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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">scbmt</journal-id><journal-title-group><journal-title xml:lang="ru">БИОМЕДИЦИНА</journal-title><trans-title-group xml:lang="en"><trans-title>Journal Biomed</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2074-5982</issn><issn pub-type="epub">2713-0428</issn><publisher><publisher-name>Scientific center of biomedical technologies of Federal Medical and Biological Agency</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.33647/2074-5982-15-3-71-77</article-id><article-id custom-type="elpub" pub-id-type="custom">scbmt-144</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>МЕТОДЫ БИОМЕДИЦИНСКИХ ИССЛЕДОВАНИЙ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>METHODS OF BIOMEDICAL RESEARCHES</subject></subj-group></article-categories><title-group><article-title>ИЗУЧЕНИЕ ФУНКЦИЙ МИТОХОНДРИЙ В ЭКСПЕРИМЕНТЕ</article-title><trans-title-group xml:lang="en"><trans-title>RESEARCH INTO THE FUNCTIONS OF MITOCHONDRIA IN EXPERIMENT</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Максимович</surname><given-names>Н. Е.</given-names></name><name name-style="western" xml:lang="en"><surname>Maksimovich</surname><given-names>N. Ye.</given-names></name></name-alternatives><bio xml:lang="ru"><p>д.м.н., проф.,</p><p>230009, Гродно, ул. Горького, д. 80</p></bio><bio xml:lang="en"><p>230009, Grodno, Gorkogo str., 80</p></bio><email xlink:type="simple">mne@grsmu.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Бонь</surname><given-names>Е. И.</given-names></name><name name-style="western" xml:lang="en"><surname>Bon</surname><given-names>E. I.</given-names></name></name-alternatives><bio xml:lang="ru"><p>к.б.н.,</p><p>230009, Гродно, ул. Горького, д. 80</p></bio><bio xml:lang="en"><p>230009, Grodno, Gorkogo str., 80</p></bio><email xlink:type="simple">asphodela@list.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дремза</surname><given-names>И. К.</given-names></name><name name-style="western" xml:lang="en"><surname>Dremza</surname><given-names>I. K.</given-names></name></name-alternatives><bio xml:lang="ru"><p>к.б.н., доц.,</p><p>230009, Гродно, ул. Горького, д. 80</p></bio><bio xml:lang="en"><p>230009, Grodno, Gorkogo str., 80</p></bio><email xlink:type="simple">idremza@rambler.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru">УО «Гродненский государственный медицинский университет»<country>Беларусь</country></aff><aff xml:lang="en">Grodno State Medical University<country>Belarus</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2019</year></pub-date><pub-date pub-type="epub"><day>06</day><month>09</month><year>2019</year></pub-date><volume>0</volume><issue>3</issue><fpage>71</fpage><lpage>77</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Максимович Н.Е., Бонь Е.И., Дремза И.К., 2019</copyright-statement><copyright-year>2019</copyright-year><copyright-holder xml:lang="ru">Максимович Н.Е., Бонь Е.И., Дремза И.К.</copyright-holder><copyright-holder xml:lang="en">Maksimovich N.Y., Bon E.I., Dremza I.K.</copyright-holder><license license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://journal.scbmt.ru/jour/article/view/144">https://journal.scbmt.ru/jour/article/view/144</self-uri><abstract><p>Митохондрии играют ключевую роль в жизнедеятельности клетки. Наиболее характерной их особенностью является наличие большого числа ферментов, участвующих в окислительном фосфорилировании и снабжении клетки энергией. Кроме того, митохондрии участвуют в хранении и передаче наследственной информации, апоптозе и пластических процессах. Нарушением функций митохондрий сопровождается любое заболевание, поэтому дальнейшее исследование функциональных особенностей митохондрий при различной патологии в клинике и эксперименте, а также поиск новых диагностических маркеров перспективны и актуальны.