Hypochlorous Acid Chemistry in Mammalian Cells—Influence on Infection and Role in Various Pathologies

Matrix Metalloproteinases: Regulators of the Tumor Microenvironment

Kessenbrock, K., Plaks, V., & Werb, Z. (2010) · Cell · doi:10.1016/j.cell.2010.03.015 · Cited by 5,151 · see citing works

Tissue Destruction by Neutrophils

Epstein, F. H., & Weiss, S. J. (1989) · New England Journal of Medicine · doi:10.1056/nejm198902093200606 · Cited by 3,950 · see citing works

The Chemistry of Reactive Oxygen Species (ROS) Revisited: Outlining Their Role in Biological Macromolecules (DNA, Lipids and Proteins) and Induced Pathologies

Juan, C. A., Pérez de la Lastra, J. M., Plou, F. J., & Pérez-Lebeña, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094642 · Cited by 2,810 · see citing works

Inside the Neutrophil Phagosome: Oxidants, Myeloperoxidase, and Bacterial Killing

Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1998) · Blood · doi:10.1182/blood.v92.9.3007.421k47_3007_3017 · Cited by 1,640 · see citing works

DNA Damage Produced by Ionizing Radiation in Mammalian Cells: Identities, Mechanisms of Formation, and Reparability

Ward, J. F. (1988) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60611-x · Cited by 1,499 · see citing works

Damage-associated molecular patterns in inflammatory diseases

Roh, J. S., & Sohn, D. H. (2018) · Immune Network · doi:10.4110/in.2018.18.e27 · Cited by 1,261 · see citing works

Functions of plasmalogen lipids in health and disease

Braverman, N. E., & Moser, A. B. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.05.008 · Cited by 1,082 · see citing works

Protein oxidation and peroxidation

Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952 · see citing works

Myeloperoxidase: Its role for host defense, inflammation, and neutrophil function

Aratani, Y. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.01.004 · Cited by 945 · see citing works

The Acid Ionization Constant of HOCl from 5 to 35°

Morris, J. C. (1966) · The Journal of Physical Chemistry · doi:10.1021/j100884a007 · Cited by 927 · see citing works

Association Between Myeloperoxidase Levels and Risk of Coronary Artery Disease

Zhang, R. (2001) · JAMA · doi:10.1001/jama.286.17.2136 · Cited by 919 · see citing works

Neutrophilic Inflammation in Severe Persistent Asthma

Jatakanon, A., Uasuf, C. G., Maziak, W., Lim, S., Chung, K. F., & Barnes, P. J. (1999) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.160.5.9806170 · Cited by 845 · see citing works

Absolute Rate Constants for the Reaction of Hypochlorous Acid with Protein Side Chains and Peptide Bonds

Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790 · see citing works

Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite

van der Vliet, A., Eiserich, J. P., Halliwell, B., & Cross, C. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7617 · Cited by 780 · see citing works

Inflammation and cancer: role of phagocyte-generated oxidants in carcinogenesis

Weitzman, S., & Gordon, L. I. (1990) · Blood · doi:10.1182/blood.v76.4.655.655 · Cited by 761 · see citing works

Protein carbamylation links inflammation, smoking, uremia and atherogenesis

Wang, Z., Nicholls, S. J., Rodríguez, E. R., Kummu, O., Hörkkö, S., Barnard, J., Reynolds, W. F., Topol, E. J., DiDonato, J. A., & Hazen, S. L. (2007) · Nature Medicine · doi:10.1038/nm1637 · Cited by 706 · see citing works

Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase

Eiserich, J. P., Baldus, S. E., Brennan, M., Ma, W., Zhang, C., Tousson, A., Castro, L., Lusis, A. J., Nauseef, W. M., White, C. R., et al. (2002) · Science · doi:10.1126/science.1106830 · Cited by 685 · see citing works

Myeloperoxidase: a key regulator of neutrophil oxidant production

Kettle, A. J., & Winterbourn, C. C. (1997) · Redox Report · doi:10.1080/13510002.1997.11747085 · Cited by 660 · see citing works

Oxidative Stress: Concept and Some Practical Aspects

Sies, H. (2020) · Antioxidants · doi:10.3390/antiox9090852 · Cited by 652 · see citing works

Modeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome

Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 633 · see citing works

Generation and Biological Activities of Oxidized Phospholipids

Bochkov, V. N., Oskolkova, O., Birukov, K. G., Levonen, A., Binder, C. J., & Stöckl, J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2597 · Cited by 611 · see citing works

Hypochlorite-induced oxidation of amino acids, peptides and proteins

Hawkins, C. L., Pattison, D. I., & Davies, M. J. (2003) · Amino Acids · doi:10.1007/s00726-003-0016-x · Cited by 600 · see citing works

Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications

Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 556 · see citing works

Taurine and Inflammatory Diseases

Marcinkiewicz, J., & Kontny, E. (2014) · Amino Acids · doi:10.1007/s00726-012-1361-4 · Cited by 531 · see citing works

Quantification of protein modification by oxidants

Hawkins, C. L., Morgan, P. E., & Davies, M. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.007 · Cited by 486 · see citing works

Myeloperoxidase – A bridge linking inflammation and oxidative stress with cardiovascular disease

Ndrepepa, G. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.02.022 · Cited by 452 · see citing works

Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase.

Albrich, J. M., McCarthy, C. A., & Hurst, J. K. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.1.210 · Cited by 442 · see citing works

Detection, identification, and quantification of oxidative protein modifications

Hawkins, C. L., & Davies, M. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006217 · Cited by 435 · see citing works

Sulfenic acid chemistry, detection and cellular lifetime

Gupta, V., & Carroll, K. S. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.040 · Cited by 427 · see citing works

Myeloperoxidase as an Active Disease Biomarker: Recent Biochemical and Pathological Perspectives

Khan, A. A., Alsahli, M. A., & Rahmani, A. H. (2018) · Medical Sciences · doi:10.3390/medsci6020033 · Cited by 419 · see citing works

A Highly Specific Fluorescent Probe for Hypochlorous Acid and Its Application in Imaging Microbe-Induced HOCl Production

Xu, Q., Lee, K.-A., Lee, S., Lee, K., Lee, W., & Yoon, J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja404649m · Cited by 418 · see citing works

Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention

Davies, M. J. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.11-006fr · Cited by 412 · see citing works

Myeloperoxidase: a target for new drug development?

Malle, E., Furtmüller, P. G., Sattler, W., & Obinger, C. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707358 · Cited by 411 · see citing works

Thiocyanate and chloride as competing substrates for myeloperoxidase

van DALEN, J. C., WHITEHOUSE, W. M., WINTERBOURN, C. C., & KETTLE, J. A. (1997) · Biochemical Journal · doi:10.1042/bj3270487 · Cited by 406 · see citing works

Oxidation of LDL by Myeloperoxidase and Reactive Nitrogen Species

Carr, A. C., McCall, M. R., & Frei, B. B. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.7.1716 · Cited by 392 · see citing works

Biomarkers of myeloperoxidase-derived hypochlorous acid

Winterbourn, C. C., & Kettle, A. J. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00204-5 · Cited by 390 · see citing works

Serum Myeloperoxidase Levels Independently Predict Endothelial Dysfunction in Humans

Vita, J. A., Brennan, M., Gokce, N., Mann, S. A., Goormastic, M., Shishehbor, M. H., Penn, M. S., Keaney, J. F., & Hazen, S. L. (2004) · Circulation · doi:10.1161/01.cir.0000140262.20831.8f · Cited by 366 · see citing works

Reactions of Myeloperoxidase-Derived Oxidants with Biological Substrates:Gaining Chemical Insight into Human Inflammatory Diseases

Pattison, D. I., & Davies, M. J. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706778773095 · Cited by 359 · see citing works

Kinetics and Mechanisms of Hypochlorous Acid Reactions

Folkes, L. K., Candeias, L. P., & Wardman, P. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.0017 · Cited by 358 · see citing works

Myeloperoxidase acts as a profibrotic mediator of atrial fibrillation

Rudolph, V., Andrié, R., Rudolph, T. K., Friedrichs, K. P., Klinke, A., Hirsch-Hoffmann, B., Schwoerer, A. P., Lau, D., Fu, X., Klingel, K., et al. (2010) · Nature Medicine · doi:10.1038/nm.2124 · Cited by 352 · see citing works

[40] Preparation and characterization of chloramines

Thomas, E. L., Grisham, M. B., & Jefferson, M. M. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)32042-1 · Cited by 348 · see citing works

Plasma Concentrations of Myeloperoxidase Predict Mortality After Myocardial Infarction

Mocatta, T. J., Pilbrow, A. P., Cameron, V. A., Senthilmohan, R., Frampton, C. M., Richards, M., & Winterbourn, C. C. (2007) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2007.02.040 · Cited by 344 · see citing works

Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate

Peskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 338 · see citing works

Neuronal expression of myeloperoxidase is increased in Alzheimer's disease

Green, P. S., Mendez, A. J., Jacob, J. S., Crowley, J. R., Growdon, W., Hyman, B. T., & Heinecke, J. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02527.x · Cited by 332 · see citing works

The Role of Myeloperoxidase in Biomolecule Modification, Chronic Inflammation, and Disease

Davies, M. J., & Hawkins, C. L. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8030 · Cited by 332 · see citing works

Chlorination of Tyrosyl Residues in Peptides by Myeloperoxidase and Human Neutrophils

Domigan, N. M., Charlton, T. S., Duncan, M. W., Winterbourn, C. C., & Kettle, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16542 · Cited by 329 · see citing works

Oxidative and nitrosative events in asthma

Andreadis, A. A., Hazen, S. L., Comhair, S. A. A., & Erzurum, S. C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00278-8 · Cited by 327 · see citing works

Hypochlorous Acid Interactions with Thiols, Nucleotides, DNA, and Other Biological Substrates

Prütz, W. A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0322 · Cited by 327 · see citing works

Glutathione redox cycle protects cultured endothelial cells against lysis by extracellularly generated hydrogen peroxide.

Harlan, J. M., Levine, J. D., Callahan, K. S., Schwartz, B. R., & Harker, L. A. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111263 · Cited by 326 · see citing works

Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation

Hawkins, C. L., & Davies, M. J. (1998) · Biochemical Journal · doi:10.1042/bj3320617 · Cited by 305 · see citing works

Constitutive and inducible nitric oxide synthases incorporate molecular oxygen into both nitric oxide and citrulline.

