Zeitschriftenartikel zum Thema „Mitofusins“
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Cohen, Mickael M., und David Tareste. „Recent insights into the structure and function of Mitofusins in mitochondrial fusion“. F1000Research 7 (28.12.2018): 1983. http://dx.doi.org/10.12688/f1000research.16629.1.
Wolf, Christina, Víctor López del Amo, Sabine Arndt, Diones Bueno, Stefan Tenzer, Eva-Maria Hanschmann, Carsten Berndt und Axel Methner. „Redox Modifications of Proteins of the Mitochondrial Fusion and Fission Machinery“. Cells 9, Nr. 4 (27.03.2020): 815. http://dx.doi.org/10.3390/cells9040815.
LeBrasseur, Nicole. „Pro-diversity mitofusins“. Journal of Cell Biology 176, Nr. 4 (12.02.2007): 373a. http://dx.doi.org/10.1083/jcb.1764iti3.
Schiavon, Cara R., Rachel E. Turn, Laura E. Newman und Richard A. Kahn. „ELMOD2 regulates mitochondrial fusion in a mitofusin-dependent manner, downstream of ARL2“. Molecular Biology of the Cell 30, Nr. 10 (Mai 2019): 1198–213. http://dx.doi.org/10.1091/mbc.e18-12-0804.
Koch, Linda. „Mitofusins and energy balance“. Nature Reviews Endocrinology 9, Nr. 12 (15.10.2013): 691. http://dx.doi.org/10.1038/nrendo.2013.202.
Escobar-Henriques, Mafalda. „Mitofusins: ubiquitylation promotes fusion“. Cell Research 24, Nr. 4 (21.02.2014): 387–88. http://dx.doi.org/10.1038/cr.2014.23.
Miao, Junru, Wei Chen, Pengxiang Wang, Xin Zhang, Lei Wang, Shuai Wang und Yuan Wang. „MFN1 and MFN2 Are Dispensable for Sperm Development and Functions in Mice“. International Journal of Molecular Sciences 22, Nr. 24 (16.12.2021): 13507. http://dx.doi.org/10.3390/ijms222413507.
Sloat, S. R., B. N. Whitley, E. A. Engelhart und S. Hoppins. „Identification of a mitofusin specificity region that confers unique activities to Mfn1 and Mfn2“. Molecular Biology of the Cell 30, Nr. 17 (August 2019): 2309–19. http://dx.doi.org/10.1091/mbc.e19-05-0291.
Alsayyah, Cynthia, Manish K. Singh, Maria Angeles Morcillo-Parra, Laetitia Cavellini, Nadav Shai, Christine Schmitt, Maya Schuldiner et al. „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.
R. Khalil, Rana, Mufeda AL-Ammar und Hayder A. L. Mossa. „Mitofusin 1 as Marker of Oocyte Maturation in Relevance to ICSI Outcome in Infertile Females“. IraQi Journal of Embryos and Infertility Researches 13, Nr. 2 (08.11.2023): 39–50. http://dx.doi.org/10.28969/ijeir.v13.i2.r4.23.
Schrepfer, Emilie, und Luca Scorrano. „Mitofusins, from Mitochondria to Metabolism“. Molecular Cell 61, Nr. 5 (März 2016): 683–94. http://dx.doi.org/10.1016/j.molcel.2016.02.022.
Ozcan, Umut. „Mitofusins: Mighty Regulators of Metabolism“. Cell 155, Nr. 1 (September 2013): 17–18. http://dx.doi.org/10.1016/j.cell.2013.09.013.
Brooks, Craig, Sung-Gyu Cho, Cong-Yi Wang, Tianxin Yang und Zheng Dong. „Fragmented mitochondria are sensitized to Bax insertion and activation during apoptosis“. American Journal of Physiology-Cell Physiology 300, Nr. 3 (März 2011): C447—C455. http://dx.doi.org/10.1152/ajpcell.00402.2010.
Giacomello, Marta, und Luca Scorrano. „The INs and OUTs of mitofusins“. Journal of Cell Biology 217, Nr. 2 (18.01.2018): 439–40. http://dx.doi.org/10.1083/jcb.201801042.
