Emiko Uchikawa

891 total citations
18 papers, 609 citations indexed

About

Emiko Uchikawa is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, Emiko Uchikawa has authored 18 papers receiving a total of 609 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 4 papers in Materials Chemistry and 2 papers in Ecology. Recurrent topics in Emiko Uchikawa's work include RNA and protein synthesis mechanisms (5 papers), Enzyme Structure and Function (4 papers) and interferon and immune responses (2 papers). Emiko Uchikawa is often cited by papers focused on RNA and protein synthesis mechanisms (5 papers), Enzyme Structure and Function (4 papers) and interferon and immune responses (2 papers). Emiko Uchikawa collaborates with scholars based in United States, Switzerland and France. Emiko Uchikawa's co-authors include Xiao‐chen Bai, Eunhee Choi, Denis Gerlier, Joanna Brunel, S. Cusack, Xuewu Zhang, Guijun Shang, Hongtao Yu, Mathilde Lethier and Zhiming Chen and has published in prestigious journals such as Nucleic Acids Research, Nature Communications and Molecular Cell.

In The Last Decade

Emiko Uchikawa

15 papers receiving 607 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Emiko Uchikawa United States 12 418 159 54 51 42 18 609
Amélie Weiss France 11 408 1.0× 176 1.1× 88 1.6× 19 0.4× 34 0.8× 18 678
Gábor Zahuczky Hungary 13 230 0.6× 268 1.7× 43 0.8× 42 0.8× 45 1.1× 27 569
Philippe Gonzalo France 17 661 1.6× 115 0.7× 109 2.0× 24 0.5× 20 0.5× 37 943
Jacky Schmitt Germany 11 568 1.4× 110 0.7× 105 1.9× 21 0.4× 19 0.5× 15 803
C. Nicolau United States 14 388 0.9× 58 0.4× 43 0.8× 57 1.1× 37 0.9× 47 665
Jonathan St‐Germain Canada 18 609 1.5× 124 0.8× 89 1.6× 18 0.4× 53 1.3× 33 841
Jianyin Lin China 17 362 0.9× 65 0.4× 96 1.8× 62 1.2× 15 0.4× 33 612
Jason Borawski United States 9 459 1.1× 193 1.2× 59 1.1× 23 0.5× 38 0.9× 11 648
Anja Mezger Sweden 13 836 2.0× 171 1.1× 59 1.1× 50 1.0× 44 1.0× 21 1.2k
Matthias Michalek Germany 13 486 1.2× 176 1.1× 125 2.3× 20 0.4× 27 0.6× 20 783

Countries citing papers authored by Emiko Uchikawa

Since Specialization
Citations

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

Fields of papers citing papers by Emiko Uchikawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Emiko Uchikawa

This figure shows the co-authorship network connecting the top 25 collaborators of Emiko Uchikawa. A scholar is included among the top collaborators of Emiko Uchikawa 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 Emiko Uchikawa. Emiko Uchikawa is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

18 of 18 papers shown
1.
Pandey, Radha Raman, et al.. (2026). Structure of the MIWI endoribonuclease bound to pachytene piRNAs from mouse testes. Cell Reports. 45(1). 116804–116804.
2.
Srivastava, Shiv, G. Sekar, Adedolapo Ojoawo, et al.. (2025). Structural basis of BAK sequestration by MCL-1 in apoptosis. Molecular Cell. 85(8). 1606–1623.e10. 2 indexed citations
3.
Li, Yan, David W. Adams, Hon Wing Liu, et al.. (2025). Structure and activation mechanism of a Lamassu phage and plasmid defense system. Nature Structural & Molecular Biology. 32(12). 2503–2516.
4.
Liu, Hon Wing, et al.. (2025). Mechanism of DNA entrapment by a loop-extruding Wadjet SMC motor. Molecular Cell. 85(21). 3898–3912.e7. 1 indexed citations
5.
Nasi, Sonia, Driss Ehirchiou, Véronique Chobaz, et al.. (2025). Allosteric activators of cystathionine γ lyase to augment endogenous hydrogen sulfide and inhibit pathologic calcification. Pharmacological Research. 219. 107869–107869.
6.
Hall, Catherine, Emiko Uchikawa, Dailu Chen, et al.. (2023). Structural basis of insulin fibrillation. Science Advances. 9(37). eadi1057–eadi1057. 21 indexed citations
7.
Ni, Dongchun, Priscilla Turelli, Bertrand Beckert, et al.. (2023). Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range. PLoS Pathogens. 19(4). e1011206–e1011206. 18 indexed citations
8.
Nguyen, Phong, Michael Fine, Trevor S. Tippetts, et al.. (2022). Structural basis for gating mechanism of the human sodium-potassium pump. Nature Communications. 13(1). 5293–5293. 32 indexed citations
9.
Li, Jie, Junhee Park, John P. Mayer, et al.. (2022). Synergistic activation of the insulin receptor via two distinct sites. Nature Structural & Molecular Biology. 29(4). 357–368. 42 indexed citations
10.
Uchikawa, Emiko, Zhiming Chen, Guan-Yu Xiao, Xuewu Zhang, & Xiao‐chen Bai. (2021). Structural basis of the activation of c-MET receptor. Nature Communications. 12(1). 4074–4074. 95 indexed citations
11.
Chen, Hua, Guijun Shang, Emiko Uchikawa, et al.. (2020). Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation. Nature Communications. 11(1). 1953–1953. 13 indexed citations
12.
Uchikawa, Emiko, Eunhee Choi, Guijun Shang, Hongtao Yu, & Xiao‐chen Bai. (2019). Activation mechanism of the insulin receptor revealed by cryo-EM structure of the fully liganded receptor–ligand complex. eLife. 8. 120 indexed citations
13.
Fernández, I., Irina Cornaciu, Emiko Uchikawa, et al.. (2017). Three-Dimensional Structure of Full-Length NtrX, an Unusual Member of the NtrC Family of Response Regulators. Journal of Molecular Biology. 429(8). 1192–1212. 20 indexed citations
14.
Uchikawa, Emiko, Mathilde Lethier, Hélène Malet, et al.. (2016). Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5. Molecular Cell. 62(4). 586–602. 114 indexed citations
15.
Louber, Jade, Joanna Brunel, Emiko Uchikawa, S. Cusack, & Denis Gerlier. (2015). Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5. BMC Biology. 13(1). 54–54. 49 indexed citations
16.
Uchikawa, Emiko, Xiao Han, Florence Proux, et al.. (2015). Structural insight into the mechanism of stabilization of the 7SK small nuclear RNA by LARP7. Nucleic Acids Research. 43(6). 3373–3388. 51 indexed citations
17.
Gajda, Michał J., et al.. (2013). Modeling the Structure of RNA Molecules with Small-Angle X-Ray Scattering Data. PLoS ONE. 8(11). e78007–e78007. 10 indexed citations
18.
Konno, Michiko, Tomomi Sumida, Emiko Uchikawa, et al.. (2009). Modeling of tRNA‐assisted mechanism of Arg activation based on a structure of Arg‐tRNA synthetase, tRNA, and an ATP analog (ANP). FEBS Journal. 276(17). 4763–4779. 21 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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