Automation of technological preparation of metal working on heavy machine tools

The programs for selection of the cutting tools construction and cutting regimes are working in unrestricted surroundings elaborate of addition SharpDevelop in language C#. By the appendix of Cosmos of the program SolidWorks the areas of plate break-age and tensions distributing arising up in it at the different values of cutting force are certain. Based on the conducted researches of durability the rational structural parameters of collapsible chisels, in particular, thickness of plate are grounded that provides the increase of efficiency of treatment of details a hard-alloy instrument on the heavy machine tool

Factors Influencing Corporate Governance in post-Socialist Companies: an Analytical Framework

In explaining the corporate governance performance of post-socialist companies, this article identifies four factors of influence: (1) pressure from majority shareholders, (2) pressure from outside minority shareholders, (3) pressure resulting from internationalization/ globalization and (4) pressure exerted by the state in the form of legal regulation. If all four factors have an impact on corporate governance performance, their interaction has to be explained. On the basis of research conducted thus far, this article suggests an analytical framework for the examination of corporate governance performance of postsocialist companies. Case studies of oil and gas firms from Central and Eastern Europe illustrate how the above factors influence a companyís corporate governance performance.http://deepblue.lib.umich.edu/bitstream/2027.42/64362/1/wp896.pd

The formal political system in Azerbaijan and Kazakhstan: a background study

by Andreas HeinrichLiteraturverz. S. 59 - 6

Characterization of the human NLR protein NLRC5

Nucleotide-binding domain, leucine-rich repeat (NLR)-containing proteins play important roles in the innate immune system as intracellular pattern recognition receptors. The most prominent members, NOD1, NOD2 and NLRP3 have been extensively shown to trigger NF-kB activation or IL-1b/IL-18 processing upon pathogen infection, respectively. Nonetheless, other functions beyond pathogen recognition have also been reported for some NLR proteins. Here we report the first characterization of the human NLR protein NLRC5. NLRC5 lacks the typical N-terminal CARD or PYRIN domain of most NLR proteins, but harbours a death do-main fold effector domain with yet unknown function. Interestingly, NACHT and LRR domain alignments reveal close homology to the MHC class II transcriptional activator (CIITA), which is responsible for the transcriptional induction of MHC class II molecules, and moderate homology to NOD1 and NOD2. In the first part of this study, we addressed the expression and regulation of NLRC5 in different tissues and cell lines. We detected NLRC5 expression primarily in cells and tissues of the immune system, including CD4+ and CD8+ T cells and spleen, lymph node and bone marrow. Furthermore, we were able to induce a TLR3-dependent NLRC5 induction upon stimula-tion with the dsRNA-mimic poly(I:C) as well as an TLR3-independent NLRC5 induction using a Sendai Virus (SeV)-based infection model. In line with that, we revealed a role for NLRC5 in type I interferon (IFN) response against RNA viruses. Moreover, we adapted an infection model of primary human dermal fibroblasts (hFibr) with Sendai Virus (SeV), depicting a distinct role for NLRC5 in anti-viral immune processes. In the second part, we investigated the role of NLRC5 in MHC class I promoter activa-tion. Similar to MHC class II promoter activation by the non-DNA binding coactivator CIITA, we were able to obtain a clear role for NLRC5 in MHC class I expression and identified the domains, which are important for nuclear translocation and MHC class I promoter activation. We further analysed the involvement of a DNA-binding complex, the so-called enhanceosome, in NLRC5-dependent MHC class I expression, which is pivotal for CIITA-dependent MHC class II expression. Finally, we generated NLRC5-CIITA-chimeric proteins to decipher the NLRC5-dependent MHC class I and CIITA-dependent class II activation in more detail. Domain swapping of the N-terminal effector domains revealed, that the NLRC5 N-terminal effector domain fused to the C-terminus of CIITA is sufficient to activate both MHC class I and MHC class II expression. Taken together, in this study we identified a role for NLRC5 in anti-viral immune responses and further contributed to the understanding of NLRC5-mediated MHC class I expression