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- 저자 : Stoiber, Walter (검색결과 2 건)
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Ultra High Conductivity Diamond Composites
Bollina Ravi,Stoiber Monika 한국분말야금학회 2006 한국분말야금학회 학술대회논문집 Vol.2006 No.1
Thermal management is one of the critical aspects in the design of highly integrated microelectronic devices. The reliability of electronic components is limited not only to operating temperature but also by the thermal stresses caused during the operation. The need for higher power densities calls for use of advanced heat spreader materials. A copper diamond composite has been developed with high thermal conductivity (λ) and tailorable coefficient of thermal expansion (CTE). Copper diamond composites are processed via gas pressure assisted infiltration with different copper alloys. Emphasis has been placed on the addition of trace elements in deisgning the copper alloys to facilitate a compromise between thermal conductivity and mechanical adhesion. The interfaces between the alloy and the diamond are related to the thermal properties of these copper composites.
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Postmortem proteomics to discover biomarkers for forensic PMI estimation
Choi, Kyoung-Min,Zissler, Angela,Kim, Eunjung,Ehrenfellner, Bianca,Cho, Eunji,Lee, Se-in,Steinbacher, Peter,Yun, Ki Na,Shin, Jong Hwan,Kim, Jin Young,Stoiber, Walter,Chung, Heesun,Monticelli, Fabio Ca Springer Berlin Heidelberg 2019 International journal of legal medicine Vol.133 No.3
<P>The assessment of postmortem degradation of skeletal muscle proteins has emerged as a novel approach to estimate the time since death in the early to mid-postmortem phase (approximately 24 h postmortem (hpm) to 120 hpm). Current protein-based methods are limited to a small number of skeletal muscle proteins, shown to undergo proteolysis after death. In this study, we investigated the usability of a target-based and unbiased system-wide protein analysis to gain further insights into systemic postmortem protein alterations and to identify additional markers for postmortem interval (PMI) delimitation. We performed proteomic profiling to globally analyze postmortem alterations of the rat and mouse skeletal muscle proteome at defined time points (0, 24, 48, 72, and 96 hpm), harnessing a mass spectrometry-based quantitative proteomics approach. Hierarchical clustering analysis for a total of 579 (rat) and 896 (mouse) quantified proteins revealed differentially expressed proteins during the investigated postmortem period. We further focused on two selected proteins (eEF1A2 and GAPDH), which were shown to consistently degrade postmortem in both rat and mouse, suggesting conserved intra- and interspecies degradation behavior, and thus preserved association with the PMI and possible transferability to humans. In turn, we validated the usefulness of these new markers by classical Western blot experiments in a rat model and in human autopsy cases. Our results demonstrate the feasibility of mass spectrometry–based analysis to discover novel protein markers for PMI estimation and show that the proteins eEF1A2 and GAPDH appear to be valuable markers for PMI estimation in humans.</P><P><B>Electronic supplementary material</B></P><P>The online version of this article (10.1007/s00414-019-02011-6) contains supplementary material, which is available to authorized users.</P>
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