Literatura académica sobre el tema "Dynamin Related Protein 1 (Drp1)"
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Artículos de revistas sobre el tema "Dynamin Related Protein 1 (Drp1)"
Perry, Heather M., Liping Huang, Rebecca J. Wilson, Amandeep Bajwa, Hiromi Sesaki, Zhen Yan, Diane L. Rosin, David F. Kashatus y Mark D. Okusa. "Dynamin-Related Protein 1 Deficiency Promotes Recovery from AKI". Journal of the American Society of Nephrology 29, n.º 1 (30 de octubre de 2017): 194–206. http://dx.doi.org/10.1681/asn.2017060659.
Texto completoBreitzig, Mason T., Matthew D. Alleyn, Richard F. Lockey y Narasaiah Kolliputi. "A mitochondrial delicacy: dynamin-related protein 1 and mitochondrial dynamics". American Journal of Physiology-Cell Physiology 315, n.º 1 (1 de julio de 2018): C80—C90. http://dx.doi.org/10.1152/ajpcell.00042.2018.
Texto completoUgarte-Uribe, Begoña, Hans-Michael Müller, Miki Otsuki, Walter Nickel y Ana J. García-Sáez. "Dynamin-related Protein 1 (Drp1) Promotes Structural Intermediates of Membrane Division". Journal of Biological Chemistry 289, n.º 44 (18 de septiembre de 2014): 30645–56. http://dx.doi.org/10.1074/jbc.m114.575779.
Texto completoOliver, Darryll y P. Reddy. "Dynamics of Dynamin-Related Protein 1 in Alzheimer’s Disease and Other Neurodegenerative Diseases". Cells 8, n.º 9 (23 de agosto de 2019): 961. http://dx.doi.org/10.3390/cells8090961.
Texto completoStrack, Stefan, Theodore J. Wilson y J. Thomas Cribbs. "Cyclin-dependent kinases regulate splice-specific targeting of dynamin-related protein 1 to microtubules". Journal of Cell Biology 201, n.º 7 (24 de junio de 2013): 1037–51. http://dx.doi.org/10.1083/jcb.201210045.
Texto completoMooli, Raja Gopal Reddy, Dhanunjay Mukhi, Zhonghe Chen, Nia Buckner y Sadeesh K. Ramakrishnan. "An indispensable role for dynamin-related protein 1 in beige and brown adipogenesis". Journal of Cell Science 133, n.º 18 (25 de agosto de 2020): jcs247593. http://dx.doi.org/10.1242/jcs.247593.
Texto completoCheng, Wen-Yu, Kuan-Chih Chow, Ming-Tsang Chiao, Yi-Chin Yang y Chiung-Chyi Shen. "Higher Levels of Dynamin-related Protein 1 are Associated with Reduced Radiation Sensitivity of Glioblastoma Cells". Current Neurovascular Research 17, n.º 4 (14 de diciembre de 2020): 446–63. http://dx.doi.org/10.2174/1567202617666200623123638.
Texto completoBian, Xiyun, Jingman Xu, Huanhuan Zhao, Quan Zheng, Xiaolin Xiao, Xiaofang Ma, Yanxia Li, Xinping Du y Xiaozhi Liu. "Zinc-Induced SUMOylation of Dynamin-Related Protein 1 Protects the Heart against Ischemia-Reperfusion Injury". Oxidative Medicine and Cellular Longevity 2019 (22 de julio de 2019): 1–11. http://dx.doi.org/10.1155/2019/1232146.
Texto completoTanner, Michael J., Jingli Wang, Rong Ying, Tisha B. Suboc, Mobin Malik, Allison Couillard, Amberly Branum, Venkata Puppala y Michael E. Widlansky. "Dynamin-related protein 1 mediates low glucose-induced endothelial dysfunction in human arterioles". American Journal of Physiology-Heart and Circulatory Physiology 312, n.º 3 (1 de marzo de 2017): H515—H527. http://dx.doi.org/10.1152/ajpheart.00499.2016.
