Katsumi Imada

6.2k total citations
116 papers, 4.6k citations indexed

About

Katsumi Imada is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, Katsumi Imada has authored 116 papers receiving a total of 4.6k indexed citations (citations by other indexed papers that have themselves been cited), including 88 papers in Molecular Biology, 54 papers in Genetics and 32 papers in Materials Chemistry. Recurrent topics in Katsumi Imada's work include Bacterial Genetics and Biotechnology (53 papers), Enzyme Structure and Function (32 papers) and Protein Structure and Dynamics (24 papers). Katsumi Imada is often cited by papers focused on Bacterial Genetics and Biotechnology (53 papers), Enzyme Structure and Function (32 papers) and Protein Structure and Dynamics (24 papers). Katsumi Imada collaborates with scholars based in Japan, United States and Hungary. Katsumi Imada's co-authors include Keiichi Namba, Tohru Minamino, Miki Kinoshita, Fadel A. Samatey, Michio Homma, Ferenc Vonderviszt, Shigehiro Nagashima, Mayuko Sakuma, Yukio Furukawa and H. Matsunami and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Katsumi Imada

115 papers receiving 4.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Katsumi Imada Japan 41 2.8k 1.9k 815 676 610 116 4.6k
Philip Matsumura United States 40 3.2k 1.1× 2.5k 1.3× 779 1.0× 569 0.8× 411 0.7× 74 4.3k
Michael D. Manson United States 39 2.8k 1.0× 1.9k 1.0× 625 0.8× 383 0.6× 214 0.4× 76 4.2k
Robert B. Bourret United States 33 3.5k 1.2× 2.2k 1.1× 611 0.7× 255 0.4× 342 0.6× 73 4.4k
Lotte Søgaard‐Andersen Germany 47 4.5k 1.6× 3.2k 1.6× 1.4k 1.8× 695 1.0× 221 0.4× 142 6.1k
Z. Hong Zhou United States 55 4.9k 1.7× 1.1k 0.6× 1.4k 1.7× 289 0.4× 794 1.3× 214 9.9k
Ariane Briegel United States 34 2.8k 1.0× 1.6k 0.8× 995 1.2× 490 0.7× 195 0.3× 92 4.0k
David F. Blair United States 47 4.4k 1.6× 2.6k 1.4× 906 1.1× 698 1.0× 234 0.4× 75 6.2k
Tohru Minamino Japan 55 5.0k 1.8× 5.0k 2.6× 2.0k 2.4× 1.7k 2.5× 650 1.1× 186 8.4k
Shin‐Ichi Aizawa Japan 51 4.9k 1.7× 3.8k 1.9× 1.9k 2.4× 2.0k 3.0× 332 0.5× 148 8.8k
Seiji Kojima Japan 36 2.4k 0.8× 1.5k 0.8× 614 0.8× 737 1.1× 117 0.2× 169 4.2k

