Artykuły w czasopismach na temat „Mitochondria fusion”
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Murata, Daisuke, Kenta Arai, Miho Iijima i Hiromi Sesaki. "Mitochondrial division, fusion and degradation". Journal of Biochemistry 167, nr 3 (4.12.2019): 233–41. http://dx.doi.org/10.1093/jb/mvz106.
Pełny tekst źródłaSeo, Young Ah, Veronica Lopez i Shannon L. Kelleher. "A histidine-rich motif mediates mitochondrial localization of ZnT2 to modulate mitochondrial function". American Journal of Physiology-Cell Physiology 300, nr 6 (czerwiec 2011): C1479—C1489. http://dx.doi.org/10.1152/ajpcell.00420.2010.
Pełny tekst źródłaTwig, Gilad, Xingguo Liu, Marc Liesa, Jakob D. Wikstrom, Anthony J. A. Molina, Guy Las, Gal Yaniv, György Hajnóczky i Orian S. Shirihai. "Biophysical properties of mitochondrial fusion events in pancreatic β-cells and cardiac cells unravel potential control mechanisms of its selectivity". American Journal of Physiology-Cell Physiology 299, nr 2 (sierpień 2010): C477—C487. http://dx.doi.org/10.1152/ajpcell.00427.2009.
Pełny tekst źródłaHaseeb, Abdul, Hong Chen, Yufei Huang, Ping Yang, Xuejing Sun, Adeela Iqbal, Nisar Ahmed i in. "Remodelling of mitochondria during spermiogenesis of Chinese soft-shelled turtle (Pelodiscus sinensis)". Reproduction, Fertility and Development 30, nr 11 (2018): 1514. http://dx.doi.org/10.1071/rd18010.
Pełny tekst źródłaHiguchi-Sanabria, Ryo, Joseph K. Charalel, Matheus P. Viana, Enrique J. Garcia, Cierra N. Sing, Andrea Koenigsberg, Theresa C. Swayne i in. "Mitochondrial anchorage and fusion contribute to mitochondrial inheritance and quality control in the budding yeast Saccharomyces cerevisiae". Molecular Biology of the Cell 27, nr 5 (marzec 2016): 776–87. http://dx.doi.org/10.1091/mbc.e15-07-0455.
Pełny tekst źródłaZheng, Yunsi, Anqi Luo i Xiaoquan Liu. "The Imbalance of Mitochondrial Fusion/Fission Drives High-Glucose-Induced Vascular Injury". Biomolecules 11, nr 12 (27.11.2021): 1779. http://dx.doi.org/10.3390/biom11121779.
Pełny tekst źródłaKnorre, Dmitry A., Konstantin Y. Popadin, Svyatoslav S. Sokolov i Fedor F. Severin. "Roles of Mitochondrial Dynamics under Stressful and Normal Conditions in Yeast Cells". Oxidative Medicine and Cellular Longevity 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/139491.
Pełny tekst źródłaKeng, T., E. Alani i L. Guarente. "The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix". Molecular and Cellular Biology 6, nr 2 (luty 1986): 355–64. http://dx.doi.org/10.1128/mcb.6.2.355-364.1986.
Pełny tekst źródłaKeng, T., E. Alani i L. Guarente. "The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix." Molecular and Cellular Biology 6, nr 2 (luty 1986): 355–64. http://dx.doi.org/10.1128/mcb.6.2.355.
Pełny tekst źródłaEisner, Verónica, Guy Lenaers i György Hajnóczky. "Mitochondrial fusion is frequent in skeletal muscle and supports excitation–contraction coupling". Journal of Cell Biology 205, nr 2 (21.04.2014): 179–95. http://dx.doi.org/10.1083/jcb.201312066.
Pełny tekst źródłaRose, Ray J. "Contribution of Massive Mitochondrial Fusion and Subsequent Fission in the Plant Life Cycle to the Integrity of the Mitochondrion and Its Genome". International Journal of Molecular Sciences 22, nr 11 (21.05.2021): 5429. http://dx.doi.org/10.3390/ijms22115429.
Pełny tekst źródłaGorsich, Steven W., i Janet M. Shaw. "Importance of Mitochondrial Dynamics During Meiosis and Sporulation". Molecular Biology of the Cell 15, nr 10 (październik 2004): 4369–81. http://dx.doi.org/10.1091/mbc.e03-12-0875.
Pełny tekst źródłaLogan, David C. "Mitochondrial fusion, division and positioning in plants". Biochemical Society Transactions 38, nr 3 (24.05.2010): 789–95. http://dx.doi.org/10.1042/bst0380789.
