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195 results on '"Severin, Fedor F."'

12. Six Functions of Respiration: Isn't It Time to Take Control over ROS Production in Mitochondria, and Aging Along with It?

Author

Skulachev, Vladimir P., Vyssokikh, Mikhail Yu., Chernyak, Boris V., Mulkidjanian, Armen Y., Skulachev, Maxim V., Shilovsky, Gregory A., Lyamzaev, Konstantin G., Borisov, Vitaliy B., Severin, Fedor F., and Sadovnichii, Victor A.

Subjects
RESPIRATION, CELL respiration, MITOCHONDRIA, BIOLOGICAL transport, REACTIVE oxygen species, MITOCHONDRIAL membranes
Abstract

Cellular respiration is associated with at least six distinct but intertwined biological functions. (1) biosynthesis of ATP from ADP and inorganic phosphate, (2) consumption of respiratory substrates, (3) support of membrane transport, (4) conversion of respiratory energy to heat, (5) removal of oxygen to prevent oxidative damage, and (6) generation of reactive oxygen species (ROS) as signaling molecules. Here we focus on function #6, which helps the organism control its mitochondria. The ROS bursts typically occur when the mitochondrial membrane potential (MMP) becomes too high, e.g., due to mitochondrial malfunction, leading to cardiolipin (CL) oxidation. Depending on the intensity of CL damage, specific programs for the elimination of damaged mitochondria (mitophagy), whole cells (apoptosis), or organisms (phenoptosis) can be activated. In particular, we consider those mechanisms that suppress ROS generation by enabling ATP synthesis at low MMP levels. We discuss evidence that the mild depolarization mechanism of direct ATP/ADP exchange across mammalian inner and outer mitochondrial membranes weakens with age. We review recent data showing that by protecting CL from oxidation, mitochondria-targeted antioxidants decrease lethality in response to many potentially deadly shock insults. Thus, targeting ROS- and CL-dependent pathways may prevent acute mortality and, hopefully, slow aging. [ABSTRACT FROM AUTHOR]

Published
2023
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14. In search of novel highly active mitochondria-targeted antioxidants: Thymoquinone and its cationic derivatives

Author

Severina, Inna I., Severin, Fedor F., Korshunova, Galina A., Sumbatyan, Natalya V., Ilyasova, Tatyana M., Simonyan, Ruben A., Rogov, Anton G., Trendeleva, Tatyana A., Zvyagilskaya, Renata A., Dugina, Vera B., Domnina, Lidia V., Fetisova, Elena K., Lyamzaev, Konstantin G., Vyssokikh, Mikhail Yu, Chernyak, Boris V., Skulachev, Maxim V., Skulachev, Vladimir P., and Sadovnichii, Viktor A.

Published
2013
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18. Derivatives of Rhodamine 19 as Mild Mitochondria-targeted Cationic Uncouplers

Author

Antonenko, Yuri N., Avetisyan, Armine V., Cherepanov, Dmitry A., Knorre, Dmitry A., Korshunova, Galina A., Markova, Olga V., Ojovan, Silvia M., Perevoshchikova, Irina V., Pustovidko, Antonina V., Rokitskaya, Tatyana I., Severina, Inna I., Simonyan, Ruben A., Smirnova, Ekaterina A., Sobko, Alexander A., Sumbatyan, Natalia V., Severin, Fedor F., and Skulachev, Vladimir P.

Published
2011
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19. Prevention of cardiolipin oxidation and fatty acid cycling as two antioxidant mechanisms of cationic derivatives of plastoquinone (SkQs)

Author

Skulachev, Vladimir P., Antonenko, Yury N., Cherepanov, Dmitry A., Chernyak, Boris V., Izyumov, Denis S., Khailova, Ludmila S., Klishin, Sergey S., Korshunova, Galina A., Lyamzaev, Konstantin G., Pletjushkina, Olga Yu., Roginsky, Vitaly A., Rokitskaya, Tatiana I., Severin, Fedor F., Severina, Inna I., Simonyan, Ruben A., Skulachev, Maxim V., Sumbatyan, Natalia V., Sukhanova, Evgeniya I., Tashlitsky, Vadim N., Trendeleva, Tatyana A., Vyssokikh, Mikhail Yu., and Zvyagilskaya, Renata A.