</p></abstract><trans-abstract xml:lang="en"><p>Mitochondria play a key role in the life of any cell. The most characteristic feature of mitochondria is the presence of a large number of enzymes involved in oxidative phosphorylation and the supply of a cell with energy. In addition, mitochondria participate in the storage and transmission of hereditary information, as well as in apoptosis and plastic processes. Any disease is associated with violation of the mitochondrion functions; therefore, research into the functional characteristics of mitochondria in various pathologies under clinical and experimental conditions, as well as a search for new diagnostic markers seem to be a promising and relevant task.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>митохондрии</kwd><kwd>метаболизм</kwd><kwd>экспериментальное изучение</kwd></kwd-group><kwd-group xml:lang="en"><kwd>mitochondria</kwd><kwd>metabolism</kwd><kwd>experimental study</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Baertling F. NDUFA9 point mutations cause a variable mitochondrial complex I assembly defect. Clinical Genet. 2018;93:111–118.</mixed-citation><mixed-citation xml:lang="en">Baertling F. NDUFA9 point mutations cause a variable mitochondrial complex I assembly defect. Clinical Genet. 2018;93:111–118.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Boumans H., Grivell L.A., Berden J.A. The respiratory chain in yeast behaves as a single functional unit. J. Biol. Chem. 1998;273:4872–4877.</mixed-citation><mixed-citation xml:lang="en">Boumans H., Grivell L.A., Berden J.A. The respiratory chain in yeast behaves as a single functional unit. J. Biol. Chem. 1998;273:4872–4877.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Boyer P.D. ATP synthase — past and future. Biochim. Biophys. Acta. 1998;1365:3–9.</mixed-citation><mixed-citation xml:lang="en">Boyer P.D. ATP synthase — past and future. Biochim. Biophys. Acta. 1998;1365:3–9.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Brand M.D., Murphy M.P. Control of electron fl ux through the respiratory chain in mitochondria and cells. Biological Review. 1987;62:141–193.</mixed-citation><mixed-citation xml:lang="en">Brand M.D., Murphy M.P. Control of electron fl ux through the respiratory chain in mitochondria and cells. Biological Review. 1987;62:141–193.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Britti E. Frataxin-defi cient neurons and mice models of Friedreich ataxia are improved by TAT-MTScsFXN treatment. J. Cell Mol. Med. 2018;22:834–848.</mixed-citation><mixed-citation xml:lang="en">Britti E. Frataxin-defi cient neurons and mice models of Friedreich ataxia are improved by TAT-MTScsFXN treatment. J. Cell Mol. Med. 2018;22:834–848.</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Capaldi R.A., Darley-Usmar V., Fuller S., Millet F. Structural and functional features of the interaction of cytochrome с with complex III and cytochrome с oxidase. FEBS Letters. 1982;138:1–7.</mixed-citation><mixed-citation xml:lang="en">Capaldi R.A., Darley-Usmar V., Fuller S., Millet F. Structural and functional features of the interaction of cytochrome с with complex III and cytochrome с oxidase. FEBS Letters. 1982;138:1–7.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Casey R.P. Membrane reconstruction of the energy-conserving enzymes of oxidative phosphorylation. Biochemistry Acta. 1984;768:319–347.</mixed-citation><mixed-citation xml:lang="en">Casey R.P. Membrane reconstruction of the energy-conserving enzymes of oxidative phosphorylation. Biochemistry Acta. 1984;768:319–347.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Chao D.T., Korsmeyer S.J. BCL-2 family: regulators of cell death. Annu. Rev. Immunol. 1998;16:395–419.</mixed-citation><mixed-citation xml:lang="en">Chao D.T., Korsmeyer S.J. BCL-2 family: regulators of cell death. Annu. Rev. Immunol. 