Countries citing papers authored by Katsumi Imada

Since Specialization
Citations

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

Fields of papers citing papers by Katsumi Imada

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Katsumi Imada

This figure shows the co-authorship network connecting the top 25 collaborators of Katsumi Imada. A scholar is included among the top collaborators of Katsumi Imada 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 Katsumi Imada. Katsumi Imada 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.
Takekawa, Norihiro, Tohru Minamino, Katsumi Imada, et al.. (2025). Cryo-EM Structure of the Flagellar Motor Complex from Paenibacillus sp. TCA20. Biomolecules. 15(3). 435–435.
2.
Takekawa, Norihiro, Jun-ichi Kishikawa, Mika Hirose, et al.. (2024). Structural analysis of S-ring composed of FliFG fusion proteins in marine Vibrio polar flagellar motor. mBio. 15(10). e0126124–e0126124. 1 indexed citations
3.
Takekawa, Norihiro, Jun-ichi Kishikawa, Mika Hirose, et al.. (2024). Structural insight into sodium ion pathway in the bacterial flagellar stator from marine Vibrio. Proceedings of the National Academy of Sciences. 122(1). e2415713122–e2415713122. 2 indexed citations
4.
Fujiwara, Ikuko, et al.. (2022). ATP-dependent polymerization dynamics of bacterial actin proteins involved in Spiroplasma swimming. Open Biology. 12(10). 220083–220083. 15 indexed citations
5.
Takekawa, Norihiro, et al.. (2021). ZomB is essential for chemotaxis of Vibrio alginolyticus by the rotational direction control of the polar flagellar motor. Genes to Cells. 26(11). 927–937. 4 indexed citations
6.
Takekawa, Norihiro, Hiroyuki Terashima, Shiwei Zhu, et al.. (2019). Structure of Vibrio FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function. mBio. 10(2). 36 indexed citations
7.
Saijo‐Hamano, Yumiko, H. Matsunami, Keiichi Namba, & Katsumi Imada. (2019). Architecture of the Bacterial Flagellar Distal Rod and Hook of Salmonella. Biomolecules. 9(7). 260–260. 13 indexed citations
8.
Terahara, Naoya, Yumi Inoue, Noriyuki Kodera, et al.. (2018). Insight into structural remodeling of the FlhA ring responsible for bacterial flagellar type III protein export. Science Advances. 4(4). eaao7054–eaao7054. 41 indexed citations
9.
Terashima, Hiroyuki, Akihiro Kawamoto, Yusuke V. Morimoto, Katsumi Imada, & Tohru Minamino. (2017). Structural differences in the bacterial flagellar motor among bacterial species. Biophysics and Physicobiology. 14(0). 191–198. 43 indexed citations
10.
Imada, Katsumi. (2017). Bacterial flagellar axial structure and its construction. Biophysical Reviews. 10(2). 559–570. 40 indexed citations
11.
Tamura, Takashi, Atsushi Sogabe, Satoshi Akanuma, et al.. (2015). Epistasis effects of multiple ancestral-consensus amino acid substitutions on the thermal stability of glycerol kinase from Cellulomonas sp. NT3060. Journal of Bioscience and Bioengineering. 121(5). 497–502. 8 indexed citations
12.
Minamino, Tohru, et al.. (2012). Crystallization and preliminary X-ray analysis of the FliH–FliI complex responsible for bacterial flagellar type III protein export. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(11). 1311–1314. 2 indexed citations
13.
Imada, Katsumi, Mayuko Sakuma, Fumiyuki Hattori, et al.. (2011). Ligand Specificity Determined by Differentially Arranged Common Ligand-binding Residues in Bacterial Amino Acid Chemoreceptors Tsr and Tar. Journal of Biological Chemistry. 286(49). 42200–42210. 54 indexed citations
14.
Imada, Katsumi, et al.. (2011). Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases. Nature Structural & Molecular Biology. 18(3). 277–282. 134 indexed citations
15.
Minamino, Tohru, Katsumi Imada, & Keiichi Namba. (2008). Mechanisms of type III protein export for bacterial flagellar assembly. Molecular BioSystems. 4(11). 1105–1115. 154 indexed citations
16.
Kitao, Akio, Koji Yonekura, Saori Maki-Yonekura, et al.. (2006). Switch interactions control energy frustration and multiple flagellar filament structures. Proceedings of the National Academy of Sciences. 103(13). 4894–4899. 46 indexed citations
17.
Iwase, Ryo, Katsumi Imada, Fumio Hayashi, et al.. (2005). Functionally Important Substructures of Circadian Clock Protein KaiB in a Unique Tetramer Complex. Journal of Biological Chemistry. 280(52). 43141–43149. 56 indexed citations
18.
Hayashi, Fumio, Hirofumi Suzuki, Ryo Iwase, et al.. (2003). ATP‐induced hexameric ring structure of the cyanobacterial circadian clock protein KaiC. Genes to Cells. 8(3). 287–296. 103 indexed citations
19.
Samatey, Fadel A., Katsumi Imada, Ferenc Vonderviszt, Yasuo Shirakihara, & Keiichi Namba. (2000). Crystallization of the F41 Fragment of Flagellin and Data Collection from Extremely Thin Crystals. Journal of Structural Biology. 132(2). 106–111. 26 indexed citations
20.
Onodera, Ko, Hideaki Moriyama, A. Takénaka, et al.. (1991). Crystallization and Preliminary X-Ray Studies of a Bacillus subtilis and Thermuts thermophilus HB8 Chimeric 3-Isopropylmalate Dehy drogenasel. The Journal of Biochemistry. 109(1). 1–2. 2 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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