T. Yano

1.9k total citations
74 papers, 1.5k citations indexed

About

T. Yano is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, T. Yano has authored 74 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 17 papers in Materials Chemistry and 10 papers in Genetics. Recurrent topics in T. Yano's work include RNA and protein synthesis mechanisms (16 papers), Enzyme Structure and Function (15 papers) and Semiconductor materials and devices (9 papers). T. Yano is often cited by papers focused on RNA and protein synthesis mechanisms (16 papers), Enzyme Structure and Function (15 papers) and Semiconductor materials and devices (9 papers). T. Yano collaborates with scholars based in Japan, Canada and United States. T. Yano's co-authors include Hiroyuki Kagamiyama, Shinya Oue, Seiki Kuramitsu, Akihiro Okamoto, E. Tschuikow‐Roux, Jan Niedzielski, Seiji Ishii, Hideyuki Hayashi, Jun Hoseki and Yasuaki Koyama and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

T. Yano

66 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. Yano Japan 20 1.0k 296 190 186 110 74 1.5k
Anne‐Marie Gilles France 29 1.9k 1.9× 676 2.3× 388 2.0× 49 0.3× 37 0.3× 81 2.6k
Georg Zocher Germany 25 1.3k 1.3× 263 0.9× 114 0.6× 47 0.3× 16 0.1× 44 2.0k
Edward J. Meehan United States 19 844 0.8× 413 1.4× 68 0.4× 15 0.1× 78 0.7× 50 1.3k
Marieke G. L. Elferink Netherlands 24 1.1k 1.1× 202 0.7× 319 1.7× 108 0.6× 6 0.1× 43 1.7k
Stefania Brocca Italy 29 2.1k 2.0× 291 1.0× 124 0.7× 87 0.5× 18 0.2× 63 2.6k
K. Gekko Japan 8 797 0.8× 267 0.9× 55 0.3× 52 0.3× 9 0.1× 11 1.3k
Patrick D. Shaw Stewart United Kingdom 16 673 0.7× 488 1.6× 58 0.3× 32 0.2× 14 0.1× 34 1.1k
Peter C. Kahn United States 24 953 0.9× 257 0.9× 102 0.5× 25 0.1× 8 0.1× 45 1.7k
J. Sygusch Canada 31 1.5k 1.4× 658 2.2× 130 0.7× 280 1.5× 10 0.1× 100 2.7k
Noriaki Okimoto Japan 19 742 0.7× 172 0.6× 90 0.5× 9 0.0× 38 0.3× 46 1.2k

Countries citing papers authored by T. Yano

Since Specialization
Citations

This map shows the geographic impact of T. Yano'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 T. Yano with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. Yano more than expected).

Fields of papers citing papers by T. Yano

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. Yano

This figure shows the co-authorship network connecting the top 25 collaborators of T. Yano. A scholar is included among the top collaborators of T. Yano 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 T. Yano. T. Yano 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.
2.
Fukui, Kenji, T. Murakawa, Seiki Baba, Takashi Kumasaka, & T. Yano. (2025). KH–R3H domain cooperation in RNA recognition by the global RNA-binding protein KhpB. Nature Communications. 16(1). 8028–8028.
3.
Fukui, Kenji, Yuki Fujii, & T. Yano. (2024). Identification of a Catalytic Lysine Residue Conserved Among GHKL ATPases: MutL, GyrB, and MORC. Journal of Molecular Biology. 436(10). 168575–168575. 1 indexed citations
4.
5.
Fukui, Kenji, Tatsuya Yamamoto, T. Murakawa, et al.. (2023). Catalytic mechanism of the zinc-dependent MutL endonuclease reaction. Life Science Alliance. 6(10). e202302001–e202302001. 2 indexed citations
6.
Fukui, Kenji, Yuki Fujii, T. Murakawa, et al.. (2022). Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8. Journal of Structural Biology. 214(4). 107904–107904. 1 indexed citations
7.
Murakawa, T., Mamoru Suzuki, Kenji Fukui, et al.. (2022). Serial femtosecond X-ray crystallography of an anaerobically formed catalytic intermediate of copper amine oxidase. Acta Crystallographica Section D Structural Biology. 78(12). 1428–1438. 5 indexed citations
8.
Watanabe, Yasuo, Youichi Suzuki, T. Murakawa, et al.. (2022). Identification of the corticotropin-releasing factor receptor 1 antagonists as inhibitors of Chikungunya virus replication using a Gaussia luciferase–expressing subgenomic replicon. Biochemical and Biophysical Research Communications. 637. 181–188. 2 indexed citations
9.
Fukui, Kenji, Masao Inoue, T. Murakawa, et al.. (2022). Structural and functional insights into the mechanism by which MutS2 recognizes a DNA junction. Structure. 30(7). 973–982.e4. 3 indexed citations
10.
Murakawa, T., Mamoru Suzuki, Toshi Arima, et al.. (2021). Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase. Acta Crystallographica Section F Structural Biology Communications. 77(10). 356–363. 2 indexed citations
11.
Murakawa, T., Kazuo Kurihara, Mitsuo Shoji, et al.. (2020). Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing. Proceedings of the National Academy of Sciences. 117(20). 10818–10824. 10 indexed citations
12.
Murakawa, T., Seiki Baba, Yoshiaki Kawano, et al.. (2018). In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase. Proceedings of the National Academy of Sciences. 116(1). 135–140. 9 indexed citations
13.
Tomoike, Fumiaki, Yasuaki Kimura, Keiko Kuwata, et al.. (2017). A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1). Chemical Communications. 53(81). 11138–11141. 48 indexed citations
14.
Ishii, Seiji, Kenji Fukui, Satoshi Yokoshima, et al.. (2017). High-throughput Screening of Small Molecule Inhibitors of the Streptococcus Quorum-sensing Signal Pathway. Kobe University Repository Kernel (Kobe University). 3 indexed citations
15.
Inoue, Masao, Kenji Fukui, Yuki Fujii, et al.. (2017). The Lon protease-like domain in the bacterial RecA paralog RadA is required for DNA binding and repair. Journal of Biological Chemistry. 292(23). 9801–9814. 12 indexed citations
16.
Tomoike, Fumiaki, Noriko Nakagawa, Kenji Fukui, et al.. (2017). Indispensable residue for uridine binding in the uridine-cytidine kinase family. Biochemistry and Biophysics Reports. 11. 93–98. 14 indexed citations
17.
Ishii, Seiji, et al.. (2010). Crystal Structure of the Peptidase Domain of Streptococcus ComA, a Bifunctional ATP-binding Cassette Transporter Involved in the Quorum-sensing Pathway. Journal of Biological Chemistry. 285(14). 10777–10785. 45 indexed citations
18.
Yano, T., Hiromi Fukamachi, Masahide Yamamoto, & Takeshi Igarashi. (2009). Characterization of L‐cysteine desulfhydrase from Prevotella intermedia. Oral Microbiology and Immunology. 24(6). 485–492. 20 indexed citations
19.
Yano, T., et al.. (2001). Disruption of Thermus thermophilus genes by homologous recombination using a thermostable kanamycin‐resistant marker. FEBS Letters. 506(3). 231–234. 91 indexed citations
20.
Hoseki, Jun, T. Yano, Yasuaki Koyama, Seiki Kuramitsu, & Hiroyuki Kagamiyama. (1999). Directed Evolution of Thermostable Kanamycin-Resistance Gene: A Convenient Selection Marker for Thermus thermophilus. The Journal of Biochemistry. 126(5). 951–956. 136 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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