Junko Ohkanda

2.4k total citations
79 papers, 1.9k citations indexed

About

Junko Ohkanda is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, Junko Ohkanda has authored 79 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 30 papers in Organic Chemistry and 28 papers in Oncology. Recurrent topics in Junko Ohkanda's work include 14-3-3 protein interactions (16 papers), Synthesis and Biological Evaluation (13 papers) and Peptidase Inhibition and Analysis (12 papers). Junko Ohkanda is often cited by papers focused on 14-3-3 protein interactions (16 papers), Synthesis and Biological Evaluation (13 papers) and Peptidase Inhibition and Analysis (12 papers). Junko Ohkanda collaborates with scholars based in Japan, United States and United Kingdom. Junko Ohkanda's co-authors include Andrew D. Hamilton, Saı̈d M. Sebti, Nobuo Kato, Michelle A. Blaskovich, Akira Katoh, Yimin Qian, David B. Knowles, Tohru Yoshida, Jiazhi Sun and Saı̈d Sebti and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Junko Ohkanda

77 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Junko Ohkanda Japan 24 1.2k 503 421 239 237 79 1.9k
Carl P. Decicco United States 33 1.3k 1.1× 1.2k 2.5× 772 1.8× 114 0.5× 263 1.1× 100 3.4k
William T. Windsor United States 23 1.5k 1.2× 302 0.6× 876 2.1× 169 0.7× 43 0.2× 42 2.5k
Maria Bretner Poland 25 1.1k 0.9× 630 1.3× 196 0.5× 125 0.5× 41 0.2× 82 1.9k
V. L. Narayanan United States 24 1.0k 0.8× 890 1.8× 411 1.0× 160 0.7× 143 0.6× 68 2.2k
David P. Baccanari United States 25 1.1k 0.9× 556 1.1× 354 0.8× 196 0.8× 94 0.4× 48 2.1k
Naoaki Fujii United States 24 1.3k 1.1× 378 0.8× 374 0.9× 164 0.7× 40 0.2× 53 2.0k
Christian Gege Germany 23 665 0.5× 353 0.7× 282 0.7× 146 0.6× 45 0.2× 60 1.4k
Joseph Schoepfer Switzerland 24 1.5k 1.2× 532 1.1× 470 1.1× 34 0.1× 119 0.5× 43 2.0k
Rongshi Li United States 23 1.0k 0.8× 789 1.6× 339 0.8× 149 0.6× 160 0.7× 44 2.2k
Vincent J. Kalish United States 15 1.0k 0.8× 619 1.2× 419 1.0× 72 0.3× 81 0.3× 24 2.0k

