Tomoshi Kameda

2.1k total citations
90 papers, 1.6k citations indexed

About

Tomoshi Kameda is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Tomoshi Kameda has authored 90 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 70 papers in Molecular Biology, 18 papers in Spectroscopy and 14 papers in Materials Chemistry. Recurrent topics in Tomoshi Kameda's work include Protein Structure and Dynamics (18 papers), Protein purification and stability (13 papers) and RNA Research and Splicing (11 papers). Tomoshi Kameda is often cited by papers focused on Protein Structure and Dynamics (18 papers), Protein purification and stability (13 papers) and RNA Research and Splicing (11 papers). Tomoshi Kameda collaborates with scholars based in Japan, United States and United Kingdom. Tomoshi Kameda's co-authors include Atsushi Hirano, Shoji Takada, Tsutomu Arakawa, Kentaro Shiraki, Tsuyoshi Terakawa, Yutaka Saitō, Koichi Kato, Kiyoshi Asai, Mitsuo Umetsu and Hikaru Nakazawa and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Angewandte Chemie International Edition and Nano Letters.

In The Last Decade

Tomoshi Kameda

89 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tomoshi Kameda Japan 22 1.2k 325 183 164 156 90 1.6k
Peter W. Thulstrup Denmark 23 952 0.8× 598 1.8× 163 0.9× 130 0.8× 191 1.2× 98 1.6k
Ming Xiao United States 26 1.4k 1.2× 335 1.0× 122 0.7× 497 3.0× 93 0.6× 68 2.6k
Lin‐Tai Da China 17 896 0.8× 320 1.0× 241 1.3× 127 0.8× 118 0.8× 60 1.3k
Qing‐Chuan Zheng China 21 946 0.8× 324 1.0× 133 0.7× 243 1.5× 195 1.3× 160 1.9k
Daniel G. Isom United States 19 1.3k 1.1× 288 0.9× 151 0.8× 54 0.3× 122 0.8× 30 1.6k
Matthew J. Cliff United Kingdom 29 1.7k 1.4× 615 1.9× 312 1.7× 130 0.8× 245 1.6× 73 2.4k
Hyung‐Ho Ha South Korea 26 848 0.7× 301 0.9× 166 0.9× 216 1.3× 276 1.8× 63 1.8k
Satoko Akashi Japan 25 1.5k 1.3× 253 0.8× 677 3.7× 165 1.0× 152 1.0× 111 2.4k
Jamie L. Betker United States 9 1.9k 1.6× 553 1.7× 78 0.4× 220 1.3× 263 1.7× 17 2.2k
Tamás Beke‐Somfai Hungary 20 1.2k 1.0× 238 0.7× 108 0.6× 142 0.9× 569 3.6× 88 1.8k

