1. Кутихин А.Г., Синицкий М.Ю., Понасенко А.В. Роль мутагенеза в развитии атеросклероза. Комплекс. проблемы серд.-сосуд. заболеваний. 2017; (1): 92–101.
Kutikhin A.G., Sinitsky M.Yu., Ponasenko A.V. The role of mutagenesis in atherosclerosis. Kompleksnye problemy serdechno-sosudistykh zabolevaniy = Complex Issues of Cardiovascular Diseases. 2017; (1): 92–101. [In Russian].
2. Шишкова Д.К., Великанова Е.А., Кривкина Е.О., Миронов А.В., Кудрявцева Ю.А., Кутихин А.Г. Кальций-фосфатные бионы специфично индуцируют гипертрофию поврежденной интимы у крыс. Рос. кардиол. журн. 2018; 23 (9): 33–38.
Shishkova D.K., Velikanova E.A., Krivkina E.O., Mironov A.V., Kudryavtseva Yu.A., Kutikhin A.G. Calcium-phosphate bions do specifically induce hypertrophy of damaged intima in rats. Rossiyskiy kardiologicheskiy zhurnal = Russian Journal of Cardiology. 2018; 23 (9): 33–38. [In Russian].
3. Шишкова Д.К., Великанова Е.А., Кривкина Е.О., Миронов А.В., Кудрявцева Ю.А., Кутихин А.Г. Токсическое действие кальций-фосфатных бионов на адвентицию брюшной аорты крыс. Атеросклероз и дислипидемии. 2018; (3): 37–43.
Shishkova D.K., Velikanova E.A., Krivkina E.O., Mironov A.V., Kudryavtseva Yu.A., Kutikhin A.G. Toxicity of calcium phosphate bions for aortic adventitia in rats. Ateroskleroz i dislipidemii = The Journal of Atherosclerosis and Dyslipidemias. 2018; 3: 37–43. [In Russian].
4. Bowman E.J., Siebers A., Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. USA. 1988; 85 (21): 7972–7976.
5. Ewence A.E., Bootman M., Roderick H.L., Skepper J.N., McCarthy G., Epple M., Neumann M., Shanahan C.M., Proudfoot D. Calcium phosphate crystals induce cell death in human vascular smooth muscle cells: a potential mechanism in atherosclerotic plaque destabilization. Circ. Res. 2008; 103 (5): e28–e34.
6. Foley R.N., Collins A.J., Ishani A., Kalra P.A. Calcium-phosphate levels and cardiovascular disease in community-dwelling adults: the Atherosclerosis Risk in Communities (ARIC) Study. Am. Heart J. 2008; 156 (3): 556–563.
7. Galluzzi L., Vitale I., Aaronson S.A., Abrams J.M., Adam D., Agostinis P., Alnemri E.S., Altucci L., Amelio I., Andrews D.W., Annicchiarico-Petruzzelli M., Antonov A.V., Arama E., Baehrecke E.H., Barlev N.A., Bazan N.G., Bernassola F., Bertrand M.J.M., Bianchi K., Blagosklonny M.V., Blomgren K., Borner C., Boya P., Brenner C., Campanella M., Candi E., Carmona-Gutierrez D., Cecconi F., Chan F.K., Chandel N.S., Cheng E.H., Chipuk J.E., Cidlowski J.A., Ciechanover A., Cohen G.M., Conrad M., Cubillos-Ruiz J.R., Czabotar P.E., D’Angiolella V., Dawson T.M., Dawson V.L., de Laurenzi V., de Maria R., Debatin K.M., de Berardinis R.J., Deshmukh M., di Daniele N., di Virgilio F., Dixit V.M., Dixon S.J., Duckett C.S., Dynlacht B.D., El-Deiry W.S., Elrod J.W., Fimia G.M., Fulda S., García-Sáez A.J., Garg A.D., Garrido C., Gavathiotis E., Golstein P., Gottlieb E., Green D.R., Greene L.A., Gronemeyer H., Gross A., Hajnoczky G., Hardwick J.M., Harris I.S., Hengartner M.O., Hetz C., Ichijo H., Jäättelä M., Joseph B., Jost P.J., Juin P.P., Kaiser W.J., Karin M., Kaufmann T., Kepp O., Kimchi A., Kitsis R.N., Klionsky D.J., Knight R.A., Kumar S., Lee S.W., Lemasters J.J., Levine B., Linkermann A., Lipton S.A., Lockshin R.A., López-Otín C., Lowe S.W., Luedde T., Lugli E., MacFarlane M., Madeo F., Malewicz M., Malorni W., Manic G., Marine J.C., Martin S.J., Martinou J.C., Medema J.P., Mehlen P., Meier P., Melino S., Miao E.A., Molkentin J.D., Moll U.M., Muñoz-Pinedo C., Nagata S., Nuñez G., Oberst A., Oren M., Overholtzer M., Pagano M., Panaretakis T., Pasparakis M., Penninger J.M., Pereira D.M., Pervaiz S., Peter M.E., Piacentini M., Pinton P., Prehn J.H.M., Puthalakath H., Rabinovich G.A., Rehm M., Rizzuto R., Rodrigues C.M.P., Rubinsztein D.C., Rudel T., Ryan K.M., Sayan E., Scorrano L., Shao F., Shi Y., Silke J., Simon H.U., Sistigu A., Stockwell B.R., Strasser A., Szabadkai G., Tait S.W.G., Tang D., Tavernarakis N., Thorburn A., Tsujimoto Y., Turk B., Vanden Berghe T., Vandenabeele P., Vander Heiden M.G., Villunger A., Virgin H.W., Vousden K.H., Vucic D., Wagner E.F., Walczak H., Wallach D., Wang Y., Wells J.A., Wood W., Yuan J., Zakeri Z., Zhivotovsky B., Zitvogel L., Melino G., Kroemer G. Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018. Cell Death Differ. 2018; 25 (3): 486–541.