Leone, A., Palmer, R. M. J., Knowles, R. G., Francis, P. L., Ashton, D., & Moncada, S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54352-0 · Cited by 290 · see citing works

Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis

Nagra, R. M., Becher, B., Tourtellotte, W. W., Antel, J. P., Gold, D. P., Paladino, T., Smith, R. A., Nelson, J. R., & Reynolds, W. F. (1997) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00089-1 · Cited by 284 · see citing works

Ablation of the Inflammatory Enzyme Myeloperoxidase Mitigates Features of Parkinson's Disease in Mice

Choi, D., Pennathur, S., Perier, C., Tieu, K., Teismann, P., Wu, D.-C., Jackson-Lewis, V. R., Vila, M., Vonsattel, J., Heinecke, J. W., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0970-05.2005 · Cited by 284 · see citing works

Targeting Myeloperoxidase (MPO) Mediated Oxidative Stress and Inflammation for Reducing Brain Ischemia Injury: Potential Application of Natural Compounds

Chen, S., Chen, H., Du, Q., & Shen, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00433 · Cited by 282 · see citing works

Myeloperoxidase in human neutrophil host defence

Nauseef, W. M. (2014) · Cellular Microbiology · doi:10.1111/cmi.12312 · Cited by 276 · see citing works

Myeloperoxidase in the inflamed colon: A novel target for treating inflammatory bowel disease

Chami, B., Martin, N., Dennis, J. M., & Witting, P. K. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.03.012 · Cited by 273 · see citing works

Chlorohydrin Formation From Unsaturated Fatty Acids Reacted With Hypochlorous Acid

Winterbourn, C. C., van den Berg, J. J. M., Roitman, E., & Kuypers, F. A. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90609-z · Cited by 258 · see citing works

The Role of Formylated Peptides and Formyl Peptide Receptor 1 in Governing Neutrophil Function during Acute Inflammation

Dorward, D. A., Lucas, C. D., Chapman, G. B., Haslett, C., Dhaliwal, K., & Rossi, A. G. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.01.020 · Cited by 258 · see citing works

Human neutrophils employ chlorine gas as an oxidant during phagocytosis.

Hazen, S. L., Hsu, F., Mueller, D. M., Crowley, J., & Heinecke, J. W. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118914 · Cited by 258 · see citing works

Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli

Thomas, E. L. (1979) · Infection and Immunity · doi:10.1128/iai.23.2.522-531.1979 · Cited by 251 · see citing works

Independent evolution of four heme peroxidase superfamilies

Zámocký, M., Hofbauer, S., Schaffner, I., Gasselhuber, B., Nicolussi, A., Soudi, M., Pirker, K. F., Furtmüller, P. G., & Obinger, C. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.12.025 · Cited by 248 · see citing works

Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid

Winterbourn, C. C. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00286-x · Cited by 247 · see citing works

The effects of neutrophil-generated hypochlorous acid and other hypohalous acids on host and pathogens

Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239 · see citing works

Hypochlorous acid as a potential wound care agent: part I. Stabilized hypochlorous acid: a component of the inorganic armamentarium of innate immunity.

Wang, L., Bassiri, M., Najafi, R., Najafi, K. H. B. R. M. A. N. R., Yang, J., Khosrovi, B., Hwong, W., Barati, E., Belisle, B., Celeri, C., et al. (2007) · PubMed Central · Cited by 237 · see citing works

Effect of the myeloperoxidase inhibitor AZD3241 on microglia: a PET study in Parkinson’s disease

Jučaitė, A., Svenningsson, P., Rinne, J. O., Cselényi, Z., Varnäs, K., Johnström, P., Amini, N., Kirjavainen, A. K., Helin, S., Minkwitz, M. C., et al. (2015) · Brain · doi:10.1093/brain/awv184 · Cited by 224 · see citing works

Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols

Hazen, S. L., Hsu, F. F., Duffin, K., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23080 · Cited by 221 · see citing works

Taurine and its chloramine: Modulators of immunity

Schuller-Levis, G. B., & Park, E. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000010440.37629.17 · Cited by 219 · see citing works

Myeloperoxidase, modified lipoproteins, and atherogenesis

Nicholls, S. J., & Hazen, S. L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800086-jlr200 · Cited by 209 · see citing works

Myeloperoxidase and protein oxidation in cystic fibrosis

van der Vliet, A., Nguyen, M. N., Shigenaga, M. K., Eiserich, J. P., Marelich, G. P., & Cross, C. E. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.3.l537 · Cited by 203 · see citing works

Reprint of Neutrophil cell surface receptors and their intracellular signal transduction pathways

Futosi, K., Fodor, S., & Mócsai, A. (2013) · International Immunopharmacology · doi:10.1016/j.intimp.2013.11.010 · Cited by 198 · see citing works

Surviving Reactive Chlorine Stress: Responses of Gram-Negative Bacteria to Hypochlorous Acid

Nizer, W. S. D. C., Inkovskiy, V., & Overhage, J. (2020) · Microorganisms · doi:10.3390/microorganisms8081220 · Cited by 196 · see citing works

Reactive nitrogen intermediates and antimicrobial activity: Role of nitrite

Klebanoff, S. J. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90084-8 · Cited by 192 · see citing works

Myeloperoxidase Delays Neutrophil Apoptosis Through CD11b/CD18 Integrins and Prolongs Inflammation

Kebir, D. E., József, L., Pan, W., & Filep, J. G. (2008) · Circulation Research · doi:10.1161/01.res.0000326772.76822.7a · Cited by 191 · see citing works

Neutrophils convert tyrosyl residues in albumin to chlorotyrosine

Kettle, A. J. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01494-2 · Cited by 188 · see citing works

Myeloperoxidase: An Oxidative Pathway for Generating Dysfunctional High-Density Lipoprotein

Shao, B., Oda, M. N., Oram, J. F., & Heinecke, J. W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx9003775 · Cited by 185 · see citing works

The inhibition of bacterial growth by hypochlorous acid. Possible role in the bactericidal activity of phagocytes

McKenna, S. M., & Davies, K. J. A. (1988) · Biochemical Journal · doi:10.1042/bj2540685 · Cited by 183 · see citing works

Myeloperoxidase attracts neutrophils by physical forces

Klinke, A., Nußbaum, C., Kubala, L., Friedrichs, K. P., Rudolph, T. K., Rudolph, V., Paust, H., Schröder, C., Benten, D., Lau, D., et al. (2010) · Blood · doi:10.1182/blood-2010-05-284513 · Cited by 179 · see citing works

Myeloperoxidase: Expressing Inflammation and Oxidative Stress in Cardiovascular Disease

Anatoliotakis, N., Deftereos, S. G., Bouras, G., Γιαννόπουλος, Γ., Tsounis, D., Angelidis, C., Kaoukis, A., & Stefanadis, C. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611313020004 · Cited by 173 · see citing works

Radical formation during the peroxidase catalyzed metabolism of carcinogens and xenobiotics: The reactivity of these radicals with GSH, DNA, and unsaturated lipid

O'Brien, P. J. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90025-1 · Cited by 166 · see citing works

Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach

Storkey, C., Davies, M. J., & Pattison, D. I. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.024 · Cited by 165 · see citing works

Oxidants and asthma

Caramori, G. (2004) · Thorax · doi:10.1136/thorax.2002.002477 · Cited by 162 · see citing works

Hypochlorous acid as a precursor of free radicals in living systems

Panasenko, O. M., Gorudko, I. V., & Av, S. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913130075 · Cited by 157 · see citing works

The Reactions of Hypochlorous Acid, the Reactive Oxygen Species Produced by Myeloperoxidase, With Lipids

Spickett, C. M., Jerlich, A., Panasenko, O. M., Arnhold, J., Pitt, A. R., Stelmaszyńska, T., & Schaur, R. J. (2000) · Acta Biochimica Polonica · doi:10.18388/abp.2000_3944 · Cited by 154 · see citing works

Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders

Heinecke, J. W. (1999) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(99)90061-6 · Cited by 150 · see citing works

Myeloperoxidase and Protein Oxidation in the Airways of Young Children with Cystic Fibrosis

Kettle, A. J., Chan, T., Osberg, I. M., Senthilmohan, R., Chapman, A., Mocatta, T. J., & Wagener, J. S. (2004) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200311-1516oc · Cited by 148 · see citing works

Characterization of the oxidation products of the reaction between reduced glutathione and hypochlorous acid

Winterbourn, C. C., & Brennan, S. O. (1997) · Biochemical Journal · doi:10.1042/bj3260087 · Cited by 146 · see citing works

Cholesterol Chlorohydrin Synthesis by the Myeloperoxidase-Hydrogen Peroxide-Chloride System: Potential Markers for Lipoproteins Oxidatively Damaged by Phagocytes

Heinecke, J. W., Li, W., Mueller, D. M., Bohrer, A., & TURK, J. W. (1994) · Biochemistry · doi:10.1021/bi00199a041 · Cited by 141 · see citing works

Chlorination studies II. The reaction of aqueous hypochlorous acid with α-amino acids and dipeptides

Pereira, W. E., Hoyano, Y., Summons, R. E., Bacon, V. A., & Duffield, A. M. (1973) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(73)90198-0 · Cited by 140 · see citing works

Myeloperoxidase-immunoreactive cells are significantly increased in brain areas affected by neurodegeneration in Parkinson’s and Alzheimer’s disease

Gellhaar, S., Sunnemark, D., Eriksson, H., Olson, L., & Galter, D. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2626-8 · Cited by 139 · see citing works

Oxidation of aliphatic amines by aqueous chlorine

ABIA, L., Armesto, X. L., Canle, M., García, M. V., & Santaballa, J. A. (1998) · Tetrahedron · doi:10.1016/s0040-4020(97)10312-x · Cited by 139 · see citing works

Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin?

