Eriko Nango

5.0k total citations
48 papers, 963 citations indexed

About

Eriko Nango is a scholar working on Molecular Biology, Materials Chemistry and Structural Biology. According to data from OpenAlex, Eriko Nango has authored 48 papers receiving a total of 963 indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 29 papers in Materials Chemistry and 11 papers in Structural Biology. Recurrent topics in Eriko Nango's work include Enzyme Structure and Function (27 papers), Advanced Electron Microscopy Techniques and Applications (11 papers) and Photosynthetic Processes and Mechanisms (10 papers). Eriko Nango is often cited by papers focused on Enzyme Structure and Function (27 papers), Advanced Electron Microscopy Techniques and Applications (11 papers) and Photosynthetic Processes and Mechanisms (10 papers). Eriko Nango collaborates with scholars based in Japan, United Kingdom and South Korea. Eriko Nango's co-authors include So Iwata, Tadashi Eguchi, Kensuke Tono, Takanori Nakane, Shizuko Kakinuma, Yasumasa Joti, Makina Yabashi, Rie Tanaka, Osamu Nureki and Michihiro Sugahara and has published in prestigious journals such as Nature Communications, Annual Review of Biochemistry and Scientific Reports.

In The Last Decade

Eriko Nango

45 papers receiving 943 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eriko Nango Japan 20 602 364 159 142 139 48 963
Benjamin Stauch United States 14 639 1.1× 193 0.5× 155 1.0× 44 0.3× 52 0.4× 17 995
Andrii Ishchenko United States 17 725 1.2× 264 0.7× 304 1.9× 72 0.5× 23 0.2× 27 959
Frédéric Poitevin United States 15 1.2k 2.1× 145 0.4× 346 2.2× 73 0.5× 12 0.1× 39 1.4k
Ulrich K. Genick United States 13 882 1.5× 227 0.6× 735 4.6× 26 0.2× 69 0.5× 16 1.1k
Mrinal Shekhar United States 17 639 1.1× 105 0.3× 150 0.9× 87 0.6× 27 0.2× 30 938
Antoine Koehl United States 12 1.3k 2.1× 62 0.2× 655 4.1× 38 0.3× 44 0.3× 15 1.5k
Janesh Kumar India 19 810 1.3× 102 0.3× 602 3.8× 85 0.6× 68 0.5× 44 1.2k
Spencer Anderson United States 17 984 1.6× 294 0.8× 568 3.6× 57 0.4× 33 0.2× 20 1.4k
Yoshiaki Kimura Japan 16 1.1k 1.9× 173 0.5× 913 5.7× 105 0.7× 16 0.1× 38 1.7k
Montserrat Samsó United States 24 1.5k 2.4× 100 0.3× 287 1.8× 121 0.9× 16 0.1× 56 1.8k

