108 research outputs found
Wi-Fi RTT を用いた位置特定手法の屋内環境での性能評価
本稿では Wi-Fi RTT (Round Trip Time)の測距,測位について実際の利用時を想定した性能評価を行っている.実験の結果,測距,測位のいずれにおいても,周波数帯,帯域幅,使用チャネル,チャネル使用量が性能に影響を与えることを示している.また,測距性能評価では,アクセスポイントの高さの設置基準,測位計算に利用するアクセスポイントの選択基準に関する知見を得ている.測距性能評価を踏まえた測位性能評価では,チャネル使用量と測位性能の関係を示し,チャネル選択の重要性に関する知見を得ている.
In this paper, we evaluate the ranging and positioning performance considering the actual usage environments about Wi-Fi RTT (Round Trip Time). As the results, we show that frequency band, band width, channel, and channel status influence the ranging and positioning performance. Also, we obtain the knowledge about the installation height criteria of access points and the selection criterion of access points. In addition, we show the relationships between channel status and positioning performance. Consequently, we obtain the knowledge about the importance of the channel selection on Wi-Fi RTT.Copyright ©2020 by IEICEtextapplication/pdftechnical repor
A Research on Cooperative Problem Solving in Mathematics Education : Object of Evaluation and Practical Trails
departmental bulletin pape
REALIZATION OF AUTOMORPHISMS sigma OF ORDER 3 AND G^{sigma} OF COMPACT EXCEPTIONAL LIE GROUPS G , II, G=E_{7}
application/pdfFor the simply connected compact exceptional Lie group E_{7} , we realize all of automorphisms sigma of order 3 and determine the group structures the fixed subgroups (E_{7})^{sigma} of E_{7}.departmental bulletin pape
Comparative Assessment of Human Health Risks from Rice Consumption in Thailand and Vietnam
Rice is the staple food of Southeast Asia, whose population consumes about 197 kg per capita per year.Heavy metals present in this rice are therefore a serious health matter. This study was conducted to i) monitor and compare the rice cultivated in both Thailand and Vietnam with respect to the heavy metals contained, and ii) assess any local human health risk from rice consumption. The results showed nonsignificant differences in heavy metal concentrations in different types of polished rice (jasmine,sticky,and white). Similar samples of brown jasmine rice were found to have higher metal concentrations compared to other polished rice samples. By the CODEX standards, most rice samples collected from Thailand and Vietnam are generally safe for consumption on a daily basis. Human health risk assessment, however, reveals daily consumption of this rice might lead to negative health impacts from Zn toxicity (at hazard quotients > 1); this held for all types of rice grains tested.othe
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TRB3 expression induces nuclear translocation of proCASP3.
<p>(A) HeLa cells were cotransfected with the C163S-proCASP3-EmGFP and V5-WT-TRB3 expression plasmids. After 24 hr, the cells were stained with anti-V5 antibody (red) and counterstained with DAPI (blue). Arrow and arrowhead indicated V5-WT-TRB3 positive and negative cells respectively. Scale bars = 10 µm. (B) Twenty-four hours after transfection with the C163S-proCASP3-EmGFP expression plasmid, HeLa cells were incubated with or without tunicamycin for 8 hr. Arrowheads showed representative phenotypes of C163S-proCASP3-EmGFP localization in each condition. Scale bars = 20 µm. (C) Twenty-four hours after transfection with the C163S-proCASP3-EmGFP expression plasmid, HeLa cells were treated with tunicamycin, and localization of C163S-proCASP3-EmGFP was simultaneously monitored for 24 hr by live imaging. Representative frames displaying scenes of nuclear translocation (arrows) are shown. Scale bars = 10 µm. (D) Localization of C163S-proCASP3-EmGFP was quantified as cytoplasmic, mainly cytoplasmic or cytoplasmic equal to nuclear (C, C>N, C = N), or as nuclear or mainly nuclear (N, N>C) under conditions described above (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042721#pone-0042721-g004" target="_blank">Figure 4A, V</a>5-WT-TRB3; <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042721#pone-0042721-g004" target="_blank">Figure 4B</a>, ctrl or Tunicamycin). This localization was also assessed in cells coexpressing V5-WT-TRB3 (right bar graph). Over 30 cells were assessed in three independent experiments. Error bar: mean ±SD. *<i>P</i><0.01, **<i>P</i><0.005. (E) HeLa cells were cotransfected with the C163S-proCASP3-HA and indicated artificial miRNA expression plasmids. After 24 hr, the cells were incubated with tunicamycin for 8 hr. The localization of C163S-proCASP3-HA was observed by immunofluorescence staining with an anti-HA antibody (red). The miRNA expressing cells of inner panel were visualized by cocistronic expression of EmGFP. Arrowheads showed the C163S-proCASP3-HA expressing cells. Scale bars = 20 µm. (F) The cells positive for nuclear C163S-proCASP3-HA (N, N>C, N = C) were quantified by immunofluorescence staining with an anti-HA antibody. Over 30 cells positive for EmGFP were assessed in six independent experiments. Error bar: mean ±SD. *<i>P</i><0.005, **<i>P</i><0.001. miR-NC denotes negative control miRNA.</p