Texto completoYu, Rong, Tong Liu, Chenfei Ning, Fei Tan, Shao-Bo Jin, Urban Lendahl, Jian Zhao y Monica Nistér. "The phosphorylation status of Ser-637 in dynamin-related protein 1 (Drp1) does not determine Drp1 recruitment to mitochondria". Journal of Biological Chemistry 294, n.º 46 (18 de septiembre de 2019): 17262–77. http://dx.doi.org/10.1074/jbc.ra119.008202.
Texto completoTesis sobre el tema "Dynamin Related Protein 1 (Drp1)"
Dickey, Audrey Sarah. "Role of pp2a/bβ2 and pka/akap1 in brain development and function via dynamin-related protein 1 (drp1) control of mitochondria shape and bioenergetics". Diss., University of Iowa, 2010. https://ir.uiowa.edu/etd/3444.
Texto completoGrohm, Julia [Verfasser] y Carsten [Akademischer Betreuer] Culmsee. "Molecular regulation of mitochondrial dynamics by dynamin-related protein 1 (Drp1) and Bid in model systems of neuronal cell death / Julia Grohm. Betreuer: Carsten Culmsee". Marburg : Philipps-Universität Marburg, 2011. http://d-nb.info/1013288408/34.
Texto completoHarder, Zdena. "The mechanism of mitochondrial fission: Dynamin-related protein 1 and its effectors". Thesis, University of Ottawa (Canada), 2004. http://hdl.handle.net/10393/26650.
Texto completoBagheri, Mehran. "Intrinsically Disordered Proteins: Mechanics, Assemblies, and Structural Transitions". Thesis, Université d'Ottawa / University of Ottawa, 2017. http://hdl.handle.net/10393/36576.
Texto completoSlupe, Andrew Michael. "Regulation of dynamin-related protein 1-mediated mitochondrial fission by reversible phosphorylation and its contribution to neuronal survival following injury". Diss., University of Iowa, 2014. https://ir.uiowa.edu/etd/4756.
Texto completoCellier, Laura. "Rôle de la dynamique mitochondriale à la phase aiguͭe de l'infarctus du myocarde Increase in Cardiac Ischemia-Reperfusion Injuries in Opa1+/- Mouse Model Remote ischemic conditioning influences mitochondrial dynamics". Thesis, Angers, 2017. http://www.theses.fr/2017ANGE0085.
Texto completoMyocardial infarction (MI) is defined in pathology as « myocardial cell death due to prolonge dischemia ». Currently, reperfusion is the most effective strategy to limit the extent of this myocardial necrosis and to improve the prognosis of patients. Paradoxically, this reperfusion is the cause of additional irreversible damage, called reperfusion injuries. A strategy that was proven efficient in reducing these injuries is the remote ischemic conditioning (RIC). This strategy consists of applying brief, non invasive, episodes of ischemia reperfusion (IR) to an organ or a tissue distant from the ischemic organ, here the heart. Mitochondria play amajor role in both reperfusion injuries and cardioprotection mechanisms. Several studies suggest that the modulation of mitochondrial dynamics, which is mitochondrial fission and fusion mechanisms, could be a new therapeutic strategy for reducing reperfusion injuries. In this work, we studied two transgenic mouse models, one model is deficient in Optic Atrophy 1(OPA1) fusion protein and the other one is deficient in Dynamin Related Protein 1 (DRP1) fission protein. We showed that a partial OPA1 deficiency was associated with an increase in IR injuries and an imbalance in mitochondrial calcium flux, whereas, a partial DRP1 deficiency decreased IR injuries. These data suggest that a therapeutic strategy modulating the mitochondrial dynamics in favor of fusion could reduce IR injuries
Lin, Ruen-Chi y 林潤琪. "GSK3β Interacts with and Phosphorylates Drp1 (Dynamin related protein 1 )/HdynIV (Human dynamin IV) that Affects Mitochondrial Morphology". Thesis, 2010. http://ndltd.ncl.edu.tw/handle/95670546959807308919.
