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31 results on '"Fukuda, Takako"'

4. Alternative atrategy for driving voltage-oscillator in neocortex of rats

Author

Fukuda, Takako, Tominaga, Takashi, Tominaga, Yoko, Kanayama, Hiroyuki, Kato, Nobuo, and Yoshimura, Hiroshi

Subjects
Signal propagation, optical recording, visual cortex, oscillation, voltage-oscillator, caffeine
Abstract

Information integration in the brain requires functional connectivity between local neural networks. Here, we investigated the interregional coupling mechanism from the viewpoint of oscillations using optical recording methods. Low-frequency electrical stimulation of rat neocortical slices in a caffeine-containing medium induced oscillatory activity between the primary visual cortex (Oc1) and medial secondary visual cortex (Oc2M), in which the oscillation generator was located in the Oc2M and was triggered by a feedforward signal. During to-and-fro oscillatory activity, neural excitation was marked in layer II/III. When the upper layer was disrupted between Oc1 and Oc2M, feedforward signals could propagate through the deep layer and switch on the oscillator in the Oc2M. When the lower layer was disrupted between Oc1 and Oc2M, feedforward signals could propagate through the upper layer and switch on the oscillator in the Oc2M. In the backward direction, neither the upper layer cut nor the lower layer cut disrupted the propagation of the oscillations. In all cases, the horizontal and vertical pathways were used as needed. Fluctuations in the oscillatory waveforms of the local field potential at the upper and lower layers in the Oc2M were reversed, suggesting that the oscillation originated between the two layers. Thus, the neocortex may work as a safety device for interregional communications in an alternative way to drive voltage oscillators in the neocortex.

Published
2023

12. The OPERA film: New nuclear emulsion for large-scale, high-precision experiments

Author

Nakamura, Taku, Ariga, A., Ban, T., Fukuda, Takako, Fukuda, Tutomu, Fujioka, T., Furukawa, T., Hamada, K., Hayashi, H., Hiramatsu, S., Hoshino, K., Kawada, J., Koike, N., Komatsu, M., Matsuoka, H., Miyamoto, S., Miyanishi, K., Miyanishi, M., Morishima, K., Nada, H., Naganawa, N., Nakano, T., Narita, K., Natsume, M., Niwa, K., Nonaka, N., Park, B.D., Sato, O., Takahashi, S., Toshito, T., Uetake, T., Nakamura, M., Kuwabara, K., Nishiyama, S., Nonoyama, Y., and Kodama, K.

Published
2006
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14. Cover Image

Author

Ohara, Ayako, primary, Yamada, Fumihiro, additional, Fukuda, Takako, additional, Suzuki, Noriyuki, additional, and Sumida, Kayo, additional

Published
2018
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16. Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2

Author

Prak, Krisna, Mikami, Bunzo, Itoh, Takafumi, Fukuda, Takako, Maruyama, Nobuyuki, and Utsumi, Shigeru

Subjects
A1bB2, homohexamer structure, Crystallization Communications, fungi, Mutation, Soybean Proteins, food and beverages, glycinin, Globulins, Soybeans, soybean, Crystallization, Crystallography, X-Ray
Abstract

Soybean mature glycinin was purified and crystallized and its preliminary crystallographic analysis is also reported., Glycinin is one of the most abundant storage-protein molecules in soybean seeds and is composed of five subunits (A1aB1b, A1bB2, A2B1a, A3B4 and A5A4B3). A1bB2 was purified from a mutant soybean cultivar containing glycinin composed of only A5A4B3 and A1bB2. At 281 K the protein formed hexagonal, rectangular and rod-shaped crystals in the first [0.1 M imidazole pH 8.0, 0.2 M MgCl2, 35%(v/v) MPD], second [0.1 M sodium citrate pH 5.6, 0.2 M ammonium acetate, 30%(v/v) MPD] and third (0.1 M phosphate–citrate pH 4.2, 2.0 M ammonium sulfate) crystallization conditions, respectively. X-ray diffraction data were collected to resolutions of 1.85, 1.85 and 2.5 Å from crystals of the three different shapes. The crystals belonged to space groups P6322, P21 and P1, with unit-cell parameters a = b = 143.60, c = 84.54 Å, a = 114.54, b = 105.82, c = 116.67 Å, β = 94.99° and a = 94.45, b = 94.96, c = 100.66 Å, α = 107.02, β = 108.44, γ = 110.71°, respectively. One, six and six subunits of A1bB2 were estimated to be present in the respective asymmetric units. The three-dimensional structure of the A1bB2 hexamer is currently being determined.

Published
2013

29. Cloning of cDNA encoding a soybean allergen, Gly m Bd 28K

Author

Tsuji, Hideaki, primary, Hiemori, Miki, additional, Kimoto, Masumi, additional, Yamashita, Hiromi, additional, Kobatake, Ryoko, additional, Adachi, Motoyasu, additional, Fukuda, Takako, additional, Bando, Noriko, additional, Okita, Misako, additional, and Utsumi, Shigeru, additional

Published
2001
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30. Letter to the Editor.

Author

Sumida, Kayo, Fukuda, Takako, Kawamoto, Kensuke, Asano, Hiroyuki, and Sogame, Yoshihisa

Subjects
*ACETAMINOPHEN, *LABORATORY rats
Abstract

A letter to the editor is presented in resaposne to an article about a cross-omics analysis of acetaminophen-induced hepatotoxicity in rat liver.

Published
2015
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31. Characterization and crystallography of recombinant 7S globulins of Adzuki bean and structure-function relationships with 7S globulins of various crops.

Author

Fukuda T, Maruyama N, Salleh MR, Mikami B, and Utsumi S

Subjects
Amino Acid Sequence, Antigens, Plant, Chemical Phenomena, Chemistry, Physical, Crystallization, DNA, Complementary genetics, Escherichia coli genetics, Fabaceae genetics, Models, Molecular, Molecular Sequence Data, Recombinant Proteins chemistry, Seed Storage Proteins, Soybean Proteins chemistry, Structure-Activity Relationship, Fabaceae chemistry, Globulins chemistry, Plant Proteins chemistry
Abstract

The recombinant proteins Adzuki 7S1, Adzuki 7S2, and Adzuki 7S3 were prepared through the Escherichia coli expression systems of three kinds of adzuki bean cDNAs. The recombinant proteins exhibited intrinsic thermal stabilities, surface hydrophobicities, and solubilities, although the homology of their amino acid sequences ranged from 95-98%. To understand why these individual proteins exhibited different properties, their three-dimensional structures were elucidated. The three proteins were successfully crystallized, and the three-dimensional structures of Adzuki 7S1 and Adzuki 7S3 were determined. The properties and structures of these two proteins were comprehensively compared with those of recombinant 7S globulins (soybean beta-conglycinins beta and alpha'c and mungbean 8Salpha) reported previously. It was likely that cavity sizes, hydrogen bonds, salt bridges, hydrophobic interactions, and lengths of loops determine the thermal stabilities of 7S globulins, and results indicated that cavity sizes strongly contribute to such stability. Surface hydrophobicity was also found to be determined not only by distributions of hydrophobic residues on the molecular surface. Furthermore, solubility at neutral and weak alkaline pH values at mu = 0.08 was found to be dominantly influenced by the electrostatic surface potentials.

Published
2008
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