Kazuhiko Ishikawa

3.0k total citations
144 papers, 2.4k citations indexed

About

Kazuhiko Ishikawa is a scholar working on Molecular Biology, Biotechnology and Biomedical Engineering. According to data from OpenAlex, Kazuhiko Ishikawa has authored 144 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 92 papers in Molecular Biology, 63 papers in Biotechnology and 52 papers in Biomedical Engineering. Recurrent topics in Kazuhiko Ishikawa's work include Enzyme Production and Characterization (61 papers), Biofuel production and bioconversion (48 papers) and Enzyme Structure and Function (32 papers). Kazuhiko Ishikawa is often cited by papers focused on Enzyme Production and Characterization (61 papers), Biofuel production and bioconversion (48 papers) and Enzyme Structure and Function (32 papers). Kazuhiko Ishikawa collaborates with scholars based in Japan, India and South Korea. Kazuhiko Ishikawa's co-authors include Ikuo Matsui, Han‐Woo Kim, Hiroyasu Ishida, Koichi Honda, Sung‐Jong Jeon, Hiroyuki Inoue, Tatsuya Fujii, Koshiki Mino, Koichi Uegaki and Yoshitsugu Kosugi and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Applied and Environmental Microbiology.

In The Last Decade

Kazuhiko Ishikawa

140 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kazuhiko Ishikawa Japan 31 1.6k 988 817 416 415 144 2.4k
Torben V. Borchert Denmark 25 2.1k 1.3× 1.4k 1.4× 801 1.0× 528 1.3× 646 1.6× 34 3.1k
T. Imanaka Japan 29 1.9k 1.2× 1.1k 1.1× 366 0.4× 574 1.4× 485 1.2× 77 3.3k
Colin Mitchinson United States 22 1.5k 1.0× 762 0.8× 1.2k 1.5× 228 0.5× 420 1.0× 32 2.3k
Hannu Maaheimo Finland 30 1.9k 1.2× 397 0.4× 776 0.9× 132 0.3× 575 1.4× 87 2.9k
Thorsten Eggert Germany 29 3.3k 2.1× 550 0.6× 622 0.8× 297 0.7× 354 0.9× 49 3.8k
Xueqin Lv China 36 2.7k 1.7× 496 0.5× 718 0.9× 238 0.6× 419 1.0× 187 4.0k
Mohini S. Ghatge United States 16 1.6k 1.0× 1.3k 1.3× 182 0.2× 203 0.5× 682 1.6× 48 2.5k
Lujia Zhang China 27 1.2k 0.8× 320 0.3× 281 0.3× 206 0.5× 178 0.4× 126 2.1k
Jürgen Seibel Germany 31 1.5k 1.0× 810 0.8× 373 0.5× 140 0.3× 427 1.0× 103 3.0k

Countries citing papers authored by Kazuhiko Ishikawa

Since Specialization
Citations

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

Fields of papers citing papers by Kazuhiko Ishikawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kazuhiko Ishikawa

