原著論文
・NMR detection of hydrogen bond network in a proton pump rhodopsin RxR and its alteration during the cyclic photoreaction
R. Suzuki, T. Nagashima, K. Kojima, R. Hironishi, M. Hirohata, T. Ueta, T. Murata, T. Yamazaki, Y. Sudo, H. Takahashi, J. Am. Chem. Soc., ,in press (2023)

・Structure and role of the linker domain of the iron surface-determinant protein IsdH in heme transportation in Staphylococcus aureus
S. V. Bellido, J. M. M. Caaveiro, K. Morante, T. Sushko, M. Nakakido, S. Nagatoishi, *K. Tsumoto, J. Biol. Chem., 298,101995 (2022), DOI: 10.1016/j.jbc.2022.101995

・Molecular mechanism underlying the increased risk of colorectal cancer metastasis caused by single nucleotide polymorphisms in LI-cadherin gene
A. Yui, D. Kuroda, T. Maruno, M. Nakakido, S. Nagatoishi, S. Uchiyama & *K. Tsumoto, Sci Rep., 13,6493 (2023), DOI: 10.1038/s41598-023-32444-4

・Assessment of anisotropic transmembrane transport coefficient vector of cell-spheroid under inhomogeneous ion concentration distribution fields by electrical impedance tomography
S. Li, D. Kawashima, K. O. Okeyo, T. Murata, *M. Takei, Meas. Sci. Technol., 34, 035701 (2022), DOI: 10.1088/1361-6501/acaa4a

・Structural characterization of proton-pumping rhodopsin lacking a cytoplasmic proton donor residue by X-ray crystallography
K. Suzuki, Mara del Carmen Marin, M. Konno, Reza Bagherzadeh, *T. Murata, and *K. Inoue, J. Biol. Chem., 298,101722 (2022), DOI: 10.1016/j.jbc.2022.101722

・Discovery of the fastest myosin, its amino acid sequence, and structural features
T. Haraguchi, M. Tamanaha, K. Suzuki, K. Yoshimura, T. Imi, M. Tominaga, H. Sakayama, T. Nishiyama, *T. Murata, and *K. Ito, J. Phys. Chem. B., 119,e212096211 (2022), DOI: 10.1073/pnas.2120962119

・Development of an outward proton pumping rhodopsin with a new record in thermostability by means of amino-acid mutations
S. Yasuda, T. Akiyama, K. Kojima, T. Ueta, T. Hayashi, S. Ogasawara, S. Nagatoishi, K. Tsumoto, N. Kunishima, Y. Sudo, *M. Kinoshita, and *T. Murata, J. Phys. Chem. B., 126,1004-1015 (2022), DOI: 10.1021/acs.jpcb.1c08684

・Controlling the rigidity of kinesin-propelled microtubules in an in vitro gliding assay using the deep-sea osmolyte trimethylamine N-oxide
*A. M. R. Kabir, T. Munmun, T. Hayashi, S. Yasuda, A. P. Kimura, M. Kinoshita, T. Murata, K. Sada and *A. Kakugo, ACS Omega , 7,3796-3803 (2022), DOI: 10.1021/acsomega.1c06699

・Structure-based screening combined with computational and biochemical analyses identified the inhibitor targeting the binding of DNA Ligase 1 to UHRF1.
S. Kori, Y. Shibahashi, T. Ekimoto, A. Nishiyama, S. Yoshimi, K. Yamaguchi, S. Nagatoishi, M. Ohta, K. Tsumoto, M. Nakanishi, PA. Defossez, M. Ikeguchi, K. Arita, Bioorg Med Chem. , 52, 116500 (2021), DOI: 10.1016/j.bmc.2021.116500

・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

・Development of biparatopic bispecific antibody possessing tetravalent scFv-Fc capable of binding to ROBO1 expressed in hepatocellular carcinoma cells.
Y. Watanabe, A. Tanabe, T. Hamakubo, S. Nagatoishi, K. Tsumoto, J Biochem. , 170, 307-315 (2021), DOI: 10.1093/jb/mvab049

・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