A first measurement of the interaction cross section of the tau neutrino

The DONuT experiment collected data in 1997 and published first results in 2000 based on four observed $\nu_\tau$ charged-current (CC) interactions. The final analysis of the data collected in the experiment is presented in this paper, based on $3.6 \times 10^{17}$ protons on target using the 800 GeV Tevatron beam at Fermilab. The number of observed $\nu_\tau$ CC interactions is 9, from a total of 578 observed neutrino interactions. We calculated the energy-independent part of the tau-neutrino CC cross section ($\nu + \bar \nu$), relative to the well-known $\nu_e$ and $\nu_\mu$ cross sections. The ratio $\sigma(\nu_\tau)$/$\sigma(\nu_{e,\mu})$ was found to be $1.37\pm0.35\pm0.77$. The $\nu_\tau$ CC cross section was found to be $0.72 \pm 0.24\pm0.36 \times 10^{-38}$ cm$^{2}\rm{GeV}^{-1}$. Both results are in agreement the Standard Model.Comment: 37 pages, 15 figure

第3回先進軽量構造およびリフレクタアンテナに関する国際会議参加報告

application/pdf日本航空宇宙学会誌. 2019, 67 (6), P.228-229journal articl

最適に回収されたスラリーを用いたタングステンCMPの評価

Chemical Mechanical Polishing (CMP) is essential for the manufacturing of recent high-performance electronic device. However, for the CMP process, huge amount of slurry is used, which is to be disposed after being used only once. From the viewpoint of reduction of environmental burdens, this study was made for exploring the possibility of recycling of slurry by focusing on the slurry used for Tungsten CMP. For that purpose, we recovered the slurry used for polishing and then tried to reuse it for polishing again. As a method for evaluation, we made comparisons of removal rates between new slurry and recovered slurry. The results shows that when recovering the slurry during CMP, it contained the water remained on the surface of the polishing pad after dressing, by which slurry was diluted and caused the reduction of removal rate of Tungsten film. However, it was found that when making polishing of Tungsten film using the slurry recovered without being diluted with water, the same level of removal rate as new slurry is obtained.textapplication/pdfdepartmental bulletin pape

Study of Time-Dependent CP Violation in B0→J/ψπ0 Decays

journal articl

図書館と情報部門の統合が図書館活動を如何に変化させたか

application/pdf第17回国立大学図書館協会シンポジウム西地区発表用資料1三重大学情報関連の事務組織と運営組織図書・情報部の業務の変化図書館と情報部門の統合による効果今後の展開conference objec

Interaction of dimeric horse cytochrome c with cyanide ion

We have previously shown that methionine-heme iron coordination is perturbed in domain-swapped dimeric horse cytochrome c. To gain insight into the effect of methionine dissociation in dimeric cytochrome c, we investigated its interaction with cyanide ion. We found that the Soret and Q bands of oxidized dimeric cytochrome c at 406.5 and 529 nm redshift to 413 and 536 nm, respectively, on addition of 1 mM cyanide ion. The binding constant of dimeric cytochrome c and cyanide ion was obtained as 2.5 × 104 M-1. The Fe-CN and C-N stretching (ν Fe-CN and ν CN) resonance Raman bands of CN--bound dimeric cytochrome c were observed at 443 and 2,126 cm-1, respectively. The ν Fe-CN frequency of dimeric cytochrome c was relatively low compared with that of other CN--bound heme proteins, and a relatively strong coupling between the Fe-C-N bending and porphyrin vibrations was observed in the 350-450-cm-1 region. The low ν Fe-CN frequency suggests weaker binding of the cyanide ion to dimeric cytochrome c compared with other heme proteins possessing a distal heme cavity. Although the secondary structure of dimeric cytochrome c did not change on addition of cyanide ion according to circular dichroism measurements, the dimer dissociation rate at 45 °C increased from (8.9 ± 0.7) × 10-6 to (3.8 ± 0.2) × 10-5 s-1, with a decrease of about 2 °C in its dissociation temperature obtained with differential scanning calorimetry. The results show that diatomic ligands may bind to the heme iron of dimeric cytochrome c and affect its stability.journal articl

