40 research outputs found

    Nanocrystallization by nitriding treatment of FeSiB-based amorphous ribbons

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    In FeSiB-based systems, nanocrystalline state needed for good soft magnetic properties is obtained by controlling nucleation and growth rates of crystallization. These rates are known to depend on the additive elements in the FeSiB alloys but also on the annealing treatment. Generally, Cu and Nb are chosen as additive elements and conventional thermal treatment (C.T.T.) is used to produce the nanocrystalline phase. In this work, we studied Fe73.5Cu1Si13.5B12, Fe74Nb3Si14B9 and Fe73.5Cu1Nb3Si13.5B9 ribbons. To obtain the nanocrystalline state, in addition to C.T.T., we used a nitriding thermochemical treatment (N.T.T.) at =520°C and we show that this treatment improves the nanocrystalline state (smaller grain size D and higher crystalline volume fraction. This treatment also increases the Curie temperature of the crystalline α-FeSi phase

    By the people for the people

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    157 p. ; 28 cm

    Synergistic effect of hypoglycemic sulfonylureas and negative phospholipids on calcium transport: ionic and conformational aspects.

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    peer reviewedIn a two-phase bulk system for the study of ionophoresis, the capacity of hypoglycemic sulfonylureas to translocate Ca2+ was enhanced in a synergistic manner by negatively charged phospholipids. High concentrations of Na+ or K+ had relatively little effect on sulfonylurea-mediated Ca2+ translocation. The acidity constant of hypoglycemic sulfonylureas ranged from 10(-5) to 10(-6). The conformation analysis of Ca2+ -gliquidone complexes with a 1:1 or 1:2 stoichiometry and of a hybrid complex between Ca2+ and both gliquidone and phosphatidylserine revealed configurations suitable for Ca2+ transport across a hydrophobic domain. These findings raise the possibility that the cationic response of the pancreatic B-cell to hypoglycemic sulfonylureas may be due primarily to an alteration of both Ca2+ and H+ transport

    J Proteome Res

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    The neurodegenerative disorder Alzheimer’s disease (AD) is the most common cause of dementia in the elderly. The presence of neurofibrillary tangles, consisting of hyperphosphorylated tau protein, is one of the major neuropathologic characteristics of the disease, making this protein an attractive biomarker for AD and a possible target for therapy. Here, we describe an optimized immunoprecipitation mass spectrometry method that enables, for the first time, detailed characterization of tau in human cerebrospinal fluid. The identities of putative tau fragments were confirmed using nanoflow liquid chromatography and tandem mass spectrometry. Nineteen tryptic fragments of tau were detected, of which 16 are found in all tau isoforms while 3 represented unique tau isoforms. These results pave the way for clinical CSF studies on the tauopathies
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