Takeshi Murata

5.5k total citations
151 papers, 3.6k citations indexed

About

Takeshi Murata is a scholar working on Molecular Biology, Spectroscopy and Cellular and Molecular Neuroscience. According to data from OpenAlex, Takeshi Murata has authored 151 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 112 papers in Molecular Biology, 23 papers in Spectroscopy and 18 papers in Cellular and Molecular Neuroscience. Recurrent topics in Takeshi Murata's work include ATP Synthase and ATPases Research (52 papers), Mitochondrial Function and Pathology (36 papers) and Receptor Mechanisms and Signaling (22 papers). Takeshi Murata is often cited by papers focused on ATP Synthase and ATPases Research (52 papers), Mitochondrial Function and Pathology (36 papers) and Receptor Mechanisms and Signaling (22 papers). Takeshi Murata collaborates with scholars based in Japan, United Kingdom and United States. Takeshi Murata's co-authors include Ichiro Yamato, Yoshimi Kakinuma, So Iwata, John E. Walker, Seiji Takahashi, Tomoya Hino, Andrew G. W. Leslie, Takuya Kobayashi, Kazuei Igarashi and K. Suzuki and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Takeshi Murata

147 papers receiving 3.5k citations

Peers

Takeshi Murata

SPECT

CMN

RNMI

Robert Aggeler United States

Tatsuro Shimamura Japan

Simon Newstead United Kingdom

José D. Faraldo‐Gómez United States

Carola Hunte Germany

Da‐Neng Wang United States

Jean‐Paul Renaud France

Annette Steward United Kingdom

Hideo Akutsu Japan

Robert Aggeler United States

Takeshi Murata

3.7k ×1.4

236 ×0.4

SPECT

196 ×0.5

CMN

234 ×0.7

RNMI

175 ×0.6

Citations per year, relative to Takeshi Murata Takeshi Murata (= 1×) peers Robert Aggeler

Countries citing papers authored by Takeshi Murata

Since Specialization

Citations

This map shows the geographic impact of Takeshi Murata's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Takeshi Murata with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Takeshi Murata more than expected).

Fields of papers citing papers by Takeshi Murata

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Takeshi Murata. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Takeshi Murata. The network helps show where Takeshi Murata may publish in the future.

Co-authorship network of co-authors of Takeshi Murata

This figure shows the co-authorship network connecting the top 25 collaborators of Takeshi Murata. A scholar is included among the top collaborators of Takeshi Murata based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Takeshi Murata. Takeshi Murata is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Ueno, Hiroshi, et al.. (2025). Engineering of ATP synthase for enhancement of proton-to-ATP ratio. Nature Communications. 16(1). 5410–5410. 2 indexed citations

Shiimura, Yuki, Dohyun Im, Hidetsugu Asada, et al.. (2025). The structure and function of the ghrelin receptor coding for drug actions. Nature Structural & Molecular Biology. 32(3). 531–542. 3 indexed citations

Lee, Yongchan, Chunhuan Jin, Ryuichi Ohgaki, et al.. (2025). Structural basis of anticancer drug recognition and amino acid transport by LAT1. Nature Communications. 16(1). 1635–1635. 10 indexed citations

Adachi, Naruhiko, Toshio Moriya, Satoshi Yasuda, et al.. (2024). Cryo-EM structure of P-glycoprotein bound to triple elacridar inhibitor molecules. Biochemical and Biophysical Research Communications. 709. 149855–149855. 9 indexed citations

Chen, Sisi, Lisa Nagase, Satoshi Yasuda, et al.. (2023). Anti-nanodisc antibodies specifically capture nanodiscs and facilitate molecular interaction kinetics studies for membrane protein. Scientific Reports. 13(1). 11627–11627. 6 indexed citations

Otomo, A., et al.. (2022). Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between V _o and V ₁ motors. Proceedings of the National Academy of Sciences. 119(42). e2210204119–e2210204119. 7 indexed citations

