Koji Inaka

2.2k total citations
75 papers, 1.6k citations indexed

About

Koji Inaka is a scholar working on Materials Chemistry, Molecular Biology and Oncology. According to data from OpenAlex, Koji Inaka has authored 75 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 48 papers in Materials Chemistry, 45 papers in Molecular Biology and 8 papers in Oncology. Recurrent topics in Koji Inaka's work include Enzyme Structure and Function (46 papers), Protein Structure and Dynamics (23 papers) and Crystallization and Solubility Studies (10 papers). Koji Inaka is often cited by papers focused on Enzyme Structure and Function (46 papers), Protein Structure and Dynamics (23 papers) and Crystallization and Solubility Studies (10 papers). Koji Inaka collaborates with scholars based in Japan, United States and Hungary. Koji Inaka's co-authors include Masaaki Matsushima, Kunio Miki, Masakazu Kikuchi, Hiroaki Tanaka, S. Takahashi, Shigeru Sugiyama, Ryota Kuroki, Satoshi Sano, H Nishida and Masaru Satô and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Koji Inaka

71 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Koji Inaka Japan 22 959 541 215 140 121 75 1.6k
Jonathan A. R. Worrall United Kingdom 27 1.5k 1.5× 468 0.9× 82 0.4× 96 0.7× 251 2.1× 79 2.1k
Laurence Serre France 22 1.5k 1.5× 285 0.5× 225 1.0× 125 0.9× 283 2.3× 44 2.1k
Timothy D. Fenn United States 23 1.2k 1.3× 442 0.8× 110 0.5× 139 1.0× 327 2.7× 30 1.8k
Arnaud Bondon France 26 732 0.8× 468 0.9× 151 0.7× 80 0.6× 174 1.4× 104 2.0k
Andrea M. Hounslow United Kingdom 29 1.3k 1.4× 530 1.0× 109 0.5× 99 0.7× 145 1.2× 76 2.1k
Filomena Sica Italy 29 2.2k 2.3× 691 1.3× 116 0.5× 61 0.4× 150 1.2× 102 2.6k
Françoise Guerlesquin France 31 1.6k 1.6× 315 0.6× 96 0.4× 53 0.4× 263 2.2× 97 2.3k
Ulrike Wagner Austria 19 1.2k 1.3× 296 0.5× 157 0.7× 85 0.6× 78 0.6× 65 1.9k
Edward A. Burstein Russia 19 1.7k 1.8× 425 0.8× 175 0.8× 174 1.2× 337 2.8× 36 2.4k
Kosuke Dodo Japan 26 1.5k 1.5× 218 0.4× 154 0.7× 101 0.7× 122 1.0× 83 3.0k

Countries citing papers authored by Koji Inaka

Since Specialization
Citations

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

Fields of papers citing papers by Koji Inaka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Koji Inaka