Pełny tekst źródłaScott, Iain, i Richard J. Youle. "Mitochondrial fission and fusion". Essays in Biochemistry 47 (14.06.2010): 85–98. http://dx.doi.org/10.1042/bse0470085.
Pełny tekst źródłaZerihun, Mulate, Surya Sukumaran i Nir Qvit. "The Drp1-Mediated Mitochondrial Fission Protein Interactome as an Emerging Core Player in Mitochondrial Dynamics and Cardiovascular Disease Therapy". International Journal of Molecular Sciences 24, nr 6 (17.03.2023): 5785. http://dx.doi.org/10.3390/ijms24065785.
Pełny tekst źródłaKarbowski, Mariusz, Damien Arnoult, Hsiuchen Chen, David C. Chan, Carolyn L. Smith i Richard J. Youle. "Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis". Journal of Cell Biology 164, nr 4 (9.02.2004): 493–99. http://dx.doi.org/10.1083/jcb.200309082.
Pełny tekst źródłaSesaki, Hiromi, Sheryl M. Southard, Michael P. Yaffe i Robert E. Jensen. "Mgm1p, a Dynamin-related GTPase, Is Essential for Fusion of the Mitochondrial Outer Membrane". Molecular Biology of the Cell 14, nr 6 (czerwiec 2003): 2342–56. http://dx.doi.org/10.1091/mbc.e02-12-0788.
Pełny tekst źródłaElizaveta, Bon. "Mitochondrial Movement: A Review". Clinical Research Notes 3, nr 3 (30.04.2022): 01–06. http://dx.doi.org/10.31579/2690-8816/059.
Pełny tekst źródłaChan, David C. "Mitochondrial Dynamics and Its Involvement in Disease". Annual Review of Pathology: Mechanisms of Disease 15, nr 1 (24.01.2020): 235–59. http://dx.doi.org/10.1146/annurev-pathmechdis-012419-032711.
Pełny tekst źródłaE.I,, Bon. "Mechanisms of Movement of Mitochondria in the Cell". Clinical Endocrinology and Metabolism 1, nr 1 (26.10.2022): 01–06. http://dx.doi.org/10.31579/2834-8761/005.
Pełny tekst źródłaSesaki, Hiromi, i Robert E. Jensen. "UGO1 Encodes an Outer Membrane Protein Required for Mitochondrial Fusion". Journal of Cell Biology 152, nr 6 (12.03.2001): 1123–34. http://dx.doi.org/10.1083/jcb.152.6.1123.
Pełny tekst źródłaFritz, Stefan, Nadja Weinbach i Benedikt Westermann. "Mdm30 Is an F-Box Protein Required for Maintenance of Fusion-competent Mitochondria in Yeast". Molecular Biology of the Cell 14, nr 6 (czerwiec 2003): 2303–13. http://dx.doi.org/10.1091/mbc.e02-12-0831.
Pełny tekst źródłaSesaki, Hiromi, i Robert E. Jensen. "Division versus Fusion: Dnm1p and Fzo1p Antagonistically Regulate Mitochondrial Shape". Journal of Cell Biology 147, nr 4 (15.11.1999): 699–706. http://dx.doi.org/10.1083/jcb.147.4.699.
Pełny tekst źródłaLiesa, Marc, Manuel Palacín i Antonio Zorzano. "Mitochondrial Dynamics in Mammalian Health and Disease". Physiological Reviews 89, nr 3 (lipiec 2009): 799–845. http://dx.doi.org/10.1152/physrev.00030.2008.
Pełny tekst źródłaChen, Hsiuchen, Scott A. Detmer, Andrew J. Ewald, Erik E. Griffin, Scott E. Fraser i David C. Chan. "Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development". Journal of Cell Biology 160, nr 2 (13.01.2003): 189–200. http://dx.doi.org/10.1083/jcb.200211046.
Pełny tekst źródłaGottlieb, Roberta A., Honit Piplani, Jon Sin, Savannah Sawaged, Syed M. Hamid, David J. Taylor i Juliana de Freitas Germano. "At the heart of mitochondrial quality control: many roads to the top". Cellular and Molecular Life Sciences 78, nr 8 (5.02.2021): 3791–801. http://dx.doi.org/10.1007/s00018-021-03772-3.
