Takahisa Ikegami

4.0k total citations
105 papers, 3.2k citations indexed

About

Takahisa Ikegami is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Takahisa Ikegami has authored 105 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 85 papers in Molecular Biology, 14 papers in Spectroscopy and 14 papers in Materials Chemistry. Recurrent topics in Takahisa Ikegami's work include Protein Structure and Dynamics (18 papers), Photosynthetic Processes and Mechanisms (15 papers) and Enzyme Structure and Function (14 papers). Takahisa Ikegami is often cited by papers focused on Protein Structure and Dynamics (18 papers), Photosynthetic Processes and Mechanisms (15 papers) and Enzyme Structure and Function (14 papers). Takahisa Ikegami collaborates with scholars based in Japan, Germany and United States. Takahisa Ikegami's co-authors include Masahiro Shirakawa, Takeshi Watanabe, Yuji Goto, Jun-Goo Jee, Masayuki Hashimoto, Young‐Ho Lee, Izuru Ohki, Shizuka Seino, Hideo Akutsu and Naoyuki Fujita and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Takahisa Ikegami

104 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Takahisa Ikegami Japan 31 2.4k 331 312 283 264 105 3.2k
Perttu Permi Finland 35 2.0k 0.8× 178 0.5× 488 1.6× 205 0.7× 288 1.1× 147 3.6k
Tiina A. Salminen Finland 33 2.6k 1.1× 547 1.7× 237 0.8× 228 0.8× 102 0.4× 114 3.6k
Katsuyuki Tanizawa Japan 41 3.9k 1.6× 297 0.9× 922 3.0× 309 1.1× 273 1.0× 210 5.3k
Peter J. Kennelly United States 25 2.5k 1.0× 185 0.6× 533 1.7× 241 0.9× 93 0.4× 62 3.1k
Oliver Zerbe Switzerland 37 2.5k 1.0× 398 1.2× 345 1.1× 478 1.7× 62 0.2× 145 4.0k
Ralph Golbik Germany 37 2.6k 1.1× 330 1.0× 649 2.1× 128 0.5× 154 0.6× 115 4.2k
S.J. Harrop Australia 27 2.0k 0.8× 148 0.4× 514 1.6× 194 0.7× 79 0.3× 57 3.0k
David Gani United Kingdom 24 2.1k 0.9× 423 1.3× 310 1.0× 140 0.5× 212 0.8× 128 3.3k
Débora Foguel Brazil 38 3.0k 1.2× 142 0.4× 568 1.8× 292 1.0× 345 1.3× 126 4.8k
Manfred Auer United Kingdom 34 3.3k 1.4× 367 1.1× 321 1.0× 245 0.9× 59 0.2× 119 5.3k

