A patent review of myeloperoxidase inhibitors for treating chronic inflammatory syndromes (focus on cardiovascular diseases, 2013-2019)

References

• Ermert D, Niemiec MJ, Röhm M, et al. Candida albicans escapes from mouse neutrophils. J Leukoc Biol. 2013;94:223–236.
   PubMed Web of Science ®Google Scholar
• Jacobs L, Nawrot TS, de Geus B, et al. Subclinical responses in healthy cyclists briefly exposed to traffic-related air pollution: an intervention study. Environ Health. 2010;9:64.
   PubMed Web of Science ®Google Scholar
• Metzler KD, Fuchs TA, Nauseef WM, et al. Myeloperoxidase is required for neutrophil extracellular trap formation: implications for innate immunity. Blood. 2011;117:953–959.
   PubMed Web of Science ®Google Scholar
• Nauseef WM. Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase. Blood. 1987;70:1143–1150.
   PubMed Web of Science ®Google Scholar
• Klebanoff SJ. Myeloperoxidase: friend and foe. J Leukoc Biol. 2005;77:598–625.
   PubMed Web of Science ®Google Scholar
• Klebanoff SJ, Kettle AJ, Rosen H, et al. Myeloperoxidase: a front-line defender against phagocytosed microorganisms. J Leukoc Biol. 2013;93(2):185–198.
   PubMed Web of Science ®Google Scholar
• Nauseef WM. Biosynthesis of human myeloperoxidase. Arch Biochem Biophys. 2018;642:1–9.
   PubMed Web of Science ®Google Scholar
• Fiedler TJ, Davey CA, Fenna RE. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem. 2000;275:11964–11971.
   PubMed Web of Science ®Google Scholar
• Van Antwerpen P, Slomianny M-C, Boudjeltia KZ, et al. Glycosylation pattern of mature Dimeric Leukocyte and recombinant Monomeric Myeloperoxidase: glycosylation is required for optimal enzymatic activity. J Biol Chem. 2010;285:16351–16359.
   PubMed Web of Science ®Google Scholar
• Furtmüller PG, Burner U, Obinger C. Reaction of Myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry. 1998;37:17923–17930.
   PubMed Web of Science ®Google Scholar
• Kettle AJ, Winterbourn CC. The mechanism of myeloperoxidase-dependent chlorination of monochlorodimedon. Biochim Biophys Acta. 1988;957:185–191.
   PubMed Web of Science ®Google Scholar
• Hoogland H, van Kuilenburg A, van Riel C, et al. Spectral properties of myeloperoxidase compounds II and III. Biochim Biophys Acta. 1987;916:76–82.
   PubMedGoogle Scholar
• Paumann-Page M, Furtmüller PG, Hofbauer S, et al. Inactivation of human myeloperoxidase by hydrogen peroxide. Arch Biochem Biophys. 2013;539:51–62.
   PubMed Web of Science ®Google Scholar
• Arnhold J, Furtmüller PG, Obinger C. Redox properties of myeloperoxidase. Redox Rep. 2003;8:179–186.
   PubMed Web of Science ®Google Scholar
• Pereira WE, Hoyano Y, Summons RE, et al. Chlorination studies. II. The reaction of aqueous hypochlorous acid with alpha-amino acids and dipeptides. Biochim Biophys Acta. 1973;313:170–180.
   PubMed Web of Science ®Google Scholar
• Ximenes VF, Maghzal GJ, Turner R, et al. Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione. Biochem J. 2009;425:285–293.
   PubMed Web of Science ®Google Scholar
• Fu X, Kassim SY, Parks WC, et al. Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation. J Biol Chem. 2003;278:28403–28409.
   PubMed Web of Science ®Google Scholar
• Prütz WA. Hypochlorous Acid Interactions with Thiols, Nucleotides, DNA, and other biological substrates. Arch Biochem Biophys. 1996;332:110–120.