Dorn, Gerald W. „Mitofusins as mitochondrial anchors and tethers“. Journal of Molecular and Cellular Cardiology 142 (Mai 2020): 146–53. http://dx.doi.org/10.1016/j.yjmcc.2020.04.016.
Parekh, Anant. „Calcium Signalling: Mitofusins Promote Interorganellar Crosstalk“. Current Biology 19, Nr. 5 (März 2009): R200—R203. http://dx.doi.org/10.1016/j.cub.2009.01.012.
Engelhart, Emily A., und Suzanne Hoppins. „A catalytic domain variant of mitofusin requiring a wildtype paralog for function uncouples mitochondrial outer-membrane tethering and fusion“. Journal of Biological Chemistry 294, Nr. 20 (01.04.2019): 8001–14. http://dx.doi.org/10.1074/jbc.ra118.006347.
Anton, Vincent, Ira Buntenbroich, Ramona Schuster, Felix Babatz, Tânia Simões, Selver Altin, Gaetano Calabrese, Jan Riemer, Astrid Schauss und Mafalda Escobar-Henriques. „Plasticity in salt bridge allows fusion-competent ubiquitylation of mitofusins and Cdc48 recognition“. Life Science Alliance 2, Nr. 6 (18.11.2019): e201900491. http://dx.doi.org/10.26508/lsa.201900491.
Song, Zhiyin, Mariam Ghochani, J. Michael McCaffery, Terrence G. Frey und David C. Chan. „Mitofusins and OPA1 Mediate Sequential Steps in Mitochondrial Membrane Fusion“. Molecular Biology of the Cell 20, Nr. 15 (August 2009): 3525–32. http://dx.doi.org/10.1091/mbc.e09-03-0252.
Mattie, Sevan, Jan Riemer, Jeremy G. Wideman und Heidi M. McBride. „A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space“. Journal of Cell Biology 217, Nr. 2 (06.12.2017): 507–15. http://dx.doi.org/10.1083/jcb.201611194.
De Vecchis, Dario, Antoine Taly, Marc Baaden und Jérôme Hénin. „Mitochondrial Membrane Fusion: Computational Modeling of Mitofusins“. Biophysical Journal 110, Nr. 3 (Februar 2016): 571a. http://dx.doi.org/10.1016/j.bpj.2015.11.3054.
Papanicolaou, Kyriakos N., Matthew M. Phillippo und Kenneth Walsh. „Mitofusins and the mitochondrial permeability transition: the potential downside of mitochondrial fusion“. American Journal of Physiology-Heart and Circulatory Physiology 303, Nr. 3 (01.08.2012): H243—H255. http://dx.doi.org/10.1152/ajpheart.00185.2012.
Schuster, Ramona, Vincent Anton, Tânia Simões, Selver Altin, Fabian den Brave, Thomas Hermanns, Manuela Hospenthal et al. „Dual role of a GTPase conformational switch for membrane fusion by mitofusin ubiquitylation“. Life Science Alliance 3, Nr. 1 (19.12.2019): e201900476. http://dx.doi.org/10.26508/lsa.201900476.
Son, M. J., Y. Kwon, M.-Y. Son, B. Seol, H.-S. Choi, S.-W. Ryu, C. Choi und Y. S. Cho. „Mitofusins deficiency elicits mitochondrial metabolic reprogramming to pluripotency“. Cell Death & Differentiation 22, Nr. 12 (17.04.2015): 1957–69. http://dx.doi.org/10.1038/cdd.2015.43.
Yu, Chia-Yi, Jian-Jong Liang, Jin-Kun Li, Yi-Ling Lee, Bi-Lan Chang, Chan-I. Su, Wei-Jheng Huang, Michael M. C. Lai und Yi-Ling Lin. „Dengue Virus Impairs Mitochondrial Fusion by Cleaving Mitofusins“. PLOS Pathogens 11, Nr. 12 (30.12.2015): e1005350. http://dx.doi.org/10.1371/journal.ppat.1005350.
