCN) was a poor oxidant for TMB, and thiocyanate inhibited the measured activities. thiocyanate 105-116 myeloperoxidase Homo sapiens 5-8 32863239-0 2020 Myeloperoxidase-derived damage to human plasma fibronectin: Modulation by protein binding and thiocyanate ions (SCN-). thiocyanate 94-105 myeloperoxidase Homo sapiens 0-15 15104210-6 2004 We conclude that the physiologic concentrations of thiocyanate found in human plasma could modulate the cytototoxicity of H2O2 and its resulting highly toxic MPO-generated hypochlorous acid by competing with chloride for MPO. thiocyanate 51-62 myeloperoxidase Homo sapiens 158-161 15104210-6 2004 We conclude that the physiologic concentrations of thiocyanate found in human plasma could modulate the cytototoxicity of H2O2 and its resulting highly toxic MPO-generated hypochlorous acid by competing with chloride for MPO. thiocyanate 51-62 myeloperoxidase Homo sapiens 221-224 15104210-7 2004 Furthermore, the oxidative products of the reaction of thiocyanate with MPO are relatively innocuous for human leukemic cells in culture. thiocyanate 55-66 myeloperoxidase Homo sapiens 72-75 2626337-7 1989 Salivary myeloperoxidase assay is interfered by the thiocyanate ions, and the observed increase in salivary "myeloperoxidase" activity may be due to the simultaneous increase in salivary thiocyanate. thiocyanate 52-63 myeloperoxidase Homo sapiens 9-24 2626337-7 1989 Salivary myeloperoxidase assay is interfered by the thiocyanate ions, and the observed increase in salivary "myeloperoxidase" activity may be due to the simultaneous increase in salivary thiocyanate. thiocyanate 187-198 myeloperoxidase Homo sapiens 109-124 3015901-4 1986 Under conditions similar to those in plasma (0.14 M Cl-, 0.02-0.12 mM SCN-), myeloperoxidase catalyzed the oxidation of Cl- to hypochlorous acid (HOCl), which reacted with ammonia and amines to yield chloramines. thiocyanate 70-74 myeloperoxidase Homo sapiens 77-92 3015901-6 1986 Under conditions similar to those in saliva and the surface of the oral mucosa (20 mM Cl-, 0.1-3 mM SCN-), myeloperoxidase catalyzed the oxidation of SCN- to OSCN-, which accumulated in the medium to concentrations of up to 40-70 microM. thiocyanate 100-103 myeloperoxidase Homo sapiens 107-122 3015901-6 1986 Under conditions similar to those in saliva and the surface of the oral mucosa (20 mM Cl-, 0.1-3 mM SCN-), myeloperoxidase catalyzed the oxidation of SCN- to OSCN-, which accumulated in the medium to concentrations of up to 40-70 microM. thiocyanate 150-153 myeloperoxidase Homo sapiens 107-122 3015901-10 1986 OSCN- was produced when SCN- was 0.1 mM or higher and myeloperoxidase, eosinophil peroxidase, or lactoperoxidase was added. thiocyanate 1-4 myeloperoxidase Homo sapiens 54-69 3477210-3 1986 Both salivary peroxidase and myeloperoxidase will catalyse the peroxidation of the thiocyanate ion; the product, hypothiocyanite ion, is a reactive oxidizing agent. thiocyanate 83-94 myeloperoxidase Homo sapiens 29-44 6331509-7 1984 From their effects on the binding of cyanide to the enzyme it is concluded that chloride and thiocyanate bind to myeloperoxidase only when the acid/base group is protonated. thiocyanate 93-104 myeloperoxidase Homo sapiens 113-128 32781424-0 2020 Role of thiocyanate in the modulation of myeloperoxidase-derived oxidant induced damage to macrophages. thiocyanate 8-19 myeloperoxidase Homo sapiens 41-56 32781424-3 2020 As such, there is increasing interest in the use of thiocyanate (SCN-) therapeutically to decrease inflammatory disease, as SCN- is the favoured substrate for MPO, and a potent competitive inhibitor of HOCl formation. thiocyanate 52-63 myeloperoxidase Homo sapiens 159-162 35304099-4 2022 The second