Tomohiko Hayashi

962 total citations
63 papers, 737 citations indexed

About

Tomohiko Hayashi is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Tomohiko Hayashi has authored 63 papers receiving a total of 737 indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 21 papers in Materials Chemistry and 11 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Tomohiko Hayashi's work include Protein Structure and Dynamics (23 papers), Spectroscopy and Quantum Chemical Studies (9 papers) and Enzyme Structure and Function (8 papers). Tomohiko Hayashi is often cited by papers focused on Protein Structure and Dynamics (23 papers), Spectroscopy and Quantum Chemical Studies (9 papers) and Enzyme Structure and Function (8 papers). Tomohiko Hayashi collaborates with scholars based in Japan, United States and Italy. Tomohiko Hayashi's co-authors include Masahiro Kinoshita, Hiraku Oshima, Satoshi Yasuda, Masato Katahira, Takashi Nagata, Ichiro Yamanaka, Mitsunori Ikeguchi, Masao Inoue, Tsukasa Mashima and Ryoichi Kanega and has published in prestigious journals such as Nucleic Acids Research, The Journal of Chemical Physics and The Journal of Physical Chemistry B.

In The Last Decade

Tomohiko Hayashi

61 papers receiving 726 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Tomohiko Hayashi Japan	17	361	129	99	91	84	63	737
Yu Xie China	15	250 0.7×	319 2.5×	66 0.7×	29 0.3×	85 1.0×	34	661
Ruihua Zhang China	14	122 0.3×	268 2.1×	140 1.4×	98 1.1×	143 1.7×	45	805
Ilan Pri‐Bar Israel	20	237 0.7×	234 1.8×	98 1.0×	35 0.4×	47 0.6×	43	1.0k
Kurt A. Kistler United States	18	419 1.2×	191 1.5×	71 0.7×	333 3.7×	167 2.0×	24	1.3k
Shane Z. Sullivan United States	14	67 0.2×	63 0.5×	103 1.0×	60 0.7×	50 0.6×	31	465
Miriam Unger Germany	16	88 0.2×	129 1.0×	174 1.8×	47 0.5×	84 1.0×	38	758
Adrian H. Kopf Netherlands	12	216 0.6×	130 1.0×	91 0.9×	61 0.7×	31 0.4×	12	535
Yufeng Shen United States	8	164 0.5×	329 2.6×	480 4.8×	41 0.5×	83 1.0×	9	1.0k
Hyejin Chang South Korea	20	382 1.1×	450 3.5×	526 5.3×	19 0.2×	99 1.2×	50	1.4k
Shukichi Tanaka Japan	18	75 0.2×	205 1.6×	181 1.8×	184 2.0×	263 3.1×	90	1.1k

Countries citing papers authored by Tomohiko Hayashi

Since Specialization

Citations

This map shows the geographic impact of Tomohiko Hayashi'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 Tomohiko Hayashi with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Tomohiko Hayashi more than expected).

Fields of papers citing papers by Tomohiko Hayashi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Tomohiko Hayashi. 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 Tomohiko Hayashi. The network helps show where Tomohiko Hayashi may publish in the future.

Co-authorship network of co-authors of Tomohiko Hayashi

This figure shows the co-authorship network connecting the top 25 collaborators of Tomohiko Hayashi. A scholar is included among the top collaborators of Tomohiko Hayashi 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 Tomohiko Hayashi. Tomohiko Hayashi 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

Lin, Peng, Tomohiko Hayashi, Huyen Dinh, et al.. (2025). Enzyme Reactions Are Accelerated or Decelerated When the Enzymes Are Located Near the DNA Nanostructure. ACS Applied Materials & Interfaces. 17(10). 15775–15792. 1 indexed citations

Hayashi, Tomohiko, Satoshi Yasuda, Minoru Katō, et al.. (2024). Statistical-Mechanics Analyses on Thermodynamics of Protein Folding Constructed by Privalov and Co-Workers. The Journal of Physical Chemistry B. 128(41). 10110–10125.

Yasuda, Satoshi, Shingo Sato, Sisi Chen, et al.. (2022). A methodology for creating thermostabilized mutants of G‐protein coupled receptors by combining statistical thermodynamics and evolutionary molecular engineering. Protein Science. 31(9). 2 indexed citations

Yasuda, Satoshi, Rinshi S. Kasai, Ryosuke Nakano, et al.. (2022). A methodology for creating mutants of G‐protein coupled receptors stabilized in active state by combining statistical thermodynamics and evolutionary molecular engineering. Protein Science. 31(10). e4425–e4425. 2 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

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

Yasuda, Satoshi, Tomohiko Hayashi, Keiichi Kojima, et al.. (2020). Methodology for Further Thermostabilization of an Intrinsically Thermostable Membrane Protein Using Amino Acid Mutations with Its Original Function Being Retained. Journal of Chemical Information and Modeling. 60(3). 1709–1716. 6 indexed citations

Inoue, Masao, et al.. (2020). Hydration properties of a protein at low and high pressures: Physics of pressure denaturation. The Journal of Chemical Physics. 152(6). 65103–65103. 14 indexed citations

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

10.

Yamada, Tatsuya, Tomohiko Hayashi, Naohiro Kobayashi, et al.. (2019). How Does the Recently Discovered Peptide MIP Exhibit Much Higher Binding Affinity than an Anticancer Protein p53 for an Oncoprotein MDM2?. Journal of Chemical Information and Modeling. 59(8). 3533–3544. 8 indexed citations

11.

Hayashi, Tomohiko, et al.. (2019). An accurate and rapid method for calculating hydration free energies of a variety of solutes including proteins. The Journal of Chemical Physics. 150(17). 175101–175101. 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.

Hayashi, Tomohiko, Masao Inoue, Satoshi Yasuda, et al.. (2018). Universal effects of solvent species on the stabilized structure of a protein. The Journal of Chemical Physics. 149(4). 15 indexed citations

14.

Hayashi, Tomohiko, et al.. (2018). Mechanism of protein–RNA recognition: analysis based on the statistical mechanics of hydration. Physical Chemistry Chemical Physics. 20(14). 9167–9180. 10 indexed citations

15.

Hayashi, Tomohiko, et al.. (2018). Statistical thermodynamics for the unexpectedly large difference between disaccharide stereoisomers in terms of solubility in water. Physical Chemistry Chemical Physics. 20(36). 23684–23693. 7 indexed citations

16.

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

17.

Hayashi, Tomohiko, et al.. (2017). Effects of salt or cosolvent addition on solubility of a hydrophobic solute in water: Relevance to those on thermal stability of a protein. The Journal of Chemical Physics. 146(5). 55102–55102. 21 indexed citations

18.

Kinoshita, Masahiro & Tomohiko Hayashi. (2017). Unified elucidation of the entropy-driven and -opposed hydrophobic effects. Physical Chemistry Chemical Physics. 19(38). 25891–25904. 20 indexed citations

19.

Hayashi, Tomohiko, Satoshi Yasuda, Tatjana Škrbić, Achille Giacometti, & Masahiro Kinoshita. (2017). Unraveling protein folding mechanism by analyzing the hierarchy of models with increasing level of detail. The Journal of Chemical Physics. 147(12). 125102–125102. 16 indexed citations

20.

Oshima, Hiraku, et al.. (2015). On the physics of thermal-stability changes upon mutations of a protein. The Journal of Chemical Physics. 143(12). 125102–125102. 13 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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