   PubMed Web of Science ®Google Scholar
• Mongirdienė A, Laukaitienė J, Skipskis V, et al. The effect of oxidant hypochlorous acid on platelet aggregation and dityrosine concentration in chronic heart failure patients and healthy controls. Medicina (Kaunas). 2019;55(5):198.
   Web of Science ®Google Scholar
• Dennisjr W, Olivieri V, Kruse C. The reaction of nucleotides with aqueous hypochlorous acid. Water Res. 1979;13:357–362.
   Web of Science ®Google Scholar
• Grotto D, Maria LS, Valentini J, et al. Importance of the lipid peroxidation biomarkers and methodological aspects for malondialdehyde quantification. Quím Nova. 2009;32:169–174.
   Web of Science ®Google Scholar
• Spickett CM, Jerlich A, Panasenko OM, et al. The reactions of hypochlorous acid, the reactive oxygen species produced by myeloperoxidase, with lipids. Acta Biochim Pol. 2000;47:889–899.
   PubMed Web of Science ®Google Scholar
• Nicholls SJ, Hazen SL. Myeloperoxidase and cardiovascular disease. Arterioscler Thromb Vasc Biol. 2005;25:1102–1111..
   PubMed Web of Science ®Google Scholar
• Green PS, Mendez AJ, Jacob JS, et al. Neuronal expression of myeloperoxidase is increased in Alzheimer’s disease. J Neurochem. 2004;90:724–733.
   PubMed Web of Science ®Google Scholar
• Gellhaar S, Sunnemark D, Eriksson H, et al. Myeloperoxidase-immunoreactive cells are significantly increased in brain areas affected by neurodegeneration in Parkinson’s and Alzheimer’s disease. Cell Tissue Res. 2017;369:445–454.
   PubMed Web of Science ®Google Scholar
• Choi D-K, Pennathur S, Perier C, et al. Ablation of the inflammatory enzyme myeloperoxidase mitigates features of Parkinson’s disease in mice. J Neurosci. 2005;25:6594–6600.
   PubMed Web of Science ®Google Scholar
• Sánchez-López F, Tasset I, Agüera E, et al. Oxidative stress and inflammation biomarkers in the blood of patients with Huntington’s disease. Neurol Res. 2012;34:721–724.
   PubMed Web of Science ®Google Scholar
• Fernandes RMSN, da Silva NP, Sato EI. Increased myeloperoxidase plasma levels in rheumatoid arthritis. Rheumatol Int. 2012;32:1605–1609.
   PubMed Web of Science ®Google Scholar
• Saed GM, Ali-Fehmi R, Jiang ZL, et al. Myeloperoxidase serves as a redox switch that regulates apoptosis in epithelial ovarian cancer. Gynecol Oncol. 2010;116:276–281.
   PubMed Web of Science ®Google Scholar
• Nagra RM, Becher B, Tourtellotte WW, et al. Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis. J Neuroimmunol. 1997;78:97–107.
   PubMed Web of Science ®Google Scholar
• Cascorbi I, Henning S, Brockmöller J, et al. Substantially reduced risk of cancer of the aerodigestive tract in subjects with variant–463A of the myeloperoxidase gene. Cancer Res. 2000;60:644–649.
   PubMed Web of Science ®Google Scholar
• Hung RJ, Boffetta P, Brennan P, et al. Genetic polymorphisms of MPO, COMT, MnSOD, NQO1, interactions with environmental exposures and bladder cancer risk. Carcinogenesis. 2004;25:973–978.
   PubMed Web of Science ®Google Scholar
• Pakakasama S, Chen TT-L, Frawley W, et al. Myeloperoxidase promotor polymorphism and risk of hepatoblastoma. Int J Cancer. 2003;106:205–207.
   PubMed Web of Science ®Google Scholar
• Lee JS, Oh TY, Ahn BO, et al. Involvement of oxidative stress in experimentally induced reflux esophagitis and Barrett’s esophagus: clue for the chemoprevention of esophageal carcinoma by antioxidants. Mutat Res. 2001;480–481:189–200.
