Mannheim University of Applied Sciences

About: Mannheim University of Applied Sciences is a education organization based out in Mannheim, Germany. It is known for research contribution in the topics: Gene & Mass spectrometry imaging. The organization has 593 authors who have published 779 publications receiving 19248 citations. The organization is also known as: FH Mannheim & Mannheim College.

A context simulator as testing support for mobile apps

Abstract: Context-aware mobile applications gain more and more influence on our daily life. Since mobile devices are equipped with various sensors to detect their environment, it is possible to receive and process information from beyond application and device borders. Within the development, these context-aware applications have to be verified to assure that they do not cause any failures. This contribution outlines challenges of testing context-aware mobile applications relating to their context factors and present our approach for a context simulator that provides support for modeling and simulation of context in different levels: physical and logical context, situations and scenarios. The simulator supports test case derivation and enables test case execution for several context sources as part of testing mobile applications.

Kinetic modeling of riboflavin biosynthesis in Bacillus subtilis under production conditions.

Abstract: To study the network dynamics of the riboflavin biosynthesis pathway and to identify potential bottlenecks in the system, an ordinary differential equation-based model was constructed using available literature data for production strains. The results confirmed that the RibA protein is rate limiting in the pathway. Under the conditions investigated, we determined a potential limiting order of the remaining enzymes under increased RibA concentration (>0.102 mM) and therefore higher riboflavin production (>0.045 mmol g(CDW)(-1) h(-1) and 0.0035 mM s(-1), respectively). The reductase activity of RibG and lumazine synthase (RibH) might be the next most limiting steps. The computational minimization of the enzyme concentrations of the pathway suggested the need for a greater RibH concentration (0.251 mM) compared with the other enzymes (RibG: 0.188 mM, RibB: 0.023 mM).

Erratum to: A coupled thermodynamic and metabolic control analysis methodology and its evaluation on glycerol biosynthesis in Saccharomyces cerevisiae

Abstract: A coupled in silico thermodynamic and probabilistic metabolic control analysis methodology was verified by applying it to the glycerol biosynthetic pathway in Saccharomyces cerevisiae. The methodology allows predictions even when detailed knowledge of the enzyme kinetics is lacking. In a metabolic steady state, we found that glycerol-3-phosphate dehydrogenase operates far from thermodynamic equilibrium ( $$\varDelta_{r} G^{\prime}_{1}$$ −15.9 to −47.5 kJ mol−1, where $$\varDelta_{r} G^{\prime}_{1}$$ is the transformed Gibbs energy of the reaction). Glycerol-3-phosphatase operates in modes near the thermodynamic equilibrium, far from the thermodynamic equilibrium or in between ( $$ \varDelta_{r} G^{\prime}_{2} $$ ≈ 0 to −23.7 kJ mol−1). From the calculated distribution of the scaled flux control coefficients (median = 0.81), we inferred that the pathway flux is primarily controlled by glycerol-3-phosphate dehydrogenase. This prediction is consistent with previous findings, verifying the efficacy of the proposed methodology.

Following spatial Aβ aggregation dynamics in evolving Alzheimer's disease pathology by imaging stable isotope labeling kinetics.

Abstract: β-Amyloid (Aβ) plaque formation is the major pathological hallmark of Alzheimer's disease (AD) and constitutes a potentially critical, early inducer driving AD pathogenesis as it precedes other pathological events and cognitive symptoms by decades. It is therefore critical to understand how Aβ pathology is initiated and where and when distinct Aβ species aggregate. Here, we used metabolic isotope labeling in APPNL-G-F knock-in mice together with mass spectrometry imaging to monitor the earliest seeds of Aβ deposition through ongoing plaque development. This allowed visualizing Aβ aggregation dynamics within single plaques across different brain regions. We show that formation of structurally distinct plaques is associated with differential Aβ peptide deposition. Specifically, Aβ1-42 is forming an initial core structure followed by radial outgrowth and late secretion and deposition of Aβ1-38. These data describe a detailed picture of the earliest events of precipitating amyloid pathology at scales not previously possible.