Published
2010
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27. Regulation of Saccharomyces cerevisiae kinetochores by the type 1 phosphatase Glc7p

Author

Sassoon, Ingrid, Severin, Fedor F., Andrews, Paul D., Taba, Maria-Rita, Kaplan, Ken B., Ashford, Anthony, Stark, Michael J.R., Sorger, Peter K., and Hyman, Anthony A.

Subjects
Cellular signal transduction -- Genetic aspects, Saccharomyces -- Genetic aspects, Mitosis -- Observations, Phosphatases -- Research, Biological sciences
Abstract

Saccharomyces cerevisiae kinetochores are regulated by a type 1 phosphatase, Glc7p. The microtubule-binding activity of the kinetochore complex is controlled by a balance between a protein kinase and the type 1 protein phosphatase (PP1) coded for in the GLC7 gene. The centromeric DNA-binding activity is not so regulated.

Published
1999

28. The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast

Author

Biggins, Sue, Severin, Fedor F., Bhalla, Needhi, Sassoon, Ingrid, Hyman, Anthony A., and Murray, Andrew W.

Subjects
Cellular signal transduction -- Genetic aspects, Chromosomes -- Observations, Protein kinases -- Observations, Microtubules -- Genetic aspects, Yeast -- Genetic aspects, Mitosis -- Observations, Biological sciences
Abstract

In budding yeast the conserved protein kinase Ipl1 regulates microtubule binding to kinetochores. Chromosome segregation is based on kinetochores, structures that mediate chromosome attachment to the mitotic spindle. Mutants in IPL1, which encodes a protein kinase, have been isolated in a screen for budding yeast mutants with defects in sister chromatid segregation and separation.

Published
1999

31. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andres, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Corte-Real, Manuela, Costa, Vitor, Cullin, Christophe, Dawes, Ian, Dengjel, Jorn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Frohlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jimenez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stephen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystrom, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polcic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria Joao, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andres, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Büttner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Corte-Real, Manuela, Costa, Vitor, Cullin, Christophe, Dawes, Ian, Dengjel, Jorn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Frohlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jimenez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stephen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystrom, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polcic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria Joao, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, and Madeo, Frank

Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cellular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the definition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death routines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the authors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the progress of this vibrant field of research.

Published
2018
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32. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, Madeo, F, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Buettner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Froehlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystroem, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, Madeo, Frank, Carmona-Gutierrez, D, Bauer, M, Zimmermann, A, Aguilera, A, Austriaco, N, Ayscough, K, Balzan, R, Bar-Nun, S, Barrientos, A, Belenky, P, Blondel, M, Braun, R, Breitenbach, M, Burhans, W, Buettner, S, Cavalieri, D, Chang, M, Cooper, K, Côrte-Real, M, Costa, V, Cullin, C, Dawes, I, Dengjel, J, Dickman, M, Eisenberg, T, Fahrenkrog, B, Fasel, N, Froehlich, K, Gargouri, A, Giannattasio, S, Goffrini, P, Gourlay, C, Grant, C, Greenwood, M, Guaragnella, N, Heger, T, Heinisch, J, Herker, E, Herrmann, J, Hofer, S, Jiménez-Ruiz, A, Jungwirth, H, Kainz, K, Kontoyiannis, D, Ludovico, P, Manon, S, Martegani, E, Mazzoni, C, Megeney, L, Meisinger, C, Nielsen, J, Nystroem, T, Osiewacz, H, Outeiro, T, Park, H, Pendl, T, Petranovic, D, Picot, S, Polčic, P, Powers, T, Ramsdale, M, Rinnerthaler, M, Rockenfeller, P, Ruckenstuhl, C, Schaffrath, R, Segovia, M, Severin, F, Sharon, A, Sigrist, S, Sommer-Ruck, C, Sousa, M, Thevelein, J, Thevissen, K, Titorenko, V, Toledano, M, Tuite, M, Voegtle, F, Westermann, B, Winderickx, J, Wissing, S, Woelfl, S, Zhang, Z, Zhao, R, Zhou, B, Galluzzi, L, Kroemer, G, Madeo, F, Carmona-Gutierrez, Didac, Bauer, Maria Anna, Zimmermann, Andreas, Aguilera, Andrés, Austriaco, Nicanor, Ayscough, Kathryn, Balzan, Rena, Bar-Nun, Shoshana, Barrientos, Antonio, Belenky, Peter, Blondel, Marc, Braun, Ralf J., Breitenbach, Michael, Burhans, William C., Buettner, Sabrina, Cavalieri, Duccio, Chang, Michael, Cooper, Katrina F., Côrte-Real, Manuela, Costa, Vítor, Cullin, Christophe, Dawes, Ian, Dengjel, Jörn, Dickman, Martin B., Eisenberg, Tobias, Fahrenkrog, Birthe, Fasel, Nicolas, Froehlich, Kai-Uwe, Gargouri, Ali, Giannattasio, Sergio, Goffrini, Paola, Gourlay, Campbell W., Grant, Chris M., Greenwood, Michael T., Guaragnella, Nicoletta, Heger, Thomas, Heinisch, Juergen, Herker, Eva, Herrmann, Johannes M., Hofer, Sebastian, Jiménez-Ruiz, Antonio, Jungwirth, Helmut, Kainz, Katharina, Kontoyiannis, Dimitrios P., Ludovico, Paula, Manon, Stéphen, Martegani, Enzo, Mazzoni, Cristina, Megeney, Lynn A., Meisinger, Chris, Nielsen, Jens, Nystroem, Thomas, Osiewacz, Heinz D., Outeiro, Tiago F., Park, Hay-Oak, Pendl, Tobias, Petranovic, Dina, Picot, Stephane, Polčic, Peter, Powers, Ted, Ramsdale, Mark, Rinnerthaler, Mark, Rockenfeller, Patrick, Ruckenstuhl, Christoph, Schaffrath, Raffael, Segovia, Maria, Severin, Fedor F., Sharon, Amir, Sigrist, Stephan J., Sommer-Ruck, Cornelia, Sousa, Maria João, Thevelein, Johan M., Thevissen, Karin, Titorenko, Vladimir, Toledano, Michel B., Tuite, Mick, Voegtle, F. -Nora, Westermann, Benedikt, Winderickx, Joris, Wissing, Silke, Woelfl, Stefan, Zhang, Zhaojie J., Zhao, Richard Y., Zhou, Bing, Galluzzi, Lorenzo, Kroemer, Guido, and Madeo, Frank

