Etsushiro Doi

3.7k total citations · 1 hit paper
140 papers, 3.1k citations indexed

About

Etsushiro Doi is a scholar working on Molecular Biology, Food Science and Biotechnology. According to data from OpenAlex, Etsushiro Doi has authored 140 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 51 papers in Food Science and 31 papers in Biotechnology. Recurrent topics in Etsushiro Doi's work include Proteins in Food Systems (44 papers), Enzyme Production and Characterization (26 papers) and Protein Hydrolysis and Bioactive Peptides (24 papers). Etsushiro Doi is often cited by papers focused on Proteins in Food Systems (44 papers), Enzyme Production and Characterization (26 papers) and Protein Hydrolysis and Bioactive Peptides (24 papers). Etsushiro Doi collaborates with scholars based in Japan, United Kingdom and Italy. Etsushiro Doi's co-authors include Naofumi Kitabatake, Teruyoshi Matoba, Daisuke Shibata, Tadao Hata, Taihei Koseki, Rikimaru Hayashi, Kaoru Kohyama, Yoh Sano, Hajime Hatta and Masaaki Hirose and has published in prestigious journals such as Biochemistry, Macromolecules and Analytical Biochemistry.

In The Last Decade

Etsushiro Doi

139 papers receiving 2.9k citations

Hit Papers

Modified colorimetric ninhydrin methods for peptidase assay 1981 2026 1996 2011 1981 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Etsushiro Doi Japan 30 1.5k 1.3k 467 400 385 140 3.1k
Henning Klostermeyer Germany 31 2.0k 1.4× 1.4k 1.0× 254 0.5× 492 1.2× 337 0.9× 129 3.6k
Antoine Puigserver France 32 484 0.3× 2.0k 1.5× 406 0.9× 591 1.5× 534 1.4× 142 4.0k
Fumio Yamauchi Japan 26 1.0k 0.7× 2.2k 1.7× 538 1.2× 354 0.9× 212 0.6× 161 3.8k
Yehudith Birk Israel 39 510 0.3× 2.1k 1.6× 1.4k 2.9× 386 1.0× 727 1.9× 138 4.1k
Stefania Iametti Italy 39 2.4k 1.6× 1.7k 1.3× 843 1.8× 1.6k 4.1× 422 1.1× 182 5.1k
Shigezo Udaka Japan 35 424 0.3× 3.0k 2.3× 416 0.9× 326 0.8× 1.3k 3.4× 188 4.4k
Makoto Yaguchi Canada 34 401 0.3× 2.4k 1.8× 807 1.7× 475 1.2× 1.2k 3.1× 133 4.0k
Ahmad Asoodeh Iran 32 336 0.2× 2.3k 1.7× 455 1.0× 188 0.5× 585 1.5× 156 3.5k
Robert M. Zacharius United States 15 313 0.2× 1.3k 1.0× 582 1.2× 229 0.6× 317 0.8× 33 2.5k
Bart Samyn Belgium 30 314 0.2× 1.3k 1.0× 522 1.1× 194 0.5× 365 0.9× 62 2.4k

Countries citing papers authored by Etsushiro Doi

Since Specialization
Citations

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

Fields of papers citing papers by Etsushiro Doi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Etsushiro Doi

