982 resultados para Ahonen, Pertti: Metamorphoses of the administrative state
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27, 1884
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Since June 2014, Islamic State (IS) has been regarded as the principal security threat in the Middle East and one of the most important problems for European and global security. Islamic State, which for many years was just one of many terror organisations with links to al-Qaeda, has succeeded in achieving much more than other similar organisations: it has taken over control of large swathes of territory in Syria and Iraq by military means, created its own para-state structures in that area, and become the greatest civilisational challenge for the region in a century as it established a self-proclaimed caliphate and credibly pledged to expand further on a global scale. Those successes have been accompanied by widely publicised acts of systemic brutality which meets the definition of crimes against humanity. One outcome of these developments is the emergence of an exotic informal alliance to combatthe Islamic State, which has brought together all the states from the Middle East and many from beyond the region. However, contrary to what could have been predicted, after almost a year of the declared war against IS, the Caliphate still holds most of the ground it gained in 2014.
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The voltage-dependent anion-selective channel (VDAC) is an intrinsic β-barrel membrane protein located within the mitochondrial outer membrane where it serves as a pore, connecting the mitochondria to the cytosol. The high-resolution structures of both the human and murine VDACs have been resolved by X-ray diffraction and nuclear magnetic resonance spectroscopy (NMR) in 2008. However, the structural data are not completely in line with the findings that were obtained after decades of research on biochemical and functional analysis of VDAC. This discrepancy may be related to the fact that structural biology studies of membrane proteins reveal specific static conformations that may not necessarily represent the physiological state. For example, overexpression of membrane proteins in bacterial inclusion bodies or simply the extraction from the native lipid environment using harsh purification methods (i.e. chaotropic agents) can disturb the physiological conformations and the supramolecular assemblies. To address these potential issues, we have developed a method, allowing rapid one step purification of endogenous VDAC expressed in the native mitochondrial membrane without overexpression of recombinant protein or usage of harsh chaotropic extraction procedures. Using the Saccharomyces cerevisiae isoform 1 of VDAC as a model, this method yields efficient purification, preserving VDAC in a more physiological, native state following extraction from mitochondria. Single particle analysis using transmission electron microscopy (TEM) demonstrated conservation of oligomeric assembly after purification. Maintenance of the native state was evaluated using functional assessment that involves an ATP-binding assay by micro-scale thermophoresis (MST). Using this approach, we were able to determine for the first time the apparent KD for ATP of 1.2 mM.
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Transportation Systems Center, Cambridge, Mass.
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Includes bibliographical references
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Continued by the Annual report of the Department of Agriculture.
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"January 2000."