研究者業績

Atsuo Miyazawa

  (宮澤 淳夫)

Profile Information

Affiliation
Professor, Graduate School of Science, University of Hyogo
Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology
Degree
Doctor(Science)(Mar, 1993, Waseda University)

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

External link

Papers

 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, Apr 10, 2024  Peer-reviewed
  • Atsushi Ohma, Kazuki Arihara, Tetsuya Mashio, Yoshiko Ito, Yuri Nishino, Atsuo Miyazawa
    International Journal of Electrochemical Science, 19 100539-100539, Mar 8, 2024  Peer-reviewedLast author
  • Koichiro Oishi, Mayu Nagamori, Yasuhiro Kashino, Hiroshi Sekiguchi, Yuji C. Sasaki, Atsuo Miyazawa, Yuri Nishino
    International Journal of Molecular Sciences, 24(15), Jul 28, 2023  Peer-reviewedCorresponding author
    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, Feb, 2023  Peer-reviewedCorresponding author
    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.
  • Yuri Nishino, Yoshiko Ito, Atsuo Miyazawa
    Kenbikyo, 57(3) 139-144, Dec, 2022  Peer-reviewedInvitedCorresponding author

Misc.

 65

Books and Other Publications

 6

Presentations

 25

Teaching Experience

 7

Professional Memberships

 6

Research Projects

 37

Industrial Property Rights

 1

Academic Activities

 5

Social Activities

 5