1. Minnerup J., Sutherland B. A., Buchan A. M., Kleinschnitz C. Neuroprotection for stroke: current status and future perspectives. International Journal of Molecular Sciences, 2012, vol. 13, no. 12, pp. 11753-11772. https://doi.org/10.3390/ijms130911753
2. Lyden P., Wahlgren N. G. Mechanisms of action of neuroprotectants in stroke. Journal of Stroke and Cerebrovascular Diseases, 2000, vol. 9, no. 6, pp. 9-14. https://doi.org/10.1053/jscd.2000.19316
3. Ginsberg M. D. Neuroprotection for ischemic stroke: Past, present and future. Neuropharmacology, 2008, vol. 55, no. 3, pp. 363-389. https://doi.org/10.1016/j.neuropharm.2007.12.007
4. Gitler A. D., Dhillon P., Shorter J. Neurodegenerative disease: models, mechanisms, and a new hope. Disease Models and Mechanisms, 2017, vol. 10, no. 5, pp. 499-502. https://doi.org/10.1242/dmm.030205
5. Liu Z., Zhou T., Ziegler A. C., Dimitrion P., Zuo L. Oxidative stress in neurodegenerative diseases: from molecular mechanisms to clinical applications. Oxidative Medicine and Cellular Longevity, 2017, vol. 2017, art. ID 2525967. https://doi.org/10.1155/2017/2525967
6. Rahal A., Kumar A., Singh V., Yadav B., Tiwari R., Chakraborty S., Dhama K. Oxidative stress, prooxidants, and antioxidants: The interplay. BioMed Research International, 2014, vol. 2014, art. ID 761264. https://doi.org/10.1155/2014/761264
7. Bacigaluppi M., Hermann D. M. New targets of neuroprotection in ischemic stroke. Scientific World Journal, 2008, vol. 8, art. ID 974246. https://doi.org/10.1100/tsw.2008.94
8. McBean G. J., Aslan M., Griffiths H. R., Torrão R. C. Thiol redox homeostasis in neurodegenerative disease. Redox Biology, 2015, vol. 5, pp. 186-194. https://doi.org/10.1016/j.redox.2015.04.004
9. Shimohama S., Tanino H., Kawakami N., Okamura N., Kodama H., Yamaguchi T. [et al.]. Activation of NADPH oxidase in Alzheimer’s disease brains. Biochemical and Biophysical Research Communications, 2000, vol. 273, no. 1, pp. 5-9. https://doi.org/10.1006/bbrc.2000.2897
10. Ben-Yoseph O., Boxer P. A., Ross B. D. Assessment of the role of the glutathione and pentose phosphate pathways in the protection of primary cerebrocortical cultures from oxidative stress. Journal of Neurochemistry, 1996, vol. 66, no. 6, pp. 2329-2337. https://doi.org/10.1046/j.1471-4159.1996.66062329.x
11. Paik S. R., Lee D., Cho H.-J., Lee E.-N., Chang Ch.-S. Oxidized glutathione stimulated the amyloid formation of α-synuclein. FEBS Letters, 2003, vol. 537, no. 1-3, pp. 63-67. https://doi.org/10.1016/s0014-5793(03)00081-4
12. Penionzhkevich D. Yu., Gorbunov F. E. New technologies of neurometabolic therapy of cerebrovascular diseases. Zhurnal nevrologii i psikhiatrii imeni C. C. Korsakova = Journal of neurology and psychiatry named after S. S. Korsakov, 2009, vol. 109, no. 7, pp. 19-22 (in Russian).
13. Tymianski M. Can molecular and cellular neuroprotection be translated into therapies for patients? Yes, but not the way we tried it before. Stroke, 2010, vol. 41, no. 10, suppl. 1, pp. S87-S90. https://doi.org/10.1161/strokeaha.110.595496
14. Couto N., Wood J., Barber J. The role of glutathione reductase and related enzymes on cellular redox homoeostasis network. Free Radical Biology and Medicine, 2016, vol. 95, pp. 27-42. https://doi.org/10.1016/j.freeradbiomed.2016.02.028
15. Moiseenok A. G., Komar V. I., Khomich T. I., Kanunnikova N. P., Slyshenkov V. S. Pantothenic acid in maintaining thiol and immune homeostasis. BioFactors, 2000, vol. 11, pp. 53-55. https://doi.org/10.1002/biof.5520110115
16. Onufriev M. V., Stepanichev M. Y., Lazareva N. V., Katkovskaya I. N., Tishkina A. O., Moiseenok A. G., Gulyaeva N. V. Panthenol as neuroprotectant: study in a rat model of middle cerebral artery occlusion. Journal of Neurochemistry, 2010, vol. 4, no. 2, pp. 148-152. https://doi.org/10.1134/s181971241002011x
17. Kovler M. A., Karaev A. L., Pomerantseva T. Ya., Kozlova G. S., Mikhailova G. S., Gunar V. I., Dorofeev B. F., Moiseenok A. G. Results of an experimental and clinical study of the domestic drug panthevitol (panthenol). Pantenol i drugie proizvodnye pantotenovoi kisloty: materialy Mezhdunarodnogo simpoziuma (Grodno, 3-5 iyunya 1998 goda) [Panthenol and other derivatives of pantothenic acid: materials of the International symposium (Grodno, June 3-5, 1998)]. Grodno, 1998, pp. 99-106 (in Russian).
