Bunzo Mikami

9.4k total citations · 1 hit paper
285 papers, 7.5k citations indexed

About

Bunzo Mikami is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, Bunzo Mikami has authored 285 papers receiving a total of 7.5k indexed citations (citations by other indexed papers that have themselves been cited), including 144 papers in Molecular Biology, 110 papers in Biotechnology and 87 papers in Plant Science. Recurrent topics in Bunzo Mikami's work include Enzyme Production and Characterization (106 papers), Enzyme Structure and Function (71 papers) and Phytase and its Applications (39 papers). Bunzo Mikami is often cited by papers focused on Enzyme Production and Characterization (106 papers), Enzyme Structure and Function (71 papers) and Phytase and its Applications (39 papers). Bunzo Mikami collaborates with scholars based in Japan, South Korea and United States. Bunzo Mikami's co-authors include Kousaku Murata, Wataru Hashimoto, Shigeru Utsumi, Motoyasu Adachi, Masaaki Hirose, Yukie Maruyama, Masayuki Yamasaki, Taro Masuda, Takafumi Itoh and H. Kurokawa and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Bunzo Mikami

279 papers receiving 7.3k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of antibodies and T cell receptors

2008 353 citations Yoshimasa Tanaka, Bunzo Mikami et al. profile →

Peers

Bunzo Mikami

BIOTE

Kousaku Murata Japan

Mirosław Cygler Canada

Masahiro Takagi Japan

David R. Rose Canada

P Andrews United Kingdom

Mark A. Hermodson United States

Takashi Matsumoto Japan

Tzu‐Ping Ko Taiwan

Nikolay E. Nifantiev Russia

Alan D. Elbein United States

Kousaku Murata Japan

Bunzo Mikami

11.5k ×3.2

2.6k ×1.3

BIOTE

3.1k ×1.6

782 ×0.6

1.0k ×1.1

Citations per year, relative to Bunzo Mikami Bunzo Mikami (= 1×) peers Kousaku Murata

Countries citing papers authored by Bunzo Mikami

Since Specialization

Citations

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

Fields of papers citing papers by Bunzo Mikami

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Bunzo Mikami

This figure shows the co-authorship network connecting the top 25 collaborators of Bunzo Mikami. A scholar is included among the top collaborators of Bunzo Mikami 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 Bunzo Mikami. Bunzo Mikami is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Kizuka, Yasuhiko, et al.. (2025). Enzymatic characterization and docking simulation of a xylan synthase catalytic subunit, <i>Setaria viridis</i> IRX10, using xylotrimer acceptors with distinct fluorescent labels. Plant Biotechnology. 42(2). 121–129.

Mikami, Bunzo, Aina Gotoh, Toshihiko Katoh, et al.. (2025). Suppression of fecal phenol production by oral supplementation of sesamol: inhibition of tyrosine phenol-lyase by sesamol. Food & Function. 16(9). 3542–3552. 1 indexed citations

Takita, Teisuke, et al.. (2024). Unveiling the reaction mechanism of arginine decarboxylase in Aspergillus oryzae: Insights from crystal structure analysis. Biochemical and Biophysical Research Communications. 733. 150728–150728. 1 indexed citations

Fujita, Ken‐ichi, Naoko Fujiwara, Tomohiro Yamazaki, et al.. (2024). Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes. Nature Communications. 15(1). 455–455. 7 indexed citations

Kondo, Keiko, et al.. (2023). Structural insights into the molecular mechanisms of substrate recognition and hydrolysis by feruloyl esterase from Aspergillus sydowii. International Journal of Biological Macromolecules. 253(Pt 5). 127188–127188. 6 indexed citations

Kobayashi, K., Masaomi Yamamura, Bunzo Mikami, et al.. (2023). Anthriscus sylvestris Deoxypodophyllotoxin Synthase Involved in the Podophyllotoxin Biosynthesis. Plant and Cell Physiology. 64(12). 1436–1448. 4 indexed citations

Kitagawa, Y., Teisuke Takita, Keisuke Tanaka, et al.. (2023). Insights into the catalytic mechanism of Grimontia hollisae collagenase through structural and mutational analyses. FEBS Letters. 597(19). 2473–2483. 1 indexed citations

