References
- Prnova MS, Kovacikova L, Svik K, et al. Triglyceride-lowering effect of the aldose reductase inhibitor cemtirestat—another factor that may contribute to attenuation of symptoms of peripheral neuropathy in STZ-diabetic rats. Naunyn Schmiedebergs Arch Pharmacol. 2020;393:651–661. doi: 10.1007/s00210-019-01769-1.
- Prnova MS, Svik K, Bezek S, et al. 3-Mercapto-5H-1,2,4-triazino[5,6-b]indole-5-acetic acid (cemtirestat) alleviates symptoms of peripheral diabetic neuropathy in zucker diabetic fatty (ZDF) rats: a role of aldose reductase. Neurochem Res. 2019:44;1056–1064. doi: 10.1007/s11064-019-02736-1.
- Prnova MS, Ballekova J, Majekova M, et al. Antioxidant action of 3-mercapto-5h-1,2,4-triazino[5,6-b]indole-5-acetic acid, an efficient aldose reductase inhibitor, in a 1,1′-diphenyl-2-picrylhydrazyl assay and in the cellular system of isolated erythrocytes exposed to tert-butyl hydroperoxide. Redox Rep. 2015:20;282–288. doi: 10.1179/1351000215Y.0000000019.
- Soltesova MP, Medina-Campos ON, Pedraza-Chaverri J, et al. Antioxidant mechanisms in the neuroprotective action of cemtirestat: studies in chemical models, liposomes and rat brain cortical slices. Neuroscience. 2020;443;206–217. doi: 10.1016/j.neuroscience.2020.07.014.
- Hlaváč M, Kováčiková L, Prnová MŠ, et al. Development of novel oxotriazinoindole inhibitors of aldose reductase: isosteric sulfur/oxygen replacement in the thioxotriazinoindole cemtirestat markedly improved inhibition selectivity. J Med Chem. 2020:63;369–381. doi: 10.1021/acs.jmedchem.9b01747.
- Bodo P, Kovacikova L, Bohac A, et al. Cu(II) mediated oxidation of Cemtirestat yields its disulfide under physiological conditions in vitro. Chem Pap. 2022:76;6783–6788. doi: 10.1007/s11696-022-02368-w.
- Rackova L, Stefek M, Majekova M. Structural aspects of antioxidant activity of substituted pyridoindoles. Redox Rep. 2002:7;207–214. doi: 10.1179/135100002125000578.
- Mihaljević B, Katusin-Razem B, Razem D. The reevaluation of the ferric thiocyanate assay for lipid hydroperoxides with special considerations of the mechanistic aspects of the response. Free Radic Biol Med. 1996:21;53–63. doi: 10.1016/0891-5849(95)02224-4.
- Elder JB, Broome JA, Bushnell EAC. Computational insights into the regeneration of ovothiol and ergothioneine and their selenium analogues by glutathione. ACS Omega 2022:7;31813–31821. doi: 10.1021/acsomega.2c02506.
- Osik NA, Zelentsova EA, Tsentalovich YP. Kinetic studies of antioxidant properties of ovothiol A. Antioxidants. 2021:10;1470. doi: 10.3390/antiox10091470.
- Yanshole VV, Yanshole LV, Zelentsova EA, et al. Ovothiol A is the main antioxidant in fish lens. Metabolites. 2019:9;95. doi: 10.3390/metabo9050095.
- Weaver KH, Rabenstein DL. Thiol/disulfide exchange reactions of ovothiol A with glutathione. J OrgChem. 1995:60;1904–1907. doi: 10.1021/jo00111a065.
- Trotta RJ, Sullivan SG, Stern A. Lipid peroxidation and haemoglobin degradation in red blood cells exposed to t-butyl hydroperoxide. The relative roles of haem and glutathione dependent decomposition of t-butyl hydroperoxide and membrane lipid hydroperoxides in lipid peroxidation and haemolysis. Biochem J. 1983:212;759–72. doi: 10.1042/bj2120759.
- Jeong EM, Yoon JH, Lim J, et al. Real-time monitoring of glutathione in living cells reveals that high glutathione levels are required to maintain stem cell function. Stem Cell Rep. 2018;10:600–614. doi: 10.1016/j.stemcr.2017.12.007.
- Munday R. Toxicity of thiols and disulphides: involvement of free-radical species. Free Radic Biol Med. 1989:7;659–673. doi: 10.1016/0891-5849(89)90147-0.