   PubMed Web of Science ®Google Scholar
• Yang X, Li Y, Li Y, et al. Oxidative Stress-Mediated Atherosclerosis: mechanisms and Therapies. Front Physiol. 2017;8:600.
   PubMed Web of Science ®Google Scholar
• Fulton DJR, Barman SA. Clarity on the Isoform-specific roles of NADPH oxidases and NADPH oxidase-4 in Atherosclerosis. Arterioscler Thromb Vasc Biol. 2016;36:579–581.
   PubMed Web of Science ®Google Scholar
• Park J-G, Oh GT. The role of peroxidases in the pathogenesis of atherosclerosis. BMB Rep. 2011;44:497–505.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Aldib I, Delporte C, et al. Myeloperoxidase as a target for the treatment of inflammatory syndromes: mechanisms and structure activity relationships of inhibitors. Curr Med Chem. 2016;23:3975–4008.
   PubMed Web of Science ®Google Scholar
• Malle E, Marsche G, Arnhold J, et al. Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid. Biochim Biophys Acta. 2006;1761:392–415.
   PubMed Web of Science ®Google Scholar
• Abu-Soud HM, Hazen SL. Nitric oxide modulates the catalytic activity of myeloperoxidase. J Biol Chem. 2000;275:5425–5430.
   PubMed Web of Science ®Google Scholar
• Harrison DG. Cellular and molecular mechanisms of endothelial cell dysfunction. J Clin Invest. 1997;100:2153–2157.
   PubMed Web of Science ®Google Scholar
• Zouaoui Boudjeltia K, Daher J, Van Antwerpen P, et al. Exposure of endothelial cells to physiological levels of myeloperoxidase-modified LDL delays pericellular fibrinolysis. PLoS ONE. 2012;7:e38810.
   PubMed Web of Science ®Google Scholar
• Ndrepepa G. Myeloperoxidase – A bridge linking inflammation and oxidative stress with cardiovascular disease. Clin Chim Acta. 2019;493:36–51.
   PubMed Web of Science ®Google Scholar
• Malle E, Furtmüller PG, Sattler W, et al. Myeloperoxidase: a target for new drug development? Br J Pharmacol. 2007;152:838–854.
   PubMed Web of Science ®Google Scholar
• Reiding KR, Franc V, Huitema MG, et al. Neutrophil myeloperoxidase harbors distinct site-specific peculiarities in its glycosylation. J Biol Chem. 2019;294:20233–20245.
   PubMed Web of Science ®Google Scholar
• Jantschko W, Furtmüller PG, Zederbauer M, et al. Exploitation of the unusual thermodynamic properties of human myeloperoxidase in inhibitor design. Biochem Pharmacol. 2005;69:1149–1157.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Meyer F, Furtmüller P, et al. Characterization of chemical features of potent myeloperoxidase inhibitors. Future Med Chem. 2016;8:1163–1177.
   PubMed Web of Science ®Google Scholar
• Aldib I, Soubhye J, Zouaoui Boudjeltia K, et al. Evaluation of new scaffolds of myeloperoxidase inhibitors by rational design combined with high-throughput virtual screening. J Med Chem. 2012;55:7208–7218.
   PubMed Web of Science ®Google Scholar
• Bensalem S, Soubhye J, Aldib I, et al. Inhibition of myeloperoxidase activity by the alkaloids of Peganum harmala L (Zygophyllaceae). J Ethnopharmacol. 2014;154:361–369.
   PubMed Web of Science ®Google Scholar
• Aldib I, Gelbcke M, Soubhye J, et al. Novel bis-arylalkylamines as myeloperoxidase inhibitors: design, synthesis, and structure-activity relationship study. Eur J Med Chem. 2016;123:746–762.
   PubMed Web of Science ®Google Scholar
• Smallheer J, Kick E, Valente M, et al. Macrocyclic Inhibitors of Myeloperoxidase. WO/2018/005336, (2018).
