Koki Makabe

1.9k total citations
76 papers, 1.5k citations indexed

About

Koki Makabe is a scholar working on Molecular Biology, Materials Chemistry and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Koki Makabe has authored 76 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 55 papers in Molecular Biology, 18 papers in Materials Chemistry and 17 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Koki Makabe's work include Protein Structure and Dynamics (25 papers), Enzyme Structure and Function (18 papers) and Monoclonal and Polyclonal Antibodies Research (17 papers). Koki Makabe is often cited by papers focused on Protein Structure and Dynamics (25 papers), Enzyme Structure and Function (18 papers) and Monoclonal and Polyclonal Antibodies Research (17 papers). Koki Makabe collaborates with scholars based in Japan, United States and Thailand. Koki Makabe's co-authors include Shohei Koide, Akiko Koide, Matthew Biancalana, Izumi Kumagai, Ryutaro Asano, Kouhei Tsumoto, Kunihiro Kuwajima, Jin Huang, Toshio Kudo and Takashi Nakamura and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Koki Makabe

71 papers receiving 1.5k citations

Peers

Koki Makabe
Marcel Joniau Belgium
Marjolein Thunnissen Sweden
Michael D. Scholle United States
Hans Ippel Netherlands
Yoshiaki Yano Japan
Henryk Mach United States
Eugene C. Petrella United States
Shawn DeFrees United States
Massimiliano Meli Italy
Nicholas M. I. Taylor Denmark
Marcel Joniau Belgium
Koki Makabe
Citations per year, relative to Koki Makabe Koki Makabe (= 1×) peers Marcel Joniau

Countries citing papers authored by Koki Makabe

Since Specialization
Citations

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

Fields of papers citing papers by Koki Makabe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Koki Makabe

This figure shows the co-authorship network connecting the top 25 collaborators of Koki Makabe. A scholar is included among the top collaborators of Koki Makabe 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 Koki Makabe. Koki Makabe 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.
Matsui, Takashi, Christos G. Gkogkas, Takeshi Yokoyama, et al.. (2025). Bispecific antibody-antigen complex structures reveal activity enhancement by domain rearrangement. Cell Reports. 44(7). 115965–115965.
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Asanuma, Taketoshi, et al.. (2025). Evaluation of an anti-CD3 VHH and construction of an anti-CD3/anti-EGFR bispecific tandem VHH as a cancer cell targeting drug construct. Biochemistry and Biophysics Reports. 42. 102015–102015. 1 indexed citations
4.
Yoshida, Junji, Yoshikazu Tanaka, Izumi Kumagai, et al.. (2024). Construction of bispecific antibodies by specific pairing between the heavy chain and the light chain using removable SpyCatcher/SnoopCatcher units. Journal of Biological Engineering. 18(1). 57–57. 1 indexed citations
5.
Xu, Fusheng, et al.. (2024). Synthesis and evaluation of catecholamine derivatives as amyloid-beta aggregation inhibitors. Bioorganic & Medicinal Chemistry Letters. 107. 129788–129788. 2 indexed citations
6.
Takahashi, Masaki, et al.. (2024). Domain structure and function of α-1,3-glucanase Agl-EK14 from the gram-negative bacterium Flavobacterium sp. EK-14. Journal of Bioscience and Bioengineering. 138(2). 118–126.
7.
Takahashi, Masaki, Shigekazu Yano, Wasana Suyotha, et al.. (2023). α-1,3-Glucanase from the gram-negative bacterium Flavobacterium sp. EK-14 hydrolyzes fungal cell wall α-1,3-glucan. Scientific Reports. 13(1). 21420–21420. 2 indexed citations
8.
Xu, Fusheng, et al.. (2023). Synthesis and evaluation of l-dopa and L-Tyr derivatives as amyloid-beta aggregation inhibitors. Phytochemistry Letters. 57. 239–247. 2 indexed citations
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Makabe, Koki, et al.. (2023). Aspergillus oryzae α‐ l ‐rhamnosidase: Crystal structure and insight into the substrate specificity. Proteins Structure Function and Bioinformatics. 92(2). 236–245. 4 indexed citations
11.
Koseki, Takuya, et al.. (2022). Mutational analysis of the effects of N-glycosylation sites on the activity and thermal stability of rutinosidase from Aspergillus oryzae. Enzyme and Microbial Technology. 161. 110112–110112. 6 indexed citations
12.
Yamada, Ryo, et al.. (2021). The total synthesis of berberine and selected analogues, and their evaluation as amyloid beta aggregation inhibitors. European Journal of Medicinal Chemistry. 215. 113289–113289. 25 indexed citations
13.
Makabe, Koki, et al.. (2020). Aspergillus oryzae Rutinosidase: Biochemical and Structural Investigation. Applied and Environmental Microbiology. 87(3). 13 indexed citations
14.
Fujiwara, Hideki, et al.. (2020). Cooperative unfolding of a single-layer β-sheet protein, CPAP G-box. Biochemical and Biophysical Research Communications. 526(1). 105–109. 1 indexed citations
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16.
Nakamura, Takashi, Koki Makabe, Toshio Takenaka, et al.. (2013). The H/D-Exchange Kinetics of the Escherichia coli Co-Chaperonin GroES Studied by 2D NMR and DMSO-Quenched Exchange Methods. Journal of Molecular Biology. 425(14). 2541–2560. 10 indexed citations
17.
Chen, Jin, Hisashi Yagi, Pietro Sormanni, et al.. (2012). Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone. FEBS Letters. 586(8). 1120–1127. 16 indexed citations
18.
Mukaiyama, Atsushi, Takashi Nakamura, Koki Makabe, et al.. (2012). The Molten Globule of β2-Microglobulin Accumulated at pH 4 and Its Role in Protein Folding. Journal of Molecular Biology. 425(2). 273–291. 20 indexed citations
19.
Nakamura, Takashi, Koki Makabe, Katsuaki Tomoyori, et al.. (2010). Different Folding Pathways Taken by Highly Homologous Proteins, Goat α-Lactalbumin and Canine Milk Lysozyme. Journal of Molecular Biology. 396(5). 1361–1378. 22 indexed citations
20.
Huang, Jin, Akiko Koide, Koki Makabe, & Shohei Koide. (2008). Design of protein function leaps by directed domain interface evolution. Proceedings of the National Academy of Sciences. 105(18). 6578–6583. 81 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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