Takashi Hayashi

9.4k total citations
356 papers, 7.9k citations indexed

About

Takashi Hayashi is a scholar working on Materials Chemistry, Molecular Biology and Organic Chemistry. According to data from OpenAlex, Takashi Hayashi has authored 356 papers receiving a total of 7.9k indexed citations (citations by other indexed papers that have themselves been cited), including 157 papers in Materials Chemistry, 132 papers in Molecular Biology and 90 papers in Organic Chemistry. Recurrent topics in Takashi Hayashi's work include Hemoglobin structure and function (80 papers), Porphyrin and Phthalocyanine Chemistry (73 papers) and Ferroelectric and Piezoelectric Materials (47 papers). Takashi Hayashi is often cited by papers focused on Hemoglobin structure and function (80 papers), Porphyrin and Phthalocyanine Chemistry (73 papers) and Ferroelectric and Piezoelectric Materials (47 papers). Takashi Hayashi collaborates with scholars based in Japan, United States and Germany. Takashi Hayashi's co-authors include Koji Oohora, Akira Onoda, Yoshio Hisaeda, Hisanobu Ogoshi, Takashi Matsuo, Kohei Tamao, Yoshihiko Ito, Hideaki Sato, Shin‐ichi Hirano and Yohei Sano and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Chemical Society Reviews.

In The Last Decade

Takashi Hayashi

342 papers receiving 7.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takashi Hayashi Japan 48 3.5k 2.8k 2.2k 1.4k 1.3k 356 7.9k
Chi K. Chang United States 51 5.3k 1.5× 3.1k 1.1× 1.4k 0.6× 2.0k 1.4× 905 0.7× 239 8.5k
John A. Shelnutt United States 56 7.5k 2.2× 3.8k 1.4× 1.8k 0.8× 1.7k 1.3× 1.4k 1.1× 177 10.7k
Kazuki Sada Japan 50 4.1k 1.2× 1.6k 0.6× 3.0k 1.4× 1.8k 1.3× 690 0.5× 280 9.1k
Kenji Wada Japan 43 3.5k 1.0× 854 0.3× 2.0k 0.9× 918 0.7× 1.4k 1.1× 362 7.2k
Stefan Stoll United States 39 3.6k 1.0× 2.1k 0.8× 1.2k 0.6× 1.5k 1.1× 1.1k 0.8× 135 9.9k
Stefan Franzen United States 53 2.6k 0.7× 4.4k 1.6× 591 0.3× 611 0.4× 1.7k 1.3× 214 9.6k
Tohru Koike Japan 46 1.6k 0.5× 4.1k 1.5× 1.7k 0.8× 943 0.7× 348 0.3× 195 8.3k
Masako Kato Japan 50 4.6k 1.3× 1.3k 0.5× 2.5k 1.2× 2.1k 1.6× 2.3k 1.8× 461 11.1k
Steven C. Zimmerman United States 62 3.7k 1.1× 4.7k 1.7× 6.4k 2.9× 1.0k 0.8× 1.2k 1.0× 220 13.5k
Ravindra K. Pandey United States 52 7.5k 2.2× 2.9k 1.0× 1.3k 0.6× 671 0.5× 497 0.4× 269 11.8k

Countries citing papers authored by Takashi Hayashi

Since Specialization
Citations

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

Fields of papers citing papers by Takashi Hayashi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takashi Hayashi