   Google Scholar
• Hair PS, Enos AI, Krishna NK, et al. Inhibition of complement activation, myeloperoxidase, NET formation and oxidant activity by PIC1 peptide variants. Li Y. editor PLoS ONE. 2019;14:e0226875..
   PubMed Web of Science ®Google Scholar
• Hair PS, Sass LA, Krishna NK, et al. Inhibition of myeloperoxidase activity in cystic fibrosis sputum by peptide inhibitor of complement C1 (PIC1). Palaniyar N. editor PLoS ONE. 2017;12:e0170203..
   PubMed Web of Science ®Google Scholar
• Krishna N, Cunnion K PIC1 inhibition of myeloperoxidase oxidative activity in an animal model. WO/2019/139886 (2019).
   Google Scholar
• Zhang H, Jing X, Shi Y, et al. N-acetyl lysyltyrosylcysteine amide inhibits myeloperoxidase, a novel tripeptide inhibitor. J Lipid Res. 2013;54:3016–3029.
   PubMed Web of Science ®Google Scholar
• Hao Z, Yang S, Hao X, et al. Peptide-based myeloperoxidase inhibitors for use in therapy. EP2485750B1 (2010).
   Google Scholar
• Yu G, Liang Y, Huang Z, et al. Inhibition of myeloperoxidase oxidant production by N-acetyl lysyltyrosylcysteine amide reduces brain damage in a murine model of stroke. J Neuroinflammation. 2016;13:119.
   PubMed Web of Science ®Google Scholar
• Yu G, Zheng S, Zhang H. Inhibition of myeloperoxidase by N-acetyl lysyltyrosylcysteine amide reduces experimental autoimmune encephalomyelitis-induced injury and promotes oligodendrocyte regeneration and neurogenesis in a murine model of progressive multiple sclerosis:. NeuroReport. 2018;29:208–213.
   PubMed Web of Science ®Google Scholar
• van der Does AM, Hensbergen PJ, Bogaards SJ, et al. The human lactoferrin-derived peptide hLF1-11 exerts immunomodulatory effects by specific inhibition of myeloperoxidase activity. J Immunol. 2012;188:5012–5019.
   PubMed Web of Science ®Google Scholar
• Liu C, Desikan R, Ying Z, et al. Effects of a novel pharmacologic inhibitor of myeloperoxidase in a mouse atherosclerosis model. Schmidt HHHW. editor PLoS ONE. 2012;7:e50767.
   PubMed Web of Science ®Google Scholar
• Jayaraj P, Narasimhulu CA, Maiseyeu A, et al. Methoxyphenol derivatives as reversible inhibitors of myeloperoxidase as potential antiatherosclerotic agents. Future Med Chem. 2020;12:95–110.
   PubMed Web of Science ®Google Scholar
• Ximenes VF, Paino IMM, Faria-oliveira de OMM, et al. Indole ring oxidation by activated leukocytes prevents the production of hypochlorous acid. Braz J Med Biol Res. 2005;38:1575–1583.
   PubMed Web of Science ®Google Scholar
• Van Antwerpen P, Zouaoui Boudjeltia K. Rational drug design applied to myeloperoxidase inhibition. Free Radic Res. 2015;49:711–720.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Prévost M, Van Antwerpen P, et al. Structure-based design, synthesis, and pharmacological evaluation of 3-(Aminoalkyl)-5-fluoroindoles as myeloperoxidase inhibitors. J Med Chem. 2010;53:8747–8759.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Dufrasne F, Van Antwerpen P 3-Alkyl-5-fluoroindole derivatives as myeloperoxidase inhibitors. WO2010136546 (2010).