Pełny tekst źródłaDürr, Mark, Mafalda Escobar-Henriques, Sandra Merz, Stefan Geimer, Thomas Langer i Benedikt Westermann. "Nonredundant Roles of Mitochondria-associated F-Box Proteins Mfb1 and Mdm30 in Maintenance of Mitochondrial Morphology in Yeast". Molecular Biology of the Cell 17, nr 9 (wrzesień 2006): 3745–55. http://dx.doi.org/10.1091/mbc.e06-01-0053.
Pełny tekst źródłaTanaka, Atsushi, Megan M. Cleland, Shan Xu, Derek P. Narendra, Der-Fen Suen, Mariusz Karbowski i Richard J. Youle. "Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin". Journal of Cell Biology 191, nr 7 (20.12.2010): 1367–80. http://dx.doi.org/10.1083/jcb.201007013.
Pełny tekst źródłaDi Nottia, Michela, Daniela Verrigni, Alessandra Torraco, Teresa Rizza, Enrico Bertini i Rosalba Carrozzo. "Mitochondrial Dynamics: Molecular Mechanisms, Related Primary Mitochondrial Disorders and Therapeutic Approaches". Genes 12, nr 2 (10.02.2021): 247. http://dx.doi.org/10.3390/genes12020247.
Pełny tekst źródłaTilokani, Lisa, Shun Nagashima, Vincent Paupe i Julien Prudent. "Mitochondrial dynamics: overview of molecular mechanisms". Essays in Biochemistry 62, nr 3 (20.07.2018): 341–60. http://dx.doi.org/10.1042/ebc20170104.
Pełny tekst źródłaSita, Giulia, Patrizia Hrelia, Agnese Graziosi i Fabiana Morroni. "Back to The Fusion: Mitofusin-2 in Alzheimer’s Disease". Journal of Clinical Medicine 9, nr 1 (2.01.2020): 126. http://dx.doi.org/10.3390/jcm9010126.
Pełny tekst źródłaKowluru, Renu A., i Kumari Alka. "Mitochondrial Quality Control and Metabolic Memory Phenomenon Associated with Continued Progression of Diabetic Retinopathy". International Journal of Molecular Sciences 24, nr 9 (29.04.2023): 8076. http://dx.doi.org/10.3390/ijms24098076.
Pełny tekst źródłaPallanck, Leo J. "Culling sick mitochondria from the herd". Journal of Cell Biology 191, nr 7 (27.12.2010): 1225–27. http://dx.doi.org/10.1083/jcb.201011068.
Pełny tekst źródłaNguyen, Nicholas, Meifang Yu, Vinit Reddy, Ariana Acevedo-Diaz, Enzo Mesarick, Joseph Abi Jaoude, Min Yuan, John Asara i Cullen Taniguchi. "Comparative Untargeted Metabolomic Profiling of Induced Mitochondrial Fusion in Pancreatic Cancer". Metabolites 11, nr 9 (15.09.2021): 627. http://dx.doi.org/10.3390/metabo11090627.
Pełny tekst źródłaPalmer, Catherine S., Kirstin D. Elgass, Robert G. Parton, Laura D. Osellame, Diana Stojanovski i Michael T. Ryan. "Adaptor Proteins MiD49 and MiD51 Can Act Independently of Mff and Fis1 in Drp1 Recruitment and Are Specific for Mitochondrial Fission". Journal of Biological Chemistry 288, nr 38 (6.08.2013): 27584–93. http://dx.doi.org/10.1074/jbc.m113.479873.
Pełny tekst źródłaLee, Jeong Eon, Bong Jong Seo, Min Ji Han, Yean Ju Hong, Kwonho Hong, Hyuk Song, Jeong Woong Lee i Jeong Tae Do. "Changes in the Expression of Mitochondrial Morphology-Related Genes during the Differentiation of Murine Embryonic Stem Cells". Stem Cells International 2020 (28.01.2020): 1–12. http://dx.doi.org/10.1155/2020/9369268.
Pełny tekst źródłaAhmed, Afsar U., Peter L. Beech, Sui T. Lay, Paul R. Gilson i Paul R. Fisher. "Import-Associated Translational Inhibition: Novel In Vivo Evidence for Cotranslational Protein Import into Dictyostelium discoideum Mitochondria". Eukaryotic Cell 5, nr 8 (sierpień 2006): 1314–27. http://dx.doi.org/10.1128/ec.00386-05.
Pełny tekst źródłaWong, Edith D., Jennifer A. Wagner, Sidney V. Scott, Voytek Okreglak, Timothy J. Holewinske, Ann Cassidy-Stone i Jodi Nunnari. "The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion". Journal of Cell Biology 160, nr 3 (3.02.2003): 303–11. http://dx.doi.org/10.1083/jcb.200209015.
