平成30年度発足 新学術領域研究
発動分子科学

News&Event

研究成果 - C01-2

【原著論文】      【書籍/総説・解説】

原著論文
Cryo-EM structure of K+-bound hERG channel complexed with the blocker astemizole
T. Asai, N. Adachi, T. Moriya, H. Oki, T. Maru, M. Kawasaki, K. Suzuki, S. Chen, R. Ishii, K. Yonemori, S. Igaki, S. Yasuda, S. Ogasawara, T. Senda, *T. Murata, Structure , 29, 203-212 (2021), DOI: 10.1016/j.str.2020.12.007

Measurement of the Intestinal pH in Mice under Various Conditions Reveals Alkalization Induced by Antibiotics
K. Shimizu, I. Seiki, Y. Goto, *T. Murata, Antibiotics , 10, 180 (2021), DOI: 10.3390/antibiotics10020180

Mitochondrial sorting and assembly machinery operates by b-barrel switching
H. Takeda, A. Tsutsumi, T. Nishizawa, C. Lindau, J. V. Busto, L. S. Wenz, L. Ellenrieder, K. Imai, S. P. Straub, W. Mossmann, J. Qiu, Y. Yamamori, K. Tomii, J. Suzuki, T. Murata, Satoshi Ogasawara, O. Nureki, T. Becker, N. Pfanner, N. Wiedemann, M. Kikkawa, *T. Endo, Nature , 590, 163-169 (2021), DOI: 10.1038/s41586-020-03113-7

Crystal structure of an anti-podoplanin antibody bound to a disialylated O-linked glycopeptide
*S. Ogasawara, K. Suzuki, K. Naruchi, S. Nakamura, J. Shimabukuro, N. Tsukahara, M. K. Kaneko, Y. Kato, *T. Murata, Biochem. Biophys. Res. Commun. , 533, 57-63 (2020), DOI: 10.1016/j.bbrc.2020.08.103

Theoretical identification of thermostabilizing amino-acid mutations for G-protein coupled receptors
*T. Murata, S. Yasuda, T. Hayashi, *M. Kinoshita, Biophys. Rev.,12,323-332(2020), DOI: 10.1007/s12551-020-00678-5

Methodology for Further Thermostabilization of an Intrinsically Thermostable Membrane Protein Using Amino Acid Mutations with Its Original Function Being Retained
S. Yasuda, T. Akiyama, S. Nemoto, T. Hayashi, T. Ueta, K. Kojima, T. Tsukamoto, S. Nagatoishi, K. Tsumoto, Y. Sudo, *M. Kinoshita, *T. Murata, J. Chem. Inf. Model., 60, 1709-1716 (2020), DOI: 10.1021/acs.jcim.0c00063

How does a microbial rhodopsin RxR realize its exceptionally high thermostability with the proton-pumping function being retained
T. Hayashi, S. Yasuda, K. Suzuki, T. Akiyama, K. Kanehara, K. Kojima, M. Tanabe, R. Kato, T. Senda, Y. Sudo, *T. Murata, *M. Kinoshita, J. Phys. Chem. B, 124, 990-1000 (2020), DOI: 10.1021/acs.jpcb.9b10700

Elucidation of cosolvent effects thermostabilizing water-soluble and membrane proteins
S. Yasuda, K. Kazama, T. Akiyama, *M. Kinoshita, *T. Murata, J. Mol. Liq., 301, 112403-112411 (2020), DOI: 10.1016/j.molliq.2019.112403

Application of High-Sensitivity UV photoemission Spectroscopy to Examine the Electronic Structure of Thermophilic Rhodopsin
D. Sano, I. Ide, T. Akiyama, Y. Tanaka, Y. Sudo, T. Murata, *H. Ishii, Mol. Cryst. Liq. Cryst., 687, 34-39 (2019), DOI: 10.1080/15421406.2019.1648052

Single-molecule analysis reveals rotational substeps and chemo-mechanical coupling scheme of Enterococcus hirae V1-ATPase
Enterococcus hirae V1-ATPase