pathway involves myeloperoxidase (MPO)-catalyzed oxidation of thiocyanate (SCN-), yielding CNO- and isocyanate. thiocyanate 73-84 myeloperoxidase Homo sapiens 28-43 35304099-4 2022 The second pathway involves myeloperoxidase (MPO)-catalyzed oxidation of thiocyanate (SCN-), yielding CNO- and isocyanate. thiocyanate 73-84 myeloperoxidase Homo sapiens 45-48 33631301-1 2021 Myeloperoxidase (MPO) is released by activated immune cells and forms the oxidants hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN) from the competing substrates chloride and thiocyanate. thiocyanate 184-195 myeloperoxidase Homo sapiens 0-15 33631301-1 2021 Myeloperoxidase (MPO) is released by activated immune cells and forms the oxidants hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN) from the competing substrates chloride and thiocyanate. thiocyanate 184-195 myeloperoxidase Homo sapiens 17-20 33631301-11 2021 Overall, these data provide new insight into pathways promoting vascular dysfunction during chronic inflammation, support the use of thiocyanate as a means to modulate MPO-induced cellular damage in atherosclerosis. thiocyanate 133-144 myeloperoxidase Homo sapiens 168-171 32899436-0 2020 The Role of Thiocyanate in Modulating Myeloperoxidase Activity during Disease. thiocyanate 12-23 myeloperoxidase Homo sapiens 38-53 32899436-2 2020 Thiocyanate can outcompete chlorine anions and other halides (F-, Br-, I-) as substrates for myeloperoxidase by undergoing two-electron oxidation with hydrogen peroxide. thiocyanate 0-11 myeloperoxidase Homo sapiens 93-108 32899436-5 2020 As such, the pharmacological capacity of thiocyanate has been recently investigated for its ability to modulate myeloperoxidase activity for HOSCN, a less potent species relative to HOCl, although outcomes vary significantly across different disease models. thiocyanate 41-52 myeloperoxidase Homo sapiens 112-127 32570189-2 2020 In the presence of thiocyanate (SCN-), the production of HOCl by MPO is decreased in favour of the formation of a milder oxidant, hypothiocyanous acid (HOSCN). thiocyanate 19-30 myeloperoxidase Homo sapiens 65-68 27343172-0 2016 New insights into thiocyanate oxidation by human myeloperoxidase. thiocyanate 18-29 myeloperoxidase Homo sapiens 49-64 31491954-5 2019 Usually, 0.8% of the molar concentration of urea is converted into cyanate, while myeloperoxidase (MPO) catalyzes the oxidation of thiocyanate to produce cyanate at the site of inflammation during smoking, inflammation, or exposure to environmental pollution. thiocyanate 131-142 myeloperoxidase Homo sapiens 82-97 31491954-5 2019 Usually, 0.8% of the molar concentration of urea is converted into cyanate, while myeloperoxidase (MPO) catalyzes the oxidation of thiocyanate to produce cyanate at the site of inflammation during smoking, inflammation, or exposure to environmental pollution. thiocyanate 131-142 myeloperoxidase Homo sapiens 99-102 29496995-5 2018 Moreover, we present two further pathways of carbamylation that involve reaction products of MPO, namely oxidation of cyanide by hypochlorous acid and reaction of thiocyanate with chloramines. thiocyanate 163-174 myeloperoxidase Homo sapiens 93-96 29258826-4 2018 We have developed an assay for myeloperoxidase activity that includes its major physiological substrates - chloride, thiocyanate, tyrosine, and urate. thiocyanate 117-128 myeloperoxidase Homo sapiens 31-46 28818791-2 2017 Thiocyanate (SCN-) ions are utilised by MPO to produce the oxidant hypothiocyanous acid (HOSCN), which reacts with LDL in a different manner to HOCl. thiocyanate 0-11 myeloperoxidase Homo sapiens 40-43 28818791-2 2017 Thiocyanate (SCN-) ions are utilised by MPO to produce the oxidant hypothiocyanous