   Google Scholar
• Soubhye J, Aldib I, Prévost M, et al. Hybrid molecules inhibiting myeloperoxidase activity and serotonin reuptake: a possible new approach of major depressive disorders with inflammatory syndrome: hybrid MPO and 5-HT reuptake inhibitors. J Pharm Pharmacol. 2014. n/a-n/a. doi:10.1111/jphp.12236
   PubMed Web of Science ®Google Scholar
• Soubhye J, Aldib I, Elfving B, et al. Design, synthesis, and structure–activity relationship studies of novel 3-alkylindole derivatives as selective and highly potent myeloperoxidase inhibitors. J Med Chem. 2013;56:3943–3958.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Dufrasne F, Zouaoui Boudjeltia K, et al. Aromatic N-heterocycle derivatives for use as medicine. EP2682119 (2013).
   Google Scholar
• A-K T, Sjögren T, Svensson M, et al. 2-thioxanthines are mechanism-based inactivators of myeloperoxidase that block oxidative stress during inflammation. J Biol Chem. 2011;286:37578–37589.
   PubMed Web of Science ®Google Scholar
• Ward J, Spath SN, Pabst B, et al. Mechanistic characterization of a 2-thioxanthine myeloperoxidase inhibitor and selectivity assessment utilizing click chemistry–activity-based protein profiling. Biochemistry. 2013;52:9187–9201.
   PubMed Web of Science ®Google Scholar
• Piek A, Koonen DPY, Schouten E-M, et al. Pharmacological myeloperoxidase (MPO) inhibition in an obese/hypertensive mouse model attenuates obesity and liver damage, but not cardiac remodeling. Sci Rep. 2019;9(1):18765..
   PubMedGoogle Scholar
• Nordvall G, Tiden A, Hanson S Thioxanthine derivatives as myeloperoxidase inhibitors. WO/2003/089430 (2003).
   Google Scholar
• Barrett E, Aylor KW, Chai W, et al. Inhibition of myeloperoxidase and MPO reverses microvascular insulin resistance in high-fat diet (HFD)-fed Rats. Diabetes. 2018;67:22–LB.
   Web of Science ®Google Scholar
• Tong X, Zhou D, Savage A, et al. Population pharmacokinetic modeling with enterohepatic circulation for AZD3241 in healthy subjects and patients with multiple system Atrophy. J Clin Pharmacol. 2018;58:1452–1460.
   PubMed Web of Science ®Google Scholar
• Jucaite A, Svenningsson P, Rinne JO, et al. Effect of the myeloperoxidase inhibitor AZD3241 on microglia: a PET study in Parkinson’s disease. Brain. 2015;138:2687–2700.
   PubMed Web of Science ®Google Scholar
• AZD3241 PET MSA trial, phase 2, randomized,12 week safety and tolerability trial with pet in MSA patients [Internet]. [cited 2017 Sep 25]. Available from: https://clinicaltrials.gov/ct2/show/NCT02388295?term=Myeloperoxidase+inhibitor&draw=2&rank=3.
   Google Scholar
• Gan L-M, Lagerström-Fermér M, Ericsson H, et al. Safety, tolerability, pharmacokinetics and effect on serum uric acid of the myeloperoxidase inhibitor AZD4831 in a randomized, placebo-controlled, phase I study in healthy volunteers. Br J Clin Pharmacol. 2019;85:762–770.
   PubMed Web of Science ®Google Scholar
• MPO inhibitor A_Zeneca for HFpEF [Internet]. [cited 2020 Feb 5]. Available from: https://clinicaltrials.gov/ct2/show/NCT03611153.
   Google Scholar
• Li Y, Ganesh T, Diebold BA, et al. Thioxo-dihydroquinazolin-one compounds as novel inhibitors of myeloperoxidase. ACS Med Chem Lett. 2015;6:1047–1052.
   PubMed Web of Science ®Google Scholar
• Lambeth JD, Ganesh T, Smith SM, et al. Quinazoline derivatives, compositions, and uses related thereto. US20160243121 (2016).
   Google Scholar
• Wurtz NR, Viet A, Shaw SA, et al. Potent triazolopyridine Myeloperoxidase inhibitors. ACS Med Chem Lett. 2018;9:1175–1180.
