Kyoko Kojima‐Aikawa

406 total citations
21 papers, 328 citations indexed

About

Kyoko Kojima‐Aikawa is a scholar working on Molecular Biology, Immunology and Organic Chemistry. According to data from OpenAlex, Kyoko Kojima‐Aikawa has authored 21 papers receiving a total of 328 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 9 papers in Immunology and 4 papers in Organic Chemistry. Recurrent topics in Kyoko Kojima‐Aikawa's work include Glycosylation and Glycoproteins Research (10 papers), Galectins and Cancer Biology (8 papers) and Blood Coagulation and Thrombosis Mechanisms (4 papers). Kyoko Kojima‐Aikawa is often cited by papers focused on Glycosylation and Glycoproteins Research (10 papers), Galectins and Cancer Biology (8 papers) and Blood Coagulation and Thrombosis Mechanisms (4 papers). Kyoko Kojima‐Aikawa collaborates with scholars based in Japan, Germany and United Kingdom. Kyoko Kojima‐Aikawa's co-authors include Isamu Matsumoto, Yukiko Nakano, Yoshiki Yamaguchi, Akemi Ikeda, Hiroaki Asou, Chika Seiwa, Mayumi Kanagawa, Junko Masuda, Ayano Satoh and Yan Liu and has published in prestigious journals such as Journal of Biological Chemistry, Clinical Cancer Research and Biochemical and Biophysical Research Communications.

In The Last Decade

Kyoko Kojima‐Aikawa

21 papers receiving 320 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kyoko Kojima‐Aikawa Japan 12 221 88 39 35 30 21 328
Nahid Saghir United Kingdom 6 282 1.3× 60 0.7× 28 0.7× 36 1.0× 12 0.4× 7 469
Uwe Eberspaecher Germany 8 263 1.2× 34 0.4× 20 0.5× 45 1.3× 24 0.8× 10 483
Dustin C. Frost United States 16 484 2.2× 163 1.9× 39 1.0× 33 0.9× 42 1.4× 25 796
Allan Mak Canada 9 222 1.0× 73 0.8× 17 0.4× 118 3.4× 29 1.0× 13 394
Christian Y. Arod United States 7 200 0.9× 82 0.9× 15 0.4× 30 0.9× 81 2.7× 9 305
John Astle United States 8 230 1.0× 52 0.6× 28 0.7× 27 0.8× 58 1.9× 17 350
Liqing Xiao United States 11 431 2.0× 86 1.0× 17 0.4× 45 1.3× 11 0.4× 13 611
Wenke Weidemann Germany 12 455 2.1× 103 1.2× 87 2.2× 56 1.6× 98 3.3× 16 537
Kyung-Jin Kim South Korea 10 202 0.9× 93 1.1× 9 0.2× 25 0.7× 58 1.9× 17 433
Ana P. G. Silva Australia 13 440 2.0× 31 0.4× 29 0.7× 28 0.8× 16 0.5× 22 546

Countries citing papers authored by Kyoko Kojima‐Aikawa

Since Specialization
Citations

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

Fields of papers citing papers by Kyoko Kojima‐Aikawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kyoko Kojima‐Aikawa. 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 Kyoko Kojima‐Aikawa. The network helps show where Kyoko Kojima‐Aikawa may publish in the future.

