TY - CHAP A1 - Faber, Christian A1 - Anthrakidis, Anette A1 - Lanz, Marco A1 - Rusack, Markus A1 - Weis, Fabian A1 - Adam, Mario A1 - Schramm, Sebastian T1 - Barriers to solar process heat applications, T2 - SWC 2011: ISES Solar World Congress, 28 August - 2 September 2011, Kassel, Germany KW - Solare-Prozesswärme-Standards Y1 - 2011 UR - https://proceedings.ises.org/swc2011/proceedings/PDF/Papers.pdf SP - 1326 EP - 1334 CY - Kassel ER - TY - JOUR A1 - Voss, Karsten A1 - Musall, Eike A1 - Lichtmeß, Markus T1 - From Low Energy to Net Zero-Energy Buildings: Status and Perspectives JF - Journal of Green Building N2 - “Net Zero-Energy Building” has become a popular catchphrase to describe the synergy between energy-efficient building and renewable energy utilisation to achieve a balanced energy budget over an annual cycle. Taking into account the energy exchange with a grid overcomes the limitations of energy-autonomous buildings with the need for seasonal energy storage on-site. Although the expression, “Net Zero-Energy Building,” appears in many energy policy documents, a harmonised definition or a standardised balancing method is still lacking. This paper reports on the background and the various effects influencing the energy balance approach. After discussing the national energy code framework in Germany, a harmonised terminology and balancing procedure is proposed. The procedure takes not only the energy balance but also energy efficiency and load matching into account. KW - Eigene Methodik Y1 - 2011 U6 - https://doi.org/10.3992/jgb.6.1.46 VL - 6 IS - 1 SP - 46 EP - 57 PB - College Publishing ER - TY - JOUR A1 - Elíasson, Jónas A1 - Palsson, Asgeir A1 - Weber, Konradin T1 - Monitoring ash clouds for aviation JF - Nature Y1 - 2011 U6 - https://doi.org/10.1038/475455b VL - 475 IS - 7357 PB - Springer Nature ER - TY - JOUR A1 - Johanning, M. A1 - Braun, Alexander A1 - Eiteneuer, D. A1 - Paape, C. A1 - Balzer, C. A1 - Neuhauser, W. A1 - Wunderlich, C. T1 - Resonance-enhanced isotope-selective photoionization of YbI for ion trap loading JF - Applied Physics B Y1 - 2011 UR - https://arxiv.org/pdf/0712.0969.pdf U6 - https://doi.org/10.1007/s00340-011-4502-7 SN - 1432-0649 VL - 103 IS - 2 SP - 327 EP - 338 PB - Springer Nature ER - TY - JOUR A1 - Stuhrmann, Björn A1 - Huber, Florian A1 - Käs, Josef T1 - Robust organizational principles of protrusive biopolymer networks in migrating living cells JF - Plos One N2 - Cell migration is associated with the dynamic protrusion of a thin actin-based cytoskeletal extension at the cell front, which has been shown to consist of two different substructures, the leading lamellipodium and the subsequent lamellum. While the formation of the lamellipodium is increasingly well understood, organizational principles underlying the emergence of the lamellum are just beginning to be unraveled. We report here on a 1D mathematical model which describes the reaction-diffusion processes of a polarized actin network in steady state, and reproduces essential characteristics of the lamellipodium-lamellum system. We observe a steep gradient in filament lengths at the protruding edge, a local depolymerization maximum a few microns behind the edge, as well as a differential dominance of the network destabilizer ADF/cofilin and the stabilizer tropomyosin. We identify simple and robust organizational principles giving rise to the derived network characteristics, uncoupled from the specifics of any molecular implementation, and thus plausibly valid across cell types. An analysis of network length dependence on physico-chemical system parameters implies that to limit array treadmilling to cellular dimensions, network growth has to be truncated by mechanisms other than aging-induced depolymerization, e.g., by myosin-associated network dissociation at the transition to the cell body. Our work contributes to the analytical understanding of the cytoskeletal extension's bisection into lamellipodium and lamellum and sheds light on how cells organize their molecular machinery to achieve motility. KW - DOAJ Y1 - 2011 