Satoru Funamoto

3.4k total citations · 1 hit paper
33 papers, 2.7k citations indexed

About

Satoru Funamoto is a scholar working on Physiology, Molecular Biology and Cell Biology. According to data from OpenAlex, Satoru Funamoto has authored 33 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Physiology, 20 papers in Molecular Biology and 12 papers in Cell Biology. Recurrent topics in Satoru Funamoto's work include Alzheimer's disease research and treatments (21 papers), Cellular Mechanics and Interactions (6 papers) and Computational Drug Discovery Methods (5 papers). Satoru Funamoto is often cited by papers focused on Alzheimer's disease research and treatments (21 papers), Cellular Mechanics and Interactions (6 papers) and Computational Drug Discovery Methods (5 papers). Satoru Funamoto collaborates with scholars based in Japan, United States and Germany. Satoru Funamoto's co-authors include Richard Firtel, Ruedi Meili, Yasuo Ihara, Susan Lee, Lisa Parry, Maho Morishima‐Kawashima, Mako Takami, Chang Y. Chung, Seiko Ishihara and Yu Nagashima and has published in prestigious journals such as Cell, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Satoru Funamoto

33 papers receiving 2.7k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Spatial and Temporal Regulation of 3-Phosphoinositides by PI 3-Kinase and PTEN Mediates Chemotaxis

2002 622 citations Satoru Funamoto, Ruedi Meili et al. Cell profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Satoru Funamoto Japan	20	1.5k	1.3k	1.0k	396	308	33	2.7k
Peer‐Hendrik Kuhn Germany	26	1.5k 1.0×	1.3k 1.1×	506 0.5×	406 1.0×	441 1.4×	43	3.0k
Regina Fluhrer Germany	30	1.5k 1.0×	948 0.7×	653 0.6×	243 0.6×	250 0.8×	51	2.5k
Yuichi Morohashi Japan	23	1.5k 1.0×	856 0.7×	559 0.5×	292 0.7×	307 1.0×	33	2.3k
Christoph Kaether Germany	35	3.1k 2.1×	2.5k 2.0×	1.6k 1.5×	603 1.5×	1.0k 3.3×	68	5.4k
Philippe Cupers Belgium	13	1.9k 1.3×	1.6k 1.3×	770 0.7×	460 1.2×	548 1.8×	17	3.1k
Toshiyuki Honda Japan	22	1.5k 1.0×	1.4k 1.1×	547 0.5×	312 0.8×	599 1.9×	60	2.7k
Austin J. Yang United States	29	1.8k 1.2×	1.5k 1.2×	489 0.5×	347 0.9×	349 1.1×	59	3.2k
Susanne Illenberger Germany	17	1.5k 1.0×	1.1k 0.9×	1.0k 1.0×	199 0.5×	474 1.5×	24	2.7k
Sebastian Munck Belgium	28	1.6k 1.1×	631 0.5×	548 0.5×	171 0.4×	526 1.7×	66	3.0k
Amantha Thathiah United States	19	1.7k 1.2×	651 0.5×	209 0.2×	221 0.6×	527 1.7×	33	2.8k

Countries citing papers authored by Satoru Funamoto

Since Specialization

Citations

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

Fields of papers citing papers by Satoru Funamoto

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Satoru Funamoto

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Saito, Takashi, et al.. (2025). High Affinity Staining for Histological Immunoreactivity revealed phosphorylated tau within amyloid-cored plaques in the brain of AD model mice. Biochemical and Biophysical Research Communications. 771. 152025–152025. 1 indexed citations

Murata, Takuya, Naoko Utsunomiya‐Tate, Jun Motoyama, et al.. (2023). A tailored tetravalent peptide displays dual functions to inhibit amyloid β production and aggregation. Communications Biology. 6(1). 383–383. 7 indexed citations

Miyasaka, Tomohiro, Satoru Funamoto, Takashi Saito, et al.. (2023). The senile plaque: Morphological differences in APP knock‐in mice brains by fixatives. Brain and Behavior. 13(4). e2953–e2953. 1 indexed citations

Hamabata, Takashi, et al.. (2021). A nontoxigenic form of Shiga toxin 2 suppresses the production of amyloid β by altering the intracellular transport of amyloid precursor protein through its receptor-binding B-subunit. Biochemical and Biophysical Research Communications. 557. 247–253. 3 indexed citations

