Junichi Takagi

16.2k total citations · 3 hit papers
202 papers, 12.4k citations indexed

About

Junichi Takagi is a scholar working on Molecular Biology, Immunology and Allergy and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Junichi Takagi has authored 202 papers receiving a total of 12.4k indexed citations (citations by other indexed papers that have themselves been cited), including 111 papers in Molecular Biology, 77 papers in Immunology and Allergy and 47 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Junichi Takagi's work include Cell Adhesion Molecules Research (77 papers), Monoclonal and Polyclonal Antibodies Research (47 papers) and Platelet Disorders and Treatments (37 papers). Junichi Takagi is often cited by papers focused on Cell Adhesion Molecules Research (77 papers), Monoclonal and Polyclonal Antibodies Research (47 papers) and Platelet Disorders and Treatments (37 papers). Junichi Takagi collaborates with scholars based in Japan, United States and Germany. Junichi Takagi's co-authors include Timothy A. Springer, Motomu Shimaoka, Thomas Walz, Benjamin M. Petre, Tsan Sam Xiao, Chafen Lu, Emiko Mihara, Yuji Saito, Jia‐Huai Wang and Bing‐Hao Luo and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Junichi Takagi

200 papers receiving 12.2k citations

Hit Papers

Global Conformational Rearrangements in Integrin Extracel... 2002 2026 2010 2018 2002 2004 2018 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Junichi Takagi Japan 59 5.8k 5.5k 2.5k 2.5k 1.8k 202 12.4k
Simon L. Goodman Germany 58 6.4k 1.1× 6.8k 1.2× 1.6k 0.6× 2.2k 0.9× 2.6k 1.4× 125 13.2k
Christopher V. Carman United States 46 4.8k 0.8× 3.5k 0.6× 3.1k 1.2× 2.0k 0.8× 805 0.4× 67 9.8k
Carl G. Gahmberg Finland 63 6.5k 1.1× 3.5k 0.6× 4.3k 1.7× 1.6k 0.7× 1.8k 1.0× 267 13.5k
Claude Boucheix France 53 4.0k 0.7× 3.5k 0.6× 2.2k 0.9× 1.7k 0.7× 1.1k 0.6× 180 10.2k
M. Amin Arnaout United States 57 5.7k 1.0× 7.5k 1.4× 5.7k 2.3× 1.9k 0.7× 2.2k 1.2× 149 15.4k
David Calderwood United States 53 5.2k 0.9× 6.5k 1.2× 1.6k 0.6× 5.6k 2.2× 667 0.4× 106 12.0k
Steven D. Rosen United States 67 7.4k 1.3× 4.9k 0.9× 5.2k 2.0× 3.3k 1.3× 1.5k 0.8× 152 13.7k
James B. McCarthy United States 61 5.2k 0.9× 3.8k 0.7× 1.3k 0.5× 4.2k 1.7× 698 0.4× 175 10.9k
Clayton A. Buck United States 36 5.5k 0.9× 4.0k 0.7× 1.9k 0.8× 2.4k 1.0× 1.1k 0.6× 59 10.8k
C H Damsky United States 37 4.0k 0.7× 3.7k 0.7× 3.3k 1.3× 1.9k 0.8× 688 0.4× 44 11.1k

Countries citing papers authored by Junichi Takagi

Since Specialization
Citations

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

Fields of papers citing papers by Junichi Takagi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Junichi Takagi

