hypochlorous acid has been researched along with heme in 20 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (5.00) | 18.2507 |
2000's | 4 (20.00) | 29.6817 |
2010's | 13 (65.00) | 24.3611 |
2020's | 2 (10.00) | 2.80 |
Authors | Studies |
---|---|
Anderson, MM; Hazen, SL; Heinecke, JW; Hsu, FF | 1 |
Exner, M; Gmeiner, B; Hartmann, B; Hermann, M; Hofbauer, R; Kapiotis, S | 1 |
Campa, A; Catalani, LH; Kettle, AJ; Maghzal, GJ; Rodrigues, MR; Silva, SO; Ximenes, VF | 1 |
Bottle, SE; Davies, MJ; Fairfull-Smith, KE; Malle, E; Rees, MD; Whitelock, JM | 1 |
Banerjee, S; Calisto, BM; Carpena, X; Fita, I; Furtmüller, PG; Obinger, C; Rovira, C; Schroettner, K; Soudi, M; Stampler, J; Vidossich, P | 1 |
Davies, MJ; Pattison, DI; Szuchman-Sapir, AJ; Witting, PK | 1 |
Abdulhamid, I; Abu-Soud, HM; Andreana, PR; Byun, J; Diamond, MP; Maitra, D; Pennathur, S; Saed, GM | 2 |
Bai, YP; Cao, ZH; Cheng, G; Hu, CP; Li, YJ; Peng, J; Shi, RZ; Yang, TL; Yuan, Q; Zhang, GG | 1 |
Abu-Soud, HM; Diamond, MP; Maitra, D; Moura, AA; Pennathur, S; Saed, GM; Souza, CE | 1 |
Abdulhamid, I; Abu-Soud, HM; Diamond, MP; Maitra, D; Saed, GM | 1 |
Banasiak, E; Gebicka, L | 1 |
Cao, Z; Cheng, G; Li, H; Thannickal, VJ; Zhang, G | 1 |
Abdulhamid, I; Abdulridha, RM; Abu-Soud, HM; Diamond, MP; Maitra, D; Pennathur, S; Saed, GM; Shaeib, F | 1 |
Abdulhamid, I; Abu-Soud, HM; Andreana, PR; Byun, J; Diamond, MP; Khan, SN; Maitra, D; Pennathur, S; Saed, GM; Shaeib, F; Yang, Z | 1 |
Abdulhamid, I; Abu-Soud, HM; Ali, I; Khan, SN; Maitra, D; Najafi, T; Pennathur, S; Saed, GM; Shaeib, F | 1 |
Li, J; Lu, N; Peng, YY; Ren, X; Tian, R | 1 |
Gebicka, L; Krych-Madej, J | 1 |
Abu-Soud, HM; Awonuga, A; Bai, D; Camp, OG; Goud, PT | 1 |
Honda, K; Imai, T; Kawamoto, J; Mihara, H; Tanaka, M; Tobe, R | 1 |
20 other study(ies) available for hypochlorous acid and heme
Article | Year |
---|---|
Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. A mechanism for the generation of highly reactive alpha-hydroxy and alpha,beta-unsaturated
Topics: Acetaldehyde; Acrolein; Aldehydes; Amino Acids; Catalase; Chlorides; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Heme; Humans; Hydrogen Peroxide; Hydroxy Acids; Hypochlorous Acid; Inflammation; Lysine; Mass Spectrometry; Molecular Structure; Neutrophil Activation; Neutrophils; Oxidation-Reduction; Peroxidase; Serine; Threonine | 1997 |
Thiocyanate catalyzes myeloperoxidase-initiated lipid oxidation in LDL.
Topics: Antioxidants; Apoproteins; Ascorbic Acid; Azoles; Catalase; Catalysis; Chlorides; Cyclooxygenase Inhibitors; Dose-Response Relationship, Drug; Female; Free Radicals; Heme; Humans; Hydrogen Peroxide; Hypochlorous Acid; Isoindoles; Lipid Metabolism; Lipid Peroxidation; Lipids; Lipoproteins, LDL; Male; Neutrophils; Nitrites; Organoselenium Compounds; Oxygen; Peroxidase; Phagocytes; Phagocytosis; Risk Factors; Smoking; Thiocyanates; Time Factors; Ultracentrifugation | 2004 |
Superoxide-dependent oxidation of melatonin by myeloperoxidase.
Topics: Animals; Antioxidants; Catalase; Catalysis; Cattle; Chromatography, High Pressure Liquid; Chromatography, Liquid; Dimerization; Dose-Response Relationship, Drug; Free Radicals; Heme; Humans; Hydrogen Peroxide; Hydroxyl Radical; Hypochlorous Acid; Kynuramine; Liver; Mass Spectrometry; Melatonin; Models, Chemical; Neutrophils; Oxygen; Ozone; Peroxidase; Protein Binding; Superoxides; Taurine; Time Factors; Xanthine Oxidase | 2005 |
Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides.
Topics: Heme; Humans; Hydroxylamines; Hypochlorous Acid; Molecular Sequence Data; Neutrophils; Nitrogen Oxides; Oxidation-Reduction; Peroxidase | 2009 |
Essential role of proximal histidine-asparagine interaction in mammalian peroxidases.
