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288 results on '"Ohmiya Y"'

1. IAFSS agenda 2030 for a fire safe world

Author

McNamee, M, Meacham, B, van Hees, P, Bisby, L, Chow, WK, Coppalle, A, Dobashi, R, Dlugogorski, B, Fahy, R, Fleischmann, C, Floyd, J, Galea, ER, Gollner, M, Hakkarainen, T, Hamins, A, Hu, L, Johnson, P, Karlsson, B, Merci, B, Ohmiya, Y, Rein, G, Trouvé, A, Wang, Y, and Weckman, B

Subjects
Patient Safety, Chemical Engineering, Maritime Engineering, Civil Engineering
Abstract

The International Association of Fire Safety Science (IAFSS) is comprised of members from some 40 countries. This paper presents the Association's thinking, developed by the Management Committee, concerning pressing research needs for the coming 10 years presented as the IAFSS Agenda 2030 for a Fire Safe World. The research needs are couched in terms of two broad Societal Grand Challenges: (1) climate change, resiliency and sustainability and (2) population growth, urbanization and globalization. The two Societal Grand Challenges include significant fire safety components, that lead both individually and collectively to the need for a number of fire safety and engineering research activities and actions. The IAFSS has identified a list of areas of research and actions in response to these challenges. The list is not exhaustive, and actions within actions could be defined, but this paper does not attempt to cover all future needs.

Published
2019

10. Present Status of the CYRIC Accelerator Facility

Author

Wakui, T., Shinozuka, T., Shimada, K., Shimbara, Y., Sakemi, Y., Itoh, M., Kawamura, H., Inoue, T., Ohmiya, Y., Takahashi, N., Takahashi, K., Suzuki, J., and Homma, T.

Published
2013

12. New Beam Transport System at CYRIC

Author

Terakawa, A., Misu, T., Itoh, K., Suzuki, H., Orihara, H., Chiba, S., Ohmiya, Y., Takahashi, N., Kan, S., Fujita, M., and Shinozuka, T.

Published
2002

14. A transcriptional timetable of autumn senescence

Author

Andersson, A., Keskitalo, J., Andreas Sjödin, Bhalerao, R., Sterky, F., Wissel, K., Tandre, K., Aspeborg, H., Moyle, R., Ohmiya, Y., Brunner, A., Gustafsson, P., Karlsson, J., Lundeberg, J., Nilsson, O., Sandberg, G., Strauss, S., Sundberg, B., Uhlen, M., Jansson, S., and Nilsson, P.

Subjects
Chronobiology Phenomena, Expressed Sequence Tags, Aging, DNA, Complementary, Cell Death, DNA, Plant, Transcription, Genetic, Gene Expression Profiling, Research, Sequence Analysis, DNA, Plant Leaves, Populus, Gene Expression Regulation, Plant, RNA, Plant, Seasons, Gene Library, Oligonucleotide Array Sequence Analysis
Abstract

A microarray has been created from 36,354 ESTs from Populus species and used to study autumn senescence in the leaves of the aspen tree Populus tremula., Background We have developed genomic tools to allow the genus Populus (aspens and cottonwoods) to be exploited as a full-featured model for investigating fundamental aspects of tree biology. We have undertaken large-scale expressed sequence tag (EST) sequencing programs and created Populus microarrays with significant gene coverage. One of the important aspects of plant biology that cannot be studied in annual plants is the gene activity involved in the induction of autumn leaf senescence. Results On the basis of 36,354 Populus ESTs, obtained from seven cDNA libraries, we have created a DNA microarray consisting of 13,490 clones, spotted in duplicate. Of these clones, 12,376 (92%) were confirmed by resequencing and all sequences were annotated and functionally classified. Here we have used the microarray to study transcript abundance in leaves of a free-growing aspen tree (Populus tremula) in northern Sweden during natural autumn senescence. Of the 13,490 spotted clones, 3,792 represented genes with significant expression in all leaf samples from the seven studied dates. Conclusions We observed a major shift in gene expression, coinciding with massive chlorophyll degradation, that reflected a shift from photosynthetic competence to energy generation by mitochondrial respiration, oxidation of fatty acids and nutrient mobilization. Autumn senescence had much in common with senescence in annual plants; for example many proteases were induced. We also found evidence for increased transcriptional activity before the appearance of visible signs of senescence, presumably preparing the leaf for degradation of its components.

