研究者業績

宮澤 淳夫

ミヤザワ アツオ  (Atsuo Miyazawa)

基本情報

所属
兵庫県立大学 大学院理学研究科 教授
(兼任)先端医療工学研究所 教授
地方独立行政法人東京都健康長寿医療センター 老年病態研究チーム 協力研究員
学位
博士(理学)(1993年3月 早稲田大学)

ORCID ID
 https://orcid.org/0000-0003-2763-7389
J-GLOBAL ID
200901007329228471
researchmap会員ID
5000072126

外部リンク

論文

 93
  • Masamitsu Wada, Takeshi Higa, Kaoru Katoh, Nobuko Moritoki, Tomonori Nakai, Yuri Nishino, Atsuo Miyazawa, Shinsuke Shibata, Yoshinobu Mineyuki
    Journal of Plant Research 137 659-667 2024年4月10日  査読有り
  • Atsushi Ohma, Kazuki Arihara, Tetsuya Mashio, Yoshiko Ito, Yuri Nishino, Atsuo Miyazawa
    International Journal of Electrochemical Science 19 100539-100539 2024年3月8日  査読有り最終著者
  • Koichiro Oishi, Mayu Nagamori, Yasuhiro Kashino, Hiroshi Sekiguchi, Yuji C. Sasaki, Atsuo Miyazawa, Yuri Nishino
    International Journal of Molecular Sciences 24(15) 2023年7月28日  査読有り責任著者
    Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that play an important role in signal transduction at the neuromuscular junction (NMJ). Movement of the nAChR extracellular domain following agonist binding induces conformational changes in the extracellular domain, which in turn affects the transmembrane domain and opens the ion channel. It is known that the surrounding environment, such as the presence of specific lipids and proteins, affects nAChR function. Diffracted X-ray tracking (DXT) facilitates measurement of the intermolecular motions of receptors on the cell membranes of living cells, including all the components involved in receptor function. In this study, the intramolecular motion of the extracellular domain of native nAChR proteins in living myotube cells was analyzed using DXT for the first time. We revealed that the motion of the extracellular domain in the presence of an agonist (e.g., carbamylcholine, CCh) was restricted by an antagonist (i.e., alpha-bungarotoxin, BGT).
  • Junichi Shimanuki, Hideto Imai, Yoshiko Ito, Yuri Nishino, Atsuo Miyazawa
    Microscopy 72(1) 60-63 2023年2月  査読有り責任著者
    It is important to understand and control the fine structure of the fuel cell catalyst layer in order to improve the battery characteristics of the fuel cell. A major challenge in observing the microstructure of the catalyst layer by electron microscopy is the visualization of ionomers, which have low contrast and are susceptible to damage by electron beam irradiation. Previous papers have reported transmission electron microscopy (TEM) observations of ionomers neutralized with cesium (Cs) ions. However, this approach involves chemical reactions and indirect visualization of ionomers. In contrast, we have previously revealed the microstructure of ionomers in frozen catalyst inks by cryogenic (cryo) scanning electron microscopy and cryo-TEM. In general, ionomers are basically used under high-temperature and humid conditions while the fuel cell is operating. Therefore, in this study, ultrathin sections prepared from the fuel cell catalyst layer (membrane electrode assemblies) were incubated in a chamber under high-temperature and humid conditions and then rapidly frozen for observation by cryo-TEM. As a result, we succeeded in observing the pore structure of the catalyst layer in the swollen state of the ionomer. The swollen ionomer surrounded and enclosed the Pt/C aggregates and bridged over the pores in the catalyst layer.
  • 西野有里, 伊藤喜子, 宮澤淳夫
    顕微鏡 57(3) 139-144 2022年12月  査読有り招待有り責任著者

MISC

 65

書籍等出版物

 6

講演・口頭発表等

 25

担当経験のある科目(授業)

 7

共同研究・競争的資金等の研究課題

 37

産業財産権

 1

学術貢献活動

 5

社会貢献活動

 5