   PubMed Web of Science ®Google Scholar
• Quoc Viet A, Wurtz NR Thioether triazolopyridine and triazolopyrimidine inhibitors of Myeloperoxidase. US20190031623 (2019).
   Google Scholar
• Ruggeri R 2-Thiopyrimidinones. WO/2016/178113 (2016).
   Google Scholar
• Ruggeri RB, Buckbinder L, Bagley SW, et al. Discovery of 2-(6-(5-Chloro-2-methoxyphenyl)-4-oxo-2-thioxo-3,4-dihydropyrimidin-1(2 H)-yl)acetamide (PF-06282999): A highly selective mechanism-based myeloperoxidase inhibitor for the treatment of cardiovascular diseases. J Med Chem. 2015;58:8513–8528.
   PubMed Web of Science ®Google Scholar
• Dong JQ, Varma MV, Wolford A, et al. Pharmacokinetics and disposition of the thiouracil derivative PF-06282999, an orally bioavailable, irreversible inactivator of Myeloperoxidase enzyme, across animals and humans. Drug Metab Dispos. 2016;44:209–219.
   PubMed Web of Science ®Google Scholar
• Dong JQ, Gosset JR, Fahmi OA, et al. Examination of the human Cytochrome P4503A4 induction potential of PF-06282999, an irreversible Myeloperoxidase inactivator: integration of Preclinical, in Silico, and biomarker methodologies in the prediction of the clinical outcome. Drug Metab Dispos. 2017;45:501–511.
   PubMed Web of Science ®Google Scholar
• Moscovitz JE, Lin Z, Johnson N, et al. Induction of human cytochrome P450 3A4 by the irreversible myeloperoxidase inactivator PF-06282999 is mediated by the pregnane X receptor. Xenobiotica. 2018;48:647–655.
   PubMed Web of Science ®Google Scholar
• Study A To evaluate the safety and effects on the body of an investigational drug using an endotoxin-induced inflammatory response model (POM) [Internet]. Available from: https://clinicaltrials.gov/ct2/show/NCT01965600?term=PF-06282999&draw=2&rank=3.
   Google Scholar
• Myeloperoxidase: AY. Its role for host defense, inflammation, and neutrophil function. Arch Biochem Biophys. 2018;640:47–52.
   PubMed Web of Science ®Google Scholar
• Lazarević-Pasti T, Leskovac A, Vasić V. Myeloperoxidase Inhibitors as Potential Drugs. Curr Drug Metab. 2015;16:168–190.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Chikh Alard I, Aldib I, et al. Discovery of novel potent reversible and irreversible Myeloperoxidase inhibitors using virtual screening procedure. J Med Chem. 2017;60:6563–6586.
   PubMed Web of Science ®Google Scholar
• Hasanpour Z, Javanmard S, Gharaaty M, et al. Association between serum myeloperoxidase levels and coronary artery disease in patients without diabetes, hypertension, obesity, and hyperlipidemia. Adv Biomed Res. 2016;5:103.
   PubMedGoogle Scholar
• Teng N, Maghzal GJ, Talib J, et al. The roles of myeloperoxidase in coronary artery disease and its potential implication in plaque rupture. Redox Rep. 2017;22:51–73.
   PubMed Web of Science ®Google Scholar
• Zeng L, Mathew AV, Byun J, et al. Myeloperoxidase-derived oxidants damage artery wall proteins in an animal model of chronic kidney disease–accelerated atherosclerosis. J Biol Chem. 2018;293:7238–7249.
   PubMed Web of Science ®Google Scholar
• Soubhye J, Gelbcke M, Van Antwerpen P, et al. From dynamic combinatorial chemistry to in vivo evaluation of reversible and irreversible Myeloperoxidase inhibitors. ACS Med Chem Lett. 2017;8:206–210.
   PubMed Web of Science ®Google Scholar
• Lemke T, Williams D. Principles of drug discovery. Foye’s principles of medicinal chemistry. 5th ed. ed. Lippincott, Philadelphia: Williams & Wilkins; 2002.
