University of Stuttgart

About: University of Stuttgart is a education organization based out in Stuttgart, Germany. It is known for research contribution in the topics: Laser & Finite element method. The organization has 27715 authors who have published 56370 publications receiving 1363382 citations. The organization is also known as: Universität Stuttgart.

Software architecture optimization methods: A systematic literature review

Abstract: Due to significant industrial demands toward software systems with increasing complexity and challenging quality requirements, software architecture design has become an important development activity and the research domain is rapidly evolving. In the last decades, software architecture optimization methods, which aim to automate the search for an optimal architecture design with respect to a (set of) quality attribute(s), have proliferated. However, the reported results are fragmented over different research communities, multiple system domains, and multiple quality attributes. To integrate the existing research results, we have performed a systematic literature review and analyzed the results of 188 research papers from the different research communities. Based on this survey, a taxonomy has been created which is used to classify the existing research. Furthermore, the systematic analysis of the research literature provided in this review aims to help the research community in consolidating the existing research efforts and deriving a research agenda for future developments.

Effects of different quinoid redox mediators on the anaerobic reduction of azo dyes by bacteria.

Abstract: The addition of quinoid redox mediators to anaerobically incubated cultures of various taxonomically different bacterial species resulted in significantly increased reduction rates for the azo dye amaranth. From different quinones tested, generally anthraquinone-2-sulfonate (AQS) and lawsone (2-hydroxy-1,4-naphthoquinone) caused the highest increase in the azoreductase activities. The effects of AQS and lawsone were studied in greater detail with Sphingomonas xenophaga BN6 and Escherichia coli K12. Both strains reduced the quinones under anaerobic conditions with significantly different relative activities. The chemically reduced forms of AQS, lawsone, and different other quinones were assayed for their ability to decolorize amaranth, and a good correlation between the redox potentials of the quinones and the reduction rates of the azo dyes was observed. The addition of AQS or lawsone also increased the ability of unacclimated sewage sludge to reduce azo dyes. Chemically pure lawsone could be replaced by the powdered leaves of the henna plant which contain significant amounts of lawsone.

High‐Accuracy Computation of Reaction Barriers in Enzymes

Abstract: With the advent of combined quantum mechanics / molecular mechanics (QM/MM) methods, enzymatic reactions have become accessible to theoretical modeling in recent years. QM/MM calculations on enzymes have generally been restricted to semiempirical or density functional QM treatments, which are realistic but of limited accuracy and cannot be improved in a systematic manner. In this work it has for the first time been possible to apply high-level coupled-cluster ab initio electronic structure methods to enzymatic catalysis, in a QM/MM framework. Excellent agreement is obtained between the computed and the experimentally determined activation barriers for two quite different enzymatic reactions, a Claisen rearrangement in chorismate mutase and an electrophilic aromatic substitution in parahydroxybenzoate hydroxylase. This agreement between experimental and converged theoretical results has broader implications concerning the role of specific dynamic effects in enzyme catalysis that are currently under debate: at least for the two enzymes studied here, such dynamic effects must be small since standard transition state theory describes the reactivity quantitatively.

Caspase-8/FLICE functions as an executioner caspase in anticancer drug-induced apoptosis.

Abstract: Caspase-8 plays an essential role in apoptosis triggered by death receptors. Through the cleavage of Bid, a proapoptotic Bcl-2 member, it further activates the mitochondrial cytochrome c/Apaf-1 pathway. Because caspase-8 can be processed also by anticancer drugs independently of death receptors, we investigated its exact role and order in the caspase cascade. We show that in Jurkat cells either deficient for caspase-8 or overexpressing its inhibitor c-FLIP apoptosis mediated by CD95, but not by anticancer drugs was inhibited. In the absence of active caspase-8, anticancer drugs still induced the processing of caspase-9, -3 and Bid, indicating that Bid cleavage does not require caspase-8. Overexpression of Bcl-xL prevented the processing of caspase-8 as well as caspase-9, -6 and Bid in response to drugs, but was less effective in CD95-induced apoptosis. Similar responses were observed by overexpression of a dominant-negative caspase-9 mutant. To further determine the order of caspase-8 activation, we employed MCF7 cells lacking caspase-3. In contrast to caspase-9 that was cleaved in these cells, anticancer drugs induced caspase-8 activation only in caspase-3 transfected MCF7 cells. Thus, our data indicate that, unlike its proximal role in receptor signaling, in the mitochondrial pathway caspase-8 rather functions as an amplifying executioner caspase.