Koji Ikura

2.2k total citations
89 papers, 1.9k citations indexed

About

Koji Ikura is a scholar working on Pulmonary and Respiratory Medicine, Molecular Biology and Biotechnology. According to data from OpenAlex, Koji Ikura has authored 89 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Pulmonary and Respiratory Medicine, 34 papers in Molecular Biology and 21 papers in Biotechnology. Recurrent topics in Koji Ikura's work include Blood properties and coagulation (36 papers), Proteins in Food Systems (15 papers) and Erythrocyte Function and Pathophysiology (13 papers). Koji Ikura is often cited by papers focused on Blood properties and coagulation (36 papers), Proteins in Food Systems (15 papers) and Erythrocyte Function and Pathophysiology (13 papers). Koji Ikura collaborates with scholars based in Japan and United Kingdom. Koji Ikura's co-authors include Ryuzo Sasaki, Hideo Chiba, Masaaki Yoshikawa, Takashi Kometani, Hiroshi Narita, Shunji Natsuka, Ryuzo Sasaki, R Sasaki, Etsuro Sugimoto and Yoichi Tsuchiya and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Analytical Biochemistry.

In The Last Decade

Koji Ikura

89 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Koji Ikura Japan 25 712 661 417 321 313 89 1.9k
Hideo Chiba Japan 28 418 0.6× 1.5k 2.2× 604 1.4× 322 1.0× 241 0.8× 163 2.9k
Takashi Sasaki Japan 33 665 0.9× 1.5k 2.2× 120 0.3× 694 2.2× 450 1.4× 181 3.8k
Paul J. Birckbichler United States 21 1.3k 1.8× 536 0.8× 111 0.3× 381 1.2× 82 0.3× 27 2.1k
Takashi Murachi Japan 31 121 0.2× 1.7k 2.6× 43 0.1× 1.2k 3.6× 169 0.5× 108 2.7k
Jeong‐Yoon Kim South Korea 26 194 0.3× 1.5k 2.2× 76 0.2× 171 0.5× 149 0.5× 92 2.1k
Xin Hu China 28 235 0.3× 2.2k 3.3× 48 0.1× 152 0.5× 78 0.2× 96 3.1k
Nawneet K. Kurrey India 14 146 0.2× 1.2k 1.8× 195 0.5× 150 0.5× 111 0.4× 22 2.2k
Lizhi Lu China 17 101 0.1× 928 1.4× 298 0.7× 123 0.4× 98 0.3× 50 2.2k
Tetsuo Kimoto Japan 19 68 0.1× 470 0.7× 272 0.7× 65 0.2× 67 0.2× 70 1.4k

