Rchr
J-GLOBAL ID:201001034801338144   Update date: Feb. 01, 2024

KEN YOKOYAMA

KEN YOKOYAMA
Research field  (4): Functional biochemistry ,  Biophysics ,  Cell biology ,  Structural biochemistry
Research keywords  (9): sensor protein ,  FoF1 ,  F1 ,  rotary molecular motor ,  ATP synthase ,  CryoEM ,  ATP ,  生体エネルギー ,  V-ATPase
Research theme for competitive and other funds  (23):
  • 2020 - 2023 クライオ電子顕微鏡による V型ATPaseの回転機構の解明
  • 2017 - 2020 Structural analysis for vacuolar type ATPase to reveal molecular mechanism of rotary proton translocation
  • 2015 - 2018 Development of variable-temperature high-speed AFM and its application to temperature-dependent ATPases
  • 2014 - 2018 The interlocked rotation between two rotary molecular motors in ATP synthase VoV1 -The mechanism of intermolecular torque transmission-
  • 2014 - 2016 Measurement of proton pump activity by single molecule of VoV1
Show all
Papers (72):
  • Atsuki Nakano, Jun-Ichi Kishikawa, Kaoru Mitsuoka, Ken Yokoyama. Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase. Nature communications. 2023. 14. 1. 4090-4090
  • Ken Yokoyama. Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?. Frontiers in Molecular Biosciences. 2023. 10
  • Atsuko Nakanishi, Jun-Ichi Kishikawa, Kaoru Mitsuoka, Ken Yokoyama. Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding. The Journal of biological chemistry. 2023. 102884-102884
  • Atsuko Nakanishi, Jun-ichi Kishikawa, Kaoru Mitsuoka, Ken Yokoyama. Structural transition of the ground-state structure to steady-state structures by sequential binding of ATP to V/A-ATPase. 2022
  • Atsuki Nakano, Jun-ichi Kishikawa, Atsuko Nakanishi, Kaoru Mitsuoka, Ken Yokoyama. Structural basis of unisite catalysis of bacterial F0F1-ATPase. PNAS Nexus. 2022. 1. 3
more...
MISC (33):
  • 岸川 淳一, 中西 温子, 横山 謙. クライオ電子顕微鏡による液胞型ATPase(V0V1)の構造解析. 京都産業大学総合学術研究所所報. 2017. 12. 47-52
  • YOKOYAMA Ken, NAKANISHI Atsuko, KISHIKAWA Jun-ichi. Structural Studies of the Vacuolar type ATPase. 2016. 11. 99-104
  • 遠藤愛子, 遠藤愛子, 牧泰史, 吉田秀司, 横山謙, 古池晶. 回転軸の長さを半分にしたF1-ATPaseの回転とATP加水分解素過程との連動. 日本物理学会講演概要集(CD-ROM). 2016. 71. 1
  • BABA Mihori, NAKANISHI Atsuko, KISHIKAWA Jun-ichi, FURUIKE Shou, YOKOYAMA Ken. Rotor function of flagella protein FliJ in A3B3 of V1-ATPase. 生物物理(Web). 2015. 55. Supplement 1-2
  • NAKANISHI Atsuko, KISHIKAWA Jun-ichi, TAMAKOSHI Masatada, FURUIKE Shou, YOKOYAMA Ken. The ingenious structure of central rotor apparatus in VoV1; torque transmission mechanism in the central rotor of VoV1. 生物物理. 2014. 54. Supplement 1-2 (Web)
more...
Books (4):
  • タンパク質の構造解析手法とIn silicoスクリーニングへの応用事例
    技術情報協会 2023 ISBN:9784861049712
  • クライオ電子顕微鏡ハンドブック = Handbook of cryo-electron microscopy
    エヌ・ティー・エス 2023 ISBN:9784860438043
  • 膜タンパク質構造研究
    化学同人 2013 ISBN:9784759815610
  • 非侵襲.可視化技術ハンドブック ー ナノ・バイオ 医療から情報システムまで ー
    NTS 2007 ISBN:9784860431334
Lectures and oral presentations  (26):
  • Structure and Mechanism of V type ATP synthase from Thermus thermophilus.
    (International Symposium “50th anniversary of Thermus thermophilus discovery” 2018)
  • Cryo EM structure of V type ATP synthase from Thermus thermophilus.
    (2018)
  • Cryo EM structure of V type ATP synthase from Thermus thermophilus.
    (2018)
  • Structural analysis of membrane protein complex by cryoEM.
    (2018)
  • ATP合成活性を阻害して寿命伸長をもたらす物質の探索
    (生命科学系学会合同年次大会 2017)
more...
Education (3):
  • - 1991 東京工業大学大学院 総合理工学研究科 生命化学専攻
  • - 1991 Tokyo Institute of Technology Graduate School, Division of Integrated Science and Engineering
  • - 1986 Shizuoka University Faculty of Science
Work history (3):
  • Kyoto Sangyo University Faculty of Life Sciences
  • 科学振興機構 ERATO-ICORP project GL
  • Kanazawa University Faculty of Pharmaceutical Sciences
Committee career (2):
  • - 現在 日本生体エネルギー研究会 常任幹事
  • 科学研究補助金 審査員
Association Membership(s) (3):
日本生物物理学会 ,  日本分子生物学会 ,  日本生化学会
※ Researcher’s information displayed in J-GLOBAL is based on the information registered in researchmap. For details, see here.

Return to Previous Page