1998;16:395–419.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Chen X., Lu J. Analysis of mitochondrial gene mutations in a child with Leigh syndrome. Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 2019;36(4):318–321.</mixed-citation><mixed-citation xml:lang="en">Chen X., Lu J. Analysis of mitochondrial gene mutations in a child with Leigh syndrome. Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 2019;36(4):318–321.</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">DePierre J.W., Ernster L. Enzyme topology of intracellular membranes. Review Biochemistry. 1988;46:201– 261.</mixed-citation><mixed-citation xml:lang="en">DePierre J.W., Ernster L. Enzyme topology of intracellular membranes. Review Biochemistry. 1988;46:201– 261.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Hackenbrock C.R. Lateral diffusion and electron transfer in the mitochondrial inner membrane. Trends Biochemistry. 1981;15:151–154.</mixed-citation><mixed-citation xml:lang="en">Hackenbrock C.R. Lateral diffusion and electron transfer in the mitochondrial inner membrane. Trends Biochemistry. 1981;15:151–154.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Hauser D.N. Hexokinases link DJ-1 to the PINK1/parkin pathway. Mol. Neurodegener. 2017;12:70–77.</mixed-citation><mixed-citation xml:lang="en">Hauser D.N. Hexokinases link DJ-1 to the PINK1/parkin pathway. Mol. Neurodegener. 2017;12:70–77.</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Hoffmann C. The effect of differentiation and TGFß on mitochondrial respiration and mitochondrial enzyme abundance in cultured primary human skeletal muscle cells. Science Report. 2018;8:737–740.</mixed-citation><mixed-citation xml:lang="en">Hoffmann C. The effect of differentiation and TGFß on mitochondrial respiration and mitochondrial enzyme abundance in cultured primary human skeletal muscle cells. Science Report. 2018;8:737–740.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Klinyerberg M. Principles of carrier catalysis elucidated by comparing two similar membrane translocators from mitochondria, the ADP/ATP carrier and the uncoupling protein. New York Academic Science. 1985;456:279–288.</mixed-citation><mixed-citation xml:lang="en">Klinyerberg M. Principles of carrier catalysis elucidated by comparing two similar membrane translocators from mitochondria, the ADP/ATP carrier and the uncoupling protein. New York Academic Science. 1985;456:279–288.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Magnoni R. The Hsp60 folding machinery is crucial for manganese superoxide dismutase folding and function. Free Radic Res. 2014;48:168–179.</mixed-citation><mixed-citation xml:lang="en">Magnoni R. The Hsp60 folding machinery is crucial for manganese superoxide dismutase folding and function. Free Radic Res. 2014;48:168–179.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Mikkilineni L., Whitaker-Menezes D., Domingo-Vidal M., Sprandio J. Hodgkin lymphoma: A complex metabolic ecosystem with glycolytic reprogramming of the tumor microenvironment. Semin Oncol. 2017;44:218–225.</mixed-citation><mixed-citation xml:lang="en">Mikkilineni L., Whitaker-Menezes D., Domingo-Vidal M., Sprandio J. Hodgkin lymphoma: A complex metabolic ecosystem with glycolytic reprogramming of the tumor microenvironment. Semin Oncol. 2017;44:218–225.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Pecina P., Nůsková H., Karbanová V., Kaplanová V., Mráček T., Houštěk J. Role of the mitochondrial ATP synthase central stalk subunits γ and δ in the activity and assembly of the mammalian enzyme. Acta Bioenergetics. 2018;1859(5):374–381.</mixed-citation><mixed-citation xml:lang="en">Pecina P., Nůsková H., Karbanová V., Kaplanová V., Mráček T., Houštěk J. Role of the mitochondrial ATP synthase central stalk subunits γ and δ in the activity and assembly of the mammalian enzyme. Acta Bioenergetics. 