IT Enabled Sophistication Banking

Globalization of financial markets resulting from both IT (particularly internet standards) and increasing homogeneity of regulation has strongly affected the environment, financial services companies are operating in. Given these changes on the market, innovation is not a choice, but a necessity to survive. Observable today, however, are defensive strategies and poor service quality. In this paper based on investments in trust relationships with customers we propose Sophistication (fit) Banking enabled by IT and qualified staff. While traditional markets are characterized by shrinking margins and declining shareholder values, which can easily be explained by considering the digital character of financial products, new intermediaries for customer-centered Sophistication (fit) Banking have the opportunity of becoming spiders in the web and increasing shareholder values constantly

Rigorous Real-Time Feynman Path Integral for Vector Potentials

we will show the existence and uniqueness of a real-time, time-sliced Feynman path integral for quantum systems with vector potential. Our formulation of the path integral will be derived on the $L^2$ transition probability amplitude via improper Riemann integrals. Our formulation will hold for vector potential Hamiltonian for which its potential and vector potential each carries at most a finite number of singularities and discontinuities

Linear response theory for magnetic Schroedinger operators in disordered media

We justify the linear response theory for an ergodic Schroedinger operator with magnetic field within the non-interacting particle approximation, and derive a Kubo formula for the electric conductivity tensor. To achieve that, we construct suitable normed spaces of measurable covariant operators where the Liouville equation can be solved uniquely. If the Fermi level falls into a region of localization, we recover the well-known Kubo-Streda formula for the quantum Hall conductivity at zero temperature.Comment: Latex, 68 pages, misprints corrected, formatting change

Podocyte specific knock out of selenoproteins does not enhance nephropathy in streptozotocin diabetic C57BL/6 mice

<p>Abstract</p> <p>Background</p> <p>Selenoproteins contain selenocysteine (Sec), commonly considered the 21^stgenetically encoded amino acid. Many selenoproteins, such as the glutathione peroxidases and thioredoxin reductases, protect cells against oxidative stress by functioning as antioxidants and/or through their roles in the maintenance of intracellular redox balance. Since oxidative stress has been implicated in the pathogenesis of diabetic nephropathy, we hypothesized that selenoproteins protect against this complication of diabetes.</p> <p>Methods</p> <p>C57BL/6 mice that have a podocyte-specific inability to incorporate Sec into proteins (denoted in this paper as PodoTrsp^-/-) and control mice were made diabetic by intraperitoneal injection of streptozotocin, or were injected with vehicle. Blood glucose, body weight, microalbuminuria, glomerular mesangial matrix expansion, and immunohistochemical markers of oxidative stress were assessed.</p> <p>Results</p> <p>After 3 and 6 months of diabetes, control and PodoTrsp^-/-mice had similar levels of blood glucose. There were no differences in urinary albumin/creatinine ratios. Periodic acid-Schiff staining to examine mesangial matrix expansion also demonstrated no difference between control and PodoTrsp^-/-mice after 6 months of diabetes, and there were no differences in immunohistochemical stainings for nitrotyrosine or NAD(P)H dehydrogenase, quinone 1.</p> <p>Conclusion</p> <p>Loss of podocyte selenoproteins in streptozotocin diabetic C57BL/6 mice does not lead to increased oxidative stress as assessed by nitrotyrosine and NAD(P)H dehydrogenase, quinone 1 immunostaining, nor does it lead to worsening nephropathy.</p

Conditional Wegner Estimate for the Standard Random Breather Potential

We prove a conditional Wegner estimate for Schr\"odinger operators with random potentials of breather type. More precisely, we reduce the proof of the Wegner estimate to a scale free unique continuation principle. The relevance of such unique continuation principles has been emphasized in previous papers, in particular in recent years. We consider the standard breather model, meaning that the single site potential is the characteristic function of a ball or a cube. While our methods work for a substantially larger class of random breather potentials, we discuss in this particular paper only the standard model in order to make the arguments and ideas easily accessible

An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea

<p>Abstract</p> <p>Background</p> <p>SelB is the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome. In archaea, only a subset of methanogens utilizes selenocysteine and encodes archaeal SelB (aSelB). A SelB-like (aSelBL) homolog has previously been identified in an archaeon that does not encode selenosysteine, and has been proposed to be a pyrrolysyl-tRNA-specific elongation factor (EF-Pyl). However, elongation factor EF-Tu is capable of binding archaeal Pyl-tRNA in bacteria, suggesting the archaeal ortholog EF1A may also be capable of delivering Pyl-tRNA to the ribosome without the need of a specialized factor.</p> <p>Results</p> <p>We have phylogenetically characterized the aSelB and aSelBL families in archaea. We find the distribution of aSelBL to be wider than both selenocysteine and pyrrolysine usage. The aSelBLs also lack the carboxy terminal domain usually involved in recognition of the selenocysteine insertion sequence in the target mRNA. While most aSelBL-encoding archaea are methanogenic Euryarchaea, we also find aSelBL representatives in Sulfolobales and Thermoproteales of Crenarchaea, and in the recently identified phylum Thaumarchaea, suggesting that aSelBL evolution has involved horizontal gene transfer and/or parallel loss. Severe disruption of the GTPase domain suggests that some family members may employ a hitherto unknown mechanism of nucleotide hydrolysis, or have lost their GTPase ability altogether. However, patterns of sequence conservation indicate that aSelBL is still capable of binding the ribosome and aminoacyl-tRNA.</p> <p>Conclusions</p> <p>Although it is closely related to SelB, aSelBL appears unlikely to either bind selenocysteinyl-tRNA or function as a classical GTP hydrolyzing elongation factor. We propose that following duplication of aSelB, the resultant aSelBL was recruited for binding another aminoacyl-tRNA. In bacteria, aminoacylation with selenocysteine is essential for efficient thermodynamic coupling of SelB binding to tRNA and GTP. Therefore, change in tRNA specificity of aSelBL could have disrupted its GTPase cycle, leading to relaxation of selective pressure on the GTPase domain and explaining its apparent degradation. While the specific role of aSelBL is yet to be experimentally tested, its broad phylogenetic distribution, surpassing that of aSelB, indicates its importance.</p