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hbz:due62-opus-34901 SN - 1932-6203 N1 - Funding: This work has been supported by the Leipzig Graduate College ‘‘GK 1097 InterNeuro - Interdisciplinary Approaches in Cellular Neuroscience’’ (http:// www.uni-leipzig.de/˜ineuro/) and the Graduate School ‘‘Leipzig School of Natural Sciences - Building with Molecules and Nano-objects (BuildMoNa)’’ (http://www. buildmona.de/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. VL - 6 IS - 1 PB - Public Library of Science (PLoS) ER - TY - JOUR A1 - Huber, Florian A1 - Käs, Josef T1 - Self-regulative organization of the cytoskeleton JF - Cytoskeleton N2 - Despite its impressive complexity the cytoskeleton succeeds to persistently organize itself and thus the cells' interior. In contrast to classical man-made machines, much of the cellular organization originates from inherent self-assembly and self-organization allowing a high degree of autonomy for various functional units. Recent experimental and theoretical studies revealed numerous examples of cytoskeleton components that arrange and organize in a self-regulative way. In the present review we want to shortly summarize some of the principle mechanisms that are able to inherently trigger and regulate the cytoskeleton organization. Although taken individually most of these regulative principles are rather simple with intuitively predictable consequences, combinations of two or more of these mechanisms can quickly give rise to very complex, unexpected behavior and might even be able to explain the formation of different functional units out of a common pool of available building blocks. Y1 - 2011 UR - http://www.ncbi.nlm.nih.gov/pubmed/21438165 U6 - https://doi.org/10.1002/cm.20509 SN - 1949-3592 N1 - Acknowledgment We would like to thank Dan Strehle for critical reading ofthis manuscript. This work was funded by the Leipzig School of Natural Sciences ‘‘BuildMoNa’’ as well as bythe Sa¨chsische Aufbaubank project number 13403 VL - 68 IS - 5 SP - 259 EP - 265 PB - Wiley ER - TY - JOUR A1 - Lyalina, Yuliya A1 - Langmann, Reinhard A1 - Krisilov, V. T1 - The Interaction Model in iLearning Environments and its Use in the Smart Lab Concept JF - International Journal of Online Engineering Y1 - 2011 U6 - https://doi.org/10.3991/ijoe.v7i4.1793 VL - 7 IS - 4 PB - iJOE ER - TY - RPRT A1 - Schmidt, Holger A1 - Jürjens, Jan T1 - UMLsec4UML2 - Adopting UMLsec to Support UML2 T2 - LS 14 Software Engineering mit dem Schwerpunkt Entwicklung evolutionsfähiger Software und Systeme N2 - In this paper, we present an approach to adopt UMLsec, which is defined for UML 1.5, to support the current UML version 2.3. The new profile UMLsec4UML2 is technically constructed as a UML profile diagram, which is equipped with a number of integrity conditions expressed using OCL. Consequently, the UMLsec4UML2-profile can be loaded in any Eclipse-based EMF- and MDT-compatible UML editing tool to develop and analyze different kinds of security models. The OCL constraints replace the static checks of the tool support for the old UMLsec defined for UML 1.5. Thus, the UMLsec4UML2-profile not only provides the whole expresiveness of UML2.3 for security modeling, it also brings considerably more freedom in selecting a basic UML editing tool, and it integrates modeling and analyzing security models. Since UML2.3 comprises new diagram types, as well as new model elements and new semantics of diagram types already contained in UML1.5, we consider a number of these changes in detail. More specifically, we consider composite structure and sequence diagrams with respect to modeling security properties according to the original version of UMLsec. The goal is to use UMLsec4UML2 to specify architectural security patterns. KW - UMLsec KW - UML2 KW - OCL KW - security architecture KW - security pattern Y1 - 2011 UR - https://eldorado.tu-dortmund.de/handle/2003/27602?locale=de U6 - https://doi.org/10.17877/DE290R-990 N1 - Der Bericht kann über die angebenen URL aufgerufen werden. PB - Technische Hochschule Dortmund CY - Dortmund ER -