T. Iida, Y. Minagawa, H. Ueno, F. Kawai, T. Murata, *R. Iino,
Journal of Biological Chemistry ,29417017-17030 (2019), DOI: 10.1074/jbc.RA119.008947

Analyses based on statistical thermodynamics for large difference between thermophilic rhodopsin and xanthorhodopsin in terms of thermostability
S. Yasuda, T. Hayashi, Y. Kajiwara, *T. Murata, *M. Kinoshita,
J. Chem. Phys., 150 ,055101-13 (2019), DOI: 10.1063/1.5082217

Metastable asymmetrical structure of shaftless V1 motor
S. Maruyama, K. Suzuki, M. Imamura, H. Sasaki, H. Matsunami, K. Mizutani, Y. Saito, F. L. Imai, Y. Ishizuka-Katsura, T. Kimura-Someya, M. Shirouzu, T. Uchihashi, T. Ando, I. Yamato, *T. Murata, Sci. Adv. , 5 ,
eaau8149 (2019) , DOI: 10.1126/sciadv.aau8149

Crystal structure and calcium-induced conformational changes of diacylglycerol kinase α EF-hand domains
D. Takahashi, K. Suzuki, T. Sakamoto, T. Iwamoto, T. Murata, *F. Sakane, Prot. Sci., 1771, 694-706 (2019), DOI: 10.1002/pro.3572

Phospholipid Membrane Fluidity Alters Ligand Binding Activity of a G Protein-Coupled Receptor by Shifting the Conformational Equilibrium
K. Yoshida, *S. Nagatoishi, D. Kuroda, N. Suzuki, T. Murata, *K. Tsumoto, Biochemistry, 58, 504-508 (2019), DOI: 10.1021/acs.biochem.8b01194

Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy
J. Tsunoda, C. Song, F. L. Imai, J. Takagi, H. Ueno, T. Murata, R. Iino, *K. Murata, Sci. Rep.,8, 15632 (2018),
DOI: 10.1038/s41598-018-33977-9

書籍/総説・解説
・“さまざまな役割をもつヒトV-ATPaseの理解に向けて”, 村田武士・鈴木花野, 実験医学, 羊土社, 38, No. 5(増刊), 124-130 (790-796) (2020)

・“サーモフィリックロドプシンとキサントロドプシンの熱安定性の大きな違いに対する統計熱力学的解析”, 安田賢司・林智彦・村田武士・木下正弘, アグリバイオ, 北隆館 ,4, No. 3, 61-67 (2020)

“表面プラズモン共鳴(SPR)法を用いた蛋白質に結合する低分子リガンドスクリーニング”
, 妹尾暁暢, 長門石曉, 津本浩平 , PSSJ Archives, , 13, e096 (2020)

・“サーモフィリックロドプシンの極めて高い熱安定性に関する統計熱力学的解析”, 安田賢司・林智彦・村田武士,実験医学,
羊土社, 38, No. 5(増刊), 124-130 (790-796) (2020)

“Rotational Mechanism Model of the Bacterial V1 Motor Based on Structural and Computational Analyses”
*A. Singharoy, C. Chipot, T. Ekimoto, K. Suzuki, M. Ikeguchi, I. Yamato, *T. Murata, Front. Physiol.,10 , 1-12 (2019), DOI: 10.3389/fphys.2019.00046

“Biophysical Analysis of the Protein-Small Molecule Interactions to Develop Small Molecule Drug Discovery”
S. Nagatoishi, Jose M. M. Caaveiro, *K. Tsumoto, Yakugaku Zasshi,138, 1033-1041 (2018),
DOI: 10.1248/yakushi.17-00211-2

“材料創製を指向したタンパク質相互作用解析”
長門石曉, 中木戸誠, 津本浩平, 高分子,68 , 126-127(2019)

On-rate modulation of cadherin interactions by chemical fragments
A. Senoo, S. Ito, *S. Nagatoishi, Y. Saito, G. Ueno, K. Yoshida, T. Tashima, S. Kudo, S. Sando, *K. Tsumoto, bioRxiv , (2021), DOI: 10.1101/2020.08.30.274647

Back