Mcr-Dependent Phagocytosis of <i>C. albicans</i>

<div><p>(A) Schematic representation of α2M-related proteins. <i>Drosophila</i> Mcr is compared with a close homolog in <i>A. gambiae</i> (Ag Mcr [Tep13]), TepI from both <i>Drosophila</i> and <i>Anopheles</i> and the human homologs CD109, α2M, and C3. Various conserved domains are colored as indicated in the gray box. Numbers correspond to amino acid position. The sequences of the conserved thioester domains are given below the schematic. Dm, <i>Drosophila melanogaster;</i> Ag, <i>Anopheles gambiae;</i> Hs, <i>Homo sapiens</i>.</p> <p>(B) RNAi against SCAR reduces phagocytosis of <i>C. albicans, E. coli,</i> and latex beads (row 2). RNAi against Mcr significantly decreased phagocytosis of only <i>C. albicans</i> (row 3). Cells were stained as in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040004#pbio-0040004-g004" target="_blank">Figure 4</a>C–<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040004#pbio-0040004-g004" target="_blank">4</a>E. Column 1, GFP expressing <i>C. albicans</i>—green, S2 cell DNA—blue, non-phagocytosed <i>C. albicans</i>—red; column 2, GFP-expressing <i>E. coli</i>—green, S2 cell DNA—blue, non-phagocytosed <i>E. coli</i>—red; column 3, latex beads—green, S2 cell DNA—blue, S2 cell actin cytoskeleton—red.</p> <p>(C) dsRNA against both SCAR and Mcr decreases phagocytosis of <i>C. albicans</i>. S2 cells were treated with dsRNA against SCAR and Mcr as described in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040004#s4" target="_blank">Materials and Methods</a> and then co-incubated with <i>C. albicans</i> for the indicated times. The percentage of S2 cells phagocytosing one or more <i>C. albicans</i> was quantified and plotted. The 3.5-h timepoints were analyzed using a <i>t</i>-test assuming unequal variance. Those values that differ significantly from untreated cells (<i>p</i> < 0.01) are indicated by asterisks.</p> <p>(D) Mcr dsRNA does not reduce phagocytosis of <i>E. coli</i>. S2 cells were treated with dsRNA against SCAR and Mcr and then co-incubated with <i>E. coli</i> for the indicated times. The percentage of S2 cells phagocytosing one or more <i>E. coli</i> was quantified and plotted. The 3.5-h timepoints were analyzed using a <i>t</i>-test assuming unequal variance. Those values that differ significantly from untreated cells (<i>p</i> < 0.01) are indicated by asterisks.</p> <p>(E) Mcr dsRNA does not reduce phagocytosis of latex beads. S2 cells were treated with dsRNA against SCAR and Mcr and then co-incubated with green fluorescent latex beads for the indicated times. The percentage of S2 cells phagocytosing one or more latex beads was quantified and plotted. The 3.5-h timepoints were analyzed using a <i>t</i>-test assuming unequal variance. Those values that differ significantly from untreated cells (<i>p</i> < 0.01) are indicated by asterisks.</p> <p>(F) An additional dsRNA against the 3′ UTR of Mcr was generated and tested for disruption of <i>C. albicans</i> phagocytosis. S2 cells were treated with RNAi directed against both the coding region and the 3′ UTR of Mcr and then co-incubated with <i>C. albicans</i> for the indicated times. The percentage of S2 cells phagocytosing one or more <i>C. albicans</i> was quantified and plotted. The 3.5-h timepoints were analyzed using a <i>t</i>-test assuming unequal variance. Those values that differ significantly from untreated cells (<i>p</i> < 0.01) are indicated by asterisks.</p></div