Published
2003

37. Structural evolution of luciferase activity in Zophobasmealworm AMP/CoA-ligase (protoluciferase) through site-directed mutagenesis of the luciferin binding site.

Author

Prado, R. A., Barbosa, J. A., Ohmiya, Y., and Viviani, V. R.

Subjects
LUCIFERASES, MEAL worms, BINDING sites, BIOLUMINESCENCE, MUTAGENESIS, BEETLES
Abstract

The structural origin and evolution of bioluminescent activity of beetle luciferases from AMP/CoA ligases remains a mystery. Previously we cloned the luciferase-like enzyme from Zophobas moriomealworm, a reasonable protoluciferase model that could shine light on this mystery. Kinetic characterization and studies with d- and l-luciferin and their adenylates showed that stereoselectivity constitutes a critical feature for the origin of luciferase activity in AMP/CoA ligases. Comparison of the primary structures and modeling studies of this protoluciferase and the three main families of beetle luciferases showed that the carboxylic acid substrate binding site of this enzyme is smaller and more hydrophobic than the luciferin binding site of beetle luciferases, showing several substitutions of otherwise conserved residues. Thus, here we performed a site-directed mutagenesis survey of the carboxylic binding site motifs of the protoluciferase by replacing their residues by the respective conserved ones found in beetle luciferases in order to identify the structural determinants of luciferase/oxygenase activity. Although most of the substitutions had negative impact on the luminescence activity of the protoluciferase, only the substitution I327T improved the luminescence activity, resulting in a broad and 15 nm blue-shifted luminescence spectrum. Such substitution indicates the importance of the loop motif 322YGMSEI327 (341YGLTETT347 in Photinus pyralisluciferase) for luciferase activity, and indicates a possible route for the evolution of bioluminescence function of beetle luciferases. [ABSTRACT FROM AUTHOR]

Published
2011
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41. Agrobacterium tumefaciens-mediated transformation of embryogenic tissue and transgenic plant regeneration in Chamaecyparis obtusaSieb. et Zucc.

Author

Taniguchi, T., Kurita, M., Ohmiya, Y., and Kondo, T.

Abstract

A genetic transformation procedure for Chamaecyparis obtusawas developed after co-cultivation of embryogenic tissues with disarmed Agrobacterium tumefaciensstrain C58/pMP90, which harbours the sgfp(synthetic green fluorescent protein) visual reporter and nptII(neomycin phoshotransferase II) selectable marker genes. The highest transformation frequency was 22.5 independent transformed lines per dish (250 mg embryogenic tissue) following selection on kanamycin medium. Transgenic plantlets were regenerated through the maturation and germination of somatic embryos. The intensity of GFP fluorescence, observed under a fluorescence microscope, varied from very faint to relatively strong, depending on the transgenic line or part of the transgenic plant. The integration of the genes into the genome of regenerated plantlets was confirmed by Southern blot analysis.

Published
2005
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42. Purification and properties of wall-bound endo-1, 4-beta-glucanase from suspension-cultured poplar cells.

Author

Ohmiya, Y, Takeda, T, Nakamura, S, Sakai, F, and Hayashi, T

Abstract

A wall-bound endo-1, 4-beta-glucanase (EC 3.2.1.4) was obtained from a preparation of the cell walls of suspension-cultured poplar cells and purified to electrophoretic homogeneity by cation-exchange, hydrophobic, and gel-filtration chromatography. The molecular mass was estimated to be 47 kDa by SDS-PAGE and 48 kDa by gel filtration on Superdex 200 pg. The isoelectric point (pI) was 5.6. The purified enzyme catalyzed the endo-hydrolysis of carboxymethylcellulose with an optimal pH of 6.5, a Km of 1.2 mg ml-1, and a Vmax of 280 units. The purified enzyme specifically hydrolyzed the 1, 4-beta-glucosyl linkages of carboxymethylcellulose, phospho-swollen cellulose, lichenan, xylan and xyloglucan. The activity of the enzyme was strongly stimulated by cysteine-HCl. The N-terminal sequence of the enzyme was similar to that of an extracellular endo-1, 4-beta-glucanase found in suspension cultures of poplar cells and some homology was recognized to avocado fruit-ripening and bean abscission endo-1, 4-beta-glucanases.

Published
1995

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