Ikuko Okazaki

507 total citations
10 papers, 435 citations indexed

About

Ikuko Okazaki is a scholar working on Immunology and Allergy, Cancer Research and Molecular Biology. According to data from OpenAlex, Ikuko Okazaki has authored 10 papers receiving a total of 435 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Immunology and Allergy, 5 papers in Cancer Research and 4 papers in Molecular Biology. Recurrent topics in Ikuko Okazaki's work include Cell Adhesion Molecules Research (9 papers), Protease and Inhibitor Mechanisms (5 papers) and Bone Metabolism and Diseases (2 papers). Ikuko Okazaki is often cited by papers focused on Cell Adhesion Molecules Research (9 papers), Protease and Inhibitor Mechanisms (5 papers) and Bone Metabolism and Diseases (2 papers). Ikuko Okazaki collaborates with scholars based in Japan, United States and Australia. Ikuko Okazaki's co-authors include Motoyoshi Nomizu, Norio Nishi, Chiemi Kimura, N. Yamamoto, Takashi Fujii, Toshimitsu Uede, Junko Morimoto, Harumi Yamazaki, Shigeyuki Kon and Nobuo Seki and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Clinical Investigation and Biochemistry.

In The Last Decade

Ikuko Okazaki

10 papers receiving 433 citations

Peers

Ikuko Okazaki
Jyrki Heino Finland
Philipp Vandenberg United States
David T. Woodley United States
Raymond Brittingham United States
Kimberly C Wynn United States
Randolph G. Brewton United States
Geraldine Chow United States
Yoshihiko Yamada United States
John J. Grzesiak United States
Jyrki Heino Finland
Ikuko Okazaki
Citations per year, relative to Ikuko Okazaki Ikuko Okazaki (= 1×) peers Jyrki Heino

Countries citing papers authored by Ikuko Okazaki

Since Specialization
Citations

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

Fields of papers citing papers by Ikuko Okazaki

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ikuko Okazaki

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

All Works

10 of 10 papers shown
1.
Yamamoto, N., Fumihiko Sakai, Shigeyuki Kon, et al.. (2003). Essential role of the cryptic epitope SLAYGLR within osteopontin in a murine model of rheumatoid arthritis. Journal of Clinical Investigation. 112(2). 181–188. 172 indexed citations
2.
Yamamoto, N., Fumihiko Sakai, Shigeyuki Kon, et al.. (2003). Essential role of the cryptic epitope SLAYGLR within osteopontin in a murine model of rheumatoid arthritis. Journal of Clinical Investigation. 112(2). 181–188. 11 indexed citations
3.
Mochizuki, Mayumi, Yuichi Kadoya, Kozue Kato, et al.. (2003). Laminin‐1 peptide‐conjugated chitosan membranes as a novel approach for cell engineering. The FASEB Journal. 17(8). 1–20. 83 indexed citations
4.
Okazaki, Ikuko, Norio Nishi, Benjamin S. Weeks, et al.. (2002). Identification of Cell Binding Sites in the Laminin α5-Chain G Domain. Experimental Cell Research. 277(1). 95–106. 35 indexed citations
5.
Okazaki, Ikuko, Nobuharu Suzuki, Norio Nishi, et al.. (2002). Identification of Biologically Active Sequences in the Laminin α4 Chain G Domain. Journal of Biological Chemistry. 277(40). 37070–37078. 39 indexed citations
6.
Hojo, Keiko, Ikuko Okazaki, Masahiko Sasaki, et al.. (2002). Preparation and Biological Activities of a Bivalent Poly(Ethylene Glycol) Hybrid Containing an Active Site and Its Synergistic Site of Fibronectin.. Chemical and Pharmaceutical Bulletin. 50(9). 1229–1232. 23 indexed citations
7.
Hojo, Keiko, Mitsuko Maeda, Ikuko Okazaki, et al.. (2001). Amino acids and peptides. Part 39: A bivalent poly(ethylene glycol) hybrid containing an active site (RGD) and its synergistic site (PHSRN) of fibronectin. Bioorganic & Medicinal Chemistry Letters. 11(11). 1429–1432. 20 indexed citations
8.
Nomizu, Motoyoshi, Ikuko Okazaki, Norio Nishi, et al.. (2001). Identification of Homologous Biologically Active Sites on the N-Terminal Domain of Laminin Alpha Chains. Biochemistry. 40(50). 15310–15317. 17 indexed citations
9.
Yamaguchi, Hirotake, Hironobu Yamashita, Hitoshi Mori, et al.. (2000). High and Low Affinity Heparin-binding Sites in the G Domain of the Mouse Laminin α4 Chain. Journal of Biological Chemistry. 275(38). 29458–29465. 27 indexed citations
10.
Okazaki, Ikuko, et al.. (1999). Biologically Active Sequences in Laminin, a Multifunctional Extracellular Matrix Protein. 31(4). 227–234. 8 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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