Segelmark, M., PERSSON, B., Hellmark, T., & Wieslander, J. (1997) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.1997.d01-992.x · Cited by 138 · see citing works

Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid

Vissers, M. C. M., & Winterbourn, C. C. (1995) · Biochemical Journal · doi:10.1042/bj3070057 · Cited by 131 · see citing works

N-chlorotaurine, a natural antiseptic with outstanding tolerability

Gottardi, W., & Nagl, M. (2010) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkp466 · Cited by 131 · see citing works

Aqueous chemistry of N-halo-compounds

Armesto, X. L., Canle, M., García, M. V., & Santaballa, J. A. (1998) · Chemical Society Reviews · doi:10.1039/a827453z · Cited by 130 · see citing works

Flavonoids as Substrates and Inhibitors of Myeloperoxidase: Molecular Actions of Aglycone and Metabolites

Shiba, Y., Kinoshita, T., Chuman, H., Taketani, Y., Takeda, E., Kato, Y., Naito, M., Kawabata, K., Ishisaka, A., Terao, J., et al. (2008) · Chemical Research in Toxicology · doi:10.1021/tx8000835 · Cited by 129 · see citing works

Elevated myeloperoxidase activity in white matter in multiple sclerosis

Gray, E., Thomas, T. L., Betmouni, S., Scolding, N. J., & Love, S. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.08.035 · Cited by 125 · see citing works

Chlorination of Cholesterol in Cell Membranes by Hypochlorous Acid

Carr, A. C., van den Berg, J. J. M., & Winterbourn, C. C. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0317 · Cited by 124 · see citing works

What really happens in the neutrophil phagosome?

Hurst, J. K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.008 · Cited by 124 · see citing works

Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride

Senthilmohan, R., & Kettle, A. J. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.005 · Cited by 122 · see citing works

Degradation of Hyaluronic Acid, Poly- and Mono-Saccharides, and Model Compounds by Hypochlorite: Evidence for Radical Intermediates and Fragmentation

Hawkins, C. L., & Davies, M. J. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00009-4 · Cited by 122 · see citing works

Physiological effects of oxidized phospholipids and their cellular signaling mechanisms in inflammation

Greig, F. H., Kennedy, S., & Spickett, C. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.481 · Cited by 122 · see citing works

Interactions of Hypochlorous Acid with Pyrimidine Nucleotides, and Secondary Reactions of Chlorinated Pyrimidines with GSH, NADH, and Other Substrates

Prütz, W. A. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0440 · Cited by 121 · see citing works

Structure and function of phosphatidylcholine transfer protein (PC-TP)/StarD2

Kanno, K., Wu, M. K., Scapa, E. F., Roderick, S. L., & Cohen, D. E. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.04.003 · Cited by 121 · see citing works

Myeloperoxidase: Bridging the gap in neurodegeneration

Ray, R. S., & Katyal, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.06.031 · Cited by 114 · see citing works

Iodine status and thyroid function of Boston-area vegetarians and vegans

Leung, A. M., LaMar, A., He, X., Braverman, L. E., & Pearce, E. N. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2011-0256 · Cited by 113 · see citing works

Oxidative Biomarkers in the Diagnosis and Prognosis of Cardiovascular Disease

Tsimikas, S. (2006) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2006.09.015 · Cited by 111 · see citing works

Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase

Furtmüller, P. G., Arnhold, J., Jantschko, W., Pichler, H., & Obinger, C. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)03075-9 · Cited by 109 · see citing works

Generation of Intramolecular and Intermolecular Sulfenamides, Sulfinamides, and Sulfonamides by Hypochlorous Acid: A Potential Pathway for Oxidative Cross-Linking of Low-Density Lipoprotein by Myeloperoxidase

Fu, X., Mueller, D. M., & Heinecke, J. W. (2001) · Biochemistry · doi:10.1021/bi015777z · Cited by 107 · see citing works

p-Hydroxyphenylacetaldehyde Is the Major Product of L-Tyrosine Oxidation by Activated Human Phagocytes

Hazen, S. L., Hsu, F., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.1861 · Cited by 106 · see citing works

Hypochlorous Acid-Mediated Modification of Proteins and its Consequences

Hawkins, C. L. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190045 · Cited by 106 · see citing works

Inhibition of myeloperoxidase oxidant production by N-acetyl lysyltyrosylcysteine amide reduces brain damage in a murine model of stroke

Yu, G., Liang, Y. S., Huang, Z., Jones, D. W., Pritchard, K. A., & Zhang, H. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0583-x · Cited by 103 · see citing works

Reactions of Hypochlorous Acid with Tyrosine and Peptidyl-tyrosyl Residues Give Dichlorinated and Aldehydic Products in Addition to 3-Chlorotyrosine

Fu, S., Wang, H., Davies, M. J., & Dean, R. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10851 · Cited by 102 · see citing works

Myeloperoxidase modulates lung epithelial responses to pro-inflammatory agents

Haegens, A., Vernooy, J. H. J., Heeringa, P., Mossman, B. T., & Wouters, E. F. �. (2007) · European Respiratory Journal · doi:10.1183/09031936.00029307 · Cited by 102 · see citing works

Myeloperoxidase-derived Hypochlorous Acid Antagonizes the Oxidative Stress-mediated Activation of Iron Regulatory Protein 1

Mütze, S., Hebling, U., Stremmel, W., Wang, J., Arnhold, J., Pantopoulos, K., & Mueller, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307159200 · Cited by 101 · see citing works

Role of Myeloperoxidase in Patients with Chronic Kidney Disease

Kisić, B., Miric, D. J., Dragojević, I. M., Rašić, J., & Popović, L. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1069743 · Cited by 101 · see citing works

Investigation of protein oxidation and lipid peroxidation in patients with rheumatoid arthritis

Başkol, G., Demir, H., Başkol, M., Kılıç, E., Ates, F., Karakükçü, Ç., & Üstdal, M. (2005) · Cell Biochemistry and Function · doi:10.1002/cbf.1257 · Cited by 95 · see citing works

Hypochlorite-Mediated Fragmentation of Hyaluronan, Chondroitin Sulfates, and RelatedN-Acetyl Glycosamines: Evidence for Chloramide Intermediates, Free Radical Transfer Reactions, and Site-Specific Fragmentation

Rees, M. D., Hawkins, C. L., & Davies, M. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0370591 · Cited by 95 · see citing works

Myeloperoxidase Inhibitors as Potential Drugs

Pašti, T. D. L., Leskovac, A. R., & Vasić, V. (2015) · Current Drug Metabolism · doi:10.2174/138920021603150812120640 · Cited by 95 · see citing works

Hypochlorite-Induced Damage to Nucleosides: Formation of Chloramines and Nitrogen-Centered Radicals

Hawkins, C. L., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx010071r · Cited by 94 · see citing works

MPO (Myeloperoxidase) Reduces Endothelial Glycocalyx Thickness Dependent on Its Cationic Charge

Manchanda, K., Kolářová, H., Kerkenpaß, C., Mollenhauer, M., Víteček, J., Rudolph, V., Kubala, L., Baldus, S. E., Adam, M., & Klinke, A. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311143 · Cited by 94 · see citing works

Einige neue Bestandtheile der Galle des Ochsen

Tiedemann, F., & Gmelin, L. (1827) · Annalen der Physik · doi:10.1002/andp.18270850214 · Cited by 93 · see citing works

Myeloperoxidase and Neurological Disorder: A Crosstalk

Pravalika, K., Sarmah, D., Kaur, H., Wanve, M., Saraf, J., Kalia, K., Borah, A., Yavagal, D. R., Dave, K. R., & Bhattacharya, P. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00462 · Cited by 91 · see citing works

Metabolic activation of phenol by human myeloperoxidase and horseradish peroxidase.

Eastmond, D. A., Smith, M. T., Ruzo, L. O., & Ross, D. (1986) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10412-4 · Cited by 90 · see citing works

The Role of Neutrophil Myeloperoxidase in Models of Lung Tumor Development

Rymaszewski, A. L., Tate, E. R., Yimbesalu, J., Gelman, A. E., Jarzembowski, J. A., Zhang, H., Pritchard, K. A., & Vikis, H. G. (2014) · Cancers · doi:10.3390/cancers6021111 · Cited by 88 · see citing works

Ability of Hypochlorous Acid and N-Chloramines to Chlorinate DNA and Its Constituents

Stanley, N., Pattison, D. I., & Hawkins, C. L. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100188b · Cited by 88 · see citing works

The Myeloperoxidase-Derived Oxidant HOSCN Inhibits Protein Tyrosine Phosphatases and Modulates Cell Signalling via the Mitogen-Activated Protein Kinase (MAPK) Pathway in Macrophages

Lane, A. E., Tan, J. T. M., Hawkins, C. L., Heather, A. K., & Davies, M. J. (2010) · Biochemical Journal · doi:10.1042/bj20100082 · Cited by 86 · see citing works

l-Arginine Chlorination Products Inhibit Endothelial Nitric Oxide Production

Zhang, C., Reiter, C., Eiserich, J. P., Boersma, B. J., Parks, D. A., Beckman, J. S., Barnes, S., KIRK, M. C., Baldus, S. E., Darley-Usmar, V. M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100191200 · Cited by 86 · see citing works

Lipid oxidation by hypochlorous acid: chlorinated lipids in atherosclerosis and myocardial ischemia

Ford, D. A. (2010) · Clinical Lipidology · doi:10.2217/clp.10.68 · Cited by 85 · see citing works

Chlorinative Stress in Age-Related Diseases: A Literature Review

Casciaro, M., Di Salvo, E., Pace, E., Ventura-Spagnolo, E., Navarra, M., & Gangemi, S. (2017) · Immunity & Ageing · doi:10.1186/s12979-017-0104-5 · Cited by 85 · see citing works

Formation of lysophospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid

Arnhold, J., Osipov, A. N., Spalteholz, H., Panasenko, O. M., & Schiller, J. (2002) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00271-4 · Cited by 82 · see citing works

Inhibition of myeloperoxidase activity by the alkaloids of Peganum harmala L. (Zygophyllaceae)

Bensalem, S., Soubhye, J., Aldib, I., Bournine, L., Nguyen, A. T., Vanhaeverbeek, M., Rousseau, A., Boudjeltia, K. Z., Sarakbi, A., Kauffmann, J. M., et al. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.03.070 · Cited by 81 · see citing works

Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid

Lloyd, M. M., van Reyk, D. M., Davies, M. J., & Hawkins, C. L. (2008) · Biochemical Journal · doi:10.1042/bj20080468 · Cited by 79 · see citing works

Intrinsic mutagenic properties of 5-chlorocytosine: A mechanistic connection between chronic inflammation and cancer

Fedeles, B. I., Freudenthal, B., Yau, E., Singh, V., Chang, S.-C., Li, D., Delaney, J. C., Wilson, S. H., & Essigmann, J. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507709112 · Cited by 79 · see citing works

Hypochlorous Acid-Derived Modification of Phospholipids: Characterization of Aminophospholipids as Regulatory Molecules for Lipid Peroxidation

Kawai, Y., Kiyokawa, H., Kimura, Y., Kato, Y., Tsuchiya, K., & Terao, J. (2006) · Biochemistry · doi:10.1021/bi0610909 · Cited by 78 · see citing works

Myeloperoxidase as an Active Disease Biomarker: Its Recent Biochemical and Pathological PerspectivesPreprint

Khan, A. A., Alsahli, M. A., & Rahmani, A. H. (2018) · Preprints.org · doi:10.20944/preprints201802.0104.v1 · Cited by 78 · see citing works

Neuropathology of HIV/AIDS with an overview of the Indian scene.

