27 research outputs found

    Paying the Prize for the German Submarine War: U-boats destroyed and the Admiralty Prize Fund, 1919–1932

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    This paper examines how the Admiralty paid prize money to the Royal Navy for the destruction of U-boats in the First World War. The research shows that the method by which it did so was distinct from the standard prize process, primarily because of secrecy surrounding the anti-Uboat effort. Prize payments were only made by the Admiralty to the crew of naval vessels after the war had ended and this was based on reports compiled during wartime. The payments made closely match the detailed analysis into U-boat losses released internally by the Anti-Submarine Division (ASD) of the Naval Staff in January 1919. This listed 186 U-boats destroyed. The Admiralty considered 93 of these cases eligible for prize bounty. At least 41 additional cases were turned down. Where inconsistencies exist between the work of the Anti-Submarine Division and the prizes paid out, they are explained by the process of post-war reassessments of U-boats destroyed. In 1917 ASD was pioneering a new type of scientific undersea warfare and it is unfair to be too critical of its work when seen in this historical context. The final prize payments were made in 1932

    Identification of amino acid residues contributing to the pore of a P2X receptor.

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    P2X receptors are ion channels opened by extracellular ATP. The seven subunits currently known are encoded by different genes. It is thought that each subunit has two transmembrane domains, a large extracellular loop, and intracellular N- and C-termini, a topology which is fundamentally different from that of other ligand-gated channels such as nicotinic acetylcholine or glutamate receptors. We used the substituted cysteine accessibility method to identify parts of the molecule that form the ionic pore of the P2X2 receptor. Amino acids preceding and throughout the second hydrophobic domain (316-354) were mutated individually to cysteine, and the DNAs were expressed in HEK293 cells. For three of the 38 residues (I328C, N333C, T336C), currents evoked by ATP were inhibited by extracellular application of methanethiosulfonates of either charge (ethyltrimethylammonium, ethylsulfonate) suggesting that they lie in the outer vestibule of the pore. For two further substitutions (L338C, D349C) only the smaller ethylamine derivative inhibited the current. L338C was accessible to cysteine modification whether or not the channel was opened by ATP, but D349C was inhibited only when ATP was concurrently applied. The results indicate that part of the pore of the P2X receptor is formed by the second hydrophobic domain, and that L338 and D349 are on either side of the channel 'gate'

    Insularity and Empire in the Late Nineteenth Century

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    'We are fish' observed Lord Salisbury of Britain's global interests at the height of the 19th century pax Britannica. Yet the relationship between the sea and Britain's empire during the Victorian era has rarely been treated in a single volume. The essays in this book do just that. Through a series of case-studies these cutting edge contributions survey the work of the Royal Navy as the policeman of imperial interests: combating piracy and the slave trade. In examining the battle for technological supremacy at sea, the role of the large shipping companies in emigration and migration, and the shipping of British culture overseas via the circulation of knowledge and artefacts, this volume gives an insight into the Victorians' understanding of their own destiny as a sea-faring island
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