acid (HOSCN), which reacts with LDL in a different manner to HOCl. thiocyanate 13-17 myeloperoxidase Homo sapiens 40-43 27343172-1 2016 Human myeloperoxidase (MPO) uses chloride and thiocyanate as physiological substrates at neutral pH. thiocyanate 46-57 myeloperoxidase Homo sapiens 6-21 27343172-1 2016 Human myeloperoxidase (MPO) uses chloride and thiocyanate as physiological substrates at neutral pH. thiocyanate 46-57 myeloperoxidase Homo sapiens 23-26 27343172-2 2016 Oxidation of thiocyanate to hypothiocyanite mediated by the redox intermediate Compound I rapidly restores the ferric state of MPO. thiocyanate 13-24 myeloperoxidase Homo sapiens 127-130 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. thiocyanate 7-18 myeloperoxidase Homo sapiens 126-129 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. thiocyanate 7-18 myeloperoxidase Homo sapiens 142-145 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. thiocyanate 7-18 myeloperoxidase Homo sapiens 142-145 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. thiocyanate 179-190 myeloperoxidase Homo sapiens 126-129 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. thiocyanate 179-190 myeloperoxidase Homo sapiens 142-145 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. thiocyanate 179-190 myeloperoxidase Homo sapiens 142-145 26061545-4 2015 An alternative pathway involves the leukocyte heme protein myeloperoxidase, which catalyzes the oxidation of thiocyanate in the presence of hydrogen peroxide, producing isocyanate at inflammation sites. thiocyanate 109-120 myeloperoxidase Homo sapiens 59-74 26616646-3 2016 Myeloperoxidase, released from activated leukocytes, catalyzes thiocyanate ion (SCN(-)) oxidation by H2O2 to form hypothiocyanous acid (HOSCN), an oxidant that targets Cys residues. thiocyanate 63-74 myeloperoxidase Homo sapiens 0-15 23059132-9 2012 Notably, diversion of MPO from HOCl production by thiocyanate or nitrite attenuated de-adhesion and associated signaling responses, despite the latter substrate supporting MPO-catalyzed fibronectin nitration. thiocyanate 50-61 myeloperoxidase Homo sapiens 22-25 25795019-5 2015 However, the reactivity of the other major MPO oxidant, hypothiocyanous acid (HOSCN) with LDL is poorly characterised, which is significant given that thiocyanate is the favoured substrate for MPO. thiocyanate 151-162 myeloperoxidase Homo sapiens 43-46 25795019-5 2015 However, the reactivity of the other major MPO oxidant, hypothiocyanous acid (HOSCN) with LDL is poorly characterised, which is significant given that thiocyanate is the favoured substrate for MPO. thiocyanate 151-162 myeloperoxidase Homo sapiens 193-196 25795019-9 2015 This suggests that a change in the ratio of HOSCN:HOCl formation by MPO from variations in plasma thiocyanate levels, will influence the nature of LDL oxidation in vivo, and has implications for the progression of atherosclerosis. thiocyanate 98-109 myeloperoxidase Homo sapiens 68-71 25556310-8 2015 Carbamylation of proteins results from nonenzymatic chemical modification by isocyanic acid derived from urea and an alternative route, the myeloperoxidase-catalyzed oxidation of thiocyanate. thiocyanate 179-190 myeloperoxidase Homo sapiens 140-155 25812586-0 2015 Thiocyanate supplementation decreases atherosclerotic plaque in mice expressing human myeloperoxidase. thiocyanate 0-11 myeloperoxidase Homo sapiens 86-101 25794932-2 2015 This process is increased during chronic kidney disease (CKD) because of hyperuremia, and in other pathologies like atherosclerosis, where isocyanic may be formed from thiocyanate by myeloperoxidase in atheroma plates. thiocyanate 168-179 myeloperoxidase Homo sapiens 183-198 24966132-8 2014 Hence, Cp