Toshio Fukui

2.3k total citations
109 papers, 1.7k citations indexed

About

Toshio Fukui is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, Toshio Fukui has authored 109 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Molecular Biology, 41 papers in Biotechnology and 26 papers in Plant Science. Recurrent topics in Toshio Fukui's work include Enzyme Production and Characterization (41 papers), Microbial Metabolites in Food Biotechnology (17 papers) and Enzyme Structure and Function (16 papers). Toshio Fukui is often cited by papers focused on Enzyme Production and Characterization (41 papers), Microbial Metabolites in Food Biotechnology (17 papers) and Enzyme Structure and Function (16 papers). Toshio Fukui collaborates with scholars based in Japan, United States and France. Toshio Fukui's co-authors include Shoji Shimomura, Mitsuo Tagaya, Katsuyuki Tanizawa, Masamitsu Futai, K. Nakano, Zirô NIKUNI, Yasuaki Kazuta, Hiroyuki Mori, Bernard Axelrod and Masao Kawakita and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Toshio Fukui

106 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Toshio Fukui Japan 26 1.0k 493 450 355 212 109 1.7k
G. Marchis-Mouren France 27 941 0.9× 351 0.7× 710 1.6× 356 1.0× 169 0.8× 72 1.8k
Shigeo Aibara Japan 21 561 0.5× 409 0.8× 210 0.5× 137 0.4× 128 0.6× 75 1.2k
Harold M. Flowers Israel 28 1.4k 1.3× 279 0.6× 302 0.7× 246 0.7× 71 0.3× 76 1.9k
Noshi Minamiura Japan 19 592 0.6× 234 0.5× 522 1.2× 379 1.1× 53 0.3× 81 1.2k
Irmentraut Löw Germany 20 823 0.8× 333 0.7× 91 0.2× 152 0.4× 76 0.4× 41 1.8k
Anja Rabijns Belgium 23 513 0.5× 694 1.4× 595 1.3× 697 2.0× 109 0.5× 44 1.6k
A.N. Radhakrishnan India 21 763 0.7× 145 0.3× 93 0.2× 142 0.4× 105 0.5× 73 1.3k
Sara H. Goldemberg Argentina 14 661 0.6× 101 0.2× 138 0.3× 139 0.4× 53 0.3× 27 1.0k
R. D. Poretz United States 21 847 0.8× 193 0.4× 134 0.3× 135 0.4× 81 0.4× 59 1.4k
John Londesborough Finland 30 2.1k 2.0× 763 1.5× 243 0.5× 140 0.4× 159 0.8× 75 2.7k

Countries citing papers authored by Toshio Fukui

Since Specialization
Citations

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

Fields of papers citing papers by Toshio Fukui

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Toshio Fukui

This figure shows the co-authorship network connecting the top 25 collaborators of Toshio Fukui. A scholar is included among the top collaborators of Toshio Fukui 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 Toshio Fukui. Toshio Fukui 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.
Hossain, Shaikh Abu, Katsuyuki Tanizawa, Yasuaki Kazuta, & Toshio Fukui. (1994). Overproduction and Characterization of Recombinant UDP-Glucose Pyrophosphorylase from Escherichia coli K-121. The Journal of Biochemistry. 115(5). 965–972. 32 indexed citations
2.
Matsuyama, Takahiro, et al.. (1992). Leucine Dehydrogenase from Bacillus stearothermophilus: Identification of Active-Site Lysine by Modification with Pyridoxal Phosphate1. The Journal of Biochemistry. 112(2). 258–265. 18 indexed citations
3.
Katsube, Takuya, Yasuaki Kazuta, Hiroyuki Mori, et al.. (1990). UDP-Glucose Pyrophosphorylase from Potato Tuber: cDNA Cloning and Sequencing1. The Journal of Biochemistry. 108(2). 321–326. 52 indexed citations
4.
Nakano, K., Hiroyuki Mori, & Toshio Fukui. (1989). Molecular Cloning of cDNA Encoding Potato Amyloplast a-Glucan Phosphorylase and the Structure of Its Transit Peptide1. The Journal of Biochemistry. 106(4). 691–695. 30 indexed citations
5.
Tagaya, Mitsuo, Takato Noumi, K. Nakano, Masamitsu Futai, & Toshio Fukui. (1988). Identification of α‐subunit Lys201 and β‐subunit Lys115 at the ATP‐binding sites inEscherichia coli F1‐ATPase. FEBS Letters. 233(2). 347–351. 38 indexed citations
6.
Fujita, Takanori, et al.. (1988). NY-198の基礎的, 臨床的検討. Chemotherapy. 36(2). 499–512. 1 indexed citations
7.
Fukui, Toshio, et al.. (1988). Basic and clinical studies on RU 28965. Chemotherapy. 36(4). 266–276. 4 indexed citations
8.
Homma, Satoki, et al.. (1988). BACTERIOLOGICAL AND CLINICAL STUDY OF CEFOTIAM HEXETIL. Chemotherapy. 36(6). 264–281. 1 indexed citations
9.
Tagaya, Mitsuo & Toshio Fukui. (1986). Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal.. Biochemistry. 25(10). 2958–2964. 47 indexed citations
10.
Fukui, Toshio, et al.. (1975). α-Glucan phosphorylase from sweet potato: Isolation and properties of the partially degraded enzyme. Biochimica et Biophysica Acta (BBA) - Protein Structure. 386(1). 301–308. 13 indexed citations
11.
Yokobayashi, Kozi, et al.. (1973). Purification and Properties of Maltose Phosphorylase fromLactobacillus brevis. Agricultural and Biological Chemistry. 37(12). 2813–2819. 19 indexed citations
12.
Doi, Kenji, et al.. (1971). Joint Action of Two Glucanases Produced by Arshrobacier in Spheroplast Formation from Baker's Yeast. The Journal of Biochemistry. 70(4). 711–714. 17 indexed citations
13.
Fukui, Toshio, et al.. (1969). Structure and Function of Potato α-Glucan Phosphorylase ; Comparison with the Muscle Enzyme. 17(1). 117–129. 1 indexed citations
14.
Fukui, Toshio & Zirô NIKUNI. (1969). Heat-Moisture Treatment of Cereal Starch Observed by X-ray Diffraction. Agricultural and Biological Chemistry. 33(3). 460–462. 2 indexed citations
15.
Fukui, Toshio, et al.. (1968). Potato alpha-glucan phosphorylase: crystallization, amino acid composition and enzymatic reaction in the absence of added primer.. PubMed. 63(3). 361–9. 33 indexed citations
16.
Fukui, Toshio, et al.. (1967). Remarks on Finite Commutative z-Semigroups. 16. 1–11. 2 indexed citations
17.
Fukui, Toshio, M. Fujii, & Zirô NIKUNI. (1964). Digestion of Raw Starch Granules by the Action of Amylase, Particualary on the Rice Starch Granule. Nippon Nōgeikagaku Kaishi. 38(5). 262–266. 5 indexed citations
18.
Harada, Tokuya, et al.. (1963). The Composition of Extracellular Polysaccharides of Rhodotorula. Nippon Nōgeikagaku Kaishi. 37(4). 226–230. 2 indexed citations
19.
Fukui, Toshio & Bernard Axelrod. (1961). Enzymatic Formation of Lipo-amino Acids by Rat Liver Preparations and the Nature of the Product. Journal of Biological Chemistry. 236(3). 811–816. 29 indexed citations
20.
Fukui, Toshio & Zirô NIKUNI. (1959). Changes in Sugar Contents during the Germination of Rice Seeds. Nippon Nōgeikagaku Kaishi. 33(1). 72–78. 4 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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