Abstract

Elucidating the biology of yeast in its full complexity has major implications for science, medicine and industry. One of the most critical processes determining yeast life and physiology is cellular demise. However, the investigation of yeast cell death is a relatively young field, and a widely accepted set of concepts and terms is still missing. Here, we propose unified criteria for the definition of accidental, regulated, and programmed forms of cell death in yeast based on a series of morphological and biochemical criteria. Specifically, we provide consensus guidelines on the differential definition of terms including apoptosis, regulated necrosis, and autophagic cell death, as we refer to additional cell death routines that are relevant for the biology of (at least some species of) yeast. As this area of investigation advances rapidly, changes and extensions to this set of recommendations will be implemented in the years to come. Nonetheless, we strongly encourage the authors, reviewers and editors of scientific articles to adopt these collective standards in order to establish an accurate framework for yeast cell death research and, ultimately, to accelerate the progress of this vibrant field of research.

Published
2018

34. Guidelines and recommendations on yeast cell death nomenclature

Author

Carmona-Gutierrez, Didac, primary, Bauer, Maria Anna, additional, Zimmermann, Andreas, additional, Aguilera, Andrés, additional, Austriaco, Nicanor, additional, Ayscough, Kathryn, additional, Balzan, Rena, additional, Bar-Nun, Shoshana, additional, Barrientos, Antonio, additional, Belenky, Peter, additional, Blondel, Marc, additional, Braun, Ralf J., additional, Breitenbach, Michael, additional, Burhans, William C., additional, Buettner, Sabrina, additional, Cavalieri, Duccio, additional, Chang, Michael, additional, Cooper, Katrina F., additional, Côrte-Real, Manuela, additional, Costa, Vítor, additional, Cullin, Christophe, additional, Dawes, Ian, additional, Dengjel, Jörn, additional, Dickman, Martin B., additional, Eisenberg, Tobias, additional, Fahrenkrog, Birthe, additional, Fasel, Nicolas, additional, Froehlich, Kai-Uwe, additional, Gargouri, Ali, additional, Giannattasio, Sergio, additional, Goffrini, Paola, additional, Gourlay, Campbell W., additional, Grant, Chris M., additional, Greenwood, Michael T., additional, Guaragnella, Nicoletta, additional, Heger, Thomas, additional, Heinisch, Juergen, additional, Herker, Eva, additional, Herrmann, Johannes M., additional, Hofer, Sebastian, additional, Jiménez-Ruiz, Antonio, additional, Jungwirth, Helmut, additional, Kainz, Katharina, additional, Kontoyiannis, Dimitrios P., additional, Ludovico, Paula, additional, Manon, Stéphen, additional, Martegani, Enzo, additional, Mazzoni, Cristina, additional, Megeney, Lynn A., additional, Meisinger, Chris, additional, Nielsen, Jens, additional, Nystroem, Thomas, additional, Osiewacz, Heinz D., additional, Outeiro, Tiago F., additional, Park, Hay-Oak, additional, Pendl, Tobias, additional, Petranovic, Dina, additional, Picot, Stephane, additional, Polčic, Peter, additional, Powers, Ted, additional, Ramsdale, Mark, additional, Rinnerthaler, Mark, additional, Rockenfeller, Patrick, additional, Ruckenstuhl, Christoph, additional, Schaffrath, Raffael, additional, Segovia, Maria, additional, Severin, Fedor F., additional, Sharon, Amir, additional, Sigrist, Stephan J., additional, Sommer-Ruck, Cornelia, additional, Sousa, Maria João, additional, Thevelein, Johan M., additional, Thevissen, Karin, additional, Titorenko, Vladimir, additional, Toledano, Michel B., additional, Tuite, Mick, additional, Voegtle, F.