   Google Scholar
• Long L, Song Y. Myeloperoxidase: A promising therapeutic target in prevention of atherosclerosis. Int J Cardiol. 2018;256:15.
   PubMed Web of Science ®Google Scholar
• Wang W, Ren D, Wang C, et al. Inhibition of myeloperoxidase might be a novel therapeutic target in the treatment of atherosclerosis. Int J Cardiol. 2018;256:33.
   PubMed Web of Science ®Google Scholar
• Senders ML, Mulder WJM. Targeting myeloperoxidase in inflammatory atherosclerosis. Eur Heart J. 2018;39:3311–3313.
   PubMed Web of Science ®Google Scholar
• Lusis AJ. Atherosclerosis. Nature. 2000;407:233–241.
   PubMed Web of Science ®Google Scholar
• Insull W. The pathology of Atherosclerosis: plaque development and plaque responses to medical treatment. Am J Med. 2009;122:S3–S14.
   PubMed Web of Science ®Google Scholar
• Aviram M, Fuhrman B. LDL oxidation by arterial wall macrophages depends on the oxidative status in the lipoprotein and in the cells: role of prooxidants vs antioxidants. Mol Cell Biochem. 1998;188:149–159.
   PubMed Web of Science ®Google Scholar
• Rifai N. Tietz Textbook of Clinical Chemistry and Molecular Diagnostics. 6th ed. Saunders, USA; 2017.
   Google Scholar
• Breese BB. The use of the fluorescent antibody technic for identification of group A streptococci in pediatric practice. Am J Public Health Nations Health. 1968;58:2295–2305.
   PubMed Web of Science ®Google Scholar
• Li X, Fang P, Li Y, et al. Mitochondrial reactive oxygen species mediate Lysophosphatidylcholine-induced Endothelial cell activation. Arterioscler Thromb Vasc Biol. 2016;36:1090–1100
   PubMed Web of Science ®Google Scholar
• Williams KJ, Tabas I. The response-to-retention hypothesis of early Atherogenesis. Arterioscler Thromb Vasc Biol. 1995;15:551–561.
   PubMed Web of Science ®Google Scholar
• Pulli B, Ali M, Forghani R, et al. Measuring Myeloperoxidase activity in biological samples. Johnson R. editor PLoS ONE. 2013;8:e67976..
   PubMed Web of Science ®Google Scholar
• Hosseini M, Rezvani HR, Aroua N, et al. Targeting Myeloperoxidase disrupts mitochondrial redox balance and overcomes Cytarabine resistance in human Acute Myeloid Leukemia. Cancer Res. 2019;79:5191–5203.
   PubMed Web of Science ®Google Scholar
• Wadghiri YZ, Hoang DM, Leporati A, et al. High-resolution imaging of Myeloperoxidase activity sensors in human cerebrovascular disease. Sci Rep. 2018;8:7687.
   PubMed Web of Science ®Google Scholar
• Roth Flach RJ, Su C, Bollinger E, et al. Myeloperoxidase inhibition in mice alters atherosclerotic lesion composition. Bader M. editor PLoS ONE. 2019;14:e0214150.
   PubMed Web of Science ®Google Scholar
• Rashid I, Maghzal GJ, Chen Y-C, et al. Myeloperoxidase is a potential molecular imaging and therapeutic target for the identification and stabilization of high-risk atherosclerotic plaque. Eur Heart J. 2018;39:3301–3310.
   PubMed Web of Science ®Google Scholar
• Kaindlstorfer C, Sommer P, Georgievska B, et al. Failure of neuroprotection despite microglial suppression by delayed-start Myeloperoxidase inhibition in a model of advanced multiple system Atrophy: clinical Implications. Neurotox Res. 2015;28:185–194.
   PubMed Web of Science ®Google Scholar
• AstraZeneca's open innovation pharmacology toolbox. [Internet]. [cited 2014 Nov]. Available from: https://openinnovation.astrazeneca.com/clinical-compound-bank.html.
   Google Scholar