Shankar, S. K., Mahadevan, A., Satishchandra, P., Kumar, R. U., Yasha, T. C., Santosh, V., Chandramuki, A., Ravi, V., & Nath, A. (2005) · PubMed · Cited by 77 · see citing works

Myeloperoxidase Mediates Postischemic Arrhythmogenic Ventricular Remodeling

Mollenhauer, M., Friedrichs, K. P., Lange, M., Gesenberg, J., Remane, L., Kerkenpaß, C., Krause, J., Schneider, J., Ravekes, T., Maaß, M., et al. (2017) · Circulation Research · doi:10.1161/circresaha.117.310870 · Cited by 76 · see citing works

Increased Myeloperoxidase Plasma Levels in Patients with Alzheimer's Disease

Tzikas, S., Schlak, D., Sopova, K., Gatsiou, A., Stakos, D., Stamatelopoulos, K. S., Stellos, K., & Laske, C. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131469 · Cited by 75 · see citing works

Myeloperoxidase Deficiency Inhibits Cognitive Decline in the 5XFAD Mouse Model of Alzheimer’s Disease

Volkman, R., Ben‐Zur, T., Kahana, A., Garty, B. Z., & Offen, D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00990 · Cited by 72 · see citing works

Myeloperoxidase aggravates pulmonary arterial hypertension by activation of vascular Rho-kinase

Klinke, A., Berghausen, E. M., Friedrichs, K. P., Molz, S., Lau, D., Remane, L., Berlin, M., Kaltwasser, C., Adam, M., Mehrkens, D., et al. (2018) · JCI Insight · doi:10.1172/jci.insight.97530 · Cited by 71 · see citing works

The development of myeloperoxidase inhibitors

Galijašević, S. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.031 · Cited by 70 · see citing works

Reaction of Sodium Hypochlorite with Nucleic Acids and Their Constituents

Hayatsu, H., Pan, S.-K., & Ukita, T. (1971) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.19.2189 · Cited by 69 · see citing works

Resveratrol Inhibits the Activity of Equine Neutrophil Myeloperoxidase by a Direct Interaction with the Enzyme

Kohnen, S. L., Franck, T. J., Antwerpen, P. V., Boudjeltia, K. Z., Mouithys-Mickalad, A. A., Deby, C. M. T., Moguilevsky, N., Deby-Dupont, G. P., Lamy, M., & Serteyn, D. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf071741n · Cited by 69 · see citing works

Sputum myeloperoxidase in chronic obstructive pulmonary disease

Zhu, A., Ge, D., Zhang, J., Teng, Y., Yuan, C., Huang, M., Adcock, I. M., Barnes, P. J., & Yao, X. (2014) · European journal of medical research · doi:10.1186/2047-783x-19-12 · Cited by 69 · see citing works

On the Irreversible Destruction of Reduced Nicotinamide Nucleotides by Hypohalous Acids

Prütz, W. A., Kissner, R., Koppenol, W. H., & Rüegger, H. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1914 · Cited by 67 · see citing works

Nucleotide chloramines and neutrophil‐mediated cytotoxicity

Bernofsky, C. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.3.1848195 · Cited by 65 · see citing works

Myeloperoxidase Immunohistochemistry as a Measure of Disease Activity in Ulcerative Colitis: Association With Ulcerative Colitis-Colorectal Cancer, Tumor Necrosis Factor Polymorphism and RUNX3 Methylation

Garrity-Park, M. M., Loftus, E. V., Sandborn, W. J., & Smyrk, T. C. (2011) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21681 · Cited by 64 · see citing works

Protection by antibiotics against myeloperoxidase-dependent cytotoxicity to lung epithelial cells in vitro.

Cantin, A. M., & Woods, D. E. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116196 · Cited by 63 · see citing works

Increased myeloperoxidase plasma levels in rheumatoid arthritis

Fernandes, R. M. S. N., da Silva, N. P., & Sato, E. I. (2011) · Rheumatology International · doi:10.1007/s00296-011-1810-5 · Cited by 62 · see citing works

Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide

Drożdż, R., Naskalski, J. W., & Sznajd, J. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90155-0 · Cited by 61 · see citing works

Hyperglycemia and Oxidative Stress Strengthen the Association Between Myeloperoxidase and Blood Pressure

van der Zwan, L., Scheffer, P. G., Dekker, J. M., Stehouwer, C. D. A., Heine, R. J., & Teerlink, T. (2010) · Hypertension · doi:10.1161/hypertensionaha.109.147231 · Cited by 60 · see citing works

Chlorination studies. I. The reaction of aqueous hypochlorous acid with cytosine

Patton, W., Bacon, V. A., Duffield, A. M., Halpern, B., Hoyano, Y., Pereira, W. E., & Lederberg, J. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90690-0 · Cited by 59 · see citing works

Investigating the Role of Myeloperoxidase and Angiopoietin-like Protein 6 in Obesity and Diabetes

Qaddoumi, M. G., Alanbaei, M., Hammad, M. M., Khairi, I. A., Cherian, P., Channanath, A. M., Thanaraj, T. A., Al‐Mulla, F., Abu‐Farha, M., & Abubaker, J. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-63149-7 · Cited by 59 · see citing works

Increased levels of serum myeloperoxidase in patients with active rheumatoid arthritis

Wang, W., Jian, Z., Guo, J., & Ning, X. (2014) · Life Sciences · doi:10.1016/j.lfs.2014.09.012 · Cited by 58 · see citing works

Hypochlorite-induced oxidation of thiols: Formation of thiyl radicals and the role of sulfenyl chlorides as intermediates

Davies, M. J., & Hawkins, C. L. (2000) · Free Radical Research · doi:10.1080/10715760000301241 · Cited by 57 · see citing works

Myeloperoxidase Is Associated with Insulin Resistance and Inflammation in Overweight Subjects with First-Degree Relatives with Type 2 Diabetes Mellitus

Gómez‐García, A., Rodríguez, M. R., Alonso, C. G., Ochoa, D. Y. R., & Aguilar, C. Á. (2015) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2015.39.1.59 · Cited by 56 · see citing works

Oxidation of heparan sulphate by hypochlorite: role of N-chloro derivatives and dichloramine-dependent fragmentation

Rees, M. D., Pattison, D. I., & Davies, M. J. (2005) · Biochemical Journal · doi:10.1042/bj20050630 · Cited by 56 · see citing works

Hypochlorite modification of sphingomyelin generates chlorinated lipid species that induce apoptosis and proteome alterations in dopaminergic PC12 neurons in vitro

Nusshold, C., Kollroser, M., Köfeler, H. C., Rechberger, G. N., Reicher, H., Üllen, A., Bernhart, E. M., Waltl, S., Kratzer, I., Hermetter, A., et al. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.037 · Cited by 53 · see citing works

Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation

Hawkins, C. L., Pattison, D. I., Stanley, N., & Davies, M. J. (2008) · Biochemical Journal · doi:10.1042/bj20070941 · Cited by 53 · see citing works

The role of reactive N-bromo species and radical intermediates in hypobromous acid-induced protein oxidation

Hawkins, C. L., & Davies, M. J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.05.011 · Cited by 52 · see citing works

Consecutive Halogen Transfer between Various Functional Groups Induced by Reaction of Hypohalous Acids: NADH Oxidation by Halogenated Amide Groups

Prütz, W. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1377 · Cited by 52 · see citing works

Status Report on Topical Hypochlorous Acid: Clinical Relevance of Specific Formulations, Potential Modes of Action, and Study Outcomes.

Rosso, J. Q. D., & Bhatia, N. D. (2018) · Europe PMC (PubMed Central) · Cited by 52 · see citing works

Chlorinated Phospholipids and Fatty Acids: (Patho)physiological Relevance, Potential Toxicity, and Analysis of Lipid Chlorohydrins

Schröter, J., & Schiller, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8386362 · Cited by 51 · see citing works

Low-density lipoprotein modified by myeloperoxidase oxidants induces endothelial dysfunction

Abdo, A. I., Rayner, B. S., van Reyk, D. M., & Hawkins, C. L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.08.004 · Cited by 51 · see citing works

4’-Aminochalcones As Novel Inhibitors of the Chlorinating Activity of Myeloperoxidase

Zeraik, M. L., Ximenes, V. F., Regasini, L. O., Dutra, L. A., Silva, D. H. S., da Fonseca, L. M., Coelho, D., Machado, S. A. S., & Bolzani, V. D. S. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712803833344 · Cited by 49 · see citing works

Myeloperoxidase deficiency ameliorates progression of chronic kidney disease in mice

Lehners, A., Lange, S., Niemann, G., Rosendahl, A., Meyer‐Schwesinger, C., Oh, J. S., Stahl, R. A. K., Ehmke, H., Benndorf, R. A., Klinke, A., et al. (2014) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00262.2014 · Cited by 48 · see citing works

Hypochlorous Acid Damages Histone Proteins Forming 3-Chlorotyrosine and 3,5-Dichlorotyrosine

Kang, J. I., & Neidigh, J. W. (2008) · Chemical Research in Toxicology · doi:10.1021/tx7003486 · Cited by 47 · see citing works

