Tohru Terada

3.7k total citations
134 papers, 2.6k citations indexed

About

Tohru Terada is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Tohru Terada has authored 134 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 101 papers in Molecular Biology, 29 papers in Materials Chemistry and 14 papers in Spectroscopy. Recurrent topics in Tohru Terada's work include Protein Structure and Dynamics (39 papers), Enzyme Structure and Function (27 papers) and RNA and protein synthesis mechanisms (19 papers). Tohru Terada is often cited by papers focused on Protein Structure and Dynamics (39 papers), Enzyme Structure and Function (27 papers) and RNA and protein synthesis mechanisms (19 papers). Tohru Terada collaborates with scholars based in Japan, United States and United Kingdom. Tohru Terada's co-authors include Kentaro Shimizu, Akinori Kidera, Kei Moritsugu, Yutaka Ito, Shugo Nakamura, Shigeyuki Yokoyama, Mikako Shirouzu, Daisuke Satoh, Ernest D. Laue and Takehiko Shibata and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Tohru Terada

131 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tohru Terada Japan 29 1.9k 459 248 216 177 134 2.6k
Edwin Pozharski United States 29 2.2k 1.2× 597 1.3× 164 0.7× 144 0.7× 166 0.9× 71 2.9k
Kaare Teilum Denmark 30 2.3k 1.2× 858 1.9× 492 2.0× 143 0.7× 179 1.0× 73 3.1k
Patrick L. Wintrode United States 28 2.0k 1.1× 636 1.4× 355 1.4× 144 0.7× 185 1.0× 67 2.7k
Radka Svobodová Vařeková Czechia 19 2.3k 1.2× 547 1.2× 214 0.9× 65 0.3× 212 1.2× 69 3.4k
Steve W. Lockless United States 20 2.8k 1.5× 428 0.9× 186 0.8× 90 0.4× 361 2.0× 26 3.3k
José Luis R. Arrondo Spain 22 1.8k 1.0× 314 0.7× 206 0.8× 82 0.4× 144 0.8× 44 2.7k
Luciano A. Abriata Switzerland 28 1.7k 0.9× 349 0.8× 107 0.4× 186 0.9× 186 1.1× 93 2.7k
Austin B. Yongye United States 17 1.5k 0.8× 329 0.7× 187 0.8× 127 0.6× 63 0.4× 30 2.5k
William E. Meador United States 14 1.9k 1.0× 821 1.8× 332 1.3× 71 0.3× 132 0.7× 29 2.6k

Countries citing papers authored by Tohru Terada

Since Specialization
Citations

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

Fields of papers citing papers by Tohru Terada

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tohru Terada

This figure shows the co-authorship network connecting the top 25 collaborators of Tohru Terada. A scholar is included among the top collaborators of Tohru Terada 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 Tohru Terada. Tohru Terada 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.
Adachi, Naruhiko, Masato Kawasaki, Toshio Moriya, et al.. (2025). Ancestral sequence reconstruction as a tool for structural analysis of modular polyketide synthases. Nature Communications. 16(1). 6847–6847. 1 indexed citations
2.
3.
Homma, M., Takatoshi Wakabayashi, Yoshitaka Moriwaki, et al.. (2024). Insights into stereoselective ring formation in canonical strigolactone: Identification of a dirigent domain-containing enzyme catalyzing orobanchol synthesis. Proceedings of the National Academy of Sciences. 121(26). e2313683121–e2313683121. 7 indexed citations
4.
Awakawa, Takayoshi, Takahiro Mori, Lena Barra, et al.. (2024). The structural basis of pyridoxal-5′-phosphate-dependent β-NAD-alkylating enzymes. Nature Catalysis. 7(10). 1099–1108. 5 indexed citations
5.
Mori, Takahiro, Yoshitaka Moriwaki, Jiřı́ Janata, et al.. (2024). Molecular basis for the diversification of lincosamide biosynthesis by pyridoxal phosphate-dependent enzymes. Nature Chemistry. 17(2). 256–264. 1 indexed citations
6.
Mori, Takahiro, et al.. (2024). Structure-function analysis of carrier protein-dependent 2-sulfamoylacetyl transferase in the biosynthesis of altemicidin. Nature Communications. 15(1). 10896–10896. 1 indexed citations
7.
Terada, Tohru, Jun-ichi Kishikawa, Mika Hirose, et al.. (2023). Enhancement of SARS-CoV-2 Infection via Crosslinking of Adjacent Spike Proteins by N-Terminal Domain-Targeting Antibodies. Viruses. 15(12). 2421–2421. 4 indexed citations
8.
9.
Terada, Tohru, et al.. (2022). Chemigenetic indicators based on synthetic chelators and green fluorescent protein. Nature Chemical Biology. 19(1). 38–44. 19 indexed citations
10.
Hayashida, Kenichi, Masakatsu Watanabe, Kazumi Kobayashi, et al.. (2022). Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids. Science Signaling. 15(720). eabg6941–eabg6941. 38 indexed citations
11.
Lü, Peng, Tohru Terada, Yukie Katayama, et al.. (2021). Quercetin 3,5,7,3′,4′-pentamethyl ether from Kaempferia parviflora directly and effectively activates human SIRT1. Communications Biology. 4(1). 209–209. 16 indexed citations
12.
Yokoyama, Yuichi, Tohru Terada, Kentaro Shimizu, et al.. (2020). Development of a deep learning-based method to identify “good” regions of a cryo-electron microscopy grid. Biophysical Reviews. 12(2). 349–354. 19 indexed citations
13.
Watanabe, Masakatsu, et al.. (2020). Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids. Science Advances. 6(7). eaax3157–eaax3157. 41 indexed citations
14.
Yasukawa, Takashi, et al.. (2020). NrBP1含有Crl2/Crl4aは分解のためのBRI2とBRI3を標的とすることによりアミロイドβ産生を調節する【JST・京大機械翻訳】. Cell Reports. 30(10). 3478–3491. 1 indexed citations
15.
Yamagata, Atsushi, Sakurako Goto‐Ito, Yusuke Sato, et al.. (2018). Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction. Nature Communications. 9(1). 3964–3964. 34 indexed citations
16.
Nagarathinam, Kumar, Yoshiko Nakada-Nakura, C. Parthier, et al.. (2018). Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism. Nature Communications. 9(1). 4005–4005. 42 indexed citations
17.
Koizumi, Ayako, Ken‐ichiro Nakajima, Keisuke Ito, et al.. (2011). Human sweet taste receptor mediates acid-induced sweetness of miraculin. Proceedings of the National Academy of Sciences. 108(40). 16819–16824. 50 indexed citations
18.
Terada, Tohru, et al.. (2011). Mechanism for folate‐independent aldolase reaction catalyzed by serine hydroxymethyltransferase. FEBS Journal. 279(3). 504–514. 21 indexed citations
19.
Arima, Kazuhiko, Kazuo Sato, Go Tanaka, et al.. (2005). Characterization of the Interaction between Interleukin-13 and Interleukin-13 Receptors. Journal of Biological Chemistry. 280(26). 24915–24922. 71 indexed citations
20.
Cao, Wei, Tohru Terada, Shugo Nakamura, & Kentaro Shimizu. (2003). Refinement of Comparative-Modeling Structures by Multicanonical Molecular Dynamics. Proceedings Genome Informatics Workshop/Genome informatics. 14. 484–485. 6 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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