Countries citing papers authored by Takahisa Ikegami

Since Specialization
Citations

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

Fields of papers citing papers by Takahisa Ikegami

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Takahisa Ikegami

This figure shows the co-authorship network connecting the top 25 collaborators of Takahisa Ikegami. A scholar is included among the top collaborators of Takahisa Ikegami 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 Takahisa Ikegami. Takahisa Ikegami 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.
Kobayashi, Naohiro, Weihua Qin, Yoshie Chiba, et al.. (2022). Structural basis for the unique multifaceted interaction of DPPA3 with the UHRF1 PHD finger. Nucleic Acids Research. 50(21). 12527–12542. 15 indexed citations
2.
Kang, Su‐Jin, Toshiharu Suzuki, Takahisa Ikegami, et al.. (2022). Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure. Journal of the American Chemical Society. 144(31). 14132–14139. 4 indexed citations
3.
Scholz, Martin, Susann Wicke, Hideaki Tanaka, et al.. (2019). Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga Chlamydomonas reinhardtii. Journal of Biological Chemistry. 295(1). 170–180. 7 indexed citations
4.
Schuller, Jan M., James A. Birrell, Hideaki Tanaka, et al.. (2018). Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science. 363(6424). 257–260. 149 indexed citations
5.
Kubota-Kawai, Hisako, Risa Mutoh, Pièrre Sétif, et al.. (2018). X-ray structure of an asymmetrical trimeric ferredoxin–photosystem I complex. Nature Plants. 4(4). 218–224. 52 indexed citations
6.
Nagadoi, Aritaka, et al.. (2016). The cyanobacterial cytochrome b6f subunit PetP adopts an SH3 fold in solution. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857(6). 705–714. 7 indexed citations
7.
Kinoshita, Misaki, Ju Yaen Kim, Satoshi Kume, et al.. (2015). Physicochemical nature of interfaces controlling ferredoxin NADP+ reductase activity through its interprotein interactions with ferredoxin. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1847(10). 1200–1211. 11 indexed citations
8.
Ikegami, Takahisa, et al.. (2014). 1H, 13C and 15N chemical shift assignments of the NDH-1 complex subunit CupS. Biomolecular NMR Assignments. 9(1). 169–171. 2 indexed citations
9.
Tanaka, Hiroaki, Ken‐ichi Akagi, Chitose Oneyama, et al.. (2013). Identification of a New Interaction Mode between the Src Homology 2 Domain of C-terminal Src Kinase (Csk) and Csk-binding Protein/Phosphoprotein Associated with Glycosphingolipid Microdomains. Journal of Biological Chemistry. 288(21). 15240–15254. 10 indexed citations
10.
Shelake, Rahul Mahadev, Hidenori Hayashi, Takahisa Ikegami, Shunnosuke Abe, & Eugene Hayato Morita. (2013). Improved Protein Overexpression and Purification Strategies for Structural Studies of Cyanobacterial Metal-Responsive Transcription Factor, SmtB from Marine Synechococcus sp. PCC 7002. The Protein Journal. 32(8). 626–634. 1 indexed citations
11.
Inaba, Satomi, Harumi Fukada, Takahisa Ikegami, & Masayuki Oda. (2013). Thermodynamic effects of multiple protein conformations on stability and DNA binding. Archives of Biochemistry and Biophysics. 537(2). 225–232. 32 indexed citations
12.
13.
Fujiwara, Yoshie, Natsuko Goda, Takeshi Tenno, et al.. (2010). A Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtubule Severing and Membrane Skeleton Reorganization. Journal of Biological Chemistry. 285(22). 16822–16829. 30 indexed citations
14.
Benz, J. Philipp, Anna Stengel, Minna Lintala, et al.. (2009). Arabidopsis Tic62 and Ferredoxin-NADP(H) Oxidoreductase Form Light-Regulated Complexes That Are Integrated into the Chloroplast Redox Poise  . The Plant Cell. 21(12). 3965–3983. 97 indexed citations
15.
Akagi, Ken‐ichi, Jun Watanabe, Masashi Hara, et al.. (2006). Identification of the Substrate Interaction Region of the Chitin-Binding Domain of Streptomyces griseus Chitinase C. The Journal of Biochemistry. 139(3). 483–493. 49 indexed citations
16.
Morishita, Hirofumi, Masataka Umitsu, Yoji Murata, et al.. (2006). Structure of the Cadherin-related Neuronal Receptor/Protocadherin-α First Extracellular Cadherin Domain Reveals Diversity across Cadherin Families. Journal of Biological Chemistry. 281(44). 33650–33663. 60 indexed citations
17.
Lee, Young‐Ho, Masahiro Maeda, Masaru Hoshino, et al.. (2006). Cores and pH-dependent Dynamics of Ferredoxin-NADP+ Reductase Revealed by Hydrogen/Deuterium Exchange. Journal of Biological Chemistry. 282(8). 5959–5967. 22 indexed citations
18.
Matsuda, Tomoki, Takahisa Ikegami, Nobuyuki Nakajima, Toshio Yamazaki, & Haruki Nakamura. (2004). Model building of a protein-protein complexed structure using saturation transfer and residual dipolar coupling without paired intermolecular NOE. Journal of Biomolecular NMR. 29(3). 325–328. 18 indexed citations
19.
Inooka, Hiroshi, Tetsuya Ohtaki, Takahisa Ikegami, et al.. (2001). Conformation of a peptide ligand bound to its G-protein coupled receptor.. Nature Structural Biology. 8(2). 161–165. 145 indexed citations
20.
Ikegami, Takahisa, Isao Kuraoka, Masafumi Saijo, et al.. (1998). Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA. Nature Structural & Molecular Biology. 5(8). 701–706. 117 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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