Shingo Nagano

2.8k total citations
55 papers, 2.3k citations indexed

About

Shingo Nagano is a scholar working on Molecular Biology, Inorganic Chemistry and Pharmacology. According to data from OpenAlex, Shingo Nagano has authored 55 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 16 papers in Inorganic Chemistry and 15 papers in Pharmacology. Recurrent topics in Shingo Nagano's work include Metal-Catalyzed Oxygenation Mechanisms (14 papers), Microbial Natural Products and Biosynthesis (13 papers) and Pharmacogenetics and Drug Metabolism (12 papers). Shingo Nagano is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (14 papers), Microbial Natural Products and Biosynthesis (13 papers) and Pharmacogenetics and Drug Metabolism (12 papers). Shingo Nagano collaborates with scholars based in Japan, United States and Israel. Shingo Nagano's co-authors include Yoshitsugu Shiro, T.L. Poulos, Yoshihito Watanabe, Hiroshi Sugimoto, Koichiro Ishimori, Isao Morishima, Tomoya Hino, Yushi Matsumoto, Osami Shoji and Takashi Fujishiro and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Shingo Nagano

53 papers receiving 2.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shingo Nagano Japan 28 1.1k 764 635 406 290 55 2.3k
Simon Daff United Kingdom 27 1.2k 1.1× 516 0.7× 719 1.1× 358 0.9× 153 0.5× 58 2.4k
Rakesh Paul India 8 1.1k 1.0× 641 0.8× 1.1k 1.8× 170 0.4× 397 1.4× 11 2.6k
Stephen E. J. Rigby United Kingdom 38 2.9k 2.6× 584 0.8× 311 0.5× 173 0.4× 465 1.6× 115 4.4k
Sandeep Modi United Kingdom 26 1.2k 1.0× 235 0.3× 987 1.6× 165 0.4× 200 0.7× 67 2.5k
Ryu Makino Japan 30 1.3k 1.2× 629 0.8× 500 0.8× 768 1.9× 283 1.0× 58 2.5k
Eric D. Coulter United States 17 1.4k 1.3× 2.0k 2.6× 437 0.7× 466 1.1× 799 2.8× 25 3.1k
Mark P. Roach United States 12 1.2k 1.1× 1.7k 2.2× 383 0.6× 615 1.5× 794 2.7× 15 2.7k
Hayley C. Angove United States 15 745 0.7× 402 0.5× 954 1.5× 120 0.3× 209 0.7× 16 2.4k
Caroline S. Miles United Kingdom 20 1.2k 1.1× 418 0.5× 789 1.2× 126 0.3× 198 0.7× 37 1.8k
Aimin Liu United States 35 1.8k 1.7× 1.4k 1.8× 124 0.2× 303 0.7× 492 1.7× 146 3.5k

