16 research outputs found

    I have lived long and variously in the World : The politics and rhetoric of Edmund Burke

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    In the words of Woodrow Wilson, the works of Edmund Burke are stamped in the colors of his extraordinary imagination. The movement takes your breath and quickens your pulses. The glow and power of the matter rejuvenates your faculties. One cannot help but react viscerally to Burke; the brilliant, blustering Irishman demands attention and response. Some regard him as the first and most important exponent of the theoretical reaction against. .. the tenets of liberalism ... [which] came to be called conservatism. Coleridge called him a great man; Victorian liberals even considered him a fellow utilitarian and the greatest thinker who ever devoted himself to English politics. Others, however, regard Burke as a hypocrite who was governed by his own prejudices. These claims of pretence stem from ambiguities and ostensible contradictions in Burke\u27s writings, words, and actions. Although Burke may appear hypocritical, a close examination of his works reveals a surprising consistence. Edmund Burke did not change his mind; the political circumstances around him changed. Though his opinions seem contradictory, they can be reconciled by examining both the historical and personal context in which Burke wrote. From his early works (specifically, A Vindication of Natural Society, Thoughts on the Cause of the Present Discontents, and Conciliation with America) to his later writings (represented by Reflections on the Revolution in France, Thoughts and Details on Scarcity, and A Letter to a Noble Lord), Burke maintains the same conservative principles: devotion to the constitution and Crown, reverence for tradition, and fear of irresponsible government. Burke cherished tradition, but championed reform-- careful reform. He supported the revolutionary efforts of the American colonists, but deplored those of the French-because the colonists sought rights within the existing system, while the French revolutionaries destroyed all vestiges of a system of government

    Tracking a Medically Important Spider: Climate Change, Ecological Niche Modeling, and the Brown Recluse (Loxosceles reclusa)

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    Most spiders use venom to paralyze their prey and are commonly feared for their potential to cause injury to humans. In North America, one species in particular, Loxosceles reclusa (brown recluse spider, Sicariidae), causes the majority of necrotic wounds induced by the Araneae. However, its distributional limitations are poorly understood and, as a result, medical professionals routinely misdiagnose brown recluse bites outside endemic areas, confusing putative spider bites for other serious conditions. To address the issue of brown recluse distribution, we employ ecological niche modeling to investigate the present and future distributional potential of this species. We delineate range boundaries and demonstrate that under future climate change scenarios, the spider's distribution may expand northward, invading previously unaffected regions of the USA. At present, the spider's range is centered in the USA, from Kansas east to Kentucky and from southern Iowa south to Louisiana. Newly influenced areas may include parts of Nebraska, Minnesota, Wisconsin, Michigan, South Dakota, Ohio, and Pennsylvania. These results illustrate a potential negative consequence of climate change on humans and will aid medical professionals in proper bite identification/treatment, potentially reducing bite misdiagnoses

    Library Discussion Panel Part III

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    Interview 3. The Library Interview Series is a set of interviews with a variety of personnel involved with the planning and building of the new Jerry Falwell Library building. The building’s history and planning are discussed as well as the history of the library in general. The recordings were made just before the opening of the new building in early 2014. Timothy Siegel; Kimberly Sandidge; Rachel Schwedt; Marcy Pride; Carl Merat; Stephen Richardson; Angela Ric

    Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit

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    G protein-coupled receptors mediate biological signals by stimulating nucleotide exchange in heterotrimeric G proteins (Gαβγ). Receptor dimers have been proposed as the functional unit responsible for catalytic interaction with Gαβγ. To investigate whether a G protein-coupled receptor monomer can activate Gαβγ, we used the retinal photoreceptor rhodopsin and its cognate G protein transducin (Gt) to determine the stoichiometry of rhodopsin/Gt binding and the rate of catalyzed nucleotide exchange in Gt. Purified rhodopsin was prepared in dodecyl maltoside detergent solution. Rhodopsin was monomeric as concluded from fluorescence resonance energy transfer, copurification studies with fluorescent labeled and unlabeled rhodopsin, size exclusion chromatography, and multiangle laser light scattering. A 1:1 complex between light-activated rhodopsin and Gt was found in the elution profiles, and one molecule of GDP was released upon complex formation. Analysis of the speed of catalytic rhodopsin/Gt interaction yielded a maximum of ≈50 Gt molecules per second and molecule of activated rhodopsin. The bimolecular rate constant is close to the diffusion limit in the diluted system. The results show that the interaction of Gt with an activated rhodopsin monomer is sufficient for fully functional Gt activation. Although the activation rate in solution is at the physically possible limit, the rate in the native membrane is still 10-fold higher. This is likely attributable to the precise orientation of the G protein to the membrane surface, which enables a fast docking process preceding the actual activation step. Whether docking in membranes involves the formation of rhodopsin dimers or oligomers remains to be elucidated

    Identification, cloning, expression and functional characterization of an astacin-like metalloprotease toxin from Loxosceles intermedia (brown spider) venom

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    Injuries caused by brown spiders (Loxosceles genus) are associated with dermonecrotic lesions with gravitational spreading and systemic manifestations. The venom has a complex composition containing many different toxins, of which metalloproteases have been described in many different species of this genus. These toxins may degrade extracellular matrix constituents acting as a spreading factor. By using a cDNA library from an Loxosceles intermedia venom gland, we cloned and expressed a 900 bp cDNA, which encoded a signal peptide and a propeptide, which corresponded to a 30 kDa metalloprotease, now named LALP (Loxosceles astacin-like protease). Recombinant LALP was refolded and used to produce a polyclonal antiserum, which showed cross-reactivity with a 29 kDa native venom protein. CD analysis provided evidence that the recombinant LALP toxin was folded correctly, was still in a native conformation and had not aggregated. LALP addition to endothelial cell cultures resulted in de-adhesion of the cells, and also in the degradation of fibronectin and fibrinogen (this could be inhibited by the presence of the bivalent chelator 1,10-phenanthroline) and of gelatin in vitro. Sequence comparison (nucleotide and deduced amino acid), phylogenetic analysis and analysis of the functional recombinant toxin revealed that LALP is related in both structure and function to the astacin family of metalloproteases. This suggests that an astacin-like toxin is present in a animal venom secretion and indicates that recombinant LALP will be a useful tool for future structural and functional studies on venom and the astacin family
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