This figure shows the co-authorship network connecting the top 25 collaborators of Junichi Takagi. A scholar is included among the top collaborators of Junichi Takagi 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 Junichi Takagi. Junichi Takagi 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.
Takahashi, Katsu, et al.. (2024). Development of a new antibody drug to treat congenital tooth agenesis. Journal of Oral Biosciences. 66(4). 1–9.
2.
Matsuoka, M., Keiko Tamura‐Kawakami, Junichi Takagi, et al.. (2024). C-terminal amino acids in the type I transmembrane domain of L-type lectin VIP36 affect γ-secretase susceptibility. Biochemical and Biophysical Research Communications. 696. 149504–149504. 1 indexed citations
3.
Ponzo, Matteo, Emiko Mihara, Atsushi Kumanogoh, et al.. (2024). PlexinB1 Inactivation Reprograms Immune Cells in the Tumor Microenvironment, Inhibiting Breast Cancer Growth and Metastatic Dissemination. Cancer Immunology Research. 12(9). 1286–1301. 2 indexed citations
4.
Matoba, Kyoko, Mika Hirose, Yukiko Matsunaga, et al.. (2022). De novo Fc-based receptor dimerizers differentially modulate PlexinB1 function. Structure. 30(10). 1411–1423.e4. 9 indexed citations
5.
Zhang, Qianli, Akitoshi Miyamoto, Shin Watanabe, et al.. (2022). Engineered fast-dissociating antibody fragments for multiplexed super-resolution microscopy. Cell Reports Methods. 2(10). 100301–100301. 8 indexed citations
6.
Arimori, Takao, Naoyuki Miyazaki, Emiko Mihara, et al.. (2021). Structural mechanism of laminin recognition by integrin. Nature Communications. 12(1). 4012–4012. 61 indexed citations
7.
Mihara, Emiko, Satoshi Watanabe, Kyoko Matoba, et al.. (2021). Lasso-grafting of macrocyclic peptide pharmacophores yields multi-functional proteins. Nature Communications. 12(1). 1543–1543. 27 indexed citations
8.
Kiso, Honoka, Yoshihito Tokita, Emiko Mihara, et al.. (2021). Anti–USAG-1 therapy for tooth regeneration through enhanced BMP signaling. Science Advances. 7(7). 22 indexed citations
9.
Sato, Nobuhiro, Saeko Yanaka, Anne Martel, et al.. (2021). A feasibility study of inverse contrast-matching small-angle neutron scattering method combined with size exclusion chromatography using antibody interactions as model systems. The Journal of Biochemistry. 169(6). 701–708. 3 indexed citations
10.
Schumacher, Stephanie, Dirk Dedden, Roberto Vázquez Nuñez, et al.. (2021). Structural insights into integrin α 5 β 1 opening by fibronectin ligand. Science Advances. 7(19). 81 indexed citations
11.
Tanaka, Rika, Tomoyo Takagi, Naoko Norioka, et al.. (2020). Negatively charged amino acids in the stalk region of membrane proteins reduce ectodomain shedding. Journal of Biological Chemistry. 295(35). 12343–12352. 9 indexed citations
12.
Sakai, Katsuya, Toby Passioura, Hiroki Sato, et al.. (2019). Macrocyclic peptide-based inhibition and imaging of hepatocyte growth factor. Nature Chemical Biology. 15(6). 598–606. 58 indexed citations
13.
Kitago, Yu, Yuki Fujii, Emiko Mihara, et al.. (2018). An anti-peptide monoclonal antibody recognizing the tobacco etch virus protease-cleavage sequence and its application to a tandem tagging system. Protein Expression and Purification. 147. 94–99. 8 indexed citations
14.
Kang, Sujin, Yoshimitsu Nakanishi, Yoshiyuki Kioi, et al.. (2018). Semaphorin 6D reverse signaling controls macrophage lipid metabolism and anti-inflammatory polarization. Nature Immunology. 19(6). 561–570. 94 indexed citations
15.
Miyazaki, Naoyuki, Kenji Iwasaki, & Junichi Takagi. (2018). A systematic survey of conformational states in β1 and β4 integrins using negative-stain electron microscopy. Journal of Cell Science. 131(10). 24 indexed citations
16.
Ushioda, Ryo, Akitoshi Miyamoto, M. Inoue, et al.. (2016). Redox-assisted regulation of Ca 2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5. Proceedings of the National Academy of Sciences. 113(41). E6055–E6063. 77 indexed citations
17.
Nogi, Terukazu, et al.. (2008). A Murine Monoclonal Antibody That Binds N-Terminal Extracellular Segment of Human Protease-Activated Receptor-4. Hybridoma. 27(5). 331–335. 7 indexed citations
18.
Yang, Wei, Motomu Shimaoka, Azucena Salas, Junichi Takagi, & Timothy A. Springer. (2004). Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring. Proceedings of the National Academy of Sciences. 101(9). 2906–2911. 77 indexed citations
19.
Takagi, Junichi, Natalia Beglova, Padmaja Yalamanchili, Stephen C. Blacklow, & Timothy A. Springer. (2001). Definition of EGF-like, closely interacting modules that bear activation epitopes in integrin β subunits. Proceedings of the National Academy of Sciences. 98(20). 11175–11180. 52 indexed citations
20.
Kushida, Ai, et al.. (1998). Screening of Hybridoma Clones Producing Antibodies Against Plasma Membrane-Associated Materials. Hybridoma. 17(2). 209–213. 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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