Texto completo高雄醫學大學
生物化學研究所
98
GSK3 (Glycogen Synthase Kinase) belongs to Serine/Theronine kinase family, with multifunction in many vital pathways. Posttranslational modification of dynamin related protein 1 (Drp1/HdynIV) emerged as regulatory mechanisms affecting various activities during mitochondrial fission. Recent study has demonstrated that S-nitrosylation of Drp1/HdynIV triggered mitochondrial fission in Alzheimer''s disease. However, the phosphorylation of Drp1/HdynIV function remains unclear. In our previous studies, we have demonstrated that Drp1/HdynIV and its splicing variants interact with the GSK3β through their carboxyl-terminal lack of proline-rich domain region. In this report, we further narrow down the binding region locates at 634-690 region in Drp1/HdynIV GTPase effector domain. We also perform in vitro kinase assays to examine whether Drp1/HdynIV is a physiological substrate for GSK3β . The data show that fragments of 691-736 a.a (Drp1/HdynIV) is phosphorylated. It is noted that 691-736 a.a of Drp1/HdynIV does not contain binding site, suggesting that binding site is not required for phosphorylation. Further, in vivo assay show that wild type and S693A were transfected into HeLa cells to assess mitochondria morphology, Intriguingly, the data indicate that phosphorylation at GED domain of Ser 693 Drp1/HdynIV results in the alterations of mitochondrial morphology which likely involved in dynamic regulation of mitochondrial division in cells. In summary, we propose that in addition to Drp1/HdynIV nitrosylation, phosphorylation of Drp1/HdynIV by GSK3β may be thought to be another key mediator of Drp1/HdynIV activity.
Liao, Huei De y 廖惠德. "GSK3β-mediated Phosphorylation of Drp1(Dynamin-related protein 1)HdynIV(Human dynamin IV)Ser693 influences its GTPase activity and Mitochondria dynamics". Thesis, 2011. http://ndltd.ncl.edu.tw/handle/43699139141853939685.
Texto completo高雄醫學大學
生物化學研究所
99
Mitochondria dynamics is involved in its’ intracellular distribution which is associated with neurondegeneration. Study indicates that mutant of Drp1 may cause mitochondrial distribution change. Some cells, such as brain cells, strongly rely on the mitochondria to generate energy in specific location at appropriate time. In addition, mitochondria dynamics is greatly shifted toward fission in Alzheimer’s disease, one of the neurondegeneration diseases, and mitochondrial fission is associated with G proteins, such as Drp1. Drp1 is regulated by different kinase, and GSK3β, one of the regulators of Drp1 plays an important role in neurongenesis. Our lab previously demonstrated that Drp1/Human dynamin IV (HdynIV) interacts with the GSK3β via its carboxyl-terminal region; suggest that Drp1/HdynIV may have correlation closely with cell signaling. Moreover, we found that Drp1/HdynIV Ser693 is phosphorylated by GSK3β and the mutant Ser693Ala of Drp1 lost most of the phosphorylation, which further confirm by S693D mutant. Drp1 interacts with its receptor hFIS1 for oligomerization and the GTPase activity is crucial for mitochondrial fission. Thus, we want to find out whether Drp1 S693 mutants reduce their GTPase activity in order to affect mitochondria dynamics. Yeast two hybrid indicated that S693A and S693D didn’t affect the intra-interaction of Drp1, but GTPase activity decreased, which was detected by GTPase coupled enzyme assay. We observed mitchondria morphology in Hela cells tranfected with Drp1 wild type and mutants. The statistic showed that S693D strong;y affected mitochondria morphology and S693A is differed from wild type. These results suggest that Ser693 site might play a role in Drp1 function and mitchochondria dynamics, which may become a drug target for neurondegeneration disease.
Fonseca, Tiago Alexandre Branco. "The role of dynamins and dynamin-related protein 1 (Drp 1) in the regulation of mitochondrial and peroxisomal fission". Master's thesis, 2017. http://hdl.handle.net/10316/82986.
