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Protein based methods for the identification and classification of mitochondrial disorders /Hanson, Bonnie Jean, January 2001 (has links)
Thesis (Ph. D.)--University of Oregon, 2001. / Typescript. Includes vita and abstract. Includes bibliographical references (leaves 96-103). Also available for download via the World Wide Web; free to University of Oregon users.
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Improving the diagnosis of mitochondrial diseases : application of monoclonal antibody technologies to NADH:ubiquinone oxidoreductase and cytochrome c oxidase defects /Oglesbee, Devin, January 2004 (has links)
Thesis (Ph. D.)--University of Oregon, 2004. / Typescript. Includes vita and abstract. Includes bibliographical references (leaves 113-119). Also available for download via the World Wide Web; free to University of Oregon users.
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Through the course of prehistory in India : tracing the mtDNA trail /Metspalu, Mait, January 2005 (has links) (PDF)
Thesis (doctoral)--University of Tartu, 2005.
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Mitochondrial protein import in genetically and chemically-derived mitochondrial defectsRungi, Arne. January 2001 (has links)
Thesis (M. Sc.)--York University, 2001. Graduate Programme in Kinesiology and Health Science. / Typescript. Includes bibliographical references (leaves 84-88). Also available on the Internet. MODE OF ACCESS via web browser by entering the following URL: http://wwwlib.umi.com/cr/yorku/fullcit?pMQ66403.
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Characterization of the Mitochondrial Fusion Protein Mgm1 Reveals Oligomerization and GTPase ActivityMeglei, Gabriela 24 February 2009 (has links)
Mitochondrial dynamics resulting from competing fusion and fission reactions are required for normal cellular function in eukaryotes. Mgm1, a dynamin related protein, is a key component in yeast mitochondrial fusion and is evolutionarily conserved. Previous in vivo studies suggest that the GTPase domain and oligomerization are required for Mgm1 mediated mitochondrial inner membrane fusion. This work demonstrates that purified Mgm1 forms dynamic low order oligomers, and has GTPase activity and kinetic properties consistent with a mechanoenzyme and with a role in inner membrane mitochondrial fusion. Mutations of key residues in the GTPase domain show diminished GTPase activity, while a mutation in the GTPase effector domain implicated in self-assembly results in a lower propensity to form oligomers. Together these data indicate that Mgm1 mediates fusion through oligomerization and GTP binding/hydrolysis in a manner similar to other dynamin mechanoenzymes.
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Characterization of the Mitochondrial Fusion Protein Mgm1 Reveals Oligomerization and GTPase ActivityMeglei, Gabriela 24 February 2009 (has links)
Mitochondrial dynamics resulting from competing fusion and fission reactions are required for normal cellular function in eukaryotes. Mgm1, a dynamin related protein, is a key component in yeast mitochondrial fusion and is evolutionarily conserved. Previous in vivo studies suggest that the GTPase domain and oligomerization are required for Mgm1 mediated mitochondrial inner membrane fusion. This work demonstrates that purified Mgm1 forms dynamic low order oligomers, and has GTPase activity and kinetic properties consistent with a mechanoenzyme and with a role in inner membrane mitochondrial fusion. Mutations of key residues in the GTPase domain show diminished GTPase activity, while a mutation in the GTPase effector domain implicated in self-assembly results in a lower propensity to form oligomers. Together these data indicate that Mgm1 mediates fusion through oligomerization and GTP binding/hydrolysis in a manner similar to other dynamin mechanoenzymes.
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Studies of mammalian mitochondrial genomes with special emphasis on the perissodactylaXu, Xiufeng. January 1996 (has links)
Thesis (doctoral)--Lund University, 1996.
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Studies of mammalian mitochondrial genomes with special emphasis on the perissodactylaXu, Xiufeng. January 1996 (has links)
Thesis (doctoral)--Lund University, 1996.
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Déficits de la chaîne respiratoire mitochondriale avec instabilité de l’ADN mitochondrial : identification de nouveaux gènes et mécanismes / Non communiquéBerg Alonso, Laetitia 10 November 2016 (has links)
Les maladies mitochondriales regroupent un ensemble de pathologies liées à un déficit de la chaînerespiratoire mitochondriale. Au laboratoire, nous focalisons notre intérêt sur les mitochondriopathies liées à undéfaut de stabilité de l’ADN mitochondrial (ADNmt), qui se traduit par des délétions multiples et/ou unedéplétion (diminution du nombre de copies). Ces pathologies sont caractérisées par une importantehétérogénéité clinique et génétique et sont secondaires à des mutations dans des gènes nucléaires codantpour des protéines impliquées dans le maintien de l’ADNmt. De nos jours, la recherche des gènesresponsables d’instabilité de l’ADNmt s’avère négative chez plus de 70% des malades, d’où un grand intérêtpour améliorer les techniques d’identification des mutations et la recherche de nouveaux gènes impliquésdans ces pathologies / Non communiqué
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The role of MGME1 in maintenance of the human mitochondrial genomeNicholls, Thomas Joseph James January 2014 (has links)
No description available.
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