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Hideaki Ogata

  (緒方 英明)

Profile Information

Affiliation
Professor, Graduate School of Science, University of Hyogo
Degree
Ph.D.(Kyoto University)

Researcher number
30795935
ORCID ID
 https://orcid.org/0000-0002-2894-2417
J-GLOBAL ID
201701006048438970
Researcher ID
J-4975-2013
researchmap Member ID
B000274859

Papers

 77
  • Hideaki OGATA
    Nihon Kessho Gakkaishi, 65(4) 220-221, Dec 15, 2023  Peer-reviewedInvitedLead authorCorresponding author
  • Takahiro Sakai, Tsuyoshi Mashima, Naoya Kobayashi, Hideaki Ogata, Lian Duan, Ryo Fujiki, Kowit Hengphasatporn, Taizo Uda, Yasuteru Shigeta, Emi Hifumi, Shun Hirota
    Nature communications, 14(1) 7807-7807, Dec 8, 2023  Peer-reviewed
    Overexpression of antibody light chains in small plasma cell clones can lead to misfolding and aggregation. On the other hand, the formation of amyloid fibrils from antibody light chains is related to amyloidosis. Although aggregation of antibody light chain is an important issue, atomic-level structural examinations of antibody light chain aggregates are sparse. In this study, we present an antibody light chain that maintains an equilibrium between its monomeric and tetrameric states. According to data from X-ray crystallography, thermodynamic and kinetic measurements, as well as theoretical studies, this antibody light chain engages in 3D domain swapping within its variable region. Here, a pair of domain-swapped dimers creates a tetramer through hydrophobic interactions, facilitating the revelation of the domain-swapped structure. The negative cotton effect linked to the β-sheet structure, observed around 215 nm in the circular dichroism (CD) spectrum of the tetrameric variable region, is more pronounced than that of the monomer. This suggests that the monomer contains less β-sheet structures and exhibits greater flexibility than the tetramer in solution. These findings not only clarify the domain-swapped structure of the antibody light chain but also contribute to controlling antibody quality and advancing the development of future molecular recognition agents and drugs.
  • Takeshi Hiromoto, Koji Nishikawa, Seiya Inoue, Hideaki Ogata, Yuta Hori, Katsuhiro Kusaka, Yu Hirano, Kazuo Kurihara, Yasuteru Shigeta, Taro Tamada, Yoshiki Higuchi
    Chemical Science, 14(35) 9306-9315, Sep 21, 2023  Peer-reviewed
    We report the first neutron structure of [NiFe]-hydrogenase in its oxidized state. This study leads to new insights into the oxidized active site and visualization of the protons characteristic of the oxidized enzyme.
  • Ami Kobayashi, Midori Taketa, Keisei Sowa, Kenji Kano, Yoshiki Higuchi, Hideaki Ogata
    IUCrJ, 10(5) 544-554, Sep 1, 2023  Peer-reviewed
    Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the dimethylsulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized.
  • Nipa Chongdar, Patricia Rodríguez-Maciá, Edward J. Reijerse, Wolfgang Lubitz, Hideaki Ogata, James A. Birrell
    Chemical Science, 14(13) 3682-3692, Apr 7, 2023  Peer-reviewedCorresponding author
    Site-directed mutagenesis of the sensory [FeFe] hydrogenase from Thermotoga maritima reveals new insight into how the protein environment tunes the active site properties for its sensory role.

Misc.

 12

Books and Other Publications

 6

Major Presentations

 20

Research Projects

 2