Countries citing papers authored by Eriko Nango

Since Specialization
Citations

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

Fields of papers citing papers by Eriko Nango

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Eriko Nango

This figure shows the co-authorship network connecting the top 25 collaborators of Eriko Nango. A scholar is included among the top collaborators of Eriko Nango 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 Eriko Nango. Eriko Nango 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.
Fujiwara, Takaaki, et al.. (2024). Structural basis for the minimal bifunctional alginate epimerase AlgE3 from Azotobacter chroococcum. FEBS Letters. 598(11). 1422–1437. 1 indexed citations
2.
Nango, Eriko & So Iwata. (2023). Recent progress in membrane protein dynamics revealed by X-ray free electron lasers: Molecular movies of microbial rhodopsins. Current Opinion in Structural Biology. 81. 102629–102629. 9 indexed citations
3.
Doura, Tomohiro, Eriko Nango, Masaki Yamamoto, et al.. (2023). Crystal structure reveals the binding mode and selectivity of a photoswitchable ligand for the adenosine A2A receptor. Biochemical and Biophysical Research Communications. 695. 149393–149393. 2 indexed citations
4.
Kashiwagi, Tatsuki, N. Kunishima, Hisashi Naitow, et al.. (2023). Ambient temperature structure of phosphoketolase from Bifidobacterium longum determined by serial femtosecond X-ray crystallography. Acta Crystallographica Section D Structural Biology. 79(4). 290–303. 3 indexed citations
5.
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
6.
Wahlgren, Weixiao Yuan, Léocadie Henry, Suraj Pandey, et al.. (2021). The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature. Acta Crystallographica Section D Structural Biology. 77(8). 1001–1009. 6 indexed citations
7.
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
8.
Wickstrand, Cecilia, Gergely Katona, Takanori Nakane, et al.. (2020). A tool for visualizing protein motions in time-resolved crystallography. Structural Dynamics. 7(2). 24701–24701. 14 indexed citations
9.
Ihara, Kentaro, Masakatsu Hato, Takanori Nakane, et al.. (2020). Isoprenoid-chained lipid EROCOC17+4: a new matrix for membrane protein crystallization and a crystal delivery medium in serial femtosecond crystallography. Scientific Reports. 10(1). 19305–19305. 13 indexed citations
10.
Mizohata, Eiichi, Takanori Nakane, Yohta Fukuda, Eriko Nango, & So Iwata. (2017). Serial femtosecond crystallography at the SACLA: breakthrough to dynamic structural biology. Biophysical Reviews. 10(2). 209–218. 15 indexed citations
11.
Andersson, Rebecka, Robert Dods, Eriko Nango, et al.. (2017). Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature. Scientific Reports. 7(1). 4518–4518. 31 indexed citations
12.
Sugahara, Michihiro, Takanori Nakane, Tetsuya Masuda, et al.. (2017). Hydroxyethyl cellulose matrix applied to serial crystallography. Scientific Reports. 7(1). 703–703. 56 indexed citations
13.
Fukuda, Yohta, Mamoru Suzuki, Kay Diederichs, et al.. (2016). Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography. The Journal of Biochemistry. 159(5). 527–538. 20 indexed citations
14.
Nango, Eriko, Shuji Akiyama, Saori Maki-Yonekura, et al.. (2016). Taste substance binding elicits conformational change of taste receptor T1r heterodimer extracellular domains. Scientific Reports. 6(1). 25745–25745. 35 indexed citations
15.
Mafuné, Fumitaka, Ken Miyajima, Kensuke Tono, et al.. (2016). Microcrystal delivery by pulsed liquid droplet for serial femtosecond crystallography. Acta Crystallographica Section D Structural Biology. 72(4). 520–523. 31 indexed citations
16.
Tono, Kensuke, Eriko Nango, Michihiro Sugahara, et al.. (2015). Diverse application platform for hard X-ray diffraction in SACLA (DAPHNIS): application to serial protein crystallography using an X-ray free-electron laser. Journal of Synchrotron Radiation. 22(3). 532–537. 44 indexed citations
17.
Mizohata, Eiichi, Eriko Nango, Michihiro Sugahara, Mamoru Suzuki, & So Iwata. (2014). Protein Structure Analyses Using X-ray Free-Electron Lasers. Nihon Kessho Gakkaishi. 56(4). 241–246. 1 indexed citations
18.
Tamegai, Hideyuki, et al.. (2010). Roles of a 20 kDa Protein Associated with a Carbocycle-Forming Enzyme Involved in Aminoglycoside Biosynthesis in Primary and Secondary Metabolism. Bioscience Biotechnology and Biochemistry. 74(6). 1215–1219. 3 indexed citations
19.
Nango, Eriko, Takashi Yamamoto, Takashi Kumasaka, & Tadashi Eguchi. (2009). Crystal structure of 3-isopropylmalate dehydrogenase in complex with NAD+ and a designed inhibitor. Bioorganic & Medicinal Chemistry. 17(22). 7789–7794. 10 indexed citations
20.
Nango, Eriko, Takashi Kumasaka, Takao Sato, et al.. (2005). Crystallization and X-ray analysis of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(7). 709–711. 8 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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