This figure shows the co-authorship network connecting the top 25 collaborators of Koji Inaka. A scholar is included among the top collaborators of Koji Inaka 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 Koji Inaka. Koji Inaka 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.
Hirokawa, Takatsugu, et al.. (2024). Structural insights into molecular-targeting helix–loop–helix peptide against vascular endothelial growth factor-A. Biochemical and Biophysical Research Communications. 734. 150749–150749. 1 indexed citations
2.
Okuda‐Shimazaki, Junko, Hiromi Yoshida, In‐Young Lee, et al.. (2022). Microgravity environment grown crystal structure information based engineering of direct electron transfer type glucose dehydrogenase. Communications Biology. 5(1). 1334–1334. 10 indexed citations
3.
Takahashi, S., et al.. (2021). Novel Device and Strategy for Growing Large, High-Quality Protein Crystals by Controlling Crystallization Conditions. Crystals. 11(11). 1311–1311. 1 indexed citations
4.
Inaka, Koji, et al.. (2020). Methods for Obtaining Better Diffractive Protein Crystals: From Sample Evaluation to Space Crystallization. Crystals. 10(2). 78–78. 12 indexed citations
5.
Nakamura, Hirohiko, S. Takahashi, Koji Inaka, & Hiroaki Tanaka. (2020). Semi-empirical model to estimate ideal conditions for the growth of large protein crystals. Acta Crystallographica Section D Structural Biology. 76(12). 1174–1183. 1 indexed citations
6.
Takaya, Daisuke, Koji Inaka, Kenji Takenuki, et al.. (2018). Characterization of crystal water molecules in a high-affinity inhibitor and hematopoietic prostaglandin D synthase complex by interaction energy studies. Bioorganic & Medicinal Chemistry. 26(16). 4726–4734. 14 indexed citations
7.
Nakamura, Akihiko, Takuya Ishida, Katsuhiro Kusaka, et al.. (2015). “Newton’s cradle” proton relay with amide–imidic acid tautomerization in inverting cellulase visualized by neutron crystallography. Science Advances. 1(7). e1500263–e1500263. 69 indexed citations
8.
Suzuki, Yoshiyuki, Koji Inaka, Hiroaki Tanaka, et al.. (2015). Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. Scientific Reports. 5(1). 11151–11151. 10 indexed citations
9.
Higashiura, Akifumi, Kazunori Ohta, Masaru Satô, et al.. (2013). High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method. Journal of Synchrotron Radiation. 20(6). 989–993. 4 indexed citations
10.
Tanaka, Hiroaki, Toshiharu Tsurumura, Kosuke Aritake, et al.. (2010). Improvement in the quality of hematopoietic prostaglandin D synthase crystals in a microgravity environment. Journal of Synchrotron Radiation. 18(1). 88–91. 19 indexed citations
11.
Takahashi, S., Hiroaki Tanaka, Masaru Satô, et al.. (2008). Protein crystallization strategy in microgravity. Acta Crystallographica Section A Foundations of Crystallography. 64(a1). C581–C582. 2 indexed citations
12.
Tanaka, Hiroaki, Masaru Satô, Koji Inaka, et al.. (2007). Prediction of improvement of protein crystal quality grown in microgravity. Acta Crystallographica Section A Foundations of Crystallography. 63(a1). s137–s138. 5 indexed citations
13.
Taniguchi, Taizo, Miho Sumida, Koji Tomoo, et al.. (2005). Effects of different anti‐tau antibodies on tau fibrillogenesis: RTA‐1 and RTA‐2 counteract tau aggregation. FEBS Letters. 579(6). 1399–1404. 29 indexed citations
14.
Hiramatsu, Hajime, Kiyoshi Kyono, Hideaki Shima, et al.. (2003). Crystallization and preliminary X-ray study of human dipeptidyl peptidase IV (DPPIV). Acta Crystallographica Section D Biological Crystallography. 59(3). 595–596. 6 indexed citations
15.
Inaka, Koji, Eiko Kanaya, Masakazu Kikuchi, & Kunio Miki. (2001). Crystal structure of a mutant human lysozyme with a substituted disulfide bond. Proteins Structure Function and Bioinformatics. 43(4). 413–419. 2 indexed citations
16.
Kita, Akiko, Koji Inaka, Takao Ishida, et al.. (1997). Crystallization and Preliminary X-Ray Diffraction Studies of Expressed Pseudomonas putida Catechol 2,3-Dioxygenase. The Journal of Biochemistry. 122(1). 201–204. 8 indexed citations
17.
18.
Yamada, Hirofumi, et al.. (1994). Stabilization and Enhanced Enzymatic Activities of a Mutant Human Lysozyme C77/95A with a Cavity Space by Amino Acid Substitution.. Biological and Pharmaceutical Bulletin. 17(2). 192–196. 6 indexed citations
19.
Katayama, Naoko, Masayuki Kobayashi, Fumihiro Motojima, et al.. (1994). Preliminary X‐ray crystallographic studies of photosynthetic reaction center from a thermophilic sulfur bacterium, Chromatium tepidum. FEBS Letters. 348(2). 158–160. 15 indexed citations
20.
Kidera, Akinori, Koji Inaka, Masaaki Matsushima, & Nobuhiro Gō. (1992). Normal mode refinement: Crystallographic refinement of protein dynamic structure applied to human lysozyme. Biopolymers. 32(4). 315–319. 11 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Jonathan A. R. Worrall Breakdown of academic impact, for papers by Laurence Serre Breakdown of academic impact, for papers by Timothy D. Fenn Breakdown of academic impact, for papers by Arnaud Bondon Breakdown of academic impact, for papers by Andrea M. Hounslow Breakdown of academic impact, for papers by Filomena Sica Breakdown of academic impact, for papers by Françoise Guerlesquin Breakdown of academic impact, for papers by Ulrike Wagner Breakdown of academic impact, for papers by Edward A. Burstein Breakdown of academic impact, for papers by Kosuke Dodo
Rankless by CCL
2026