Stress-Inducible Caspase Substrate TRB3 Promotes Nuclear Translocation of Procaspase-3
<div><p>Pseudokinase TRB3 is a stress-inducible nuclear protein, which has recently been shown to be involved in ER stress-induced apoptosis. However, it remains unclear how TRB3 contributes to the process. We recently demonstrated that TRB3 was cleaved by caspase-3 (CASP3) <em>in vitro</em> and also in apoptosis-induced cells. Thus, we investigate the role of TRB3 cleavage in the apoptotic process to address the above question. Overexpression studies revealed that the cleavage of TRB3 promoted CASP3/7 activation and apoptosis. In contrast, the anti-apoptotic effects were found under TRB3 non-cleavable conditions, such as ER stress, and also when the CASP3/7 activation was enhanced by knockdown of endogenous TRB3 expression. Interestingly, nuclear translocation of procaspase-3 (proCASP3) was observed in cells either overexpressing TRB3 or under tunicamycin-induced ER stress. Although forced cytoplasmic expression of proCASP3 enhanced apoptosis significantly, its nuclear expression did not produce any pro-apoptotic effect, suggesting that nuclear distribution of proCASP3 is not critical for the execution of apoptosis. Thus, TRB3 might prevent cytoplasmic activation of CASP3 by promoting proCASP3 entry into the nucleus, and thereby inhibit apoptosis. Taken together, our results suggest that TRB3, through its own cleavage, functions as a molecular switch between the cell survival and apoptotic pathways under stressful conditions.</p> </div
Cleavage of TRB3 promotes apoptosis along with CASP3 activation.
<p>(A and B) Twenty-four hours after transfection of HeLa (A) and Jurkat (B) cells with the indicated V5-TRB3 expression plasmid or control (ctrl) vector, the cells were treated with TNFα/CHX for 4 hr (HeLa cells) or anti-Fas antibody for 6 hr (Jurkat cells). The resulting dead cells were counted by trypan blue staining. Error bars indicate mean ±SD of three independent experiments. *<i>P</i><0.05, **<i>P</i><0.005, ***<i>P</i><0.001, statistically significant difference. (C and D) Twenty-four hours after transfection with the indicated V5-TRB3 expression plasmid or control vector, HeLa (C) and Jurkat (D) cells were reseeded in 96-well plates (1.0×10<sup>4</sup> cells/well), and then treated with TNFα/CHX and anti-Fas antibody, respectively, for the indicated times and CASP3/7 activity was then measured using the luminometric Caspase-Glo® 3/7 Assay Kit. Each data point represents mean ±SD of three independent experiments.</p
Simple Screening Method for Autoantigen Proteins Using the N-Terminal Biotinylated Protein Library Produced by Wheat Cell-Free Synthesis
Autoimmune diseases are a heterogeneous group of diseases characterized by immune reactions against either a major or a limited number of the bodies own autoantigens, causing inflammation and damage to tissues and organs. Thus, identification of autoantigens is an important first step to understanding autoimmune diseases. Here we demonstrate a simple screening method for identification of autoantigens reacting with patient serum antibodies by combination of an N-terminal biotinylated protein library (BPL), produced using a wheat cell-free protein production system, and a commercially available luminescence system. Optimization studies using well-characterized autoantigens showed specific interactions between N-terminal biotinylated proteins and antibody that were sensitively detected under homogeneous reaction conditions. In this optimized assay, 1 μL of the translation mixture expressing the biotinylated proteins produced significant luminescence signal by addition of diluted serum between 1:500 and 1:10 000 in 25 μL of reaction volume. For the BPL construction, 214 mouse genes, consisting of 103 well-known autoantigens and 111 genes in the mouse autoimmune susceptibility loci, and the sera of MRL/lpr mouse were used as an autoimmune model. By this screening method, 25 well-known autoantigens and 71 proteins in the loci were identified as autoantigen proteins specifically reacting with sera antibodies. Cross-referencing with the Gene Ontology Database, 26 and 38 of autoantigen proteins were predicted to have nuclear localization and identified as membrane and/or extracellular proteins. The immune reaction of six randomly selected proteins was confirmed by immunoprecipitation and/or immunoblot analyses. Interestingly, three autoantigen proteins were recognized by immunoprecipitation but not by immunoblot analysis. These results suggest that the BPL-based method could provide a simple system for screening of autoantigen proteins and would help with identification of autoantigen proteins reacting with antibodies that recognize folded proteins, rather than denatured or unfolded forms
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