Co-authorship network of co-authors of Kyoko Kojima‐Aikawa

This figure shows the co-authorship network connecting the top 25 collaborators of Kyoko Kojima‐Aikawa. A scholar is included among the top collaborators of Kyoko Kojima‐Aikawa 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 Kyoko Kojima‐Aikawa. Kyoko Kojima‐Aikawa 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.
Yamaguchi, Yoshiki, et al.. (2020). Annexin A4 inhibits sulfatide‐induced activation of coagulation factor XII. Journal of Thrombosis and Haemostasis. 18(6). 1357–1369. 9 indexed citations
2.
Nakano, Yukiko, Takako Saitoh, Sabine S. Gouraud, et al.. (2017). Lectin ZG16p inhibits proliferation of human colorectal cancer cells via its carbohydrate-binding sites. Glycobiology. 28(1). 21–31. 11 indexed citations
3.
Hanashima, Shinya, Sebastian Götze, Yan Liu, et al.. (2015). Defining the Interaction of Human Soluble Lectin ZG16p and Mycobacterial Phosphatidylinositol Mannosides. ChemBioChem. 16(10). 1502–1511. 18 indexed citations
4.
Kojima‐Aikawa, Kyoko. (2014). Solid-Phase Assay of Lectin Activity Using HRP-Conjugated Glycoproteins. Methods in molecular biology. 1200. 101–106. 1 indexed citations
5.
Kanagawa, Mayumi, Yan Liu, Shinya Hanashima, et al.. (2014). Structural Basis for Multiple Sugar Recognition of Jacalin-related Human ZG16p Lectin. Journal of Biological Chemistry. 289(24). 16954–16965. 30 indexed citations
6.
Kojima‐Aikawa, Kyoko, et al.. (2012). HMMC‐1, a human monoclonal antibody to fucosylated core 1 O‐glycan, suppresses growth of uterine endometrial cancer cells. Cancer Science. 104(1). 62–69. 1 indexed citations
7.
Ito, Mika, Jie Zhang, Michio Hiroshima, et al.. (2012). Universal Caging Group for the in‐Cell Detection of Glutathione Transferase Applied to 19F NMR and Bioluminogenic Probes. ChemBioChem. 13(10). 1428–1432. 15 indexed citations
8.
9.
Wang, Ping, Shin‐Yi Yu, Chi‐Chi Chou, et al.. (2011). Identification of Mono- and Disulfated N-Acetyl-lactosaminyl Oligosaccharide Structures as Epitopes Specifically Recognized by Humanized Monoclonal Antibody HMOCC-1 Raised against Ovarian Cancer. Journal of Biological Chemistry. 287(9). 6592–6602. 19 indexed citations
10.
Takeuchi, Tomoharu, Atsushi Yamada, Mayumi Tamura, et al.. (2011). Caenorhabditis elegans proteins captured by immobilized Galβ1-4Fuc disaccharide units: assignment of 3 annexins. Carbohydrate Research. 346(13). 1837–1841. 11 indexed citations
11.
Kanagawa, Mayumi, Tadashi Satoh, Akemi Ikeda, et al.. (2010). Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related β-prism fold. Biochemical and Biophysical Research Communications. 404(1). 201–205. 43 indexed citations
12.
Nishioka, Satoshi, et al.. (2006). Ligand-binding Activity and Expression Profile of Annexins in Caenorhabditis elegans. The Journal of Biochemistry. 141(1). 47–55. 11 indexed citations
13.
Yuasa, Hideya, et al.. (2006). Pentamer is the minimum structure for oligomannosylpeptoids to bind to concanavalin A. Bioorganic & Medicinal Chemistry Letters. 17(18). 5274–5278. 14 indexed citations
14.
Masuda, Junko, Kimihiro Suzuki, Ayano Satoh, et al.. (2005). Beta-2-glycoprotein I and urinary trypsin inhibitor levels in the plasma of pregnant and postpartum women. Thrombosis Research. 117(3). 255–261. 3 indexed citations
15.
Masuda, Junko, et al.. (2004). A novel expression vector, designated as pHisJM, for producing recombinant His-fusion proteins. Biotechnology Letters. 26(20). 1543–1548. 5 indexed citations
16.
Gotoh, Mari, Kahori Kurosaka, Junko Masuda, et al.. (2004). Annexins I and IV inhibit Staphylococcus aureus attachment to human macrophages. Immunology Letters. 98(2). 297–302. 20 indexed citations
17.
Masuda, Junko, Ayano Satoh, Michiru Ida‐Eto, et al.. (2004). Levels of annexin IV and V in the plasma of pregnant and postpartum women. Thrombosis and Haemostasis. 91(6). 1129–1136. 31 indexed citations
18.
Suzuki, Nao, Daisuke Aoki, Yutaka Tamada, et al.. (2004). HMOCC-1, a human monoclonal antibody that inhibits adhesion of ovarian cancer cells to human mesothelial cells. Gynecologic Oncology. 95(2). 290–298. 16 indexed citations
19.
Yamagaki, Tohru, et al.. (2002). A Potential Endogenous Ligand of Annexin IV in the Exocrine Pancreas. Journal of Biological Chemistry. 277(49). 47493–47499. 8 indexed citations
20.
Seiwa, Chika, Kyoko Kojima‐Aikawa, Isamu Matsumoto, & Hiroaki Asou. (2002). CNS myelinogenesis in vitro: Myelin basic protein deficient shiverer oligodendrocytes. Journal of Neuroscience Research. 69(3). 305–317. 34 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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