{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T11:48:18Z","timestamp":1773661698108,"version":"3.50.1"},"reference-count":30,"publisher":"Pleiades Publishing Ltd","issue":"8","license":[{"start":{"date-parts":[[2019,8,1]],"date-time":"2019-08-01T00:00:00Z","timestamp":1564617600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2019,8,1]],"date-time":"2019-08-01T00:00:00Z","timestamp":1564617600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biochemistry Moscow"],"published-print":{"date-parts":[[2019,8]]},"DOI":"10.1134\/s000629791908008x","type":"journal-article","created":{"date-parts":[[2019,8,15]],"date-time":"2019-08-15T02:08:39Z","timestamp":1565834919000},"page":"923-930","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Comparison of the Size and Properties of the Cytochrome c\/Cardiolipin Nanospheres in a Sediment and Non-polar Medium"],"prefix":"10.1134","volume":"84","author":[{"given":"G. K.","family":"Vladimirov","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"V. E.","family":"Remenshchikov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A. M.","family":"Nesterova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"V. V.","family":"Volkov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu. A.","family":"Vladimirov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"137","published-online":{"date-parts":[[2019,8,15]]},"reference":[{"key":"808_CR1","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1111\/j.1365-2184.2012.00845.x","volume":"45","author":"L Ouyang","year":"2012","unstructured":"Ouyang, L., Shi, Z., Zhao, S., Wang, F. T., Zhou, T. T., Liu, B., and Bao, J. K. (2012) Programmed cell death pathways in cancer: a review of apoptosis, autophagy and programmed necrosis, Cell Prolif., 45, 487\u2013498, doi: https:\/\/doi.org\/10.1111\/j.1365-2184.2012.00845.x.","journal-title":"Cell Prolif."},{"key":"808_CR2","doi-asserted-by":"publisher","first-page":"1650","DOI":"10.2174\/1871520618666180105161136","volume":"18","author":"M Saleem","year":"2018","unstructured":"Saleem, M., Asif, J., Asif, M., and Saleem, U. (2018) Amygdalin, from apricot kernels, induces apoptosis and causes cell cycle arrest in cancer cells: an updated review, Anticancer Agents Med. Chem., 18, 1650\u20131655, doi: https:\/\/doi.org\/10.2174\/1871520618666180105161136.","journal-title":"Anticancer Agents Med. Chem."},{"key":"808_CR3","doi-asserted-by":"publisher","first-page":"1963","DOI":"10.1016\/j.freeradbiomed.2004.08.016","volume":"37","author":"V E Kagan","year":"2004","unstructured":"Kagan, V. E., Borisenko, G. G., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Potapovich, A. I., Kini, V., Amoscato, A. A., and Fujii, Y. (2004) Oxidative lipidomics of apoptosis: redox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine, Free Radic. Biol. Med., 37, 1963\u20131985, doi: https:\/\/doi.org\/10.1016\/j.freeradbiomed.2004.08.016.","journal-title":"Free Radic. Biol. Med."},{"key":"808_CR4","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1038\/nchembio727","volume":"1","author":"V E Kagan","year":"2005","unstructured":"Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., and Kini, V. (2005) Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors, Nature Chem. Biol., 1, 223\u2013232, doi: https:\/\/doi.org\/10.1038\/nchembio727.i.","journal-title":"Nature Chem. Biol."