Kakuda, Nobuto, Haruyasu Yamaguchi, Kohei Akazawa, et al.. (2020). γ-Secretase Activity Is Associated with Braak Senile Plaque Stages. American Journal Of Pathology. 190(6). 1323–1331. 19 indexed citations

Nakano, Masaki, Seiko Ishihara, Nobuto Kakuda, et al.. (2020). A potential defense mechanism against amyloid deposition in cerebellum. Biochemical and Biophysical Research Communications. 535. 25–32. 11 indexed citations

Funamoto, Satoru, Shinji Tagami, Masayasu Okochi, & Maho Morishima‐Kawashima. (2020). Successive cleavage of β-amyloid precursor protein by γ-secretase. Seminars in Cell and Developmental Biology. 105. 64–74. 31 indexed citations

Moniruzzaman, Mohammad, et al.. (2018). Glycosylation status of nicastrin influences catalytic activity and substrate preference of γ-secretase. Biochemical and Biophysical Research Communications. 502(1). 98–103. 17 indexed citations

Umeda, Masato, Satoru Funamoto, Yoshiro Saito, et al.. (2017). Pleckstrin homology domain of p210 BCR‐ABL interacts with cardiolipin to regulate its mitochondrial translocation and subsequent mitophagy. Genes to Cells. 23(1). 22–34. 9 indexed citations

10.

Ishihara, Seiko, et al.. (2015). The A673T mutation in the amyloid precursor protein reduces the production of β-amyloid protein from its β-carboxyl terminal fragment in cells. Acta Neuropathologica Communications. 3(1). 66–66. 19 indexed citations

11.

Funamoto, Satoru, Toru Sasaki, Seiko Ishihara, et al.. (2013). Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase. Nature Communications. 4(1). 2529–2529. 47 indexed citations

12.

Matsumura, Nobutaka, Mako Takami, Masayasu Okochi, et al.. (2013). γ-Secretase Associated with Lipid Rafts. Journal of Biological Chemistry. 289(8). 5109–5121. 81 indexed citations

13.

Kang, Min Suk, Seung‐Hoon Baek, Yoon S. Chun, et al.. (2013). Modulation of Lipid Kinase PI4KIIα Activity and Lipid Raft Association of Presenilin 1 Underlies γ-Secretase Inhibition by Ginsenoside (20S)-Rg3. Journal of Biological Chemistry. 288(29). 20868–20882. 36 indexed citations

14.

Saito, Takashi, Takahiro Suemoto, Nathalie Brouwers, et al.. (2011). Potent amyloidogenicity and pathogenicity of Aβ43. Nature Neuroscience. 14(8). 1023–1032. 222 indexed citations

15.

Takami, Mako, Yu Nagashima, Y Sano, et al.. (2009). γ-Secretase: Successive Tripeptide and Tetrapeptide Release from the Transmembrane Domain of β-Carboxyl Terminal Fragment. Journal of Neuroscience. 29(41). 13042–13052. 404 indexed citations

16.

Shimojo, Masafumi, Naruhiko Sahara, Tatsuya Mizoroki, et al.. (2008). Enzymatic Characteristics of I213T Mutant Presenilin-1/γ-Secretase in Cell Models and Knock-in Mouse Brains. Journal of Biological Chemistry. 283(24). 16488–16496. 27 indexed citations

17.

Lee, Susan, et al.. (2004). DictyosteliumPAKc Is Required for Proper Chemotaxis. Molecular Biology of the Cell. 15(12). 5456–5469. 34 indexed citations

18.

Huang, Yi Elaine, Miho Iijima, Carole A. Parent, et al.. (2003). Receptor-mediated Regulation of PI3Ks Confines PI(3,4,5)P₃to the Leading Edge of Chemotaxing Cells. Molecular Biology of the Cell. 14(5). 1913–1922. 174 indexed citations

19.

Funamoto, Satoru, Ruedi Meili, Susan Lee, Lisa Parry, & Richard Firtel. (2002). Spatial and Temporal Regulation of 3-Phosphoinositides by PI 3-Kinase and PTEN Mediates Chemotaxis. Cell. 109(5). 611–623. 622 indexed citations breakdown →

20.

Funamoto, Satoru, Masashi Fukuzawa, Jill Meisenhelder, et al.. (2001). An SH2-domain-containing kinase negatively regulates the phosphatidylinositol-3 kinase pathway. Genes & Development. 15(6). 687–698. 23 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.

Explore authors with similar magnitude of impact