Texto completoPeroxisomas e mitocôndrias são organelos extremamente dinâmicos presentes em quase todas as células. As mitocôndrias, fábricas energéticas, apresentam ciclos contínuos de fusão e fissão que constantemente influenciam e adaptam o retículo mitocondrial às necessidades das células. Por outro lado, peroxisomas conseguem proliferar continuamente através de processos de divisão, mas também são capazes de ser formados a partir de outros compartimentos celulares. Em ambos os casos, estes processos dinâmicos são regulados por proteínas capazes de remodelarem membranas, algumas das quais são mesmo partilhadas entre estes dois organelos, nomeadamente a Dynamin-related protein 1 (Drp1), uma proteína que pertence à superfamília das dinaminas. Quando recrutada, a Drp1 forma estruturas em hélice em torno das membranas de um peroxisoma ou de uma mitocôndria para completar a separação das suas membranas. Contudo, foi recentemente sugerido que o diâmetro destas hélices da Drp1 parece não proporcionar a energia necessária para a divisão das mitocôndrias e que a Dinamina 2 (Dyn 2), também da superfamília das dinaminas, seria capaz de resolver esta limitação da Drp1, provocando a clivagem final das membranas durante a sua divisão. No entanto, este mecanismo ainda não foi estudado para a fissão dos peroxisomas.Dado que a Dyn2 e outras duas isoformas (Dyn1/2/3) constituem as dinaminas clássicas, nós decidimos usar um modelo condicional para eliminar todas estas isoformas de forma a estudar o seu papel na fissão dos peroxisomas e em mais detalhe na divisão mitocondrial. Os nossos resultados mostram que a morfologia dos peroxisomas não depende destas proteínas. Além disso, a eliminação das três isoformas não resulta na elongação das mitocôndrias, ao contrário do que acontece com a inibição da Drp1. Por outro lado, através de live-cell imaging observámos diversos estímulos que induziram a fragmentação mitocondrial independentemente das Dyn1/2/3. Contudo, é importante realçar que a funcionalidade da mitocôndria poderá estar alterada neste modelo de triple knockout das Dyn1/2/3.Os nossos resultados revelam a complexidades de ambos os processos de divisão e ajudam a compreender mais a regulação dos mesmos, mostrando que provavelmente as Dyn1/2/3 são dispensáveis tanto para a divisão dos peroxisomas como para a divisão mitocondrial em resposta a certos estímulos ou em condições basais.
Peroxisomes and mitochondria are extremely dynamic organelles. Mitochondria, the cellular powerhouse, present ongoing cycles of fusion and fission that constantly influence and reshape the mitochondrial reticulum. Peroxisomes, in turn, proliferate through growth and division processes, being also capable of arising from different cellular compartments. These dynamic processes are regulated by membrane-remodelling proteins, some of which are shared between the two organelles, such as Dynamin-related protein 1 (Drp1), a member of the superfamily of dynamin proteins. Drp1 is recruited and assembled in helical rings around peroxisomes or mitochondria undergoing division to fully separate their membranes. However, the diameter of Drp1 rings has been suggested to not provide the necessary constricting force in mitochondrial fission. Recently, Dynamin 2 (Dyn 2), another member of this family, seems to assume the final cleavage step in Drp1-mediated mitochondrial division, thereby resolving this conundrum in Drp1 fission. Whether this mutual Drp1-Dyn2 division is involved in peroxisome division is unknown. Since Dyn2 is one of the three classical dynamins (Dyn1/2/3) expressed in mammalian cells, we decided to use a conditional-triple knockout model of these three dynamins to investigate their role in peroxisome division and mitochondrial division. Our results suggest that peroxisome morphology is unaltered regardless of Dyn1/2/3 deletion. Moreover, depletion of Dyn1/2/3 did not result in mitochondrial elongation, whereas knockdown of Drp1 induced the formation of a hyperfused mitochondrial network. Furthermore, in live-cell imaging of calcium- and depolarisation-induced fragmentation of mitochondria, Dyn1/2/3-depleted cells did not reveal a division blockage. However, mitochondrial metabolism in this triple knockout model is altered. Our results shed light on the complexity of mitochondrial and peroxisomal fission and help understand in more detail how peroxisome and mitochondrial fission are regulated, suggesting that Dyn1/2/3 are not involved in peroxisomal fission and that certain stimuli might not require Dyn2 and/or that Dyn2 is not absolutely needed for mitochondrial fission.