Countries citing papers authored by Tomoshi Kameda

Since Specialization
Citations

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

Fields of papers citing papers by Tomoshi Kameda

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tomoshi Kameda

This figure shows the co-authorship network connecting the top 25 collaborators of Tomoshi Kameda. A scholar is included among the top collaborators of Tomoshi Kameda 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 Tomoshi Kameda. Tomoshi Kameda 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.
Ikebe, Jinzen, et al.. (2025). Computational Design of Burkholderia cepacia Lipase Mutants that Show Enhanced Stereoselectivity in the Production of l-Menthol. Journal of Agricultural and Food Chemistry. 73(8). 4829–4839. 2 indexed citations
2.
Kozawa, Daichi, et al.. (2023). Diameter-Selective Sorting of Single-Walled Carbon Nanotubes Using π-Molecular Tweezers for Energy Materials. ACS Applied Nano Materials. 6(3). 1919–1926. 6 indexed citations
3.
Kameda, Tomoshi, et al.. (2023). Dissociation Rate Calculation via Constant-Force Steered Molecular Dynamics Simulation. Journal of Chemical Information and Modeling. 63(11). 3369–3376. 6 indexed citations
4.
Watanabe, Motoki, Shogen Boku, Mamiko Sukeno, et al.. (2022). A chemoproteoinformatics approach demonstrates that aspirin increases sensitivity to MEK inhibition by directly binding to RPS5. PNAS Nexus. 1(2). pgac059–pgac059. 1 indexed citations
5.
Iizumi, Yosuke, Yoshihiro Sowa, Motoki Watanabe, et al.. (2022). Stabilization of CDK6 by ribosomal protein uS7, a target protein of the natural product fucoxanthinol. Communications Biology. 5(1). 564–564. 1 indexed citations
6.
Saitō, Yutaka, Hikaru Nakazawa, Tomoyuki Ito, et al.. (2021). Machine-Learning-Guided Library Design Cycle for Directed Evolution of Enzymes: The Effects of Training Data Composition on Sequence Space Exploration. ACS Catalysis. 11(23). 14615–14624. 46 indexed citations
7.
Sakuraba, Shun, Junichi Iwakiri, Michiaki Hamada, et al.. (2020). Free-Energy Calculation of Ribonucleic Inosines and Its Application to Nearest-Neighbor Parameters. Journal of Chemical Theory and Computation. 16(9). 5923–5935. 3 indexed citations
8.
Kamagata, Kiyoto, Yuji Itoh, Hiroto Takahashi, et al.. (2020). Liquid-like droplet formation by tumor suppressor p53 induced by multivalent electrostatic interactions between two disordered domains. Scientific Reports. 10(1). 580–580. 83 indexed citations
9.
Saitō, Yutaka, et al.. (2018). Machine-Learning-Guided Mutagenesis for Directed Evolution of Fluorescent Proteins. ACS Synthetic Biology. 7(9). 2014–2022. 111 indexed citations
10.
Hirano, Atsushi, Kentaro Shiraki, & Tomoshi Kameda. (2018). Effects of Arginine on Multimodal Chromatography: Experiments and Simulations. Current Protein and Peptide Science. 20(1). 40–48. 16 indexed citations
11.
Hirano, Atsushi, Kazuki Iwashita, Shun Sakuraba, et al.. (2018). Salt-dependent elution of uncharged aromatic solutes in ion-exchange chromatography. Journal of Chromatography A. 1546. 46–55. 12 indexed citations
12.
Tomoike, Fumiaki, Yasuaki Kimura, Keiko Kuwata, et al.. (2017). A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1). Chemical Communications. 53(81). 11138–11141. 48 indexed citations
13.
Takano, Satoshi, Takashi Murayama, Tomoshi Kameda, et al.. (2017). Synthesis of 8-Substituted Analogues of Cyclic ADP-4-Thioribose and Their Unexpected Identification as Ca2+-Mobilizing Full Agonists. Journal of Medicinal Chemistry. 60(13). 5868–5875. 7 indexed citations
14.
Kawamura, Takahiro, et al.. (2017). Analysis of O 2 -binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A. Biophysical Journal. 112(9). 1820–1828. 5 indexed citations
15.
Hirano, Atsushi, Tomoshi Kameda, Shun Sakuraba, et al.. (2017). Disulfide bond formation of thiols by using carbon nanotubes. Nanoscale. 9(17). 5389–5393. 10 indexed citations
16.
Kitahara, Ryo, Yuichi Yoshimura, Mengjun Xue, Tomoshi Kameda, & Frans A. A. Mulder. (2016). Detecting O2 binding sites in protein cavities. Scientific Reports. 6(1). 20534–20534. 20 indexed citations
17.
Hirano, Atsushi, Tsutomu Arakawa, & Tomoshi Kameda. (2014). Interaction of arginine with Capto MMC in multimodal chromatography. Journal of Chromatography A. 1338. 58–66. 38 indexed citations
18.
Kudoh, Takashi, Satoshi Takano, Masato Uehara, et al.. (2013). Design and Synthesis of Cyclic ADP‐4‐Thioribose as a Stable Equivalent of Cyclic ADP‐Ribose, a Calcium Ion‐Mobilizing Second Messenger. Angewandte Chemie International Edition. 52(26). 6633–6637. 17 indexed citations
19.
Yagi‐Utsumi, Maho, Tomoshi Kameda, Yoshiki Yamaguchi, & Koichi Kato. (2010). NMR characterization of the interactions between lyso‐GM1 aqueous micelles and amyloid β. FEBS Letters. 584(4). 831–836. 55 indexed citations
20.
Kameda, Tomoshi. (2003). Importance of sequence specificity for predicting protein folding pathways: Perturbed Gaussian chain model. Proteins Structure Function and Bioinformatics. 53(3). 616–628. 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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