This figure shows the co-authorship network connecting the top 25 collaborators of Kazuhiko Ishikawa. A scholar is included among the top collaborators of Kazuhiko Ishikawa 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 Kazuhiko Ishikawa. Kazuhiko Ishikawa 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.
Ishikawa, Kazuhiko, et al.. (2024). Effects of heterologous expression and N-glycosylation on the hyperthermostable endoglucanase of Pyrococcus furiosus. Journal of Bioscience and Bioengineering. 137(5). 329–334.
2.
Uechi, Keiko, et al.. (2022). Structural Analysis and Construction of a Thermostable Antifungal Chitinase. Applied and Environmental Microbiology. 88(12). e0065222–e0065222. 16 indexed citations
3.
Kim, Han‐Woo, et al.. (2022). Recognition mechanism of endocellulase for β-glucan containing β(1 → 3),(1 → 4) mixed-linkages. Carbohydrate Research. 522. 108682–108682. 2 indexed citations
4.
Fujiwara, Masahiro, et al.. (2020). Macroporous Silica Microcapsules Immobilizing Esterase with High Hydrolysis Reactivity. Bulletin of the Chemical Society of Japan. 93(9). 1043–1045. 6 indexed citations
5.
Fujii, Tatsuya, Hiroyuki Inoue, Kazuhiko Ishikawa, & Tamotsu Hoshino. (2017). Deletion Analysis of GH7 Endoglucanase Gene (cel7B) Promoter Region in a Talaromyces cellulolyticus ligD-Disrupted Strain. Applied Biochemistry and Biotechnology. 183(4). 1516–1525. 4 indexed citations
6.
Ishikawa, Kazuhiko, et al.. (2017). Accurate measurement of the optical activity of alanine crystals and the determination of their absolute chirality. Journal of Physics and Chemistry of Solids. 104. 257–266. 8 indexed citations
7.
Nakabayashi, Makoto, et al.. (2014). Structural analysis of β-glucosidase mutants derived from a hyperthermophilic tetrameric structure. Acta Crystallographica Section D Biological Crystallography. 70(3). 877–888. 8 indexed citations
8.
Ishikawa, Kazuhiko, et al.. (2014). Crystal structure of (S)-4-carbamoyl-4-(1,3-dioxoisoindolin-2-yl)butanoic acid. Acta Crystallographica Section E Crystallographic Communications. 71(1). 107–109. 4 indexed citations
9.
Watanabe, Seiya, et al.. (2014). RNAi Knockdown of Potent Sugar Sensor in Cellulase-Producing Fungus Acremonium cellulolyticus. Applied Biochemistry and Biotechnology. 172(6). 3009–3015. 3 indexed citations
10.
Hirano, Yuki, Ngoc‐Anh Le, Nana Kawasaki, et al.. (2012). Functional Regulation of Sugar Assimilation by N-Glycan-specific Interaction of Pancreatic α-Amylase with Glycoproteins of Duodenal Brush Border Membrane. Journal of Biological Chemistry. 287(27). 23104–23118. 21 indexed citations
11.
Nishioka, Masateru, et al.. (2008). Alteration of metal ions improves the activity and thermostability of aminoacylase from hyperthermophilic archaeon Pyrococcus horikoshii. Biotechnology Letters. 30(9). 1639–1643. 3 indexed citations
12.
Ishikawa, Kazuhiko, Hiroshi Nakatani, Yoshio Katsuya, & Chikafusa Fukazawa. (2006). Kinetic and Structural Analysis of Enzyme Sliding on a Substrate:  Multiple Attack in β-Amylase. Biochemistry. 46(3). 792–798. 18 indexed citations
13.
Nakamura, T., Shouhei Mine, Yoshihisa Hagihara, Kazuhiko Ishikawa, & Koichi Uegaki. (2006). Structure of the catalytic domain of the hyperthermophilic chitinase fromPyrococcus furiosus. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(1). 7–11. 30 indexed citations
14.
Matsubara, Seijiro, Hideaki Yoshino, Yuhei Yamamoto, et al.. (2005). Structure and reactivity of bis(iodozincio)methane solution. Journal of Organometallic Chemistry. 690(24-25). 5546–5551. 12 indexed citations
15.
Mori, Kazushige, et al.. (2004). Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose. Extremophiles. 9(1). 37–43. 34 indexed citations
16.
Ishikawa, Kazuhiko, et al.. (2003). A hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii. Archives of Biochemistry and Biophysics. 418(2). 179–185. 37 indexed citations
17.
Kosugi, Yoshitsugu, et al.. (2002). Kinetic study of sn‐glycerol‐1‐phosphate dehydrogenase from the aerobic hyperthermophilic archaeon, Aeropyrum pernix K1. European Journal of Biochemistry. 269(3). 969–976. 16 indexed citations
18.
Aoki, Takayoshi, et al.. (1997). Principle of structural restoration for Hagia Sophia Dome. WIT transactions on the built environment. 29. 467–476. 3 indexed citations
19.
Ueda, Masahiro, et al.. (1993). Thickness Measurement of Polyethylene Foam by Light Attenuation.. The Review of Laser Engineering. 21(12). 1266–1272. 5 indexed citations
20.
Matsui, Ikuo, Kazuhiko Ishikawa, Sachio Miyairi, Sakuzo Fukui, & Koichi Honda. (1992). A mutant α‐amylase with enhanced activity specific for short substrates. FEBS Letters. 310(3). 216–218. 14 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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