This figure shows the co-authorship network connecting the top 25 collaborators of Takashi Hayashi. A scholar is included among the top collaborators of Takashi 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 Takashi Hayashi. Takashi Hayashi is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Kagawa, Yoshiyuki, et al.. (2024). Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity. Angewandte Chemie International Edition. 63(36). e202403485–e202403485. 6 indexed citations
2.
Kato, Shunsuke, et al.. (2024). Reconstitution of Myoglobin with Iron Porphycene Generates an Artificial Aldoxime Dehydratase with Expanded Catalytic Activities. ACS Catalysis. 14(17). 13081–13087. 8 indexed citations
3.
Oohora, Koji, et al.. (2023). A polyacrylamide gel containing an engineered hexameric hemoprotein as a cross-linking unit toward redox-responsive materials. RSC Advances. 13(49). 34610–34617. 1 indexed citations
4.
5.
Oohora, Koji, et al.. (2022). Focusing on a nickel hydrocorphinoid in a protein matrix: methane generation by methyl-coenzyme M reductase with F430 cofactor and its models. Chemical Society Reviews. 51(5). 1629–1639. 16 indexed citations
6.
Rosier, Bas J. H. M., et al.. (2021). Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA‐Based Recruitment Domains. Angewandte Chemie International Edition. 60(20). 11262–11266. 6 indexed citations
7.
Das, Pradip, Stéphane Le Gac, Bernard Boitrel, et al.. (2021). Functional Myoglobin Model Composed of a Strapped Porphyrin/Cyclodextrin Supramolecular Complex with an Overhanging COOH That Increases O2/CO Binding Selectivity in Aqueous Solution. Inorganic Chemistry. 60(16). 12392–12404. 4 indexed citations
8.
9.
Kato, Shunsuke, et al.. (2020). Directed Evolution of a Cp*RhIII‐Linked Biohybrid Catalyst Based on a Screening Platform with Affinity Purification. ChemBioChem. 22(4). 679–685. 16 indexed citations
10.
Shimizu, Tomoko K., Carlos Romero‐Muñiz, Oleksandr Stetsovych, et al.. (2020). Effect of Molecule–Substrate Interactions on the Adsorption of meso-Dibenzoporphycene Tautomers Studied by Scanning Probe Microscopy and First-Principles Calculations. The Journal of Physical Chemistry C. 124(49). 26759–26768. 8 indexed citations
11.
Oohora, Koji, et al.. (2020). Thermoresponsive Micellar Assembly Constructed from a Hexameric Hemoprotein Modified with Poly(N-isopropylacrylamide) toward an Artificial Light-Harvesting System. Journal of the American Chemical Society. 142(4). 1822–1831. 66 indexed citations
12.
Oohora, Koji, et al.. (2019). Myoglobin Reconstituted with Ni Tetradehydrocorrin as a Methane‐Generating Model of Methyl‐coenzyme M Reductase. Angewandte Chemie. 131(39). 13951–13955. 5 indexed citations
13.
Wytko, Jennifer A., Koji Oohora, Stéphane Campidelli, et al.. (2019). Light triggers molecular shuttling in rotaxanes: control over proximity and charge recombination. Chemical Science. 10(13). 3846–3853. 25 indexed citations
14.
Onoda, Akira, Yuta Tanaka, Koki Matsumoto, et al.. (2018). Bimetallic M/N/C catalysts prepared from π-expanded metal salen precursors toward an efficient oxygen reduction reaction. RSC Advances. 8(6). 2892–2899. 23 indexed citations
15.
Kitagishi, Hiroaki, Takehiro Ohta, Akira Onoda, et al.. (2018). A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochromecoxidase. Chemical Science. 9(7). 1989–1995. 30 indexed citations
16.
Tanaka, Yuta, Akira Onoda, Shin‐ichi Okuoka, et al.. (2018). Nonprecious‐metal Fe/N/C Catalysts Prepared from π‐Expanded Fe Salen Precursors toward an Efficient Oxygen Reduction Reaction. ChemCatChem. 10(4). 653–653. 2 indexed citations
17.
Oohora, Koji, et al.. (2017). Manganese(V) Porphycene Complex Responsible for Inert C–H Bond Hydroxylation in a Myoglobin Matrix. Journal of the American Chemical Society. 139(51). 18460–18463. 65 indexed citations
18.
Oohora, Koji, et al.. (2017). Successive energy transfer within multiple photosensitizers assembled in a hexameric hemoprotein scaffold. Physical Chemistry Chemical Physics. 20(5). 3200–3209. 8 indexed citations
19.
Onoda, Akira, Takayuki Uchihashi, Hiroki Watanabe, et al.. (2017). Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis. Chemical Science. 8(9). 6561–6565. 26 indexed citations
20.
Oohora, Koji & Takashi Hayashi. (2014). Incorporation of Modified and Artificial Cofactors into Naturally Occurring Protein Scaffolds. Methods in molecular biology. 1216. 251–263. 2 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Chi K. Chang Breakdown of academic impact, for papers by John A. Shelnutt Breakdown of academic impact, for papers by Kazuki Sada Breakdown of academic impact, for papers by Kenji Wada Breakdown of academic impact, for papers by Stefan Stoll Breakdown of academic impact, for papers by Stefan Franzen Breakdown of academic impact, for papers by Tohru Koike Breakdown of academic impact, for papers by Masako Kato Breakdown of academic impact, for papers by Steven C. Zimmerman Breakdown of academic impact, for papers by Ravindra K. Pandey
Rankless by CCL
2026