Search

Your search keyword '"Togashi, S."' showing total 187 results
Start Over Author "Togashi, S."
187 results on '"Togashi, S."'

3. Laser-excited photoemission spectroscopy study of superconducting boron-doped diamond

Author

K. Ishizaka, R. Eguchi, S. Tsuda, T. Kiss, T. Shimojima, T. Yokoya, S. Shin, T. Togashi, S. Watanabe, C.-T. Chen, C.Q. Zhang, Y. Takano, M. Nagao, I. Sakaguchi, T. Takenouchi and H. Kawarada

Subjects
Materials of engineering and construction. Mechanics of materials, TA401-492, Biotechnology, TP248.13-248.65
Abstract

We have investigated the low-energy electronic state of boron-doped diamond thin film by the laser-excited photoemission spectroscopy. A clear Fermi-edge is observed for samples doped above the semiconductor–metal boundary, together with the characteristic structures at 150×n meV possibly due to the strong electron–lattice coupling effect. In addition, for the superconducting sample, we observed a shift of the leading edge below Tc indicative of a superconducting gap opening. We discuss the electron–lattice coupling and the superconductivity in doped diamond.

Published
2006

13. Further characterisation of the 91500 zircon crystal

Author

Wiedenbeck, Michael, Hanchar, John M, Peck, William H., Sylvester, Paul, Valley, John, Whitehouse, M.J., Kronz, Andreas, Morishita, Yuichi, Nasdala, L, Fiebig, J., Franchi, I., Girard, J_P, Greenwood, R C, Hinton, R., Kita, N T, Mason, P.R.D., Norman, Marc, Ogasawara, M., Piccoli, P M, Rhede, D, Satoh, H., Schulz-Dobrick, B, Skår, Ø., Spicuzza, M.J., Terada, K, Tindle, A., Togashi, S., Vennemann, T., Xie, Q., Zheng, Y.-F., Wiedenbeck, Michael, Hanchar, John M, Peck, William H., Sylvester, Paul, Valley, John, Whitehouse, M.J., Kronz, Andreas, Morishita, Yuichi, Nasdala, L, Fiebig, J., Franchi, I., Girard, J_P, Greenwood, R C, Hinton, R., Kita, N T, Mason, P.R.D., Norman, Marc, Ogasawara, M., Piccoli, P M, Rhede, D, Satoh, H., Schulz-Dobrick, B, Skår, Ø., Spicuzza, M.J., Terada, K, Tindle, A., Togashi, S., Vennemann, T., Xie, Q., and Zheng, Y.-F.

Abstract

This paper reports the results from a second characterisation of the 91500 zircon, including data from electron probe microanalysis, laser ablation inductively coupled plasma-mass spectrometry (LA-ICP-MS), secondary ion mass spectrometry (SIMS) and laser

Published
2004

17. Further Characterisation of the 91500 Zircon Crystal

Author

Wiedenbeck, Michael, primary, Hanchar, John M., additional, Peck, William H., additional, Sylvester, Paul, additional, Valley, John, additional, Whitehouse, Martin, additional, Kronz, Andreas, additional, Morishita, Yuichi, additional, Nasdala, Lutz, additional, Fiebig, J., additional, Franchi, I., additional, Girard, J.-P., additional, Greenwood, R.C., additional, Hinton, R., additional, Kita, N., additional, Mason, P.R.D., additional, Norman, M., additional, Ogasawara, M., additional, Piccoli, P.M., additional, Rhede, D., additional, Satoh, H., additional, Schulz-Dobrick, B., additional, Skår, O., additional, Spicuzza, MJ., additional, Terada, K., additional, Tindle, A., additional, Togashi, S., additional, Vennemann, T., additional, Xie, Q., additional, and Zheng, Y.-F., additional

Published
2004
Full Text
View/download PDF

19. Structural identification of the myo-inositol 1,4,5-trisphosphate-binding domain in rat brain inositol 1,4,5-trisphosphate 3-kinase.

Author

Togashi, S, Takazawa, Kazunaga, Endo, T, Erneux, Christophe, Onaya, T, Togashi, S, Takazawa, Kazunaga, Endo, T, Erneux, Christophe, and Onaya, T