Mourier, Arnaud, Elisa Motori, Eduardo Silva Ramos, Tobias Brandt, Marie Lagouge, Ilian Atanassov, Anne Galinier et al. „Role of Mitofusins proteins in maintaining OXPHOS function“. Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857 (August 2016): e15. http://dx.doi.org/10.1016/j.bbabio.2016.04.386.
Santel, A., und M. T. Fuller. „Control of mitochondrial morphology by a human mitofusin“. Journal of Cell Science 114, Nr. 5 (01.03.2001): 867–74. http://dx.doi.org/10.1242/jcs.114.5.867.
Tanaka, Atsushi, Megan M. Cleland, Shan Xu, Derek P. Narendra, Der-Fen Suen, Mariusz Karbowski und 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.
Samanas, Nyssa B., Emily A. Engelhart und Suzanne Hoppins. „Defective nucleotide-dependent assembly and membrane fusion in Mfn2 CMT2A variants improved by Bax“. Life Science Alliance 3, Nr. 5 (03.04.2020): e201900527. http://dx.doi.org/10.26508/lsa.201900527.
Pellattiero, Anna, und Luca Scorrano. „Flaming Mitochondria: The Anti-inflammatory Drug Leflunomide Boosts Mitofusins“. Cell Chemical Biology 25, Nr. 3 (März 2018): 231–33. http://dx.doi.org/10.1016/j.chembiol.2018.02.014.
Zhang, Lihong, Xiawei Dang, Antonietta Franco, Haiyang Zhao und Gerald W. Dorn. „Piperine Derivatives Enhance Fusion and Axonal Transport of Mitochondria by Activating Mitofusins“. Chemistry 4, Nr. 3 (23.06.2022): 655–68. http://dx.doi.org/10.3390/chemistry4030047.
Ryan, Michael T., und Diana Stojanovski. „Mitofusins ‘bridge’ the gap between oxidative stress and mitochondrial hyperfusion“. EMBO reports 13, Nr. 10 (11.09.2012): 870–71. http://dx.doi.org/10.1038/embor.2012.132.
Daumke, Oliver, und Aurélien Roux. „Mitochondrial Homeostasis: How Do Dimers of Mitofusins Mediate Mitochondrial Fusion?“ Current Biology 27, Nr. 9 (Mai 2017): R353—R356. http://dx.doi.org/10.1016/j.cub.2017.03.024.
Santel, Ansgar. „Get the balance right: Mitofusins roles in health and disease“. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1763, Nr. 5-6 (Mai 2006): 490–99. http://dx.doi.org/10.1016/j.bbamcr.2006.02.004.
Ding, Wen-Xing, Fengli Guo, Hong-Min Ni, Abigail Bockus, Sharon Manley, Donna B. Stolz, Eeva-Liisa Eskelinen, Hartmut Jaeschke und Xiao-Ming Yin. „Parkin and Mitofusins Reciprocally Regulate Mitophagy and Mitochondrial Spheroid Formation“. Journal of Biological Chemistry 287, Nr. 50 (24.10.2012): 42379–88. http://dx.doi.org/10.1074/jbc.m112.413682.
Vlieghe, Anaïs, Kristina Niort, Hugo Fumat, Jean-Michel Guigner, Mickaël M. Cohen und David Tareste. „Role of Lipids and Divalent Cations in Membrane Fusion Mediated by the Heptad Repeat Domain 1 of Mitofusin“. Biomolecules 13, Nr. 9 (02.09.2023): 1341. http://dx.doi.org/10.3390/biom13091341.
Ugarte-Uribe, Begoña, und Ana J. García-Sáez. „Membranes in motion: mitochondrial dynamics and their role in apoptosis“. Biological Chemistry 395, Nr. 3 (01.03.2014): 297–311. http://dx.doi.org/10.1515/hsz-2013-0234.
Papanicolaou, Kyriakos N., Ryosuke Kikuchi, Gladys A. Ngoh, Kimberly A. Coughlan, Isabel Dominguez, William C. Stanley und Kenneth Walsh. „Mitofusins 1 and 2 Are Essential for Postnatal Metabolic Remodeling in Heart“. Circulation Research 111, Nr. 8 (28.09.2012): 1012–26. http://dx.doi.org/10.1161/circresaha.112.274142.
