Tatsuhiko Yagi

3.7k total citations
87 papers, 2.9k citations indexed

About

Tatsuhiko Yagi is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Materials Chemistry. According to data from OpenAlex, Tatsuhiko Yagi has authored 87 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 26 papers in Renewable Energy, Sustainability and the Environment and 18 papers in Materials Chemistry. Recurrent topics in Tatsuhiko Yagi's work include Metalloenzymes and iron-sulfur proteins (25 papers), Photosynthetic Processes and Mechanisms (17 papers) and Electrocatalysts for Energy Conversion (13 papers). Tatsuhiko Yagi is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (25 papers), Photosynthetic Processes and Mechanisms (17 papers) and Electrocatalysts for Energy Conversion (13 papers). Tatsuhiko Yagi collaborates with scholars based in Japan, France and Hungary. Tatsuhiko Yagi's co-authors include Yoshiki Higuchi, Noritake Yasuoka, Hiroo Inokuchi, Keisaku Kimura, Nobuo Tamiya, Kunio Miki, Hideaki Ogata, Katsumi Niki, Kiyofumi MARUYAMA and Masura Honya and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and The Journal of Chemical Physics.

In The Last Decade

Tatsuhiko Yagi

86 papers receiving 2.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tatsuhiko Yagi Japan 31 1.3k 1.0k 674 547 417 87 2.9k
Gerald D. Watt United States 31 1.1k 0.8× 912 0.9× 468 0.7× 379 0.7× 288 0.7× 114 2.9k
Mireille Bruschi France 41 1.3k 1.0× 2.4k 2.4× 767 1.1× 651 1.2× 794 1.9× 147 4.9k
Xiaoxi Chen United States 12 432 0.3× 1.4k 1.4× 438 0.6× 1.0k 1.8× 385 0.9× 19 3.2k
Hans E. M. Christensen Denmark 22 308 0.2× 1.1k 1.1× 414 0.6× 639 1.2× 378 0.9× 79 2.6k
Robert Bartsch United States 32 672 0.5× 2.2k 2.1× 544 0.8× 158 0.3× 117 0.3× 83 2.8k
S. Samar Hasnain United Kingdom 39 750 0.6× 1.4k 1.4× 918 1.4× 187 0.3× 124 0.3× 93 3.5k
Kara L. Bren United States 37 2.3k 1.7× 1.9k 1.9× 1.8k 2.6× 659 1.2× 258 0.6× 101 5.4k
Hendrik A. Heering Netherlands 27 638 0.5× 959 0.9× 914 1.4× 1.9k 3.4× 1.2k 2.9× 45 3.5k
Ole Farver Israel 31 292 0.2× 1.1k 1.1× 363 0.5× 675 1.2× 545 1.3× 92 2.4k
Marie‐Thérèse Giudici‐Orticoni France 31 777 0.6× 965 1.0× 357 0.5× 517 0.9× 201 0.5× 69 2.5k

Countries citing papers authored by Tatsuhiko Yagi

Since Specialization
Citations

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

Fields of papers citing papers by Tatsuhiko Yagi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tatsuhiko Yagi