Multiple Sclerosis: Myeloperoxidase Immunoradiology Improves Detection of Acute and Chronic Disease in Experimental Model

Pulli, B., Buré, L., Wojtkiewicz, G. R., Iwamoto, Y., Ali, M. Y. J., Li, D., Schob, S., Hsieh, K. L., Jacobs, A. H., & Chen, J. W. (2014) · Radiology · doi:10.1148/radiol.14141495 · Cited by 46 · see citing works

Fragmentation of extracellular matrix by hypochlorous acid

Woods, A. A., & Davies, M. J. (2003) · Biochemical Journal · doi:10.1042/bj20030715 · Cited by 45 · see citing works

Myeloperoxidase inhibition in mice alters atherosclerotic lesion composition

Flach, R. J. R., Su, C., Bollinger, E., Cortes, C., Robertson, A. W., Opsahl, A., Coskran, T., Maresca, K. P., Keliher, E. J., Yates, P. D., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0214150 · Cited by 43 · see citing works

Myeloperoxidase in Chronic Kidney Disease

Rao, A. M., Anand, U., & Anand, C. V. (2010) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-010-0075-1 · Cited by 42 · see citing works

Glutathione revisited: a better scavenger than previously thought

Haenen, G. R. M. M., & Bast, A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00260 · Cited by 42 · see citing works

Cellular targets of the myeloperoxidase-derived oxidant hypothiocyanous acid (HOSCN) and its role in the inhibition of glycolysis in macrophages

Love, D. T., Barrett, T. J., White, M. Y., Cordwell, S. J., Davies, M. J., & Hawkins, C. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.016 · Cited by 41 · see citing works

Pharmacological myeloperoxidase (MPO) inhibition in an obese/hypertensive mouse model attenuates obesity and liver damage, but not cardiac remodeling

Piek, A., Koonen, D. P. Y., Schouten, E., Lindtstedt, E. L., Michaëlsson, E., de Boer, R. A., & Silljé, H. H. W. (2019) · Scientific Reports · doi:10.1038/s41598-019-55263-y · Cited by 41 · see citing works

Mechanisms of Extracellular Matrix Proteoglycan Degradation by Human Neutrophils

McGowan, S. E. (1990) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/2.3.271 · Cited by 39 · see citing works

The Role of Taurine in Skeletal Muscle Functioning and Its Potential as a Supportive Treatment for Duchenne Muscular Dystrophy

Merckx, C., & Paepe, B. D. (2022) · Metabolites · doi:10.3390/metabo12020193 · Cited by 39 · see citing works

Increased plasma myeloperoxidase levels in systemic lupus erythematosus

Telles, R. W., Ferreira, G. A., da Silva, N. P., & Sato, E. I. (2009) · Rheumatology International · doi:10.1007/s00296-009-1067-4 · Cited by 38 · see citing works

Binding of myeloperoxidase to bacteria: effect on hydroxyl radical formation and susceptibility to oxidant-mediated killing

Britigan, B. E. (1996) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(96)00014-1 · Cited by 36 · see citing works

Taurine bromamine (TauBr) - its role in immunity and new perspectives for clinical use

Marcinkiewicz, J. (2010) · Journal of Biomedical Science · doi:10.1186/1423-0127-17-s1-s3 · Cited by 36 · see citing works

Taurine Protects against Postischemic Brain Injury via the Antioxidant Activity of Taurine Chloramine

Seol, S.-I., Kim, H. J., Choi, E. B., Kang, I. S., Lee, H., Lee, J.-K., & Kim, C. (2021) · Antioxidants · doi:10.3390/antiox10030372 · Cited by 36 · see citing works

DICHLORO-AMINE

Chapin, R. M. (1929) · Journal of the American Chemical Society · doi:10.1021/ja01382a018 · Cited by 36 · see citing works

The kinetics and primary products of uracil chlorination

Gould, J. P., Richards, J. T., & Miles, M. G. (1984) · Water Research · doi:10.1016/0043-1354(84)90070-8 · Cited by 35 · see citing works

3-chlorotyrosine in Sputum of COPD Patients: Relationship with Airway Inflammation

O’Donnell, C., Newbold, P., White, P., Thong, B., Stone, H., & Stockley, R. A. (2010) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.3109/15412555.2010.528086 · Cited by 35 · see citing works

Iron, Nitric Oxide, and Myeloperoxidase in Asthmatic Patients

Ekmekçi, Ö. B., Donma, O., Sardogan, E., Yildirim, N., Uysal, Ö., Demirel, H. S., & Demir, T. (2004) · Biochemistry (Moscow) · doi:10.1023/b:biry.0000026205.89894.25 · Cited by 34 · see citing works

395. Studies of N-halogeno-compounds. Part IV. The reaction between ammonia and chlorine in aqueous solution, and the hydrolysis constants of chloroamines

Corbett, R. E., Metcalf, W. S., & Soper, F. G. (1953) · Journal of the Chemical Society (Resumed) · doi:10.1039/jr9530001927 · Cited by 33 · see citing works

Myeloperoxidase and Risk of Recurrence of Atrial Fibrillation after Catheter Ablation

Li, S.-B., Yang, F., Li, J., Ma, J., Jia, Y.-D., Dong, S.-Y., Zheng, W.-F., & Zhao, L. (2013) · Journal of Investigative Medicine · doi:10.2310/jim.0b013e3182857fa0 · Cited by 33 · see citing works

The formation of stable organic chloramines during the aqueous chlorination of cytosine and 5-methylcytosine

Gould, J. (1984) · Water Research · doi:10.1016/0043-1354(84)90250-1 · Cited by 32 · see citing works

Myeloperoxidase in Hypertensive Disorders of Pregnancy and Its Relation With Nitric Oxide

Rocha-Penha, L., Caldeira-Dias, M., Tanus-Santos, J. E., Cavalli, R. D. C., & Sandrim, V. C. (2017) · Hypertension · doi:10.1161/hypertensionaha.116.08854 · Cited by 31 · see citing works

Degradation Mechanisms and Substituent Effects of N-Chloro-α-Amino Acids: A Computational Study

Zhao, H., Zhou, Y., Han, C., Liu, Y. D., & Zhong, R. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b04440 · Cited by 31 · see citing works

Neutrophils as Sentinel Cells of the Immune System: A Role of the MPO-halide-system in Innate and Adaptive Immunity

Marcinkiewicz, J., & Walczewska, M. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666190819123300 · Cited by 30 · see citing works

Oxidative modification of ovalbumin.

Olszowski, S., Olszowska, E., Stelmaszyńska, T., Krawczyk, A., Marcinkiewicz, J., & Baczek, N. (1996) · Acta Biochimica Polonica · doi:10.18388/abp.1996_4462 · Cited by 29 · see citing works

Plasma myeloperoxidase levels in patients with acute ischemic stroke.

Cojocaru, I. M., Cojocaru, M., Iliescu, I., Botnaru, L., Gurban, C., Sfrijan, F., & Tănăsescu, R. (2010) · PubMed · Cited by 27 · see citing works

Detection of 3-chlorotyrosine in proteins exposed to neutrophil oxidants

Kettle, A. J. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00119-6 · Cited by 27 · see citing works

Serum myeloperoxidase levels in predicting the severity of stroke and mortality in acute ischemic stroke patients.

Tay, A., Tamam, Y., Yokuş, B., Ustundag, M., & Orak, M. (2015) · PubMed · Cited by 27 · see citing works

Role of myeloperoxidase in early diagnosis of acute myocardial infarction in patients admitted with chest pain

Omran, M. M., Zahran, F. M., Kadry, M., Belal, A. A. M., & Emran, T. M. (2018) · Journal of Immunoassay and Immunochemistry · doi:10.1080/15321819.2018.1492423 · Cited by 27 · see citing works

Myeloperoxidase-catalyzed chlorination: The quest for the active species

Ramos, D. R., García, M. V., Canle, M., Santaballa, J. A., Furtmüller, P. G., & Obinger, C. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2008.01.003 · Cited by 26 · see citing works

Evaluation of thiol-based antioxidant therapeutics in cystic fibrosis sputum: Focus on myeloperoxidase

Vasu, V. T., de Cruz, S. J., Houghton, J. S., Hayakawa, K. A., Morrissey, B. M., Cross, C. E., & Eiserich, J. P. (2010) · Free Radical Research · doi:10.3109/10715762.2010.521154 · Cited by 25 · see citing works

Regulation of hepatic lipase activity by sphingomyelin in plasma lipoproteins

Yang, P., & Subbaiah, P. V. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.07.003 · Cited by 23 · see citing works

Interaction of human myeloperoxidase with nitrite

Cooper, C. E., & Odell, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81461-t · Cited by 23 · see citing works

Several lines of antioxidant defense against oxidative stress: antioxidant enzymes, nanomaterials with multiple enzyme-mimicking activities, and low-molecular-weight antioxidants

Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445 · see citing works

Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity

Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works

Reactive Oxygen Species (ROS)-Mediated Antibacterial Oxidative Therapies: Available Methods to Generate ROS and a Novel Option Proposal

Alfei, S., Schito, G. C., Schito, A. M., & Zuccari, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137182 · Cited by 316 · see citing works

The Role of Reactive Species on Innate Immunity

Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works

Role of antioxidants in skin aging and the molecular mechanism of ROS: A comprehensive review

Hussen, N. H., Abdulla, S. K., Ali, N. M., Ahmed, V. A., Hasan, A. H., & Qadir, E. E. (2025) · Aspects of Molecular Medicine · doi:10.1016/j.amolm.2025.100063 · Cited by 116 · see citing works

Lipid peroxidation: Reactive carbonyl species, protein/DNA adducts, and signaling switches in oxidative stress and cancer

Moldogazieva, N. T., Zavadskiy, S. P., Astakhov, D. V., & Terentiev, A. A. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.149167 · Cited by 82 · see citing works

Multimetallic transition metal complexes:Luminescent probes for biomolecule sensing, ion detection, imaging and therapeutic application

Das, B., & Gupta, P. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.215656 · Cited by 77 · see citing works

Antimicrobial use guidelines for canine pyoderma by the International Society for Companion Animal Infectious Diseases (ISCAID)

Loeffler, A., Cain, C. L., Ferrer, L., Nishifuji, K., Varjonen, K., Papich, M. G., Guardabassi, L., Frosini, S., Barker, E., & Weese, J. S. (2025) · Veterinary Dermatology · doi:10.1111/vde.13342 · Cited by 56 · see citing works