Abstract

A series of key amino acids involved in Ins(1,4,5)P3 (InsP3) binding and catalytic activity of rat brain InsP3 3-kinase has been identified. The catalytic domain is at the C-terminal end and restricted to a maximum of 275 amino acids [Takazawa and Erneux (1991) Biochem. J. 280, 125-129]. In this study, newly prepared 5'-deletion and site-directed mutants have been compared both for InsP3 binding and InsP3 3-kinase activity. When the protein was expressed from L259 to R459, the activity was lost but InsP3 binding was conserved. Another deletion mutant that had lost only four amino acids after L259 had lost InsP3 binding, and this finding suggests that these residues (i.e. L259DCK262) are involved in InsP3 binding. To further support the data, we have produced two mutants by site-directed mutagenesis on residues C261 and K262. The two new enzymes were designated M4 (C261S) and M5 (K262A). M4 showed similar Vmax and Km values for InsP3 and ATP to wild-type enzyme. In contrast, M5 was totally inactive but had kept the ability to bind to calmodulin-Sepharose. C-terminal deletion mutants that had lost five, seven or nine amino acids showed a large decrease in InsP3 binding and InsP3 3-kinase activity. One mutant that had lost five amino acids (M2) was purified to apparent homogeneity: Km values for both substrates appeared unchanged but Vmax was decreased approx. 40-fold compared with the wild-type enzyme. The results indicate that (1) a positively charged amino acid residue K262 is essential for InsP3 binding and (2) amino acids at the C-terminal end of the protein are necessary to act as a catalyst in the InsP3 3-kinase reaction., Journal Article, info:eu-repo/semantics/published

Published
1997

32. Newly established cell lines from Drosophila larval CNS express neural specific characteristics.

Author

Ui, Kumiko, Nishihara, Shoko, Sakuma, M., Togashi, S., Ueda, R., Miyata, Y., and Miyake, T.

Abstract

From the central nervous system of Drosophila melanogaster 3rd instar larvae, eight continuous cell lines have been established (named ML-DmBG1 to 8). Using ML-DmBG2, single colony isolation was carried out and six colonial clones were obtained. All reacted to the antibody to horseradish peroxidase, which is a neuronal marker in insects. Acetylcholine, a known neurotransmitter in Drosophila, was detected in three of the colonial clones by high performance liquid chromatography. Therefore, it is concluded that the established colonial clones are neural cells originating in the larval central nervous system. Among them, some variation was observed with respect to morphology, acetylcholine content, and reactivity to anti-HRP. The variation may reflect the heterogeneity of cells composing the central nervous system. [ABSTRACT FROM AUTHOR]

Published
1994
Full Text
View/download PDF

35. Molecular Cloning of a Mouse G-Protein-Activated K+Channel (mGIRK1) and Distinct Distributions of 3 GIRK (GIRK1, 2 and 3) mRNAs in Mouse Brain

Author

Kobayashi, T., Ikeda, K., Ichikawa, T., Abe, S., Togashi, S., and Kumanishi, T.

Abstract

We cloned the mouse brain G-protein-activated K+channel 1 (mGIRK1) cDNA and determined the complete nucleotide and amino acid sequences of the coding region. In in situhybridization using specific oligonucleotide probes, the signals for the three mGIRK (mGIRK1, mGIRK2 and mGIRK3) mRNAs were shown to be distributed widely as well as differently in most brain regions except for the caudate-putamen. Further, at least one, usually several, mGIRK mRNA with variable combinations was observed in most brain regions. These findings suggested that mGIRK channels may be essential in most brain regions in a signal transduction mediated by various G-protein-coupled receptors and that different subunit organizations of the mGIRK channel might occur in different neurons, resulting in diversity of their channel function in vivo.

Published
1995
Full Text
View/download PDF

36. Cortactin associates with the cell-cell junction protein ZO-1 in both Drosophila and mouse.

Author

Katsube, T, Takahisa, M, Ueda, R, Hashimoto, N, Kobayashi, M, and Togashi, S

Abstract

Cortactin is an actin filament-binding protein localizing at cortical regions of cells and a prominent substrate for Src family protein-tyrosine kinases in response to multiple extracellular stimuli. Human cortactin has been identified as a protein product of a putative oncogene, EMS1. In this report, we describe the identification of a Drosophila homolog of cortactin as a molecule that interacts with Drosophila ZO-1 using yeast two-hybrid screening. Drosophila cortactin is a 559-amino acid protein highly expressed in embryos, larvae, and pupae but relatively underexpressed in adult flies. Deletion and substitution mutant analyses revealed that the SH3 domain of Drosophila cortactin binds to a PXXP motif in the proline-rich domain of Drosophila ZO-1. Colocalization of these proteins at cell-cell junction sites was evident under a confocal laser-scanning microscope. In vivo association was confirmed by coimmunoprecipitation of cortactin and ZO-1 from Drosophila embryo lysates. We also demonstrate an association for each of the murine homologs by immunoprecipitation analyses of mouse tissue lysates. Our previous work has demonstrated the involvement of ZO-1 in a signaling pathway that regulates expression of the emc gene in Drosophila. The potential roles of the cortactin.ZO-1 complex in cell adhesion and cell signaling are discussed.

Published
1998

40. Geochemical map of Japan

Author

Imai, N., Terashima, S., Takashi Okai, Kanai, Y., Mikoshiba, M., Ohta, A., Tachibana, Y., Kamioka, H., Togashi, S., and Matsuhisa, Y.

Catalog

Books, media, physical & digital resources
See catalog results