Národní úložiště šedé literatury Nalezeno 2 záznamů.  Hledání trvalo 0.01 vteřin. 
Characterization of pore opening relevant residues in TM3 and TM4 domains of Orai1
ANDOVA, Ana-Marija
Calcium (Ca2+) ions play a crucial role in almost every aspect of cellular life. The most prominent calcium entry pathway into the cell is the calcium release-activated calcium (CRAC) channel, composed of the Orai1 protein, and the stromal interaction molecule STIM1. The channel is activated through conformational changes upon STIM1 coupling to the C-terminus of Orai1 protein following store depletion, which in turn allows Ca2+ influx into the cell. The abnormal function of the CRAC channel caused by mutations gives rise to distinct pathologies. Since it has not yet been elucidated how the signal propagation moves to the pore upon coupling, this thesis dives into its investigation by focusing on characterizing the TM3 and TM4 domains and their importance in leading to an open permissive conformation of the channel. The pivotal foundation for the creation of novel strategies in the modulation of the Orai1 function lies with the understanding of the dynamics of the Orai1 pore opening.
Determining the subcellular compartment in which the unique cleavage of mitochondrial F1 ATPase subunit alpha happens
ANDOVA, Ana-Marija
The T. brucei's infectious stage is characterized by its unique metabolism which requires the mitochondrial FoF1-ATPase to hydrolyze ATP in order to maintain the essential mitochondrial membrane potential. This complex rotary machine has several extraordinary features including the proteolytic cleavage of the F1-ATPase subunit alpha that results in the expulsion of an internal octapeptide. This thesis is focused on whether the proteolytic processing of the essential F1-ATPase subunit already begins in the cytosol.

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