Rakovic, Aleksandar, Anne Grünewald, Jan Kottwitz, Norbert Brüggemann, Peter P. Pramstaller, Katja Lohmann und Christine Klein. „Mutations in PINK1 and Parkin Impair Ubiquitination of Mitofusins in Human Fibroblasts“. PLoS ONE 6, Nr. 3 (08.03.2011): e16746. http://dx.doi.org/10.1371/journal.pone.0016746.
Brooks, C., Q. Wei, L. Feng, G. Dong, Y. Tao, L. Mei, Z. J. Xie und Z. Dong. „Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins“. Proceedings of the National Academy of Sciences 104, Nr. 28 (02.07.2007): 11649–54. http://dx.doi.org/10.1073/pnas.0703976104.
Du, Mengyan, Si Yu, Wenhua Su, Mengxin Zhao, Fangfang Yang, Yangpei Liu, Zihao Mai, Yong Wang, Xiaoping Wang und Tongsheng Chen. „Mitofusin 2 but not mitofusin 1 mediates Bcl-XL-induced mitochondrial aggregation“. Journal of Cell Science 133, Nr. 20 (21.09.2020): jcs245001. http://dx.doi.org/10.1242/jcs.245001.
Wiedemann, Nils, Sebastian B. Stiller und Nikolaus Pfanner. „Activation and Degradation of Mitofusins: Two Pathways Regulate Mitochondrial Fusion by Reversible Ubiquitylation“. Molecular Cell 49, Nr. 3 (Februar 2013): 423–25. http://dx.doi.org/10.1016/j.molcel.2013.01.027.
Yin, Xiao-Ming, und Wen-Xing Ding. „The reciprocal roles of PARK2 and mitofusins in mitophagy and mitochondrial spheroid formation“. Autophagy 9, Nr. 11 (03.11.2013): 1687–92. http://dx.doi.org/10.4161/auto.24871.
Dietrich, Marcelo O., Zhong-Wu Liu und Tamas L. Horvath. „Mitochondrial Dynamics Controlled by Mitofusins Regulate Agrp Neuronal Activity and Diet-Induced Obesity“. Cell 155, Nr. 1 (September 2013): 188–99. http://dx.doi.org/10.1016/j.cell.2013.09.004.
Lee, Crystal A., Lih-Shen Chin und Lian Li. „Hypertonia-linked protein Trak1 functions with mitofusins to promote mitochondrial tethering and fusion“. Protein & Cell 9, Nr. 8 (18.09.2017): 693–716. http://dx.doi.org/10.1007/s13238-017-0469-4.
Bhatia, Divya, Eleni Kallinos, Edwin Patino, Maria Plataki, Augustine M. Choi und Mary E. Choi. „Alveolar Type II Cell-Specific Mitofusins Modulate Kidney Fibrosis and Associated Lung Injury“. Journal of the American Society of Nephrology 34, Nr. 11S (November 2023): 701. http://dx.doi.org/10.1681/asn.20233411s1701b.
Wakai, Takuya, Yuichirou Harada, Kenji Miyado und Tomohiro Kono. „Mitochondrial dynamics controlled by mitofusins define organelle positioning and movement during mouse oocyte maturation“. MHR: Basic science of reproductive medicine 20, Nr. 11 (11.08.2014): 1090–100. http://dx.doi.org/10.1093/molehr/gau064.
Chen, Hsiuchen, Scott A. Detmer, Andrew J. Ewald, Erik E. Griffin, Scott E. Fraser und 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.
Wu, Zhaofei, Yushan Zhu, Xingshui Cao, Shufeng Sun und Baolu Zhao. „Mitochondrial Toxic Effects of Aβ Through Mitofusins in the Early Pathogenesis of Alzheimer’s Disease“. Molecular Neurobiology 50, Nr. 3 (08.04.2014): 986–96. http://dx.doi.org/10.1007/s12035-014-8675-z.
Nakamura, Nobuhiro, und Shigehisa Hirose. „Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane“. Molecular Biology of the Cell 19, Nr. 5 (Mai 2008): 1903–11. http://dx.doi.org/10.1091/mbc.e07-11-1103.