Asada, Hidetsugu, Dohyun Im, Satoshi Yasuda, et al.. (2022). Molecular basis for anti-insomnia drug design from structure of lemborexant-bound orexin 2 receptor. Structure. 30(12). 1582–1589.e4. 11 indexed citations

Haraguchi, Takeshi, K. Suzuki, M. Tominaga, et al.. (2022). Discovery of ultrafast myosin, its amino acid sequence, and structural features. Proceedings of the National Academy of Sciences. 119(8). 13 indexed citations

Kabir, Arif Md. Rashedul, Tomohiko Hayashi, Satoshi Yasuda, et al.. (2022). Controlling the Rigidity of Kinesin-Propelled Microtubules in an In Vitro Gliding Assay Using the Deep-Sea Osmolyte Trimethylamine N-Oxide. ACS Omega. 7(4). 3796–3803. 2 indexed citations

10.

Yasuda, Satoshi, Keiichi Kojima, Tomohiko Hayashi, et al.. (2022). Development of an Outward Proton Pumping Rhodopsin with a New Record in Thermostability by Means of Amino Acid Mutations. The Journal of Physical Chemistry B. 126(5). 1004–1015. 6 indexed citations

11.

Hayashi, Tomohiko, Satoshi Yasuda, K. Suzuki, et al.. (2020). How Does a Microbial Rhodopsin RxR Realize Its Exceptionally High Thermostability with the Proton-Pumping Function Being Retained?. The Journal of Physical Chemistry B. 124(6). 990–1000. 17 indexed citations

12.

Yasuda, Satoshi, et al.. (2019). Analyses based on statistical thermodynamics for large difference between thermophilic rhodopsin and xanthorhodopsin in terms of thermostability. The Journal of Chemical Physics. 150(5). 55101–55101. 9 indexed citations

13.

Suzuki, K., H. Matsunami, K. Mizutani, et al.. (2019). Metastable asymmetrical structure of a shaftless V ₁ motor. Science Advances. 5(1). eaau8149–eaau8149. 11 indexed citations

14.

Yasuda, Satoshi, et al.. (2018). Physical Origin of Thermostabilization by a Quadruple Mutation for the Adenosine A_2a Receptor in the Active State. The Journal of Physical Chemistry B. 122(16). 4418–4427. 8 indexed citations

15.

Suno, Ryoji, Sangbae Lee, Shoji Maeda, et al.. (2018). Structural insights into the subtype-selective antagonist binding to the M2 muscarinic receptor. Nature Chemical Biology. 14(12). 1150–1158. 54 indexed citations

16.

Yasuda, Satoshi, Yosuke Toyoda, Kazushi Morimoto, et al.. (2017). Hot-Spot Residues to be Mutated Common in G Protein-Coupled Receptors of Class A: Identification of Thermostabilizing Mutations Followed by Determination of Three-Dimensional Structures for Two Example Receptors. The Journal of Physical Chemistry B. 121(26). 6341–6350. 25 indexed citations

17.

Alam, Md. Jahangir, Satoshi Arai, Shinya Saijo, et al.. (2013). Loose Binding of the DF Axis with the A3B3 Complex Stimulates the Initial Activity of Enterococcus hirae V1-ATPase. PLoS ONE. 8(9). e74291–e74291. 6 indexed citations

18.

Mizutani, K., K. Suzuki, Ichiro Yamato, et al.. (2011). Structure of the rotor ring modified with N , N ^′ -dicyclohexylcarbodiimide of the Na ⁺ -transporting vacuolar ATPase. Proceedings of the National Academy of Sciences. 108(33). 13474–13479. 35 indexed citations

19.

Murata, Takeshi, Ichiro Yamato, Yoshimi Kakinuma, Andrew G. W. Leslie, & John E. Walker. (2005). Structure of the Rotor of the V-Type Na ⁺ -ATPase from Enterococcus hirae. Science. 308(5722). 654–659. 301 indexed citations

20.

Hibasami, Hiroshige, et al.. (1992). Cepharanthine potentiates the antitumor effect of methylglyoxal bis (cyclopentylamidinohydrazone) on human leukemia cells.. PubMed. 11(4). 1543–7. 5 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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