Countries citing papers authored by Koji Ikura

Since Specialization
Citations

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

Fields of papers citing papers by Koji Ikura

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Koji Ikura

This figure shows the co-authorship network connecting the top 25 collaborators of Koji Ikura. A scholar is included among the top collaborators of Koji Ikura 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 Koji Ikura. Koji Ikura 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.
Ichikawa, Akira, et al.. (2010). Overexpression of Transglutaminase in theDrosophilaWing Imaginal Disc Induced an Extra Wing Crossvein Phenotype. Bioscience Biotechnology and Biochemistry. 74(12). 2494–2496. 6 indexed citations
2.
Ichikawa, Akira, et al.. (2010). Over-expression of transglutaminase in the Drosophila eye imaginal disc induces a rough eye phenotype. Molecular and Cellular Biochemistry. 342(1-2). 223–232. 7 indexed citations
3.
Ichikawa, Akira, et al.. (2008). Identification of New Amine Acceptor Protein Substrate Candidates of Transglutaminase in Rat Liver Extract: Use of 5-(Biotinamido) Pentylamine as a Probe. Bioscience Biotechnology and Biochemistry. 72(4). 1056–1062. 8 indexed citations
4.
Natsuka, Shunji, et al.. (2005). Characterization of Wheat Germ Agglutinin Ligand on Soluble Glycoproteins in Caenorhabditis elegans. The Journal of Biochemistry. 138(2). 209–213. 20 indexed citations
5.
Ichikawa, Akira, et al.. (2004). In vitro modification of betaine-homocysteine S-methyltransferase by tissue-type transglutaminase. The International Journal of Biochemistry & Cell Biology. 36(10). 1981–1992. 12 indexed citations
6.
Kato, Toshihiko, Kiyotaka Fujita, Makoto Takeuchi, et al.. (2002). Identification of an endo- -N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli. Glycobiology. 12(10). 581–587. 59 indexed citations
7.
Ikura, Koji, Shunji Natsuka, Akira Ichikawa, et al.. (2002). CO-OVEREXPRESSION OF FOLDING MODULATORS IMPROVES THE SOLUBILITY OF THE RECOMBINANT GUINEA PIG LIVER TRANSGLUTAMINASE EXPRESSED INESCHERICHIA COLI. Preparative Biochemistry & Biotechnology. 32(2). 189–205. 31 indexed citations
8.
Masuda, Seiji, et al.. (1997). In vitro neurotoxicity of amyloid β-peptide cross-linked by transglutaminase. Cytotechnology. 23(1-3). 77–85. 9 indexed citations
9.
Hashimoto, Hiroyuki, Koji Ikura, Tatsuyuki Okinaga, et al.. (1996). Purification and some properties of cell-bound α-galactosidase from Candida guilliermondii H-404. Journal of Applied Glycoscience. 43(1). 25–33. 2 indexed citations
10.
11.
Ikura, Koji, et al.. (1994). Increase Caused by Interleukin-6 in Promoter Activity of Guinea Pig Liver Transglutaminase Gene. Bioscience Biotechnology and Biochemistry. 58(8). 1540–1541. 18 indexed citations
12.
Matsumura, Yasuki, et al.. (1994). Gelation of Bean 11S Globulins by Ca2+-Independent Transglutaminase. Bioscience Biotechnology and Biochemistry. 58(5). 864–869. 27 indexed citations
13.
Ikura, Koji, Kyoya Takahata, & Ryuzo Sasaki. (1993). Cross‐linking of a synthetic partial‐length (1–28) peptide of the Alzheimer β/A4 amyloid protein by transglutaminase. FEBS Letters. 326(1-3). 109–111. 65 indexed citations
14.
Ikura, Koji, Katsuzumi Okumura, Masaaki Yoshikawa, Ryuzo Sasaki, & Hideo Chiba. (1985). Incorporation of lysyldipeptides into food protein by transglutaminase.. Agricultural and Biological Chemistry. 49(6). 1877–1878. 20 indexed citations
15.
Ikura, Koji, Masaaki Goto, Masaaki Yoshikawa, Ryuzo Sasaki, & Hideo Chiba. (1984). Use of transglutaminase. Reversible blocking of amino groups in substrate proteins for a high yield of specific products.. Agricultural and Biological Chemistry. 48(9). 2347–2354. 28 indexed citations
16.
Sasaki, Ryuzo, et al.. (1981). Storage of Soybean under High Temperature and Low Humidity. Eiyo to shokuryo. 34(3). 201–209. 3 indexed citations
17.
Chiba, Hayato, et al.. (1977). Regulaton of 2,3-bisphosphoglycerate metabolism in erythrocytes by a multifunctional enzyme.. PubMed. 36(3-4). 491–5. 1 indexed citations
18.
Ikura, Koji, Ryuzo Sasaki, Hiroshi Narita, Etsuro Sugimoto, & Hideo Chiba. (1976). Multifunctional Enzyme, Bisphosphoglyceromutase/2,3‐Bisphosphoglycerate Phosphatase/Phosphoglyceromutase, from Human Erythrocytes. European Journal of Biochemistry. 66(3). 515–522. 28 indexed citations
19.
Sasaki, Ryuzo, Koji Ikura, Etsuro Sugimoto, & Hideo Chiba. (1975). Purification of Bisphosphoglyceromutase, 2, 3-Bisphosphoglycerate Phosphatase and Phosphoglyceromutase from Human Erythrocytes. Three Enzyme Activities in One Protein. European Journal of Biochemistry. 50(3). 581–593. 93 indexed citations
20.
Chiba, Hideo, et al.. (1974). 2, 3-Diphosphoglycerate and Phosphoglycerate Mutase Levels in Animal Tissues and Erythrocytes. The Journal of Biochemistry. 76(1). 91–97. 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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