This figure shows the co-authorship network connecting the top 25 collaborators of Tatsuhiko Yagi. A scholar is included among the top collaborators of Tatsuhiko Yagi 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 Tatsuhiko Yagi. Tatsuhiko Yagi 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.
Tamiya, Nobuo & Tatsuhiko Yagi. (2006). Evolution without divergence. IUBMB Life. 58(5-6). 309–311. 3 indexed citations
2.
Ogata, Hideaki, Nobuhiro Mizuno, Kunio Miki, et al.. (2002). Structural Studies of the Carbon Monoxide Complex of [NiFe]hydrogenase fromDesulfovibriovulgarisMiyazaki F:  Suggestion for the Initial Activation Site for Dihydrogen. Journal of the American Chemical Society. 124(39). 11628–11635. 172 indexed citations
3.
Higuchi, Yoshiki, Hideaki Ogata, Kunio Miki, Noritake Yasuoka, & Tatsuhiko Yagi. (1999). Removal of the bridging ligand atom at the Ni–Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 Å resolution. Structure. 7(5). 549–556. 258 indexed citations
4.
Misaki, S., et al.. (1999). Structure determination of rubredoxin from Desulfovibrio vulgaris Miyazaki F in two crystal forms. Acta Crystallographica Section D Biological Crystallography. 55(2). 408–413. 8 indexed citations
5.
Higuchi, Yoshiki, Tatsuhiko Yagi, & Noritake Yasuoka. (1997). Unusual ligand structure in Ni–Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. Structure. 5(12). 1671–1680. 283 indexed citations
6.
Asso, Marcel, Bruno Guigliarelli, Tatsuhiko Yagi, & Patrick Bertrand. (1992). EPR and redox properties of Desulfovibrio vulgaris Miyazaki hydrogenase: Comparison with the NiFe enzyme from Desulfovibrio gigas. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1122(1). 50–56. 43 indexed citations
7.
Saito, Hiroshi, et al.. (1991). Resonance Raman Active Vibrations of Rubredoxin. Normal Coordinate Analysis of a 423-Atom Model. Bulletin of the Chemical Society of Japan. 64(3). 829–836. 9 indexed citations
8.
Nakagawa, Atsushi, Yoshiki Higuchi, Noritake Yasuoka, Yukiteru Katsube, & Tatsuhiko Yagi. (1990). S-Class Cytochromes c Have a Variety of Folding Patterns: Structure of Cytochrome c-553 from Desulfovibrio vulgaris Determined by the Multi-Wavelength Anomalous Dispersion Method1. The Journal of Biochemistry. 108(5). 701–703. 31 indexed citations
9.
Yagi, Tatsuhiko, et al.. (1989). Amino acid sequence and function of rebredoxin from Desulfovibrio vulgaris Miyazaki. Biochimie. 71(11-12). 1171–1177. 24 indexed citations
10.
Yagi, Tatsuhiko, et al.. (1988). Amino Acid Sequence of Ferredoxin I from Desulfovibrio vulgaris Miyazaki1. The Journal of Biochemistry. 104(2). 196–199. 27 indexed citations
11.
Tabushi, Iwao, Takako Nishiya, Tatsuhiko Yagi, & Hiroo Inokuchi. (1983). Kinetic Study on the Successive Four-Step Reduction of Cyt c3. The Journal of Biochemistry. 94(5). 1375–1385. 20 indexed citations
12.
Evans, Dennis H., et al.. (1980). Reversible voltammetric response for a molecule containing four non-equivalent redox sites with application to cytochrome c3 of Desulfovibrio vulgaris, strain Miyazaki. Journal of Electroanalytical Chemistry. 108(1). 107–115. 83 indexed citations
13.
Ôno, Kazuo, et al.. (1980). Kinetics of cytochrome c3 reduction with hydrogenase: A Mössbauer effect study. The Journal of Chemical Physics. 72(4). 2264–2266. 6 indexed citations
14.
Kimura, Keisaku, Yü̅suke Nakahara, Tatsuhiko Yagi, & Hiroo Inokuchi. (1979). Electrical conduction of hemoprotein in the solid phase: Anhydrous cytochrome c3 film. The Journal of Chemical Physics. 70(7). 3317–3323. 41 indexed citations
15.
Yagi, Tatsuhiko, et al.. (1977). 1-Methoxy-5-Methylphenazinium Methyl Sulfate. The Journal of Biochemistry. 82(5). 1469–1473. 68 indexed citations
16.
Yagi, Tatsuhiko, et al.. (1969). Hydrogenase activity in the dry state. Journal of the American Chemical Society. 91(10). 2801–2801. 29 indexed citations
17.
Yagi, Tatsuhiko, et al.. (1963). Phosphorylations and Phosphonations of Glycerol by Recoil Atoms. Journal of the American Chemical Society. 85(21). 3462–3465. 8 indexed citations
18.
Yagi, Tatsuhiko. (1958). Enzymic oxidation of carbon monoxide. Biochimica et Biophysica Acta. 30(1). 194–195. 56 indexed citations
19.
Ishimoto, Makoto, et al.. (1957). BIOCHEMICAL STUDIES ON SULFATE-REDUCING BACTERIA:VIII. THE FUNCTION OF CYTOCHROME OF SULFATE-REDUCING BACTERIA IN DECOMPOSITION OF FORMATE AND REDUCTION OF SULFUR AND HYDROXYLAMINE. The Journal of Biochemistry. 44(11). 707–714. 6 indexed citations
20.
Ishimoto, Makoto, et al.. (1957). BIOCHEMICAL STUDIES ON SULFATE-REDUCING BACTERIA. The Journal of Biochemistry. 44(11). 707–714. 9 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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