Mikihiro Shibata

2.8k total citations
58 papers, 1.9k citations indexed

About

Mikihiro Shibata is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Mikihiro Shibata has authored 58 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 32 papers in Cellular and Molecular Neuroscience and 15 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Mikihiro Shibata's work include Photoreceptor and optogenetics research (29 papers), Neuroscience and Neuropharmacology Research (23 papers) and Force Microscopy Techniques and Applications (11 papers). Mikihiro Shibata is often cited by papers focused on Photoreceptor and optogenetics research (29 papers), Neuroscience and Neuropharmacology Research (23 papers) and Force Microscopy Techniques and Applications (11 papers). Mikihiro Shibata collaborates with scholars based in Japan, United States and China. Mikihiro Shibata's co-authors include Hideki Kandori, Takayuki Uchihashi, Toshio Ando, Hayato Yamashita, Ryohei Yasuda, Makoto Demura, Noriyuki Kodera, Hiroki Watanabe, Keiichi Inoue and Yuji Furutani and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Mikihiro Shibata

55 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mikihiro Shibata Japan 25 957 791 625 238 182 58 1.9k
Ruixuan Gao United States 20 469 0.5× 511 0.6× 176 0.3× 820 3.4× 299 1.6× 50 1.9k
Benjamin M. Gaub United States 14 729 0.8× 656 0.8× 373 0.6× 338 1.4× 287 1.6× 16 1.7k
Catherine Tardin France 15 1.6k 1.7× 236 0.3× 346 0.6× 782 3.3× 245 1.3× 28 2.7k
Bibiana Onoa United States 13 1.1k 1.1× 468 0.6× 514 0.8× 229 1.0× 80 0.4× 22 2.2k
K. Tanuj Sapra Switzerland 22 1.3k 1.4× 236 0.3× 475 0.8× 221 0.9× 54 0.3× 40 1.8k
Sonia Contera United Kingdom 20 549 0.6× 111 0.1× 575 0.9× 438 1.8× 212 1.2× 56 1.5k
Ingmar Schoen Switzerland 22 458 0.5× 203 0.3× 147 0.2× 473 2.0× 68 0.4× 48 1.6k
David Dunlap United States 25 1.6k 1.6× 110 0.1× 403 0.6× 332 1.4× 64 0.4× 78 2.2k
Irene Wacker Germany 23 684 0.7× 211 0.3× 114 0.2× 316 1.3× 344 1.9× 61 1.9k
Yuki Suzuki Japan 27 1.7k 1.8× 77 0.1× 269 0.4× 406 1.7× 131 0.7× 105 2.2k