2018;1859(5):374–381.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Pirson M. The curious case of peroxiredoxin-5: what its absence in aves can tell us and how it can be used. BMC Evolution Biology. 2018;18:18–22.</mixed-citation><mixed-citation xml:lang="en">Pirson M. The curious case of peroxiredoxin-5: what its absence in aves can tell us and how it can be used. BMC Evolution Biology. 2018;18:18–22.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Powell K.A., Davies J.R., Taylor E., Wride M.A., Votruba M. Mitochondrial localization and ocular expression of mutant Opa3 in a mouse model of 3-methylglutaconicaciduria type III. Invest Ophthalmology Vis Science. 2011;52(7):4369– 4380.</mixed-citation><mixed-citation xml:lang="en">Powell K.A., Davies J.R., Taylor E., Wride M.A., Votruba M. Mitochondrial localization and ocular expression of mutant Opa3 in a mouse model of 3-methylglutaconicaciduria type III. Invest Ophthalmology Vis Science. 2011;52(7):4369– 4380.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Prince R.C. The proton pump of cytochrome oxidase. Trends Biochemistry Science. 1988;13:159–160.</mixed-citation><mixed-citation xml:lang="en">Prince R.C. The proton pump of cytochrome oxidase. Trends Biochemistry Science. 1988;13:159–160.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Sas K., Robotka H., Toldi J., Vécsei L. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J. Neurol. Sci. 2007;15:221–239.</mixed-citation><mixed-citation xml:lang="en">Sas K., Robotka H., Toldi J., Vécsei L. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J. Neurol. Sci. 2007;15:221–239.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Serricchio M., Vissa A., Kim P.K., Yip C.M., McQuibban G.A. Cardiolipin synthesizing enzymes form a complex that interacts with cardiolipin-dependent membrane organizing proteins. Acta Molecular Cell Biology Lipids. 2018;4:447–457.</mixed-citation><mixed-citation xml:lang="en">Serricchio M., Vissa A., Kim P.K., Yip C.M., McQuibban G.A. Cardiolipin synthesizing enzymes form a complex that interacts with cardiolipin-dependent membrane organizing proteins. Acta Molecular Cell Biology Lipids. 2018;4:447–457.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Shiba S., Ikeda K., Horie-Inoue K., Nakayama A., Tanaka T., Inoue S. Defi ciency of COX7RP, a mitochondrial supercomplex assembly promoting factor, lowers blood glucose level in mice. Sci. Rep. 2017;7:7606–7610.</mixed-citation><mixed-citation xml:lang="en">Shiba S., Ikeda K., Horie-Inoue K., Nakayama A., Tanaka T., Inoue S. Defi ciency of COX7RP, a mitochondrial supercomplex assembly promoting factor, lowers blood glucose level in mice. Sci. Rep. 2017;7:7606–7610.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Silva S., Ghiarone T., Schreiber K., Grant D., White T., Frisard M., et al. Angiotensin II suppresses autophagy and disrupts the ultrastructural morphology and function of mitochondria in mouse skeletal muscle. J. Appl Physiol. 2019;12:34–42.</mixed-citation><mixed-citation xml:lang="en">Silva S., Ghiarone T., Schreiber K., Grant D., White T., Frisard M., et al. Angiotensin II suppresses autophagy and disrupts the ultrastructural morphology and function of mitochondria in mouse skeletal muscle. J. Appl Physiol. 2019;12:34–42.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Slater Е.С. The Q Cycle, an ubiquitous mechanism of electron transfer. Trends Biochemistry Science. 1983;8:239–242.</mixed-citation><mixed-citation xml:lang="en">Slater Е.С. The Q Cycle, an ubiquitous mechanism of electron transfer. Trends Biochemistry Science. 1983;8:239–242.</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Srere P.A. The structure of the mitochondrial inner membrane-matrix compartment. Trends Biochemistry Science. 1982;7:375–378.