-Nora, additional, Westermann, Benedikt, additional, Winderickx, Joris, additional, Wissing, Silke, additional, Woelfl, Stefan, additional, Zhang, Zhaojie J., additional, Zhao, Richard Y., additional, Zhou, Bing, additional, Galluzzi, Lorenzo, additional, Kroemer, Guido, additional, and Madeo, Frank, additional

Published
2018
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40. Roles of Mitochondrial Dynamics under Stressful and Normal Conditions in Yeast Cells

Author

Knorre, Dmitry A., Popadin, Konstantin Y., Sokolov, Svyatoslav S., and Severin, Fedor F.

Subjects
Article Subject
Abstract

Eukaryotic cells contain dynamic mitochondrial filaments: they fuse and divide. Here we summarize data on the protein machinery driving mitochondrial dynamics in yeast and also discuss the factors that affect the fusion-fission balance. Fission is a general stress response of cells, and in the case of yeast this response appears to be prosurvival. At the same time, even under normal conditions yeast mitochondria undergo continuous cycles of fusion and fission. This seems to be a futile cycle and also expensive from the energy point of view. Why does it exist? Benefits might be the same as in the case of sexual reproduction. Indeed, mixing and separating of mitochondrial content allows mitochondrial DNA to segregate and recombine randomly, leading to high variation in the numbers of mutations per individual mitochondrion. This opens a possibility for effective purifying selection-elimination of mitochondria highly contaminated by deleterious mutations. The beneficial action presumes a mechanism for removal of defective mitochondria. We argue that selective mitochondrial autophagy or asymmetrical distribution of mitochondria during cell division could be at the core of such mechanism.

Published
2013
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44. Penetrating Cations Enhance Uncoupling Activity of Anionic Protonophores in Mitochondria

Author

Antonenko, Yuri N., primary, Khailova, Ljudmila S., additional, Knorre, Dmitry A., additional, Markova, Olga V., additional, Rokitskaya, Tatyana I., additional, Ilyasova, Tatyana M., additional, Severina, Inna I., additional, Kotova, Elena A., additional, Karavaeva, Yulia E., additional, Prikhodko, Anastasia S., additional, Severin, Fedor F., additional, and Skulachev, Vladimir P., additional

Published
2013
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47. Penetrating cation/fatty acid anion pair as a mitochondria-targeted protonophore

Author

Severin, Fedor F., primary, Severina, Inna I., additional, Antonenko, Yury N., additional, Rokitskaya, Tatiana I., additional, Cherepanov, Dmitry A., additional, Mokhova, Elena N., additional, Vyssokikh, Mikhail Yu., additional, Pustovidko, Antonina V., additional, Markova, Olga V., additional, Yaguzhinsky, Lev S., additional, Korshunova, Galina A., additional, Sumbatyan, Nataliya V., additional, Skulachev, Maxim V., additional, and Skulachev, Vladimir P., additional

Published
2009
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