Pełny tekst źródłaAnand, Ruchika, Timothy Wai, Michael J. Baker, Nikolay Kladt, Astrid C. Schauss, Elena Rugarli i Thomas Langer. "The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission". Journal of Cell Biology 204, nr 6 (10.03.2014): 919–29. http://dx.doi.org/10.1083/jcb.201308006.
Pełny tekst źródłaUddin, Golam M., Rafa Abbas i Timothy E. Shutt. "The role of protein acetylation in regulating mitochondrial fusion and fission". Biochemical Society Transactions 49, nr 6 (23.11.2021): 2807–19. http://dx.doi.org/10.1042/bst20210798.
Pełny tekst źródłaChidipi, Bojjibabu, Syed Islamuddin Shah, Michelle Reiser, Manasa Kanithi, Amanda Garces, Byeong J. Cha, Ghanim Ullah i Sami F. Noujaim. "All-Trans Retinoic Acid Increases DRP1 Levels and Promotes Mitochondrial Fission". Cells 10, nr 5 (14.05.2021): 1202. http://dx.doi.org/10.3390/cells10051202.
Pełny tekst źródłaFaustini, Gaia, Elena Marchesan, Laura Zonta, Federica Bono, Emanuela Bottani, Francesca Longhena, Elena Ziviani, Alessandra Valerio i Arianna Bellucci. "Alpha-Synuclein Preserves Mitochondrial Fusion and Function in Neuronal Cells". Oxidative Medicine and Cellular Longevity 2019 (23.11.2019): 1–11. http://dx.doi.org/10.1155/2019/4246350.
Pełny tekst źródłaQin, Lingyu, i Shuhua Xi. "The role of Mitochondrial Fission Proteins in Mitochondrial Dynamics in Kidney Disease". International Journal of Molecular Sciences 23, nr 23 (25.11.2022): 14725. http://dx.doi.org/10.3390/ijms232314725.
Pełny tekst źródłaPila-Castellanos, Irene, Diana Molino, Joe McKellar, Laetitia Lines, Juliane Da Graca, Marine Tauziet, Laurent Chanteloup i in. "Mitochondrial morphodynamics alteration induced by influenza virus infection as a new antiviral strategy". PLOS Pathogens 17, nr 2 (17.02.2021): e1009340. http://dx.doi.org/10.1371/journal.ppat.1009340.
Pełny tekst źródłaMigliaccio, Sica, Di Gregorio, Putti i Lionetti. "High-Fish Oil and High-Lard Diets Differently Affect Testicular Antioxidant Defense and Mitochondrial Fusion/Fission Balance in Male Wistar Rats: Potential Protective Effect of ω3 Polyunsaturated Fatty Acids Targeting Mitochondria Dynamics". International Journal of Molecular Sciences 20, nr 12 (25.06.2019): 3110. http://dx.doi.org/10.3390/ijms20123110.
Pełny tekst źródłaTokuyama, Takeshi, i Shigeru Yanagi. "Role of Mitochondrial Dynamics in Heart Diseases". Genes 14, nr 10 (26.09.2023): 1876. http://dx.doi.org/10.3390/genes14101876.
Pełny tekst źródłaSantel, A., i M. T. Fuller. "Control of mitochondrial morphology by a human mitofusin". Journal of Cell Science 114, nr 5 (1.03.2001): 867–74. http://dx.doi.org/10.1242/jcs.114.5.867.
Pełny tekst źródłaSugioka, Rie, Shigeomi Shimizu i Yoshihide Tsujimoto. "Fzo1, a Protein Involved in Mitochondrial Fusion, Inhibits Apoptosis". Journal of Biological Chemistry 279, nr 50 (30.09.2004): 52726–34. http://dx.doi.org/10.1074/jbc.m408910200.
Pełny tekst źródłaBraun, Ralf J., i Benedikt Westermann. "Mitochondrial dynamics in yeast cell death and aging". Biochemical Society Transactions 39, nr 5 (21.09.2011): 1520–26. http://dx.doi.org/10.1042/bst0391520.
Pełny tekst źródłaAlsayyah, Cynthia, Manish K. Singh, Maria Angeles Morcillo-Parra, Laetitia Cavellini, Nadav Shai, Christine Schmitt, Maya Schuldiner i in. "Mitofusin-mediated contacts between mitochondria and peroxisomes regulate mitochondrial fusion". PLOS Biology 22, nr 4 (26.04.2024): e3002602. http://dx.doi.org/10.1371/journal.pbio.3002602.
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