Structure and microstructure of the high pressure synthesised misfit layer compound [Sr2O2][CrO2]1.85

The strontium chromium oxide [Sr2O2][CrO2]1.85 misfit layer compound has been synthesised at high pressure and high-temperature conditions. Electron diffraction patterns and high-resolution transmission electron microscopy images along [001] show the misfit character of the different layers composing the structure with a supercell along the incommensurate parameter b=7b1=13b2. The modulated crystal structure has been refined within the superspace formalism against single-crystal X-ray diffraction data, employing the (3+1)-dimensional superspace group Cnmb(0s20)0 0 s. The compound has a composite structure with lattice parameters a1=5.182(1)A˚ , b1=5.411(1)A˚ , c1=18.194(3)A˚ for the first, SrO, subsystem and the same a and c, but with b2=2.925(1)A˚ for the second, CrO2, subsystem. The layer stacking is similar to that of orthorhombic PbS(TiS2)1.18, but with a much stronger intersubsytem bonding in the case of the oxide. The intersubsystem lattice mismatch is mainly handled by displacement modulations of the Sr atoms, correlated with modulations of the valence, the coordination and the anisotropic displacement parameters

Hybrid Local Search for Constrained Financial Portfolio Selection Problems

Abstract. Portfolio selection is a relevant problem arising in finance and economics. While its basic formulations can be efficiently solved through linear or quadratic programming, its more practical and realistic variants, which include various kinds of constraints and objectives, have in many cases to be tackled by approximate algorithms. In this work, we present a hybrid technique that combines a local search, as master solver, with a quadratic programming procedure, as slave solver. Experimental results show that the approach is very promising and achieves results comparable with, or superior to, the state of the art solvers.

Heterogeneous multiple bank financing: does it reduce inefficient credit-renegotiation incidences?

Relationship lending, Asymmetric information, Financial distress, Hold-up, Coordination failure, D82, G21, L14,

Advillin acts upstream of phospholipase C ?1 in steroid-resistant nephrotic syndrome

PubMed ID: 29058690Steroid-resistant nephrotic syndrome (SRNS) is a frequent cause of chronic kidney disease. Here, we identified recessive mutations in the gene encoding the actin-binding protein advillin (AVIL) in 3 unrelated families with SRNS. While all AVIL mutations resulted in a marked loss of its actin-bundling ability, truncation of AVIL also disrupted colocalization with F-actin, thereby leading to impaired actin binding and severing. Additionally, AVIL colocalized and interacted with the phospholipase enzyme PLCE1 and with the ARP2/3 actin-modulating complex. Knockdown of AVIL in human podocytes reduced actin stress fibers at the cell periphery, prevented recruitment of PLCE1 to the ARP3-rich lamellipodia, blocked EGF-induced generation of diacylglycerol (DAG) by PLCE1, and attenuated the podocyte migration rate (PMR). These effects were reversed by overexpression of WT AVIL but not by overexpression of any of the 3 patient-derived AVIL mutants. The PMR was increased by overexpression of WT Avil or PLCE1, or by EGF stimulation; however, this increased PMR was ameliorated by inhibition of the ARP2/3 complex, indicating that ARP-dependent lamellipodia formation occurs downstream of AVIL and PLCE1 function. Together, these results delineate a comprehensive pathogenic axis of SRNS that integrates loss of AVIL function with alterations in the action of PLCE1, an established SRNS protein.VE 196/1-1, HE 7456/1-1, Jo 1324/1-1 U.S. Public Health Service: DK-56338 National Institutes of Health: DK076683 National Institute of Diabetes and Digestive and Kidney Diseases: DK-98120 National Research Foundation of Korea, NRF: 2015R1D1A1A01056685 Department of Science and Technology, Government of Kerala NAS LPDS-2015-07 Fudan UniversityWe are grateful to the families and study participants for their contributions. We thank the Yale Center for Mendelian Genomics (U54HG006504) for WES analysis. FH is a William E. Harmon Professor of Pediatrics. This research was supported by the NIH (DK076683, to FH); the Young Scholars Program of Children’s Hospital of Fudan University (to JR); Basic Science Research Program through the National Research Foundation of Korea 2015R1D1A1A01056685 (to HYG); DFG fellowships (VE 196/1-1, to ATvdV; Jo 1324/1-1, to TJS; and HE 7456/1-1, to TH); the German National Academy of Sciences Leopoldina (LPDS-2015-07, to EW); the Egyptian Group for Orphan Renal Diseases (EGORD) (to NAS); the Department of Science and Technology, Government of India (DST-SERB, to MAJ); the National Institute of Diabetes and Digestive and Kidney Diseases (DK-98120, to SK); and the Public Health Service (DK-56338, to SK). -