18. Oleshkevich F. V., Skorokhod A. A., Moiseenok A. G. Neuroprotective effect of pantothenic acid derivatives in surgical treatment of arterial aneurysms of the brain. Zhurnal teoreticheskoi i klinicheskoi meditsiny [Journal of theoretical and clinical medicine], 2000, no. 3, pp. 232-233 (in Russian).
19. Yamagata K., Ichinose S., Miyashita A., Tagami M. Protective effect of ebselen, a seleno-organic antioxidant on neurodegeneration induced by hypoxia and reperfusion in stroke-prone spontaneously hypertensive rat. Neuroscience, 2008, vol. 153, no. 2, pp. 428-435. https://doi.org/10.1016/j.neuroscience.2008.02.028
20. Parnham M., Sies H. Ebselen: prospective therapy for cerebral ischaemia. Expert Opinion on Investigational Drugs, 2000, vol. 9, no. 3, pp. 607-619. https://doi.org/10.1517/13543784.9.3.607
21. Lejay A., Paradis S., Lambert A., Charles A.-L., Talha S., Enache I., Thaveau F., Chakfe N., Geny B. N-acetyl cysteine restores limb function, improves mitochondrial respiration, and reduces oxidative stress in a murine model of critical limb ischaemia. European Journal of Vascular and Endovascular Surgery, 2018, vol. 56, no. 5, pp. 730-738. https://doi.org/10.1016/j.ejvs.2018.07.025
22. Lobanova N. N., Medvedev N. I., Popov V. I., Murashev A. N. Modeling global cerebral ischemia by bilateral carotid artery occlusion in awake hypertensive rats (SHR-SP). Byulleten’ eksperimental’noi biologii i meditsiny [Bulletin of experimental biology and medicine], 2008, vol. 146, no. 12, pp. 627-630 (in Russian).
23. Verde V., Fogliano V., Ritieni A., Maiani G., Morisco F., Caporaso N. Use of N,N-dimethyl-p-phenylenediamine to evaluate the oxidative status of human plasma. Free Radical Research, 2002, vol. 36, no. 8, pp. 869-873. https://doi.org/10.1080/1071576021000005302
24. Williamson K. S., Hensley K., Floyd R. A. Fluorometric and colorimetric assessment of thiobarbituric acid-reactive lipid aldehydes in biological matrices. Methods in Biological Oxidative Stress. New York, 2003, pp. 57-65.
25. Hermes-Lima M., Willmore W. G., Storey K. B. Quantification of lipid peroxidation in tissue extracts based on Fe(III) xylenol orange complex formation. Free Radical Biology and Medicine, 1995, vol. 19, no. 3, pp. 271-280. https://doi.org/10.1016/0891-5849(95)00020-x
26. Arutyunyan A. V., Dubinina E. E., Zybina N. N. Methods for assessing free radical oxidation and antioxidant system of the body. St. Petersburg, St. Petersburg Institute of Bioregulation and Gerontology, 2000. 102 p. (in Russian).
27. Ninfali P., Aluigi G., Pompella A. Methods for studying the glucose-6-phosphate dehydrogenase activity in brain areas. Brain Reserch Protocols, 1997, vol. 1, no. 4, pp. 357-363. https://doi.org/10.1016/s1385-299x(97)00011-1
28. Quirós P. M. Determination of aconitase activity: a substrate of the mitochondrial ion protease. Methods in Molecular Biology. New York, 2018, vol. 1731, pp. 49-56. https://doi.org/10.1007/978-1-4939-7595-2_5
29. Eshchenko N. D., Vol’skii G. G. Determination of the amount of succinic acid and the activity of succinate dehydrogenase. Biochemical research methods (lipid and energy metabolism). Leningrad, 1982, pp. 207-212 (in Russian).
30. Bisswanger H. Practical Enzymology. 2nd ed. Weinheim, Wiley-VCH Verlag GmbH and Co., 2013. 376 p.
31. Anderson M. Determination of glutathione and glutathione disulfide in biological samples. Methods in Enzymology. Glutamate, Glutamine, Glutathione, and Related Compounds. Vol. 113. Orlando, 1985, pp. 548-555.
32. Rahman I., Kode A., Biswas S. K. Assay for quantitative determination of glutathione and glutathione disulfide levels using enzymatic recycling method. Nature Protocols, 2006, vol. 1, no. 6, pp. 3159-3165. https://doi.org/10.1038/nprot.2006.378
33. Smith I. K., Vierheller T. L., Thorne C. A. Assay of glutathione reductase in crude tissue homogenates using 5,5ˊ-dithiobis(2-nitrobenzoic acid). Analytical Biochemistry, 1988, vol. 175, no. 2, pp. 408-413. https://doi.org/10.1016/0003-2697(88)90564-7
34. Flohé L., Günzler W. A. Assays of glutathione peroxidase. Methods in Enzymology. Oxygen Radicals in Biological Systems. Vol. 105. Orlando, 1984, pp. 114-121.
35. Menon D., Board P. G. A fluorometric method to quantify protein glutathionylation using glutathione derivatization with 2,3-naphthalenedicarboxaldehyde. Analytical Biochemistry, 2013, vol. 433, no. 2, pp. 132-136. https://doi.org/10.1016/j.ab.2012.10.009