65 research outputs found

    第2人工島の植物目録

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    Search for the decay KL03γK_L^0 \rightarrow 3\gamma

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    We performed a search for the decay KL03γK_L^0 \rightarrow 3\gamma with the E391a detector at KEK. In the data accumulated in 2005, no event was observed in the signal region. Based on the assumption of KL03γK_L^0 \rightarrow 3\gamma proceeding via parity-violation, we obtained the single event sensitivity to be (3.23±0.14)×108(3.23\pm0.14)\times10^{-8}, and set an upper limit on the branching ratio to be 7.4×1087.4\times10^{-8} at the 90% confidence level. This is a factor of 3.2 improvement compared to the previous results. The results of KL03γK_L^0 \rightarrow 3\gamma proceeding via parity-conservation were also presented in this paper

    Long-lived neutral-kaon flux measurement for the KOTO experiment

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    The KOTO (K0K^0 at Tokai) experiment aims to observe the CP-violating rare decay KLπ0ννˉK_L \rightarrow \pi^0 \nu \bar{\nu} by using a long-lived neutral-kaon beam produced by the 30 GeV proton beam at the Japan Proton Accelerator Research Complex. The KLK_L flux is an essential parameter for the measurement of the branching fraction. Three KLK_L neutral decay modes, KL3π0K_L \rightarrow 3\pi^0, KL2π0K_L \rightarrow 2\pi^0, and KL2γK_L \rightarrow 2\gamma were used to measure the KLK_L flux in the beam line in the 2013 KOTO engineering run. A Monte Carlo simulation was used to estimate the detector acceptance for these decays. Agreement was found between the simulation model and the experimental data, and the remaining systematic uncertainty was estimated at the 1.4\% level. The KLK_L flux was measured as (4.183±0.017stat.±0.059sys.)×107(4.183 \pm 0.017_{\mathrm{stat.}} \pm 0.059_{\mathrm{sys.}}) \times 10^7 KLK_L per 2×10142\times 10^{14} protons on a 66-mm-long Au target.Comment: 27 pages, 16 figures. To be appeared in Progress of Theoretical and Experimental Physic

    Quantitative Mass Spectrometry Analysis Reveals Similar Substrate Consensus Motif for Human Mps1 Kinase and Plk1

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    Background Members of the Mps1 kinase family play an essential and evolutionarily conserved role in the spindle assembly checkpoint (SAC), a surveillance mechanism that ensures accurate chromosome segregation during mitosis. Human Mps1 (hMps1) is highly phosphorylated during mitosis and many phosphorylation sites have been identified. However, the upstream kinases responsible for these phosphorylations are not presently known. Methodology/Principal Findings Here, we identify 29 in vivo phosphorylation sites in hMps1. While in vivo analyses indicate that Aurora B and hMps1 activity are required for mitotic hyper-phosphorylation of hMps1, in vitro kinase assays show that Cdk1, MAPK, Plk1 and hMps1 itself can directly phosphorylate hMps1. Although Aurora B poorly phosphorylates hMps1 in vitro, it positively regulates the localization of Mps1 to kinetochores in vivo. Most importantly, quantitative mass spectrometry analysis demonstrates that at least 12 sites within hMps1 can be attributed to autophosphorylation. Remarkably, these hMps1 autophosphorylation sites closely resemble the consensus motif of Plk1, demonstrating that these two mitotic kinases share a similar substrate consensus. Conclusions/Significance hMps1 kinase is regulated by Aurora B kinase and its autophosphorylation. Analysis on hMps1 autophosphorylation sites demonstrates that hMps1 has a substrate preference similar to Plk1 kinase
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