Countries citing papers authored by Mikihiro Shibata

Since Specialization
Citations

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

Fields of papers citing papers by Mikihiro Shibata

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mikihiro Shibata

This figure shows the co-authorship network connecting the top 25 collaborators of Mikihiro Shibata. A scholar is included among the top collaborators of Mikihiro Shibata 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 Mikihiro Shibata. Mikihiro Shibata 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.
Yamaguchi, Takayuki, Kei Okatsu, Masato Kubota, et al.. (2025). Structural insights into heterohexameric assembly of epilepsy-related ligand–receptor complex LGI1–ADAM22. eLife. 14.
2.
Tanaka, Hiroki, Shunsuke Kita, Hiroyuki Takeda, et al.. (2025). Structural basis of the hepatitis B virus X protein in complex with DDB1. Proceedings of the National Academy of Sciences. 122(24). e2421325122–e2421325122.
3.
Yilmaz, Neval, Shun Sakuraba, Holger Flechsig, et al.. (2025). Ligand Binding to the Membrane-Distal Domain of the Met Receptor Induces Dimerization at the Membrane-Proximal Domain. ACS Nano. 19(48). 40746–40758.
4.
Morioka, Shin, Takahiro Kakuta, Tomoki Ogoshi, et al.. (2024). High-Speed Atomic Force Microscopy Reveals the Nucleosome Sliding and DNA Unwrapping/Wrapping Dynamics of Tail-less Nucleosomes. Nano Letters. 24(17). 5246–5254. 4 indexed citations
5.
Sumino, Ayumi, Takashi Sumikama, Yimeng Zhao, et al.. (2024). High-Speed Atomic Force Microscopy Reveals Fluctuations and Dimer Splitting of the N-Terminal Domain of GluA2 Ionotropic Glutamate Receptor-Auxiliary Subunit Complex. ACS Nano. 18(36). 25018–25035. 4 indexed citations
6.
Sumino, Ayumi, et al.. (2023). Antithetic effects of agonists and antagonists on the structural fluctuations of TRPV1 channel. Proceedings of the National Academy of Sciences. 120(20). e2301013120–e2301013120. 3 indexed citations
7.
Morioka, Shin, Naoki Horikoshi, Tomoya Kujirai, et al.. (2023). High-Speed Atomic Force Microscopy Reveals Spontaneous Nucleosome Sliding of H2A.Z at the Subsecond Time Scale. Nano Letters. 23(5). 1696–1704. 8 indexed citations
8.
Sumino, Ayumi, Takashi Sumikama, Holger Flechsig, et al.. (2023). Imaging single CaMKII holoenzymes at work by high-speed atomic force microscopy. Science Advances. 9(26). eadh1069–eadh1069. 10 indexed citations
9.
Sakai, Katsuya, Emiko Mihara, Hiroki Sato, et al.. (2022). Designing receptor agonists with enhanced pharmacokinetics by grafting macrocyclic peptides into fragment crystallizable regions. Nature Biomedical Engineering. 7(2). 164–176. 10 indexed citations
10.
Sakai, Katsuya, Toby Passioura, Hiroki Sato, et al.. (2019). Macrocyclic peptide-based inhibition and imaging of hepatocyte growth factor. Nature Chemical Biology. 15(6). 598–606. 58 indexed citations
11.
Matsui, Shusuke, et al.. (2017). Fast Adsorption of Soft Hydrogel Microspheres on Solid Surfaces in Aqueous Solution. Angewandte Chemie. 129(40). 12314–12317. 7 indexed citations
12.
Matsui, Shusuke, et al.. (2017). Fast Adsorption of Soft Hydrogel Microspheres on Solid Surfaces in Aqueous Solution. Angewandte Chemie International Edition. 56(40). 12146–12149. 38 indexed citations
13.
Shibata, Mikihiro, Hiroshi Nishimasu, Noriyuki Kodera, et al.. (2017). Real-space and real-time dynamics of CRISPR-Cas9 visualized by high-speed atomic force microscopy. Nature Communications. 8(1). 1430–1430. 152 indexed citations
14.
Shibata, Mikihiro, Takayuki Uchihashi, Toshio Ando, & Ryohei Yasuda. (2015). Long-tip high-speed atomic force microscopy for nanometer-scale imaging in live cells. Scientific Reports. 5(1). 8724–8724. 83 indexed citations
15.
Uchihashi, Takayuki, Hiroki Watanabe, Shingo Fukuda, Mikihiro Shibata, & Toshio Ando. (2015). Functional extension of high-speed AFM for wider biological applications. Ultramicroscopy. 160. 182–196. 60 indexed citations
16.
Kambara, Ohki, et al.. (2010). Low-frequency dynamics of bacteriorhodopsin studied by terahertz time-domain spectroscopy. Physical Chemistry Chemical Physics. 12(35). 10255–10255. 16 indexed citations
17.
Yamamoto, Daisuke, Takayuki Uchihashi, Noriyuki Kodera, et al.. (2010). High-Speed Atomic Force Microscopy Techniques for Observing Dynamic Biomolecular Processes. Methods in enzymology on CD-ROM/Methods in enzymology. 475. 541–564. 58 indexed citations
18.
Kambara, Ohki, et al.. (2010). Low-frequency dynamics of biological molecules studied by terahertz time-domain spectroscopy. 24. 153–158. 5 indexed citations
19.
Shibata, Mikihiro, et al.. (2008). Color Change of Proteorhodopsin by a Single Amino Acid Replacement at a Distant Cytoplasmic Loop. Angewandte Chemie International Edition. 47(21). 3923–3926. 27 indexed citations
20.
Asano, S. & Mikihiro Shibata. (1982). The hydrogen-induced cold work peak of internal friction in FeCr alloys. Scripta Metallurgica. 16(10). 1171–1174. 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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