},{"key":"808_CR5","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1002\/mnfr.200700402","volume":"53","author":"V E Kagan","year":"2009","unstructured":"Kagan, V. E., Bayir, A., Bayir, H., Stoyanovsky, D., Borisenko, G. G., Tyurina, Y. Y., Wipf, P., Atkinson, J., Greenberger, J. S., Chapkin, R. S., and Belikova, N. A. (2009) Mitochondria-targeted disruptors and inhibitors of cytochrome c\/cardiolipin peroxidase complexes: a new strategy in anti-apoptotic drug discovery, Mol. Nutr. Food Res., 53, 104\u2013114, doi: https:\/\/doi.org\/10.1002\/mnfr.200700402.","journal-title":"Mol. Nutr. Food Res."},{"key":"808_CR6","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1016\/0005-2736(77)90290-5","volume":"468","author":"L R Brown","year":"1977","unstructured":"Brown, L. R., and Wuthrich, K. (1977) NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin-phosphatidylcholine vesicles, Biochim. Biophys. Acta, 468, 389\u2013410, doi: https:\/\/doi.org\/10.1016\/0005-2736(77)90290-5.","journal-title":"Biochim. Biophys. Acta"},{"key":"808_CR7","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1007\/s00775-010-0636-z","volume":"15","author":"F Sinibaldi","year":"2010","unstructured":"Sinibaldi, F., Howes, B. D., Piro, M. C., Polticelli, F., Bombelli, C., Ferri, T., Coletta, M., Smulevich, G., and Santucci, R. (2010) Extended cardiolipin anchorage to cytochrome c: a model for protein-mitochondrial membrane binding, J. Biol. Inorg. Chem., 15, 689\u2013700, doi: https:\/\/doi.org\/10.1007\/s00775-010-0636-z.","journal-title":"J. Biol. Inorg. Chem."},{"key":"808_CR8","doi-asserted-by":"publisher","first-page":"1873","DOI":"10.1016\/j.bpj.2015.09.016","volume":"109","author":"A Mandal","year":"2015","unstructured":"Mandal, A., Hoop, C. L., DeLucia, M., Kodali, R., Kagan, V. E., Ahn, J., and van der Wel, P. C. (2015) Structural changes and proapoptotic peroxidase activity of cardiolipin-bound mitochondrial cytochrome c, Biophys. J., 109, 1873\u20131884, doi: https:\/\/doi.org\/10.1016\/j.bpj.2015.09.016.","journal-title":"Structural changes and proapoptotic peroxidase activity of cardiolipin-bound mitochondrial cytochrome c"},{"key":"808_CR9","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1073\/pnas.1112312108","volume":"109","author":"J Hanske","year":"2012","unstructured":"Hanske, J., Toffey, J. R., Morenz, A. M., Bonilla, A. J., Schiavoni, K. H., and Pletneva, E. V. (2012) Conformational properties of cardiolipin-bound cytochrome c, Proc. Natl. Acad. Sci. USA, 109, 125\u2013130, doi: https:\/\/doi.org\/10.1073\/pnas.1112312108.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"808_CR10","doi-asserted-by":"publisher","first-page":"1439","DOI":"10.1016\/j.freeradbiomed.2009.03.004","volume":"46","author":"V E Kagan","year":"2009","unstructured":"Kagan, V. E., Bayir, H. A., Belikova, N. A., Kapralov, O., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Stoyanovsky, D. A., Wipf, P., Kochanek, P. M., Greenberger, J. S., Pitt, B., Shvedova, A. A., and Borisenko, G. (2009) Cytochrome c\/cardiolipin relations in mitochondria: a kiss of death, Free Rad. Biol. Med., 46, 1439\u20131453, doi: https:\/\/doi.org\/10.1016\/j.freeradbiomed.2009.03.004.","journal-title":"Free Rad. Biol. Med."