Topics: Asparagine; Cell Line; Chlorides; Crystallography, X-Ray; Glycosylation; Heme; Histidine; Humans; Hypochlorous Acid; Lactoperoxidase; Leukocytes; Mutation, Missense; Oxidation-Reduction; Peroxidase; Protein Processing, Post-Translational; Protein Structure, Tertiary | 2009 |
Site-specific hypochlorous acid-induced oxidation of recombinant human myoglobin affects specific amino acid residues and the rate of cytochrome b5-mediated heme reduction.
Topics: Amino Acids; Cytochromes b5; Heme; Humans; Hypochlorous Acid; Iron; Myoglobin; Oxidation-Reduction; Recombinant Proteins | 2010 |
Mechanism of hypochlorous acid-mediated heme destruction and free iron release.
Topics: Chromatography, High Pressure Liquid; Heme; Hypochlorous Acid; Iron; Spectrometry, Mass, Electrospray Ionization | 2011 |
Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release.
Topics: Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Heme; Hemoglobins; Hypochlorous Acid; Iron; Mass Spectrometry; Spectrometry, Fluorescence | 2011 |
Role of VPO1, a newly identified heme-containing peroxidase, in ox-LDL induced endothelial cell apoptosis.
Topics: Acetophenones; Apoptosis; Caspase 3; Cell Line; Endothelium, Vascular; Gene Expression Regulation; Heme; Humans; Hypochlorous Acid; Imidazoles; Lipoproteins, LDL; Membrane Glycoproteins; NADPH Oxidase 2; NADPH Oxidases; p38 Mitogen-Activated Protein Kinases; Peroxidases; Phosphorylation; Pyridines; Reactive Oxygen Species; RNA, Small Interfering; Signal Transduction | 2011 |
Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases.
Topics: Animals; Biocatalysis; Cattle; Chromatography, High Pressure Liquid; Fluorescence; Heme; Hypochlorous Acid; Inflammation; Iron; Kinetics; Lactoperoxidase; Models, Biological; Organ Specificity; Protein Structure, Quaternary; Spectrum Analysis; Thiocyanates | 2011 |
Melatonin attenuates hypochlorous acid-mediated heme destruction, free iron release, and protein aggregation in hemoglobin.
Topics: Electrophoresis, Polyacrylamide Gel; Heme; Hemoglobins; Hypochlorous Acid; Iron; Melatonin; Oxidative Stress; Peroxidase; Spectrophotometry | 2012 |
Hypochlorous acid-induced heme damage of hemoglobin and its inhibition by flavonoids.
Topics: Animals; Cattle; Flavonoids; Heme; Hypochlorous Acid; Methemoglobin; Oxidants; Oxyhemoglobins; Protective Agents | 2012 |
Vascular peroxidase 1 catalyzes the formation of hypohalous acids: characterization of its substrate specificity and enzymatic properties.
Topics: Biocatalysis; Bromates; Heme; Humans; Hydrogen Peroxide; Hypochlorous Acid; Kinetics; Oxidation-Reduction; Peroxidase; Peroxidases; Substrate Specificity; Taurine; Thiocyanates | 2012 |
Myeloperoxidase acts as a source of free iron during steady-state catalysis by a feedback inhibitory pathway.
Topics: Catalysis; Chlorides; Feedback, Physiological; Ferrozine; Free Radicals; Heme; Humans; Hydrogen Peroxide; Hypochlorous Acid; Inflammation; Iron; Kinetics; Metabolic Networks and Pathways; Oxidation-Reduction; Peroxidase | 2013 |
Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid.
Topics: Biocatalysis; Chromatography, Liquid; Heme; Humans; Hypochlorous Acid; Oxidative Stress; Peptides; Peroxidases; Spectrometry, Mass, Electrospray Ionization | 2014 |
Melatonin prevents myeloperoxidase heme destruction and the generation of free iron mediated by self-generated hypochlorous acid.
Topics: Catalysis; Enzyme Activation; Heme; Humans; Hydrogen Peroxide; Hypochlorous Acid; Iron; Leukocytes; Melatonin; Oxidation-Reduction; Peroxidase | 2015 |
Nitrite attenuated hypochlorous acid-mediated heme degradation in hemoglobin.
Topics: Animals; Cattle; Heme; Hemoglobins; Hydrogen Peroxide; Hypochlorous Acid; Iron; Nitrites; Oxidation-Reduction; Peroxidases; Protein Structure, Tertiary; Sulfhydryl Compounds | 2015 |
Do pH and flavonoids influence hypochlorous acid-induced catalase inhibition and heme modification?
Topics: Animals; Catalase; Catechin; Cattle; Heme; Hydrogen-Ion Concentration; Hypochlorous Acid; Kinetics; Liver; Quercetin | 2015 |
Hypochlorous acid facilitates inducible nitric oxide synthase subunit dissociation: The link between heme destruction, disturbance of the zinc-tetrathiolate center, and the prevention by melatonin.
Topics: Arginine; Heme; Humans; Hydrogen Peroxide; Hypochlorous Acid; Melatonin; Nitric Oxide; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Oxidoreductases; Oxygenases; Zinc | 2022 |
Group II truncated haemoglobin YjbI prevents reactive oxygen species-induced protein aggregation in
Topics: Bacillus subtilis; Bacterial Proteins; Biofilms; Heme; Hydrogen Peroxide; Hypochlorous Acid; Membrane Proteins; Oxidoreductases; Peroxidases; Phenylalanine; Protein Aggregates; Serum Albumin, Bovine; Truncated Hemoglobins; Water | 2022 |