can be regarded as an anti-inflammatory factor that restrains the halogenating cycle and redirects the synergistic system Mpo-H2O2-chloride/thiocyanate to production of hypothiocyanate, which is relatively harmless for the human organism. thiocyanate 150-161 myeloperoxidase Homo sapiens 132-135 25050609-0 2014 High plasma thiocyanate levels are associated with enhanced myeloperoxidase-induced thiol oxidation and long-term survival in subjects following a first myocardial infarction. thiocyanate 12-23 myeloperoxidase Homo sapiens 60-75 25050609-2 2014 MPO uses H2O2 to generate oxidants including HOCl and HOSCN, from chloride and thiocyanate (SCN(-)) ions, respectively. thiocyanate 79-90 myeloperoxidase Homo sapiens 0-3 24112082-6 2014 eNOS activity was increasingly compromised by MPO/H2O2/Cl(-) with increasing SCN(-) concentrations. thiocyanate 77-83 myeloperoxidase Homo sapiens 46-49 22462773-0 2012 Myeloperoxidase-derived chlorinating species induce protein carbamylation through decomposition of thiocyanate and urea: novel pathways generating dysfunctional high-density lipoprotein. thiocyanate 99-110 myeloperoxidase Homo sapiens 0-15 22462773-3 2012 RESULTS: Here, we show that MPO-derived chlorinating species rapidly decompose the plasma components thiocyanate (SCN) and urea, thereby promoting (lipo)protein carbamylation. thiocyanate 101-112 myeloperoxidase Homo sapiens 28-31 22609005-0 2012 High plasma thiocyanate levels modulate protein damage induced by myeloperoxidase and perturb measurement of 3-chlorotyrosine. thiocyanate 12-23 myeloperoxidase Homo sapiens 66-81 22348603-2 2012 MPO is released by activated neutrophils, monocytes and some tissue macrophages, where it catalyses the conversion of hydrogen peroxide to hypohalous acids (HOX; X = Cl, Br, SCN) in the presence of halide and pseudo-halide ions. thiocyanate 174-177 myeloperoxidase Homo sapiens 0-3 22348603-3 2012 The major reactive species produced by MPO under physiological conditions are hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN), with the ratio of these oxidants critically dependent on the concentration of thiocyanate ions (SCN-). thiocyanate 215-226 myeloperoxidase Homo sapiens 39-42 22348603-3 2012 The major reactive species produced by MPO under physiological conditions are hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN), with the ratio of these oxidants critically dependent on the concentration of thiocyanate ions (SCN-). thiocyanate 233-237 myeloperoxidase Homo sapiens 39-42 21892922-2 2012 MPO catalyses the oxidation of Cl-, Br- and SCN- by H2O2 to generate the powerful oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) respectively. thiocyanate 44-47 myeloperoxidase Homo sapiens 0-3 19968966-1 2010 The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions. thiocyanate 272-275 myeloperoxidase Homo sapiens 27-42 19968966-1 2010 The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions. thiocyanate 272-275 myeloperoxidase Homo sapiens 44-47 21884783-0 2011 High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase. thiocyanate 12-23 myeloperoxidase Homo sapiens 94-109 21884783-2 2011 We hypothesized that smokers would have a high level of thiocyanate (SCN(-)), a preferred substrate for MPO, which in turn would predispose to thiol oxidation, an established independent risk factor for atherosclerosis. thiocyanate 56-67 myeloperoxidase Homo sapiens 104-107 20085320-1 2010 Thiocyanate reacts noncatalytically with myeloperoxidase-derived HOCl to produce hypothiocyanite (OSCN(-)), thereby potentially limiting the propensity of HOCl to inflict host tissue damage that can lead to inflammatory diseases. thiocyanate 0-11 myeloperoxidase Homo sapiens 41-56