Reactive Oxygen Species: Role in Pathophysiology, and Mechanism of Endogenous and Dietary Antioxidants during Oxidative Stress

Sikder, M. M., Li, X., Akumwami, S., & Labony, S. A. (2025) · Chonnam Medical Journal · doi:10.4068/cmj.2025.61.1.32 · Cited by 55 · see citing works

Nano‐biotechnology in tumour and cancerous disease: A perspective review

Soni, A., Bhandari, M. P., Tripathi, G. K., Bundela, P., Khiriya, P. K., Khare, P. S., Kashyap, M. K., Dey, A., Vellingiri, B., Suresh, S., et al. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17677 · Cited by 52 · see citing works

Peroxiredoxin 2: An Important Element of the Antioxidant Defense of the Erythrocyte

Sadowska‐Bartosz, I., & Bartosz, G. (2023) · Antioxidants · doi:10.3390/antiox12051012 · Cited by 47 · see citing works

Green synthesized Cobalt oxide nanoparticles using Curcuma longa for anti-oxidant, antimicrobial, dye degradation and anti-cancer property

Shanmuganathan, R., Sathiyavimal, S., Le, Q. H., Al‐Ansari, M. M., Al-Humaid, L. A., Jhanani, G. K., Lee, J., & Barathi, S. (2023) · Environmental Research · doi:10.1016/j.envres.2023.116747 · Cited by 43 · see citing works

Surface-Enhanced Raman Spectroscopy for the Detection of Reactive Oxygen Species

Yang, D., Youden, B., Yu, N., Carrier, A. J., Jiang, R., Servos, M. R., Oakes, K. D., & Zhang, X. (2025) · ACS Nano · doi:10.1021/acsnano.4c15509 · Cited by 43 · see citing works

Chlorine Dioxide: Friend or Foe for Cell Biomolecules? A Chemical Approach

Andrés, C. M. C., de la Lastra, J. M. P., Andrés, C., Plou, F. J., & Pérez‐Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415660 · Cited by 39 · see citing works

A tumor-targeting two-photon fluorescent probe with a far-red to NIR emission for imaging basal hypochlorite in cancer cells and tumor

Mao, G., Zhang, S., Yang, T.-T., Zhu, B., Sun, X.-Y., Wang, Q.-Q., & Zhang, G. (2024) · Talanta · doi:10.1016/j.talanta.2024.126436 · Cited by 32 · see citing works

Sulfur-based fluorescent probes for biological analysis: A review

Hu, G., Xu, H.-D., & Fang, J. (2024) · Talanta · doi:10.1016/j.talanta.2024.126515 · Cited by 32 · see citing works

Role of Myeloperoxidase, Oxidative Stress, and Inflammation in Bronchopulmonary Dysplasia

Wu, T.-J., Jing, X., Teng, M., Pritchard, K. A., Day, B. W., Naylor, S., & Teng, R. (2024) · Antioxidants · doi:10.3390/antiox13080889 · Cited by 31 · see citing works

Reactive oxygen species-mediated signal transduction and utilization strategies in microalgae

Tang, D., Li, X., Zhang, L., Xiao, P., Nie, Y., Qiu, F., Cheng, Z., Li, W., & Zhao, Y. (2024) · Bioresource Technology · doi:10.1016/j.biortech.2024.132004 · Cited by 29 · see citing works

Oxidative Stress in Health and Disease: Mechanisms and Therapeutic Perspectives

Anwar, S., Alharbi, H., Babiker, A., & Rahmani, A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27062681 · Cited by 35 · see citing works

Manipulation of Oxidative Stress Responses by Non-Thermal Plasma to Treat Herpes Simplex Virus Type 1 Infection and Disease

Sutter, J., Bruggeman, P., Wigdahl, B. L., Krebs, F. C., & Miller, V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054673 · Cited by 26 · see citing works

A lysosome-targeted fluorescent probe for fluorescence imaging of hypochlorous acid in living cells and in vivo

An, K., Fan, J., Lin, B., & Han, Y. (2024) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2024.124316 · Cited by 25 · see citing works

Longitudinal Magnetic Resonance Imaging with ROS‐Responsive Bilirubin Nanoparticles Enables Monitoring of Nonalcoholic Steatohepatitis Progression to Cirrhosis

Jung, W., Asaduddin, M., Keum, H., Son, Y., Yoo, D., Kim, D. H., Lee, S., Lee, D. Y., Roh, J., Park, S., et al. (2024) · Advanced Materials · doi:10.1002/adma.202305830 · Cited by 24 · see citing works

Myeloperoxidase as a therapeutic target for oxidative damage in Alzheimer’s disease

Rivera-Antonio, A. M., Martínez, I. I. P., Torres-Ramos, M., & Rosales‐Hernández, M. C. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2456282 · Cited by 23 · see citing works

A Ratiometric Fluorescent Probe for Hypochlorite and Lipid Droplets to Monitor Oxidative Stress

Baruah, M., Jana, A., Pareek, N., Singh, S., & Samanta, A. (2023) · Biosensors · doi:10.3390/bios13060662 · Cited by 17 · see citing works

Early Depletion of Neutrophils Reduces Retinal Inflammation and Neovascularization in Mice with Oxygen-Induced Retinopathy

Deliyanti, D., Suphapimol, V., Ang, P., Tang, X., Jayasimhan, A., & Wilkinson‐Berka, J. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115680 · Cited by 20 · see citing works

Quaternary Treatment of Urban Wastewater for Its Reuse

Jurík, J., Jankovičová, B., Zakhar, R., Šoltýsová, N., & Derco, J. (2024) · Processes · doi:10.3390/pr12091905 · Cited by 19 · see citing works

Enhanced stem cell-mediated therapeutic immune modulation with zinc oxide nanoparticles in liver regenerative therapy

Park, N., Kim, K. S., Lee, S.-H., Choi, J. H., & Na, K. (2025) · Biomaterials · doi:10.1016/j.biomaterials.2025.123232 · Cited by 18 · see citing works

Chemical characterization, pathway enrichments and bioactive potentials of catechin-producing endophytic fungi isolated from tea leaves

Sidhu, D., Vasundhara, M., & Dey, P. (2024) · RSC Advances · doi:10.1039/d4ra05758a · Cited by 16 · see citing works

The Ion Channels Involved in Oxidative Stress-Related Gastrointestinal Diseases

Miranda, M. R., Vestuto, V., Moltedo, O., Manfra, M., Campiglia, P., & Pepe, G. (2023) · Oxygen · doi:10.3390/oxygen3030022 · Cited by 15 · see citing works

(Chemical) Roles of HOCl in Rheumatic Diseases

Leopold, J., & Schiller, J. (2024) · Antioxidants · doi:10.3390/antiox13080921 · Cited by 14 · see citing works

The Lesson Learned from the COVID-19 Pandemic: Can an Active Chemical Be Effective, Safe, Harmless-for-Humans and Low-Cost at a Time? Evidence on Aerosolized Hypochlorous Acid

Benedusi, M., Tamburini, E., Sicurella, M., Summa, D., Ferrara, F., Marconi, P., Cervellati, F., Costa, S., & Valacchi, G. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph192013163 · Cited by 15 · see citing works

A Photoelectrochemical Sensor for the Detection of Hypochlorous Acid with a Phenothiazine-Based Photosensitizer

Luo, L., Yang, Y., Chen, S., Zhang, P., & Zeng, R. (2024) · Molecules · doi:10.3390/molecules29030614 · Cited by 12 · see citing works

A mitochondria-targeted NIR fluorescence/photoacoustic dual-modality probe for highly sensitive and selective imaging of HClO in vivo

Liao, Y., Yi, T., Tan, K., Su, X., Chen, S., Lu, M., Yang, Y., Huang, X., Zhao, Y., Huang, H. B., et al. (2024) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2024.125680 · Cited by 12 · see citing works

Membrane-Targetable Dual-Responsive Fluorescent Probe for Simultaneous Detection of Polarity and Hypochlorite and Its Application in Apoptosis and Cancer Models

Gu, B., Zhao, J., Tang, S., Li, H., Long, R., Wang, L., Liao, Y., Li, Y., Chen, W., & Zhang, Y. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06383 · Cited by 10 · see citing works

A New and Fast-Response Fluorescent Probe for Monitoring Hypochlorous Acid Derived from Myeloperoxidase

Świerczyńska, M., Słowiński, D., Michalski, R., Romański, J., & Podsiadły, R. (2023) · Molecules · doi:10.3390/molecules28166055 · Cited by 10 · see citing works

In vivo glycation—interplay between oxidant and carbonyl stress in bone

Sroga, G. E., & Vashishth, D. (2024) · JBMR Plus · doi:10.1093/jbmrpl/ziae110 · Cited by 12 · see citing works

Enriched detection nanoparticles for hypochlorite prepared by electrostatic spray, applied to tumor imaging, antibacterial and antiviral

Wu, L., Liu, X., Liu, B., Guan, Q., Guo, M., Li, Y., Fei, H., Li, Y., Yang, Q., Shan, Y., et al. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.157990 · Cited by 10 · see citing works

Hypochlorous Acid (HOCl) as a Promising Respiratory Antiseptic

Winter, M., Boecker, D., & Posch, W. (2025) · Viruses · doi:10.3390/v17091219 · Cited by 10 · see citing works

Myeloid-Derived Suppressor Cells in Cancer and COVID-19 as Associated with Oxidative Stress

Andrés, C., de la Lastra, J. M. P., Juan, C., Plou, F. J., & Pérez‐Lebeña, E. (2023) · Vaccines · doi:10.3390/vaccines11020218 · Cited by 9 · see citing works

The effect of hypochlorous acid inhalation on the activity of antioxidant system enzymes in rats of different ages

Murashevych, B. V., Sergiivna, M. H., Girenko, D., Абраимова, О. Е., Netronina, O., & Vn, S. (2024) · Free Radical Research · doi:10.1080/10715762.2024.2386688 · Cited by 9 · see citing works

Determination of the Inhibitory Potential of Chalcones on Myeloperoxidase Enzyme Activity: In vitro and Molecular Docking Studies

