Rchr
J-GLOBAL ID:201701009226284573   Update date: May. 11, 2021

Takahiro Nakayama

ナカヤマタカ ヒロ | Takahiro Nakayama
Affiliation and department:
Job title: Associate Professor
Homepage URL  (2): https://ridb.kanazawa-u.ac.jp/public/detail.php?id=4087https://ridb.kanazawa-u.ac.jp/public/detail_en.php?id=4087
Research field  (2): Molecular biology ,  Biophysics
Research keywords  (1): Single molecule observation, Cell biophysics, Atomic force microscopy
Research theme for competitive and other funds  (8):
  • 2020 - 2021 がん抑制因子p53の凝集の立体構造動態と機能の解明
  • 2017 - 2021 Aβ凝集体の個体間伝播とその 防御に関する研究
  • 2016 - 2019 食品関連の危険因子・防御因子が作用する 認知症の分子標的の解明と予防・治療法の開発
  • 2016 - 2019 高速AFMによるアミロイド脱凝集酵素Hsp104の分子動態の解明
  • 2017 - 2018 脳蛋白凝集の立体構造動態の動画撮影
Show all
Papers (33):
  • Goro Nishide, Keesiang Lim, Mahmoud Shaaban Mohamed, Akiko Kobayashi, Masaharu Hazawa, Takahiro Watanabe-Nakayama, Noriyuki Kodera, Toshio Ando, Richard W. Wong. High-Speed Atomic Force Microscopy Reveals Spatiotemporal Dynamics of Histone Protein H2A Involution by DNA Inchworming. The Journal of Physical Chemistry Letters. 2021. 12. 15. 3837-3846
  • Mingbo Qu, Takahiro Watanabe-Nakayama, Shaopeng Sun, Kenichi Umeda, Xiaoxi Guo, Yuansheng Liu, Toshio Ando, Qing Yang. High-Speed Atomic Force Microscopy Reveals Factors Affecting the Processivity of Chitinases during Interfacial Enzymatic Hydrolysis of Crystalline Chitin. ACS Catalysis. 2020. 10. 22. 13606-13615
  • Mahmoud Shaaban Mohamed, Masaharu Hazawa, Akiko Kobayashi, Laurent Guillaud, Takahiro Watanabe-Nakayama, Mizuho Nakayama, Hanbo Wang, Noriyuki Kodera, Masanobu Oshima, Toshio Ando, et al. Spatiotemporally tracking of nano-biofilaments inside the nuclear pore complex core. Biomaterials. 2020. 256. 120198-120198
  • Takahiro Watanabe-Nakayama, Maika Nawa, Hiroki Konno, Noriyuki Kodera, Toshio Ando, David B Teplow, Kenjiro Ono. Self- and Cross-Seeding on α-Synuclein Fibril Growth Kinetics and Structure Observed by High-Speed Atomic Force Microscopy. ACS nano. 2020. 14. 8. 9979-9989
  • Takahiro Watanabe-Nakayama, Bikash R Sahoo, Ayyalusamy Ramamoorthy, Kenjiro Ono. High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways. International journal of molecular sciences. 2020. 21. 12
more...
MISC (28):
Books (2):
  • Cells, Forces, and the Microenvironment
    CRC Press 2015 ISBN:9789814613361
  • Atomic force microscopy in liquid : biological applications
    Wiley-VCH 2012 ISBN:9783527327584
Lectures and oral presentations  (12):
  • 高速原子間力顕微鏡による医学薬学研究への展開-アミロイド凝集過程とその抑制因子の作用機序の解明を目指して-
    (単一生体分子の動的プロセス評価に向けた高速AFM技術 2020)
  • Do the individual amyloid aggregates follow the prion model?
    (International Symposium on Pathomechanism of Amyloid Diseases 2019)
  • 「高速原子間力顕微鏡の医学・薬学分野への展開と応用」 (アミロイド凝集過程と制御機構の解明方法)
    (MS-NEX発売記念セミナー(株式会社生体分子計測研究所) 2019)
  • Nano-space video imaging of amyloidogenic protein aggregation
    (International Symposium on Pathomechanisms of Amyloid Diseases 2018)
  • Nano-space video imaging reveals structural dynamics of amyloidogenic protein aggregation inhibition by food components
    (The 56th Annual Meeting of the BSJ 2018)
more...
Education (3):
  • 2005 - 2008 Tokyo Institute of Technology Department of Electronic Chemistry
  • 2001 - 2003 Hiroshima University Department of Biological Science
  • 1997 - 2001 Hiroshima University
Professional career (1):
  • Ph.D. (Tokyo Institute of Technology)
Work history (6):
  • 2017/10 - 現在 Nano Life Science Institute, Kanazawa University Associate Professor
  • 2017/04 - 2017/09 Bio-AFM Frontier Research Center, Kanazawa University Associate Professor
  • 2012/04 - 2017/03 Bio-AFM Frontier Research Center, Kanazawa University Assistant Professor
  • 2008/04/01 - 2012/03/31 Tokyo Institute of Technology Postdoctoral Researcher
  • 2004/04/01 - 2005/03/01 Japan Science and Technology Agency
Show all
Association Membership(s) (3):
Biophysical Society ,  日本生物物理学会 ,  日本分子生物学会
※ Researcher’s information displayed in J-GLOBAL is based on the information registered in researchmap. For details, see here.

Return to Previous Page