Erscheinungsdatum: 12.04.2005, Medium: Buch, Einband: Gebunden, Titel: Nuclear Import and Export in Plants and Animals, Auflage: 2005, Autor: Citovsky, Vitaly // Tzfira, Tzvi, Verlag: Springer US, Sprache: Englisch, Schlagworte: Botanik // Biologie // Molekularbiologie // Tiergarten // Zoo // Tierpark // Zoologe // Zoologischer Garten, Rubrik: Biologie // Grundlagen, Seiten: 244, Informationen: HC runder Rücken kaschiert, Gewicht: 580 gr, Verkäufer: averdo
At a time of discussion about the safe use of nuclear power to generate electricity and the unsolved problem of radioactive waste deposit, the importance of hydropower is increasing. Furthermore the power market liberalization enabled the development of power generation methods, like the use of pumped storage hydro power plants, which can now be realized economically. Nevertheless the planning effort is still considerable when constructing hydro power plants and therefore the use of computer aided design is indispensable. This master thesis deals with the software based calculation of the 3D coordinates of double curved arch dams and the additional processing of these coordinates using Finite Element software. To calculate these 3D coordinates, a program based on Visual Basic for Applications has been developed. By varying the input parameters and using different calculation methods, it is possible to determine the geometry of double curved arch dams and modify it for optimization purposes. As this calculation and optimization is done, an automated Python script export, which enables the import of the chosen dam geometry into the Finite Element program Abaqus CAE, has been implemented. Finally a structural analysis investigating the stresses and displacements is done within Abaqus CAE.
The RNA editing enzyme hsADAR1 (human adenosine deaminase that acts on RNA 1) converts adenosines to inosines in double-stranded RNA and is a transcription-dependent shuttling protein. To enter the nucleus ADAR1 contains an atypical nuclear localization signal (NLS) overlapping the third double-stranded RNA binding domain (dsRBD) in the center of the enzyme. This study is concentrating on the characterization of the roles of dsRBD1 and 3 in the shuttling behavior of the enzyme. On the one hand our results indicate that NLS comprising residues are spread throughout the entire dsRBD. Additionally, several karyopherins were tested whether they can interact with dsRBD3 and mediate nuclear import of hsADAR1. Recent data revealed Transportin-1 as the most probable candidate. On the other hand to elucidate the mechanism that interferes with nuclear accumulation of hsADAR1, experiments were focused on Exportin-5, a karyopherin exporting dsRBDs and micro RNAs. Although the export factor binds ADAR1's dsRBDs in a RNA- and RanGTP dependent manner in vitro, cell based assays fail to confirm an involvement of Exportin-5 in the export of ADAR1.