Abul, N., Demir, Y., Öztekіn, A., & Özdemіr, H. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01719-0 · Cited by 8 · see citing works

A NIR ratiometric probe for detecting hypochlorite and bisulfite/sulfite in aqueous media

Kodiyawala, A., & Dutta, S. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.126204 · Cited by 8 · see citing works

Easy and portable fluorescent probe for ClO− detection in pure water: A versatile platform for environmental samples, bioimaging, and smartphone-assisted technologies

Nam, H., Batsaikhan, O., Park, S., Kim, K., & Kim, C. (2025) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2025.116804 · Cited by 8 · see citing works

Influence of twisted intramolecular charge transfer for two “OFF-ON” fluorescent probes in hypochlorite detection

Liu, Q., Wu, D., Huang, X., Xia, Z., Hao, W., Huang, A., Xu, H., & He, H. (2025) · Dyes and Pigments · doi:10.1016/j.dyepig.2025.112914 · Cited by 8 · see citing works

Protic small molecule bioregulators

Davis, A. G., & Pluth, M. D. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103921 · Cited by 8 · see citing works

Biological evaluation of a new highly sensitive and selective fluorescent probe for hypochlorous acid and its imaging application in cell and zebrafish

Zheng, M., Wen, H., Meng, Z., Guo, W., Wang, K., Yu, M., Li, L., Zhang, Y. L., Liu, K., Cai, L., et al. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108358 · Cited by 8 · see citing works

Age-Related Diseases and Foods Generating Chlorinative Stress

Salvo, E. D., Casciaro, M., Giorgianni, C. M., Cicero, N., & Gangemi, S. (2023) · Antioxidants · doi:10.3390/antiox12020249 · Cited by 8 · see citing works

Plasmalogen, a glycerophospholipid crucial for Streptococcus mutans acid tolerance and colonization

Mu, R., Momeni, S. S., Krieger, M., Xie, B., Cao, X., Merritt, J. L., & Wu, H. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.01500-23 · Cited by 7 · see citing works

A novel hepatocyte-targeting fluorescent probe of rhodamine analogues to detect hypochlorite in lysosomes: Design, synthesis and evaluation

Qin, X., Mei, J., Wang, Y., Jiang, N., Chen, J., Yang, M., Jing, L., Tang, C., Wang, J., & Tang, W. (2024) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2024.115597 · Cited by 7 · see citing works

HOCl forms lipid N-chloramines in cell membranes of bacteria and immune cells

Knoke, L. R., Herrera, S. A., Heinrich, S., Peeters, F. M. L., Lupilov, N., Bandow, J. E., & Pomorski, T. G. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.09.014 · Cited by 7 · see citing works

Biocatalysis: modern challenges and applications

Varfolomeev, S. D., Švedas, V. K., Efremenko, E. N., Egorov, A. M., Khrenova, M. G., Tishkov, V. I., Atroshenko, D. L., POMETUN, A. A., Сергеевич, С. С., Угарова, Н. Н., et al. (2024) · Russian Chemical Reviews · doi:10.59761/rcr5144 · Cited by 7 · see citing works

Identification of Tie2 as a sensor for reactive oxygen species and its therapeutic implication

Pham, A. V. Q., Na, Y., Suk, G., Yang, C., Kang, S. M., Lee, J., Choi, H., Kim, W., Chi, S. W., Han, S., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103555 · Cited by 6 · see citing works

Beyond anaerobic respiration—new physiological roles for DmsABC and other S-/N-oxide reductases in Escherichia coli

Zhong, Q., Nasreen, M., Yang, R., Struwe, M. A., Kobe, B., & Kappler, U. (2025) · Journal of Bacteriology · doi:10.1128/jb.00463-24 · Cited by 6 · see citing works

Hypochlorous Acid-Modified Serum Albumin Causes NETosis in the Whole Blood Ex Vivo and in Isolated Neutrophils

Basyreva, L. Y., Shmeleva, E. V., Vakhrusheva, T. V., Gorudko, I. V., Grigorieva, D. V., Kostevich, V. A., Gorbunov, N., Sokolov, A. V., Гусев, С. А., Panasenko, O. M., et al. (2024) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-024-06155-3 · Cited by 6 · see citing works

Structural and functional characteristics of the pulmonary hemomicrocirculatory bed in induced systemic sclerosis: an experimental study

Doskaliuk, B., & Zaiats, L. (2023) · Rheumatology International · doi:10.1007/s00296-023-05328-z · Cited by 6 · see citing works

Oxidative degradation pathways of carrot carotenes and their protection via chitosan-TPP encapsulation

Ali, H. M., Eid, S. A., Eldeen, H. A. S., & Ebrahim, M. Z. (2025) · Chemical and Biological Technologies in Agriculture · doi:10.1186/s40538-025-00855-2 · Cited by 5 · see citing works

Oxidative degradation of alpha-tocopherol by reactive oxygen species, identifying products, and product anticancer activity

Ali, H. M., Attia, M. H., Mamdouh, W., Rashed, E. N., & Ali, I. H. (2025) · BMC Chemistry · doi:10.1186/s13065-025-01665-1 · Cited by 5 · see citing works

Multimodal HOCl-responsive MEH-PPV nanoparticles for anti-inflammatory imaging and therapy

Villar‐Álvarez, E., Parron-Onate, S., Wienskowska, O., Carrascull‐Marín, A., Bellacanzone, C., Lorenzo, J., Ruiz‐Molina, D., & Roscini, C. (2024) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2024.136150 · Cited by 5 · see citing works

Advances in design strategies and imaging applications of specific butyrylcholinesterase probes

Sun, T., Dong, Z., Malugulu, P. M., Zhen, T., Wang, L., Chen, Y., & Sun, H. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.110451 · Cited by 5 · see citing works

Discovery of Thiazole Carboxamides as Novel Vanin-1 Inhibitors for Inflammatory Bowel Disease Treatment

Xie, T., Cao, G.-Y., Zhang, S., Li, M., Jin, X., Liu, L., Wang, G., & Zhen, L. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01838 · Cited by 5 · see citing works

A Mitochondria-Targeted Fluorescence/Photoacoustic Dual-Modality imaging probe for Hypochlorous Acid-Related inflammatory Responses in vivo

Liao, Y., Yi, T., Su, X., Chen, S., Lu, M., Huang, X., Yang, Y., Qin, X., Tang, C., Zhao, Y., et al. (2024) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2024.116232 · Cited by 5 · see citing works

Determination of the patterns of hypochlorous acid release from foamed sodium hypochlorite solutions into the air in an evaporator of special design

Murashevych, B. V., Girenko, D., Lebed, O. S., Sergiivna, M. H., & Bilenkyi, E. (2024) · Eastern-European Journal of Enterprise Technologies · doi:10.15587/1729-4061.2024.319053 · Cited by 5 · see citing works

Efficacy of hypochlorous acid solution in comparison with povidone iodine solution for the management of infected diabetic foot ulcers

Shukur, A. A., & Zeiny, S. M. (2025) · Medical Journal Armed Forces India · doi:10.1016/j.mjafi.2024.11.015 · Cited by 5 · see citing works

A phenothiazine-based fluorescent probe for ultrafast and selective hypochlorous acid detection with hydrogel-integrated smartphone readout

Ma, H., Li, Y., Zhang, X., Yan, L., Gao, H., Liu, L., & Xu, L. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.127114 · Cited by 4 · see citing works

Targeting redox homeostasis in cancer: Inhibitors of Reactive Oxygen Species regulating cellular signalling pathways and their therapeutic implications

Sahu, M., & Jain, U. (2026) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2026.105204 · Cited by 4 · see citing works

Hypochlorous acid-activatable two-photon excited NIR fluorescent probe with a high signal-to-background ratio for imaging osteoarthritis

Zhu, Y., Lian, Y., Cui, M., Ru, Q., Lu, J., Guo, H., Yuan, J., Wang, H., & Mao, G. (2026) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2026.127786 · Cited by 4 · see citing works

5-Chloro-2′-deoxycytidine Induces a Distinctive High-Resolution Mutational Spectrum of Transition Mutations In Vivo

Chancharoen, M., Yang, Z., Dalvie, E. D., Gubina, N., Ruchirawat, M., Croy, R. G., Fedeles, B. I., & Essigmann, J. M. (2024) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.3c00358 · Cited by 4 · see citing works

The interplay between the myeloperoxidase-hypochlorous acid system, heme oxygenase, and free iron in inflammatory diseases

Biernat, M. M., Camp, O. G., Moussa, D. N., Awonuga, A. O., & Abu‐Soud, H. M. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112927 · Cited by 4 · see citing works

Hypochlorous acid as a potential cavity conditioner for caries-affected dentin

Sanon, K., Elseoudy, N., Hiraishi, N., Tamura, Y., Sanchavanakit, N., ThanNaing, S., Shimada, Y., Tagami, J., & Thongthai, P. (2025) · Scientific Reports · doi:10.1038/s41598-025-06191-7 · Cited by 4 · see citing works

Equine Muscle Derived Mesenchymal Stem Cells Loaded with Water-Soluble Curcumin: Modulation of Neutrophil Activation and Enhanced Protection against Intracellular Oxidative Attack

Franck, T. J., Ceusters, J. D., Graide, H., Niesten, A., Duysens, J., Mickalad, A. M., & Serteyn, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021030 · Cited by 4 · see citing works

Carbon-coated nickel foam for hypochlorous acid sensor

Sanjaya, A. R., Riyanto, H. G., Rahmawati, I., Putri, Y. M. T. A., Nurhalimah, D., Saepudin, E., Yudhistira, T., & Krisnandi, Y. K. (2023) · Environmental and Materials · doi:10.61511/eam.v1i1.2023.105 · Cited by 4 · see citing works

Heme–Aβ compound 0: a common intermediate in ROS generation and peroxidase activity

Dey, C., Pal, P., Samanta, S., & Dey, S. G. (2025) · Dalton Transactions · doi:10.1039/d5dt00234f · Cited by 4 · see citing works

Commercially available antiseptics show high in vitro efficacy against pathogens most commonly associated with canine and feline infectious keratitis

Wolff, H. T., Piroth, A. C., Oltmanns, H., Meißner, J., Verspohl, J., Volk, H. A., & Busse, C. (2025) · Frontiers in Veterinary Science · doi:10.3389/fvets.2025.1552230 · Cited by 3 · see citing works