8. Julien O., Wells J.A. Caspases and their substrates. Cell Death Differ. 2017; 24 (8): 1380–1389.
9. Kumar S., Kasseckert S., Kostin S., Abdallah Y., Schafer C., Kaminski A., Reusch H.P., Piper H.M., Steinhoff G., Ladilov Y. Ischemic acidosis causes apoptosis in coronary endothelial cells through activation of caspase-12. Cardiovasc. Res. 2007; 73 (1): 172–180.
10. Kutikhin A.G., Velikanova E.A., Mukhamadiyarov R.A., Glushkova T.V., Borisov V.V., Matveeva V.G., Antonova L.V., Filipev D.E., Golovkin A.S., Shishkova D.K., Burago A.Y., Frolov A.V., Dolgov V.Y., Efimova O.S., Popova A.N., Malysheva V.Y., Vladimirov A.A., Sozinov S.A., Ismagilov Z.R., Russakov D.M., Lomzov A.A., Pyshnyi D.V., Gutakovsky A.K., Zhivodkov Y.A., Demidov E.A., Peltek S.E., Dolganyuk V.F., Babich O.O., Grigoriev E.V., Brusina E.B., Barbarash O.L., Yuzhalin A.E. Apoptosis-mediated endothelial toxicity but not direct calcification or functional changes in anti-calcification proteins defines pathogenic effects of calcium phosphate bions. Sci. Rep. 2016; 6: 27255.
11. Larsson T.E., Olauson H., Hagström E., Ingelsson E., Arnlöv J., Lind L., Sundström J. Conjoint effects of serum calcium and phosphate on risk of total, cardiovascular, and noncardiovascular mortality in the community. Arterioscler. Thromb. Vasc. Biol. 2010; 30 (2): 333–339.
12. Lind L., Skarfors E., Berglund L., Lithell H., Ljunghall S. Serum calcium: a new, independent, prospective risk factor for myocardial infarction in middle-aged men followed for 18 years. J. Clin. Epidemiol. 1997; 50 (8): 967–973.
13. Liu Z., Xiao Y., Chen W., Wang Y., Wang B., Wang G., Xu X., Tang R. Calcium phosphate nanoparticles primarily induce cell necrosis through lysosomal rupture: the origination of material cytotoxicity. J. Mater. Chem. B. 2014; 2: 3480–3489.
14. Shalini S., Dorstyn L., Dawar S., Kumar S. Old, new and emerging functions of caspases. Cell Death Differ. 2015; 22 (4): 526–539.
15. Shyong Y.J., Wang M.H., Kuo L.W., Su C.F., Kuo W.T., Chang K.C., Lin F.H. Mesoporous hydroxyapatite as a carrier of olanzapine for long-acting antidepression treatment in rats with induced depression. J. Control Release. 2017; 255: 62–72.
16. Shyong Y.J., Wang M.H., Tseng H.C., Cheng C., Chang K.C., Lin F.H. Mesoporous hydroxyapatite as olanzapine carrier provides a long-acting effect in antidepression treatment. J. Med. Chem. 2015; 58 (21): 8463–8474.
17. Tewari M., Quan L.T., O’Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 1995; 81 (5): 801–809.
18. Wu C.Y., Young L., Young D., Martel J., Young J.D. Bions: a family of biomimetic mineralo-organic complexes derived from biological fluids. PLoS One. 2013; 8 (9): e75501.
19. Yoshimori T., Yamamoto A., Moriyama Y., Futai M., Tashiro Y. Bafilomycin A1, a specific inhibitor of vacuolar-type H+-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells. J. Biol. Chem. 1991; 266 (26): 17707–17712.
20. Yuan Y., Liu C., Qian J., Wang J., Zhang Y. Size-mediated cytotoxicity and apoptosis of hydroxyapatite nanoparticles in human hepatoma HepG2 cells. Biomaterials. 2010; 31 (4): 730–740.
21. Zhang C.Y., Sun X.Y., Ouyang J.M., Gui B.S. Diethyl citrate and sodium citrate reduce the cytotoxic effects of nanosized hydroxyapatite crystals on mouse vascular smooth muscle cells. Int. J. Nanomedicine. 2017; 12: 8511–8525.