},{"key":"808_CR11","doi-asserted-by":"publisher","first-page":"1086","DOI":"10.1134\/S0006297913100027","volume":"78","author":"Y A Vladimirov","year":"2013","unstructured":"Vladimirov, Y. A., Proskurnina, E. V., and Alekseev, A. V. (2013) Molecular mechanisms of apoptosis. Structure of cytochrome c-cardiolipin complex, Biochemistry (Moscow), 78, 1086\u20131097, doi: https:\/\/doi.org\/10.1134\/S0006297913100027.","journal-title":"Biochemistry (Moscow)"},{"key":"808_CR12","doi-asserted-by":"publisher","first-page":"3599","DOI":"10.1021\/bi9809268","volume":"38","author":"R Jemmerson","year":"1999","unstructured":"Jemmerson, R., Liu, J., Hausauer, D., Lam, K. P., Mondino, A., and Nelson, R. D. (1999) A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles, Biochemistry, 38, 3599\u20133609, doi: https:\/\/doi.org\/10.1021\/bi9809268.","journal-title":"Biochemistry"},{"key":"808_CR13","doi-asserted-by":"publisher","first-page":"19356","DOI":"10.1074\/jbc.M100853200","volume":"276","author":"E K Tuominen","year":"2001","unstructured":"Tuominen, E. K., Zhu, K., Wallace, C. J., Clark-Lewis, I., Craig, D. B., Rytomaa, M., and Kinnunen, P. K. (2001) ATP induces a conformational change in lipid-bound cytochrome c, J. Biol. Chem., 276, 19356\u201319362, doi: https:\/\/doi.org\/10.1074\/jbc.M100853200.","journal-title":"J. Biol. Chem."},{"key":"808_CR14","doi-asserted-by":"publisher","first-page":"504","DOI":"10.1021\/ja0678727","volume":"129","author":"G Balakrishnan","year":"2007","unstructured":"Balakrishnan, G., Hu, Y., Oyerinde, O. F., Su, J., Groves, J. T., and Spiro, T. G. (2007) A conformational switch to beta-sheet structure in cytochrome c leads to heme exposure. Implications for cardiolipin peroxidation and apoptosis, J. Amer. Chem. Soc., 129, 504\u2013505, doi: https:\/\/doi.org\/10.1021\/ja0678727.","journal-title":"J. Amer. Chem. Soc."},{"key":"808_CR15","doi-asserted-by":"publisher","first-page":"18713","DOI":"10.1021\/ja307426k","volume":"134","author":"Y Hong","year":"2012","unstructured":"Hong, Y., Muenzner, J., Grimm, S. K., and Pletneva, E. V. (2012) Origin of the conformational heterogeneity of cardiolipin-bound cytochrome c, J. Amer. Chem. Soc., 134, 18713\u201318723, doi: https:\/\/doi.org\/10.1021\/ja307426k.","journal-title":"J. Amer. Chem. Soc."},{"key":"808_CR16","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1134\/S1063774511040250","volume":"56","author":"Y A Vladimirov","year":"2011","unstructured":"Vladimirov, Y. A., Nol\u2019, Y. T., and Volkov, V. V. (2011) Protein-lipid nanoparticles that determine whether cells will live or die, Crystallogr. Rep., 56, 553\u2013559, doi: https:\/\/doi.org\/10.1134\/S1063774511040250.","journal-title":"Crystallogr. Rep."},{"key":"808_CR17","doi-asserted-by":"publisher","first-page":"2147","DOI":"10.1016\/j.bbamem.2011.04.009","volume":"1808","author":"A A Kapralov","year":"2011","unstructured":"Kapralov, A. A., Yanamala, N., Tyurina, Y. Y., Castro, L., Samhan-Arias, A., Vladimirov, Y. A., Maeda, A., Weitz, A.A., Peterson, J., Mylnikov, D., Demicheli, V., Tortora, V., Klein-Seetharaman, J., Radi, R., and Kagan, V. E. (2011) Topography of tyrosine residues and their involvement in peroxidation of polyunsaturated cardiolipin in cytochrome c\/cardiolipin peroxidase complexes, Biochim. Biophys. Acta, 1808, 2147\u20132155, doi: https:\/\/doi.org\/10.1016\/j.bbamem.2011.04.009.","journal-title":"Biochim. Biophys. Acta"},{"key":"808_CR18","doi-asserted-by":"publisher","first-page":"4998","DOI":"10.1021\/bi0525573","volume":"45","author":"N A Belikova","year":"2006","unstructured":"Belikova, N. A., Vladimirov, Y. A., Osipov, A. N., Kapralov, A. A., Tyurin, V. A., Potapovich, M. V., Basova, L. V., Peterson, J., Kurnikov, I. V., and Kagan, V. E. (2006) Peroxidase activity and structural transitions of cytochrome c bound to cardiolipin-containing membranes, Biochemistry, 45, 4998\u20135009, doi: https:\/\/doi.org\/10.1021\/bi0525573.","journal-title":"Biochemistry"},{"key":"808_CR19","doi-asserted-by":"publisher","first-page":"14232","DOI":"10.1021\/bi701237b","volume":"46","author":"A A Kapralov","year":"2007","unstructured":"Kapralov, A. A., Kurnikov, I. V., Vlasova, I. I., Belikova, N. A., Tyurin, V. A., Basova, L. V., Zhao, Q., Tyurina, Y. Y., Jiang, J., Bayir, H., Vladimirov, Y. A., and Kagan, V. E. (2007) The hierarchy of structural transitions induced in cytochrome c by anionic phospholipids determines its peroxidase activation and selective peroxidation during apoptosis in cells, Biochemistry, 46, 14232\u201314244, doi: https:\/\/doi.org\/10.1021\/bi701237b.","journal-title":"Biochemistry"},{"key":"808_CR20","first-page":"264","volume":"280","author":"E V Proskurnina","year":"2013","unstructured":"Proskurnina, E. V., Alekseev, A. V., Demin, E. M., Izmailov, D. Y., and Vladimirov, Y. A. (2013) Cyt-CL complex: peroxidase activity and role in lipid peroxidation, FEBS J., 280, 264\u2013264.","journal-title":"FEBS J."},{"key":"808_CR21","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.chemphyslip.2018.05.007","volume":"214","author":"G K Vladimirov","year":"2018","unstructured":"Vladimirov, G. K., Vikulina, A. S., Volodkin, D., and Vladimirov, Y. A. (2018) Structure of the complex of cytochrome c with cardiolipin in non-polar environment, Chem. Phys. Lipids, 214, 35\u201345, doi: https:\/\/doi.org\/10.1016\/j.chemphyslip.2018.05.007.","journal-title":"Chem. Phys. Lipids"},{"key":"808_CR22","doi-asserted-by":"publisher","first-page":"1277","DOI":"10.1107\/S0021889803012779","volume":"36","author":"P V Konarev","year":"2003","unstructured":"Konarev, P. V., Volkov, V. V., Sokolova, A. V., Koch, M. H. J., and Svergun, D. I. (2003) PRIMUS: a Windows PC-based system for small-angle scattering data analysis, J. Appl. Crystallogr., 36, 1277\u20131282, doi: https:\/\/doi.org\/10.1107\/S002188980301277923.","journal-title":"J. Appl. Crystallogr."},{"key":"808_CR23","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/S0021-9258(18)64849-5","volume":"226","author":"J Folch","year":"1957","unstructured":"Folch, J., Lees, M., and Sloane Stanley, G. H. (1957) A simple method for the isolation and purification of total lipids from animal tissues, J. Biol. Chem., 226, 497\u2013509","journal-title":"J. Biol. Chem."},{"key":"808_CR24","doi-asserted-by":"publisher","first-page":"1298","DOI":"10.1134\/S0006297915100107","volume":"80","author":"A S Vikulina","year":"2015","unstructured":"Vikulina, A. S., Alekseev, A. V., Proskurnina, E. V., and Vladimirov, Y. A. (2015) The complex of cytochrome c with cardiolipin in non-polar environment, Biochemistry (Moscow), 80, 1298\u20131302, doi: https:\/\/doi.org\/10.1134\/S0006297915100107.","journal-title":"Biochemistry (Moscow)"},{"key":"808_CR25","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1016\/j.ijbiomac.2010.05.013","volume":"47","author":"S Ali","year":"2010","unstructured":"Ali, S., Farooqi, H., Prasad, R., Naime, M., Routray, I., Yadav, S., and Ahmad, F. (2010) Boron stabilizes peroxide mediated changes in the structure of heme proteins, Int. J. Biol. Macromol., 47, 109\u2013115, doi: https:\/\/doi.org\/10.1016\/j.ijbiomac.2010.05.013.","journal-title":"Int. J. Biol. Macromol."},{"key":"808_CR26","doi-asserted-by":"publisher","first-page":"14019","DOI":"10.1002\/anie.201607419","volume":"55","author":"H Kobayashi","year":"2016","unstructured":"Kobayashi, H., Nagao, S., and Hirota, S. (2016) Characterization of the cytochrome c membrane-binding site using cardiolipin-containing bicelles with NMR, Angewandte Chem. Int. Ed., 55, 14019\u201314022, doi: https:\/\/doi.org\/10.1002\/anie.201607419.","journal-title":"Angewandte Chem. Int. Ed."