Countries citing papers authored by Junko Ohkanda

Since Specialization
Citations

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

Fields of papers citing papers by Junko Ohkanda

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Junko Ohkanda

This figure shows the co-authorship network connecting the top 25 collaborators of Junko Ohkanda. A scholar is included among the top collaborators of Junko Ohkanda 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 Junko Ohkanda. Junko Ohkanda 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.
Inoue, Yoshihisa, et al.. (2025). Design and Evaluation of Bivalent K‐Ras Inhibitors That Target the CAAX Binding Site and the Acidic Surface of Farnesyltransferase and Geranylgeranyltransferase I. Chemistry - A European Journal. 31(27). e202500306–e202500306. 1 indexed citations
2.
Hayashi, Yuki, et al.. (2024). Fungal toxin fusicoccin enhances plant growth by upregulating 14-3-3 interaction with plasma membrane H+-ATPase. Scientific Reports. 14(1). 23431–23431. 2 indexed citations
3.
Niwa, Takashi, et al.. (2022). Expression and purification of DYRK1A kinase domain in complex with its folding intermediate-selective inhibitor FINDY. Protein Expression and Purification. 195-196. 106089–106089. 5 indexed citations
4.
Inoue, Yoshihisa, et al.. (2022). Structure-activity-relationship study of semi-synthetically modified fusicoccins on their stabilization effect for 14-3-3-phospholigand interactions. Bioorganic & Medicinal Chemistry. 73. 117020–117020. 4 indexed citations
5.
Harada, Kazuo, Akimasa Matsugami, Penmetcha K. R. Kumar, et al.. (2014). RNA‐Directed Amino Acid Coupling as a Model Reaction for Primitive Coded Translation. ChemBioChem. 15(6). 794–798. 11 indexed citations
6.
Hayashi, Daisuke, Nobuo Kato, Tomohisa Kuzuyama, Yasuo Satô, & Junko Ohkanda. (2013). Antimicrobial N-(2-chlorobenzyl)-substituted hydroxamate is an inhibitor of 1-deoxy-d-xylulose 5-phosphate synthase. Chemical Communications. 49(49). 5535–5535. 20 indexed citations
7.
Maki, Toshio, Akie Kawamura, Nobuo Kato, & Junko Ohkanda. (2012). Chemical ligation of epoxide-containing fusicoccins and peptide fragments guided by 14-3-3 protein. Molecular BioSystems. 9(5). 940–943. 26 indexed citations
8.
Kato, Nobuo, et al.. (2012). Peptidomimetic modification improves cell permeation of bivalent farnesyltransferase inhibitors. Bioorganic & Medicinal Chemistry. 21(14). 4004–4010. 6 indexed citations
9.
Takahashi, Michiko, Akie Kawamura, Nobuo Kato, et al.. (2011). Phosphopeptide‐Dependent Labeling of 14–3–3 ζ Proteins by Fusicoccin‐Based Fluorescent Probes. Angewandte Chemie International Edition. 51(2). 509–512. 46 indexed citations
10.
Ohkanda, Junko, et al.. (2009). Protein surface recognition by dendritic ruthenium(ii) tris(bipyridine) complexes. Chemical Communications. 6949–6949. 23 indexed citations
11.
Blaskovich, Michelle A., Akiko Yano, Kazuo Harada, et al.. (2008). Module Assembly for Protein‐Surface Recognition: Geranylgeranyltransferase I Bivalent Inhibitors for Simultaneous Targeting of Interior and Exterior Protein Surfaces. Chemistry - A European Journal. 14(5). 1392–1401. 9 indexed citations
12.
13.
Ohkanda, Junko, Corey L. Strickland, Michelle A. Blaskovich, et al.. (2006). Structure-based design of imidazole-containing peptidomimetic inhibitors of protein farnesyltransferase. Organic & Biomolecular Chemistry. 4(3). 482–482. 9 indexed citations
14.
Ohkanda, Junko, Howard Kendrick, Kohei Yokoyama, et al.. (2004). In vitro and in vivo antimalarial activity of peptidomimetic protein farnesyltransferase inhibitors with improved membrane permeability. Bioorganic & Medicinal Chemistry. 12(24). 6517–6526. 35 indexed citations
15.
Bordier, Bruno B., Junko Ohkanda, Ping Liu, et al.. (2003). In vivo antiviral efficacy of prenylation inhibitors against hepatitis delta virus. Journal of Clinical Investigation. 112(3). 407–414. 145 indexed citations
16.
Delarue, Frédéric, et al.. (2002). The farnesyltransferase inhibitor, FTI-2153, inhibits bipolar spindle formation during mitosis independently of transformation and Ras and p53 mutation status. Cell Death and Differentiation. 9(7). 702–709. 27 indexed citations
17.
Ohkanda, Junko, David B. Knowles, Michelle A. Blaskovich, Saı̈d Sebti, & Andrew D. Hamilton. (2002). Inhibitors of Protein Farnesyltransferase as Novel Anticancer Agents. Current Topics in Medicinal Chemistry. 2(3). 303–323. 66 indexed citations
18.
Ohkanda, Junko, Jeffrey W. Lockman, Kohei Yokoyama, et al.. (2001). Peptidomimetic inhibitors of protein farnesyltransferase show potent antimalarial activity. Bioorganic & Medicinal Chemistry Letters. 11(6). 761–764. 61 indexed citations
19.
20.
Adnane, Jalila, Zhi Chen, Junko Ohkanda, et al.. (2000). Inhibition of farnesyltransferase increases TGFβ type II receptor expression and enhances the responsiveness of human cancer cells to TGFβ. Oncogene. 19(48). 5525–5533. 19 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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