Outro - European Research Council grant received by Doctor Nuno Raimundo.
Prasanna, Katti. "Investigating the Novel Roles of miR-9a and the Regulators of Mitochondrial Dynamics During the Development and Functioning of Indirect Flight Muscles in Drosophila melanogaster". Thesis, 2016. http://etd.iisc.ac.in/handle/2005/4330.
Texto completoCapítulos de libros sobre el tema "Dynamin Related Protein 1 (Drp1)"
Montecinos-Franjola, Felipe y Rajesh Ramachandran. "Imaging Dynamin-Related Protein 1 (Drp1)-Mediated Mitochondrial Fission in Living Cells". En Methods in Molecular Biology, 205–17. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0676-6_16.
Texto completoMontecinos-Franjola, Felipe y Rajesh Ramachandran. "Correction to: Imaging Dynamin-Related Protein 1 (Drp1)-Mediated Mitochondrial Fission in Living Cells". En Methods in Molecular Biology, C1. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0676-6_17.
Texto completoClinton, Ryan W., Brianna L. Bauer y Jason A. Mears. "Affinity and Functional Characterization of Dynamin-Related Protein 1". En Methods in Molecular Biology, 41–53. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0676-6_4.
Texto completoVarlakhanova, Natalia V. y Marijn G. J. Ford. "Purification of the Dynamin-Related Protein Using Mammalian and Bacterial Expression Systems". En Methods in Molecular Biology, 17–27. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0676-6_2.
Texto completo"DRP (dynamin-related protein)". En Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 563. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_4900.
Texto completoGriparic, Lorena y Alexander M. van der Bliek. "Assay and Properties of the Mitochondrial Dynamin Related Protein Opa1". En Methods in Enzymology, 620–31. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)04054-1.
Texto completoCribbs, J. Thomas y Stefan Strack. "Chapter 13 Functional Characterization of Phosphorylation Sites in Dynamin‐Related Protein 1". En Methods in Enzymology, 231–53. Elsevier, 2009. http://dx.doi.org/10.1016/s0076-6879(09)05013-7.
Texto completoActas de conferencias sobre el tema "Dynamin Related Protein 1 (Drp1)"
Qian, Wei, Vera Roginskaya, Sandra Strychor, Jan Beumer, Lee McDermott, Jingnan Wang y Bennett Van Houten. "Abstract 946: Mitochondrial division inhibitor 1 (mdivi-1) overcomes cisplatin resistance independent of dynamin-related protein 1 (Drp1)." En Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-946.
Texto completoAbu-Hanna, Jeries, Jan-Willem Taanman, David Abraham y Lucie Clapp. "Impact of treprostinil on dynamin-related protein 1 (DRP1) and mitochondrial fragmentation in pulmonary arterial hypertension (PAH)." En ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa3059.
Texto completoWu, D., A. Dasgupta, K. H. Chen, T. Hurst, M. Neuber-Hess, A. Martin, J. Mewburn et al. "Novel Dynamin-Related Protein 1 GTPase Inhibitor Prevents Myocardial Ischemia-Reperfusion Injury". En American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2799.
Texto completoBruno, S., B. Korwin-Mihavics, A. Kumar, Z. Mark, B. Cunniff y V. Anathy. "Dynamin Related Protein 1-Mediated Mitochondrial Fission Regulates the Lung Epithelial Response to Allergen". En American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2137.
Texto completoZhang, Zhenzhen, Jie Feng y Shengnan Wu. "Roles of dynamin-related protein 1 in the regulation of mitochondrial fission and apoptosis in response to UV stimuli". En SPIE BiOS, editado por Wei R. Chen. SPIE, 2011. http://dx.doi.org/10.1117/12.874292.
Texto completoInformes sobre el tema "Dynamin Related Protein 1 (Drp1)"
Avni, Adi y Gitta L. Coaker. Proteomic investigation of a tomato receptor like protein recognizing fungal pathogens. United States Department of Agriculture, enero de 2015. http://dx.doi.org/10.32747/2015.7600030.bard.
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