Structural study on hole-doped superconductors Pr1-xSrxFeAsO

The structural details in Pr1-xSrxFeAsO (1111) superconducting system are analyzed using data obtained from synchrotron X-ray diffraction and the structural parameters are carefully studied as the system is moving from non-superconducting to hole-doped superconducting with the Sr concentration. Superconductivity emerges when the Sr doping amount reaches 0.221. The linear increase of the lattice constants proves that Sr is successfully introduced into the system and its concentration can accurately be determined by the electron density analyses. The evolution of structural parameters with Sr concentration in Pr1-xSrxFeAsO and their comparison to other similar structural parameters of the related Fe-based superconductors suggest that the interlayer space between the conducting As-Fe-As layer and the insulating Pr-O-Pr layer is important for improving Tc in the hole-doped (1111) superconductors, which seems to be different from electron-doped systems.Comment: 17 pages, 7 figures, 1 tabl

Effect of the tetrahedral distortion on the electronic properties of iron-pnictides

We study the dependence of the electronic structure of iron pnictides on the angle formed by the arsenic-iron bonds. Within a Slater-Koster tight binding model which captures the correct symmetry properties of the bands, we show that the density of states and the band structure are sensitive to the distortion of the tetrahedral environment of the iron atoms. This sensitivity is extremely strong in a two-orbital (d_xz, d_yz) model due to the formation of a flat band around the Fermi level. Inclusion of the d_xy orbital destroys the flat band while keeping a considerable angle dependence in the band structure.Comment: 5 pages, including 5 figures. Fig. 5 replaced. Minor changes in the tex

SUMO-mediated regulation of NLRP3 modulates inflammasome activity.

The NLRP3 inflammasome responds to infection and tissue damage, and rapidly escalates the intensity of inflammation by activating interleukin (IL)-1β, IL-18 and cell death by pyroptosis. How the NLRP3 inflammasome is negatively regulated is poorly understood. Here we show that NLRP3 inflammasome activation is suppressed by sumoylation. NLRP3 is sumoylated by the SUMO E3-ligase MAPL, and stimulation-dependent NLRP3 desumoylation by the SUMO-specific proteases SENP6 and SENP7 promotes NLRP3 activation. Defective NLRP3 sumoylation, either by NLRP3 mutation of SUMO acceptor lysines or depletion of MAPL, results in enhanced caspase-1 activation and IL-1β release. Conversely, depletion of SENP7 suppresses NLRP3-dependent ASC oligomerisation, caspase-1 activation and IL-1β release. These data indicate that sumoylation of NLRP3 restrains inflammasome activation, and identify SUMO proteases as potential drug targets for the treatment of inflammatory diseases

Crystal growth and superconductivity of FeSe_x

Single crystals FeSe_x have been grown in evacuated sealed quartz tube using a NaCl/KCl flux. The products include two crystal structures of tetragon and hexagon. The electronic transport and magnetic properties measurements of FeSe_x single crystal exhibits a superconducting transition at about 10K.Comment: 9 pages, 4 Figure

Super-silent FRET Sensor Enables Live Cell Imaging and Flow Cytometric Stratification of Intracellular Serine Protease Activity in Neutrophils

Abstract Serine proteases are released by neutrophils to act primarily as antimicrobial proteins but excessive and unbalanced serine protease activity results in serious host tissue damage. Here the synthesis of a novel chemical sensor based on a multi-branched fluorescence quencher is reported. It is super-silent, exhibiting no fluorescence until de-quenched by the exemplar serine protease human neutrophil elastase, rapidly enters human neutrophils, and is inhibited by serine protease inhibitors. This sensor allows live imaging of intracellular serine protease activity within human neutrophils and demonstrates that the unique combination of a multivalent scaffold combined with a FRET peptide represents a novel and efficient strategy to generate super-silent sensors that permit the visualisation of intracellular proteases and may enable point of care whole blood profiling of neutrophils