Neuro-Inflammatory and Behavioral Changes Are Selectively Reversed by Sceletium tortuosum (Zembrin®) and Mesembrine in Male Rats Subjected to Unpredictable Chronic Mild Stress

Gericke, J., Steyn, S. F., Viljoen, F. P., & Harvey, B. H. (2025) · Cells · doi:10.3390/cells14131029 · Cited by 3 · see citing works

Azithromycin and Gallic acid alleviate neurobehavioral deficits in rats resulting from chronic Aflatoxin B1 exposure

Owumi, S. E., Chimezie, J., Bello, I. O., Otunla, M. T., Arunsi, U. O., Akomolafe, A. P., Babalola, J. O., Irozuru, C. E., & Owoeye, O. (2025) · Toxicon · doi:10.1016/j.toxicon.2025.108552 · Cited by 3 · see citing works

In vivo monitoring of hypochlorous acid in epileptic brains via a competitive absorption-based photoelectrochemical microsensor

Gao, S., Song, Y., Jiang, Y., Wang, X., & Ye, X. (2025) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2025.139284 · Cited by 3 · see citing works

Targeting Highly Reactive Oxygen Species (hROS) for Prodrug Activation through a Cascade Reaction with Kinetic Tunability (CReKT) to Effect Linker Cleavage

Kondengadan, S. M., Bansal, S., 鲁文, Choudhury, M. R., & Wang, B. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03627 · Cited by 3 · see citing works

AIE-based dual-mode chemosensor for hypochlorite detection in water: Environmental and biological applications in diverse water samples, zebrafish, artemia, and plants

Kim, S., Lee, Y.-S., Lee, S., Lee, J. J., Yun, K., Kim, K.-T., & Kim, C. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109815 · Cited by 3 · see citing works

Cost Analysis of Pure Hypochlorous Acid Preserved Wound Cleanser versus Mafenide for the Irrigation of Burn Wounds

Rizzo, E. J., Mallow, P. J., Noble, A., & Foster, K. N. (2024) · ClinicoEconomics and Outcomes Research · doi:10.2147/ceor.s476201 · Cited by 3 · see citing works

Monocationic versus dicationic-based monomethine cyanine dyes for ultrasensitive colorimetric detection of hypochlorite ion in water

Hafez, N. S., Amer, W. A., Okba, E. A., Sakr, M. A. S., Alganzory, H. H., Khalil, S. M., & Ebeid, E. M. (2025) · Scientific Reports · doi:10.1038/s41598-025-88839-y · Cited by 3 · see citing works

Application of nanomaterial-based fluorescent probes for diabetes detection and care triggered by reactive oxygen species

Sreejaya, M. M., Mekkeparambath, V., Pillai, P. S., Kumar, L. A., M., K. P., Gauri, V., Nair, A., Bera, M., & Gangopadhyay, M. (2025) · Journal of Materials Chemistry B · doi:10.1039/d5tb01327e · Cited by 3 · see citing works

Comparative Evaluation of Human Pulp Tissue Dissolution by 500-ppm and 200-ppm Hypochlorous Acid and 5.25% Sodium Hypochlorite: An In Vitro Study

Vijayaraghavan, S., & Menon, K. (2023) · The Journal of Contemporary Dental Practice · doi:10.5005/jp-journals-10024-3462 · Cited by 3 · see citing works

Two 5-Methoxyindole Carboxylic Acid-Derived Hydrazones of Neuropharmacological Interest: Synthesis, Crystal Structure, and Chemiluminescent Study of Radical Scavenging Properties

Anastassova, N., Hristova-Avakumova, N. G., Rusew, R., Shivachev, B. L., & Yancheva, D. Y. (2024) · Crystals · doi:10.3390/cryst14050396 · Cited by 3 · see citing works

Reaction sites of pyrimidine bases and nucleosides during chlorination: A computational study

Cao, X., Mo, Y., Zhang, F., Zhou, Y., Liu, Y. D., & 钟儒刚 (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.142189 · Cited by 3 · see citing works

Evaluation of treatment of methicillin-resistant Staphylococcus aureus biofilms with intermittent electrochemically generated H 2 O 2 or HOCl

Anoy, M. M. I., Kim, W., Gelston, S., Fleming, D. F., Patel, R., & Beyenal, H. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01722-23 · Cited by 3 · see citing works

A water-soluble phenothiazine-based fluorescent probe for selective detection and bioimaging of hypochlorite

Yang, Y., Shao, Y., Bao, X., Xu, N., Dong, W., & Gao, C. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.126892 · Cited by 3 · see citing works

Electrochemical Catheter Hub Operated by a Wearable Micropotentiostat Prevents Acinetobacter baumannii Infection In Vitro

Al‐Qurahi, M., Fleming, D. F., Kim, W., Bozyel, I., Patel, R., & Beyenal, H. (2025) · Biotechnology and Bioengineering · doi:10.1002/bit.28990 · Cited by 2 · see citing works

Hypochlorous Acid-Gated Hydrolysis of a Phosphinate Ester Dye in Living Cells

Yuan, F., Zhou, X., McAfee, J. L., Faulkner, B. M., Lesiak, L., He, Y., Brøndsted, F., Fan, H., Donarski, E. D., Hu, X., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12615 · Cited by 2 · see citing works

Mapping of HOCl-oxidized RNA identifies abasic sites as major damage and oxidation product of oxo8G

Weber, M., Raorane, K., Grampp, C. J., Bourguignon‐Igel, V., Kilz, L.-M., Glänzer, D., Marchand, V., Kreutz, C., Motorin, Y., & Helm, M. (2025) · Nature Communications · doi:10.1038/s41467-025-65108-0 · Cited by 2 · see citing works

Dissecting HOCl Action in Chronic Wound Biofilms: Proteomic Insights From a Host‐Relevant Model of Pseudomonas aeruginosa

Robins, L. I., Gafken, P. R., Lin, C., Jones, L. A., & Hooper, S. E. (2025) · MicrobiologyOpen · doi:10.1002/mbo3.70181 · Cited by 3 · see citing works

Synergistic microbicidal effects of plasma-activated sodium hypochlorite on fresh produce surfaces

Ryu, J.-W., Han, J.-Y., Kim, S.-H., & Kang, D. (2025) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2025.104388 · Cited by 2 · see citing works

A novel camphor-modified phenothiazine-based colorimetric and ratiometric fluorescent probe with ultrasensitive and ultrafast response to HClO in foods and water environment

Xu, S., Liang, Y., Xu, T., Gu, Y., Li, L., Meng, Z., Wang, Z., & Wang, S. (2026) · Dyes and Pigments · doi:10.1016/j.dyepig.2026.113624 · Cited by 2 · see citing works

Oxidative Stress Biomarkers: Molecular Mechanisms, Detection Techniques, and Clinical Applications: A Comprehensive Review

Qadir, A. M., & Omer, R. A. (2026) · Journal of Analytical Chemistry · doi:10.1134/s1061934825701357 · Cited by 2 · see citing works

A mitochondrion targeted fluorescent sensor for real-time ClO− imaging in living cells

Li, H., Qi, G., Yang, H., Bu, L., Han, S., & (54275), X. Z. (2026) · Microchemical Journal · doi:10.1016/j.microc.2026.117588 · Cited by 2 · see citing works

Myeloperoxidase in the pathogenesis of sickle cell disease

Biernat, M. M., Camp, O. G., Awonuga, A. O., Abu‐Soud, H. M., Chatzicharalampous, C., Kofinas, G., & Kofinas, J. D. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110800 · Cited by 2 · see citing works

Unveiling a simple thiomorpholine AIE probe for HClO detection: Off-on-off from theory to bioassays

Wang, X., Zhang, Z., Zeng, X., Liu, P., Chen, Z. X., Fan, B., He, Y., Li, Y. X., & Zhang, F. (2026) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2026.146866 · Cited by 2 · see citing works

Identification of reaction sites and chlorinated products of purine bases and nucleosides during chlorination: a computational study

Zhang, F., Mo, Y., Cao, X., Zhou, Y., Liu, Y. D., & Zhong, R. (2024) · Organic & Biomolecular Chemistry · doi:10.1039/d3ob02111d · Cited by 2 · see citing works

The Role of the Dysregulation of circRNAs Expression in Glioblastoma Multiforme

Wang, Y., Yu, Y., Yu, J., Wang, C., Wang, Y., Fu, R., & Zhang, C. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-024-02285-5 · Cited by 2 · see citing works

Electrophilic Susceptibility of Graphene Quantum Dots: Hypochlorous versus Hypobromous Acids─Experimental and Theoretical Study

Mizumoto, G. J., Morgon, N. H., de Souza, A. R., & Ximenes, V. F. (2025) · ACS Omega · doi:10.1021/acsomega.5c01500 · Cited by 2 · see citing works

Efficient chlorine production from nanostructured cobalt manganese oxide derived from spent battery

Devi, S., Sunaina, S., Rana, S., Sood, K., Kumari, S., & Jha, M. (2025) · Separation and Purification Technology · doi:10.1016/j.seppur.2025.133213 · Cited by 2 · see citing works

Hypochlorous acid-mediated oxidative stress and its pathophysiological significance

Peng, J. (2010) · Zhongguo yaolixue yu dulixue zazhi · Cited by 3 · see citing works

Hypochlorous acid as a precursor of free radicals in living systems

Panasenko, O. M., Gorudko, I. V., & Av, S. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913130075 · Cited by 157 · see citing works

Comparative reactivity of myeloperoxidase-derived oxidants with mammalian cells

Rayner, B. S., Love, D. T., & Hawkins, C. L. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.004 · Cited by 114 · see citing works

The Reactions of Hypochlorous Acid, the Reactive Oxygen Species Produced by Myeloperoxidase, With Lipids

Spickett, C. M., Jerlich, A., Panasenko, O. M., Arnhold, J., Pitt, A. R., Stelmaszyńska, T., & Schaur, R. J. (2000) · Acta Biochimica Polonica · doi:10.18388/abp.2000_3944 · Cited by 154 · see citing works

What Are the Plasma Targets of the Oxidant Hypochlorous Acid? A Kinetic Modeling Approach

Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800372d · Cited by 123 · see citing works