Takehara, Sayaka, Aya Ito, Yosuke Toda, et al.. (2022). Evolutionary alterations in gene expression and enzymatic activities of gibberellin 3-oxidase 1 in Oryza. Communications Biology. 5(1). 13 indexed citations

Hibi, Makoto, Ryotaro Hara, Michiki Takeuchi, et al.. (2021). A three-component monooxygenase from Rhodococcus wratislaviensis may expand industrial applications of bacterial enzymes. Communications Biology. 4(1). 16–16. 6 indexed citations

10.

Masuda, Taro, Seiki Baba, Koichi Matsuo, Shinji Ito, & Bunzo Mikami. (2020). The high-resolution crystal structure of lobster hemocyanin shows its enzymatic capability as a phenoloxidase. Archives of Biochemistry and Biophysics. 688. 108370–108370. 13 indexed citations

11.

Takehara, Sayaka, Maki Onda, Juan Zhang, et al.. (2009). The 2.1-Å Crystal Structure of Native Neuroserpin Reveals Unique Structural Elements That Contribute to Conformational Instability. Journal of Molecular Biology. 388(1). 11–20. 37 indexed citations

12.

Terawaki, Seigo, Yoshimasa Tanaka, Tateki Hayashi, et al.. (2007). Specific and high-affinity binding of tetramerized PD-L1 extracellular domain to PD-1-expressing cells: possible application to enhance T cell function. International Immunology. 19(7). 881–890. 11 indexed citations

13.

Itoh, Takafumi, Motoyasu Adachi, Yukie Maruyama, et al.. (2006). Structure of 8Sα globulin, the major seed storage protein of mung bean. Acta Crystallographica Section D Biological Crystallography. 62(7). 824–832. 44 indexed citations

14.

Aso, Yuji, Yukiko Miyamoto, Keiko Momma, et al.. (2006). Engineered membrane superchannel improves bioremediation potential of dioxin-degrading bacteria. Nature Biotechnology. 24(2). 188–189. 40 indexed citations

15.

Miyagawa, Fumi, Yoshimasa Tanaka, Bunzo Mikami, et al.. (2001). Essential Contribution of Germline-Encoded Lysine Residues in Jγ1.2 Segment to the Recognition of Nonpeptide Antigens by Human γδ T Cells. The Journal of Immunology. 167(12). 6773–6779. 74 indexed citations

16.

Yoon, Hye‐Jin, Yong-Jin Choi, Osamu Miyake, et al.. (2001). Effect of His192 mutation on the activity of alginate lyase A1-III from Sphingomonas species A1. Journal of Microbiology and Biotechnology. 11(1). 118–123. 6 indexed citations

17.

Hashimoto, Wataru, Keiko Momma, Yumiko Mishima, Bunzo Mikami, & Kousaku Murata. (2001). Super-channel in Bacteria: Function and Structure of a Macromolecule Import System Mediated by a Pit-dependent ABC Transporter. Bioscience Biotechnology and Biochemistry. 65(9). 1949–1956. 10 indexed citations

18.

Korematsu, Seigo, Yoshimasa Tanaka, Susumu Hosoi, et al.. (2000). C8/119S Mutation of Major Mite Allergen Derf-2 Leads to Degenerate Secondary Structure and Molecular Polymerization and Induces Potent and Exclusive Th1 Cell Differentiation. The Journal of Immunology. 165(5). 2895–2902. 42 indexed citations

19.

Yoon, Hye‐Jin, et al.. (1999). Structure of the Starch-Binding Domain of Bacillus cereus $\beta-Amylase$. Journal of Microbiology and Biotechnology. 9(5). 619–623. 5 indexed citations

20.

Sano, Satoshi, Chikahiro Miyake, Bunzo Mikami, & Kozi Asada. (1995). Molecular Characterization of Monodehydroascorbate Radical Reductase from Cucumber Highly Expressed in Escherichia coli. Journal of Biological Chemistry. 270(36). 21354–21361. 61 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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