</mixed-citation><mixed-citation xml:lang="en">Srere P.A. The structure of the mitochondrial inner membrane-matrix compartment. Trends Biochemistry Science. 1982;7:375–378.</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Teixeira F.K., Sanchez C.G., Hurd T.R., Seifert J.R., Czech B., Preall J.B., et al. ATP synthase promotes germ cell differentiation independent of oxidative phosphorylation. Natural Cell Biology. 2015;17(5):689–696.</mixed-citation><mixed-citation xml:lang="en">Teixeira F.K., Sanchez C.G., Hurd T.R., Seifert J.R., Czech B., Preall J.B., et al. ATP synthase promotes germ cell differentiation independent of oxidative phosphorylation. Natural Cell Biology. 2015;17(5):689–696.</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Thorwald M. Angiotensin receptor blockade improves cardiac mitochondrial activity in response to an acute glucose load in obese insulin resistant rats. Redox Biol. 2018;14:371–378.</mixed-citation><mixed-citation xml:lang="en">Thorwald M. Angiotensin receptor blockade improves cardiac mitochondrial activity in response to an acute glucose load in obese insulin resistant rats. Redox Biol. 2018;14:371–378.</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">van Eden W., Jansen M., Ludwig I., Leufkens P. Heat Shock Proteins Can Be Surrogate Autoantigens for Induction of Antigen Specifi c Therapeutic Tolerance in Rheumatoid Arthritis. Front Immunol. 2019;10:279–284.</mixed-citation><mixed-citation xml:lang="en">van Eden W., Jansen M., Ludwig I., Leufkens P. Heat Shock Proteins Can Be Surrogate Autoantigens for Induction of Antigen Specifi c Therapeutic Tolerance in Rheumatoid Arthritis. Front Immunol. 2019;10:279–284.</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Veis D.J., Sorenson C.M., Shutter J.R., Korsmeyer S.J. Bcl-2-defi cient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell. 1993;75:229–240.</mixed-citation><mixed-citation xml:lang="en">Veis D.J., Sorenson C.M., Shutter J.R., Korsmeyer S.J. Bcl-2-defi cient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell. 1993;75:229–240.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Wallace L., Cherian A., Adamson P. Comparison of Pre- and Post-translational Expressions of COXIV-1 and MT-ATPase 6 Genes in Colorectal Adenoma-Carcinoma Tissues. J. Carcinog Mutagen. 2018;9:319–324.</mixed-citation><mixed-citation xml:lang="en">Wallace L., Cherian A., Adamson P. Comparison of Pre- and Post-translational Expressions of COXIV-1 and MT-ATPase 6 Genes in Colorectal Adenoma-Carcinoma Tissues. J. Carcinog Mutagen. 2018;9:319–324.</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Zawislak A. Neuron-derived transthyretin modulates astrocytic glycolysis in hormone-independent manner. Oncotarget. 2017;8:106–118.</mixed-citation><mixed-citation xml:lang="en">Zawislak A. Neuron-derived transthyretin modulates astrocytic glycolysis in hormone-independent manner. Oncotarget. 2017;8:106–118.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang K., Wang G., Zhang X. COX7AR is a Stressinducible Mitochondrial COX Subunit that Promotes Breast Cancer Malignancy. Sci. Rep. 2016;6:31–36.</mixed-citation><mixed-citation xml:lang="en">Zhang K., Wang G., Zhang X. COX7AR is a Stressinducible Mitochondrial COX Subunit that Promotes Breast Cancer Malignancy. Sci. Rep. 2016;6:31–36.</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang X., Zhao X., Li Y., Zhou Y., Zhang Z. Long noncoding RNA SOX21-AS1 promotes cervical cancer progression by competitively sponging miR-7/ VDAC1. J. Cell Physiol. 2019;25:56–67.</mixed-citation><mixed-citation xml:lang="en">Zhang X., Zhao X., Li Y., Zhou Y., Zhang Z. Long noncoding RNA SOX21-AS1 promotes cervical cancer progression by competitively sponging miR-7/ VDAC1. J. Cell Physiol. 2019;25:56–67.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