Countries citing papers authored by Shingo Nagano

Since Specialization
Citations

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

Fields of papers citing papers by Shingo Nagano

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shingo Nagano

This figure shows the co-authorship network connecting the top 25 collaborators of Shingo Nagano. A scholar is included among the top collaborators of Shingo Nagano 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 Shingo Nagano. Shingo Nagano 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.
Kato, Naoki & Shingo Nagano. (2025). Iminium catalysis meets Diels–Alderase. Nature Catalysis. 8(3). 202–203.
2.
Sato, Yusuke, et al.. (2023). Anammox Bacterial S-Adenosyl-l-Methionine Dependent Methyltransferase Crystal Structure and Its Interaction with Acyl Carrier Proteins. International Journal of Molecular Sciences. 24(1). 744–744. 3 indexed citations
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Yamanaka, Kazuya, et al.. (2022). Crystal structure of the adenylation domain from an ε-poly-l-lysine synthetase provides molecular mechanism for substrate specificity. Biochemical and Biophysical Research Communications. 596. 43–48. 7 indexed citations
5.
Kato, Naoki, Suyong Re, Kohei Watanabe, et al.. (2021). Molecular Basis for Two Stereoselective Diels–Alderases that Produce Decalin Skeletons**. Angewandte Chemie International Edition. 60(41). 22401–22410. 20 indexed citations
6.
Kato, Naoki, Suyong Re, Kohei Watanabe, et al.. (2021). Molecular Basis for Two Stereoselective Diels–Alderases that Produce Decalin Skeletons**. Angewandte Chemie. 133(41). 22575–22584. 1 indexed citations
7.
Yun, Choong‐Soo, Takayuki Motoyama, Takeshi Shimizu, et al.. (2020). Unique features of the ketosynthase domain in a nonribosomal peptide synthetase–polyketide synthase hybrid enzyme, tenuazonic acid synthetase 1. Journal of Biological Chemistry. 295(33). 11602–11612. 20 indexed citations
8.
Kojima, Keiichi, et al.. (2020). Applicability of Styrene-Maleic Acid Copolymer for Two Microbial Rhodopsins, RxR and HsSRI. Biophysical Journal. 119(9). 1760–1770. 9 indexed citations
9.
Hino, Tomoya, et al.. (2017). Crystal structures of TdsC, a dibenzothiophene monooxygenase from the thermophile Paenibacillus sp. A11-2, reveal potential for expanding its substrate selectivity. Journal of Biological Chemistry. 292(38). 15804–15813. 11 indexed citations
10.
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Takahashi, Shunji, Shingo Nagano, Toshihiko Nogawa, et al.. (2014). Structure-Function Analyses of Cytochrome P450revI Involved in Reveromycin A Biosynthesis and Evaluation of the Biological Activity of Its Substrate, Reveromycin T. Journal of Biological Chemistry. 289(47). 32446–32458. 16 indexed citations
13.
Hino, Tomoya, Shingo Nagano, Hiroshi Sugimoto, Takehiko Tosha, & Yoshitsugu Shiro. (2011). Molecular structure and function of bacterial nitric oxide reductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(4). 680–687. 50 indexed citations
14.
Shoji, Osami, et al.. (2010). Understanding substrate misrecognition of hydrogen peroxide dependent cytochrome P450 from Bacillus subtilis. JBIC Journal of Biological Inorganic Chemistry. 15(8). 1331–1339. 32 indexed citations
15.
Shoji, Osami, Takashi Fujishiro, Hiroshi Nakajima, et al.. (2007). Hydrogen Peroxide Dependent Monooxygenations by Tricking the Substrate Recognition of Cytochrome P450BSβ. Angewandte Chemie International Edition. 46(20). 3656–3659. 122 indexed citations
16.
Nagano, Shingo, Jill R. Cupp‐Vickery, & T.L. Poulos. (2005). Crystal Structures of the Ferrous Dioxygen Complex of Wild-type Cytochrome P450eryF and Its Mutants, A245S and A245T. Journal of Biological Chemistry. 280(23). 22102–22107. 74 indexed citations
17.
Egawa, Tsuyoshi, Shiro Yoshioka, Satoshi Takahashi, et al.. (2003). Kinetic and Spectroscopic Characterization of a Hydroperoxy Compound in the Reaction of Native Myoglobin with Hydrogen Peroxide. Journal of Biological Chemistry. 278(43). 41597–41606. 35 indexed citations
18.
Nagano, Shingo, et al.. (2001). Putidaredoxin–cytochrome P450cam interaction. Journal of Inorganic Biochemistry. 83(4). 255–260. 32 indexed citations
19.
Shimada, Hideo, Shingo Nagano, Masashi Unno, et al.. (1999). Putidaredoxin-Cytochrome P450cam Interaction. Journal of Biological Chemistry. 274(14). 9363–9369. 27 indexed citations
20.
Nagano, Shingo, Motomasa Tanaka, Yoshihito Watanabe, & Isao Morishima. (1995). Putative Hydrogen Bond Network in the Heme Distal Site of Horseradish Peroxidase. Biochemical and Biophysical Research Communications. 207(1). 417–423. 23 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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