Phagocytosis of <i>C. albicans</i> by <i>Drosophila</i> S2 Cells

<div><p>(A) The <i>Drosophila</i> hemocyte-like S2 cell line phagocytoses <i>C. albicans</i>. S2 cells were co-incubated with GFP expressing <i>C. albicans</i> for the indicated times. Cells were fixed, and the filamentous actin of S2 cells was stained with rhodamine phalloidin and the S2 cell DNA with Hoechst 33258.</p> <p>(B) Quantification of phagocytosis of <i>C. albicans</i> and <i>S. cerevisiae</i> by S2 cells. S2 cells and the indicated fungal strain were co-incubated for various times, and the percentage of S2 cells that had phagocytosed one or more <i>C. albicans</i> was quantified by counting 50–100 S2 cells. The maximum time shown is 3 h, as the levels of phagocytosis did not significantly increase after this timepoint. Results are the average of four experiments, and the error bars indicate the standard deviation. As described in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040004#s4" target="_blank">Materials and Methods</a>, the 3-h results were evaluated for statistical significance using the <i>t</i>-test, assuming unequal variance. As indicated by the asterisks, the values for heat-killed <i>C. albicans</i> and <i>S. cerevisiae</i> were statistically different from that of live <i>C. albicans,</i> with a confidence level <i>p</i> < 0.01.</p></div

Figure 7

<div><p>Genes Identified in the Screen as Being Required for Phagocytosis of <i>C. albicans</i> Were Superimposed onto a <i>Drosophila</i> Genomic Yeast Two-Hybrid Interaction Map</p> <p>Interactions are displayed, and several pathways are outlined. Dark-blue circles indicate genes identified as reduced phagocytosis of <i>C. albicans,</i> with light-blue circles indicating genes present in the two-hybrid map but not identified in the phagocytosis screen. Several functional groups are circled as indicated. This diagram represents only a portion of the complete two-hybrid map [<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040004#pbio-0040004-b035" target="_blank">35</a>], indicating that the genes identified in the phagocytosis screen affect a limited number of cellular processes.</p></div

S2 Cells Secrete Mcr into the Culture Media

<div><p>(A) Mcr is secreted into the culture media. Whole-cell lysates were prepared from S2 cells (lane 1) and compared to Schneider's medium with 2% FBS (lane 2) or Schneider's medium with 2% FBS collected from S2 cells (conditioned media, lane 3) by immunoblotting with an anti-Mcr antibody.</p> <p>(B) RNAi against Mcr depletes Mcr protein from cell lysates and from the conditioned media. Cell lysates and conditioned media were collected from wild-type S2 cells or cells treated with RNAi against Mcr or SCAR and probed by immunoblotting with an anti-Mcr antibody.</p> <p>(C) Conditioned media rescues the phagocytosis defect of Mcr RNAi-treated cells. Wild-type S2 cells or cells treated with RNAi against Mcr or SCAR were plated in new Schneider's medium with 10% FBS or conditioned media with 10% FBS from wild-type S2 cells and incubated with <i>C. albicans</i> for various times. The percentage of S2 cells that had phagocytosed one or more <i>C. albicans</i> was quantified and graphed. A <i>t</i>-test was used to test the statistical significance between wild-type cells in new media versus SCAR- or Mcr RNAi–treated cells in new media and wild-type cells in conditioned media versus SCAR- or Mcr RNAi–treated cells in conditioned media (see <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040004#s4" target="_blank">Materials and Methods</a>). An asterisk indicates comparisons that showed statistically significant differences (<i>p</i> < 0.01). Mcr RNAi–treated cells in wild-type-conditioned media were not significantly different from wild-type cells in conditioned media.</p> <p>(D) Mcr interacts with <i>C. albicans</i> cells. <i>C. albicans</i> was co-incubated either with new media containing 2% FBS or conditioned media containing 2% FBS from wild-type S2 cells for 2 h, washed, and analyzed by immunoblotting with anti-Mcr. Lane 1, S2 cell lysates; lane 2, new media; lane 3, conditioned media; lane 4, <i>C. albicans</i> incubated in new media; lane 5, <i>C. albicans</i> incubated in conditioned media.</p></div