This figure shows the co-authorship network connecting the top 25 collaborators of Etsushiro Doi. A scholar is included among the top collaborators of Etsushiro Doi 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 Etsushiro Doi. Etsushiro Doi 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.
Tani, Fumito, et al.. (1997). Temperature control for kinetic refolding of heat‐denatured ovalbumin. Protein Science. 6(7). 1491–1502. 40 indexed citations
2.
Kohyama, Kaoru, Yoh Sano, & Etsushiro Doi. (1995). Rheological Characteristics and Gelation Mechanism of Tofu (Soybean Curd). Journal of Agricultural and Food Chemistry. 43(7). 1808–1812. 203 indexed citations
3.
Nemoto, Norio, et al.. (1993). Dynamic light scattering of aqueous solutions of linear aggregates induced by thermal denaturation of ovalbumin. Biopolymers. 33(4). 551–559. 46 indexed citations
4.
Kitabatake, Naofumi, et al.. (1993). Toxicity evaluation of the mycotoxins, citrinin and ochratoxin a, using several animal cell lines. Comparative Biochemistry and Physiology Part C Comparative Pharmacology. 105(3). 429–433. 23 indexed citations
5.
Tani, Fumito, et al.. (1993). Heat-induced Transparent Gel from Hen Egg Lysozyme by a Two-step Heating Method. Bioscience Biotechnology and Biochemistry. 57(2). 209–214. 18 indexed citations
6.
Doi, Etsushiro, et al.. (1992). Detoxification of Ochratoxin A on Heating under Acidic and Alkaline Conditions. Bioscience Biotechnology and Biochemistry. 56(5). 741–745. 29 indexed citations
7.
Doi, Etsushiro, et al.. (1992). Cytotoxicity of Citrinin Heated at Temperatures above 100°C. Bioscience Biotechnology and Biochemistry. 56(3). 423–426. 7 indexed citations
8.
Takahashi, Nobuyuki, Taihei Koseki, Etsushiro Doi, & Masaaki Hirose. (1991). Role of an Intrachain Disulfide Bond in the Conformation and Stability of Ovalbumin. The Journal of Biochemistry. 109(6). 846–851. 37 indexed citations
9.
Takahashi, Nobuyuki, et al.. (1989). Effects of Anion Binding on the Conformations of the Two Domains of Ovotransferrin. The Journal of Biochemistry. 106(5). 858–863. 24 indexed citations
10.
Doi, Etsushiro. (1988). Mechanism of gel formation of food protein. Mechanism of gel formation of ovalbumin.. Nippon Nōgeikagaku Kaishi. 62(5). 886–888. 1 indexed citations
11.
Koseki, Taihei, Naofumi Kitabatake, & Etsushiro Doi. (1988). Conformational Changes in Ovalbumin at Acid pH. The Journal of Biochemistry. 103(3). 425–430. 59 indexed citations
12.
Hirose, Masaaki, et al.. (1988). Analyses of intramolecular disulfide bonds in proteins by polyacrylamide gel electrophoresis following two-step alkylation. Analytical Biochemistry. 168(1). 193–201. 24 indexed citations
13.
Kitabatake, Naofumi, Hirotaka Sasaki, & Etsushiro Doi. (1982). Scanning electron microscopy of freeze-dried protein foams.. Agricultural and Biological Chemistry. 46(11). 2881–2883. 4 indexed citations
14.
Doi, Etsushiro, et al.. (1975). Lysosomal enzyme activities in the central vacuole of the internodal cells of Nitella. Plant Science Letters. 4(4). 243–247. 6 indexed citations
15.
Doi, Etsushiro, Yukio Kawamura, Teruyoshi Matoba, & Tadao Hata. (1974). Cathepsin A of Two Different Molecular Sizes in Pig Kidney. The Journal of Biochemistry. 75(4). 889–894. 12 indexed citations
16.
Hayashi, Rikimaru, Y. OKA, Etsushiro Doi, & Tadao Hata. (1968). Activation of Intracellular Proteinases of Yeast:Part I. Occurrences of Inactive Precursors of Proteinases B and C and Their Activation. Agricultural and Biological Chemistry. 32(3). 359–366. 8 indexed citations
17.
Hayashi, Rikimaru, Y. OKA, Etsushiro Doi, & Tadao Hata. (1968). Activation of Intracellular Proteinases of Yeast:Part II. Activation and Some Properties of Pro-proteinase C. Agricultural and Biological Chemistry. 32(3). 367–373. 5 indexed citations
18.
Hata, Tadao, Rikimaru Hayashi, & Etsushiro Doi. (1967). Purification of Yeast Proteinases:Part I. Fractionation and Some Properties of the Proteinases. Agricultural and Biological Chemistry. 31(2). 150–159. 11 indexed citations
19.
Doi, Etsushiro, Rikimaru Hayashi, & Tadao Hata. (1967). Purification of Yeast Proteinases:Part II. Purification and Some Properties of Yeast Proteinase C. Agricultural and Biological Chemistry. 31(2). 160–169. 15 indexed citations
20.
Hata, Tadao & Etsushiro Doi. (1959). Measurement of Protease Activities Using the Dinitrophenyl Protein as the Substrate. Nippon Nōgeikagaku Kaishi. 33(5). 366–369. 2 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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