},{"key":"808_CR27","first-page":"27","volume":"15","author":"E V Proskurnina","year":"2018","unstructured":"Proskurnina, E. V., Proskurnin, M. A., Alekseev, A. V., Galimova, V. R., and Vladimirov, Yu. A. (2018) Determination of a composition of cytochrome c\/cardiolipin complex by spectrophotometry and thermal-lens spectrometry, Tekhnol. Zhivykh Sistem, 15, 27\u201333.","journal-title":"Tekhnol. Zhivykh Sistem"},{"key":"808_CR28","doi-asserted-by":"publisher","first-page":"4578","DOI":"10.1021\/bi400324c","volume":"52","author":"F Sinibaldi","year":"2013","unstructured":"Sinibaldi, F., Howes, B. D., Droghetti, E., Polticelli, F., Piro, M. C., Di Pierro, D., Fiorucci, L., Coletta, M., Smulevich, G., and Santucci, R. (2013) Role of lysins in cytochrome c-cardiolipin interaction, Biochemistry, 52, 4578\u20134588, doi: https:\/\/doi.org\/10.1021\/bi400324c.","journal-title":"Biochemistry"},{"key":"808_CR29","doi-asserted-by":"publisher","first-page":"3851","DOI":"10.1021\/jacs.7b00238","volume":"139","author":"J P Kitt","year":"2017","unstructured":"Kitt, J. P., Bryce, D. A., Minteer, S. D., and Harris, J. M. (2017) Raman spectroscopy reveals selective interactions of cytochrome c with cardiolipin that correlate with membrane permeability, J. Am. Chem. Soc., 139, 3851\u20133860, doi: https:\/\/doi.org\/10.1021\/jacs.7b00238.","journal-title":"J. Am. Chem. Soc."},{"key":"808_CR30","doi-asserted-by":"publisher","first-page":"1536","DOI":"10.1039\/c2pp25119a","volume":"11","author":"S Miyamoto","year":"2012","unstructured":"Miyamoto, S., Nantes, I. L., Faria, P. A., Cunha, D., Ronsein, G. E., Medeiros, M. H., and Di Mascio, P. (2012) Cytochrome c-promoted cardiolipin oxidation generates singlet molecular oxygen, Photochem. Photobiol. Sci., 11, 1536\u20131546, doi: https:\/\/doi.org\/10.1039\/c2pp25119a.","journal-title":"Photochem. Photobiol. Sci."}],"container-title":["Biochemistry (Moscow)"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S000629791908008X.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1134\/S000629791908008X","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S000629791908008X.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T00:16:41Z","timestamp":1773620201000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1134\/S000629791908008X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,8]]},"references-count":30,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2019,8]]}},"alternative-id":["808"],"URL":"https:\/\/doi.org\/10.1134\/s000629791908008x","relation":{},"ISSN":["0006-2979","1608-3040"],"issn-type":[{"value":"0006-2979","type":"print"},{"value":"1608-3040","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,8]]},"assertion":[{"value":"20 February 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"28 March 2019","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 April 2019","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 August 2019","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Conflict of interest.\n                      The authors declare no conflict of interest in financial or any other sphere.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics"}},{"value":"Ethical approval.\n                      This article contains no studies with human participants or animals performed by any of the authors.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics"}}]}}