Sayoko Ihara

1.8k total citations
41 papers, 1.5k citations indexed

About

Sayoko Ihara is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Sayoko Ihara has authored 41 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 15 papers in Cell Biology and 7 papers in Cellular and Molecular Neuroscience. Recurrent topics in Sayoko Ihara's work include Protein Kinase Regulation and GTPase Signaling (12 papers), Cellular transport and secretion (9 papers) and Olfactory and Sensory Function Studies (7 papers). Sayoko Ihara is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (12 papers), Cellular transport and secretion (9 papers) and Olfactory and Sensory Function Studies (7 papers). Sayoko Ihara collaborates with scholars based in Japan, United States and Taiwan. Sayoko Ihara's co-authors include Yasuhisa Fukui, Satoshi Nagata, Kazushige Touhara, Michimoto Kobayashi, Akihiro Iwamatsu, Tsutomu Oka, Keiichi Yoshikawa, Hiroaki Konishi, Yoshihiro Kita and Ushio Kikkawa and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Sayoko Ihara

41 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sayoko Ihara Japan 20 826 322 299 254 218 41 1.5k
Nicolas Bourmeyster France 24 1.2k 1.4× 221 0.7× 310 1.0× 106 0.4× 173 0.8× 51 1.7k
Sascha E. Dho Canada 15 1.4k 1.7× 458 1.4× 198 0.7× 189 0.7× 95 0.4× 21 1.8k
Nobuhiko Yokoyama Japan 17 1.6k 1.9× 430 1.3× 537 1.8× 444 1.7× 164 0.8× 35 2.4k
Hiroshi Ueda Japan 18 847 1.0× 180 0.6× 248 0.8× 83 0.3× 110 0.5× 50 1.1k
Ilia A. Yamboliev United States 21 1.1k 1.4× 278 0.9× 189 0.6× 121 0.5× 145 0.7× 33 1.6k
Michael F. Crouch Australia 25 1.1k 1.4× 351 1.1× 370 1.2× 167 0.7× 160 0.7× 59 1.7k
Sheryl P. Denker United States 8 1.1k 1.3× 326 1.0× 194 0.6× 104 0.4× 90 0.4× 10 1.6k
Paschal A. Oude Weernink Germany 20 1.2k 1.5× 458 1.4× 233 0.8× 115 0.5× 109 0.5× 27 1.6k
Felicity M. Davis Australia 22 1.1k 1.3× 150 0.5× 260 0.9× 492 1.9× 194 0.9× 36 1.9k
Steve Stippec United States 19 1.5k 1.8× 276 0.9× 93 0.3× 142 0.6× 96 0.4× 28 1.9k

Countries citing papers authored by Sayoko Ihara

Since Specialization
Citations

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

Fields of papers citing papers by Sayoko Ihara

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sayoko Ihara

This figure shows the co-authorship network connecting the top 25 collaborators of Sayoko Ihara. A scholar is included among the top collaborators of Sayoko Ihara 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 Sayoko Ihara. Sayoko Ihara 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.
Inaba, Toshiki, Takahiro Osada, Tomohiro Nishizawa, et al.. (2024). Bicarbonate signalling via G protein-coupled receptor regulates ischaemia-reperfusion injury. Nature Communications. 15(1). 1530–1530. 6 indexed citations
2.
Nagata, Koji, et al.. (2022). Structural model for ligand binding and channel opening of an insect gustatory receptor. Journal of Biological Chemistry. 298(11). 102573–102573. 15 indexed citations
3.
Horio, Nao, Keiichi Yoshikawa, Yoshihito Niimura, et al.. (2016). Ligand Specificity and Evolution of Mammalian Musk Odor Receptors: Effect of Single Receptor Deletion on Odor Detection. Journal of Neuroscience. 36(16). 4482–4491. 49 indexed citations
4.
Kodama, Hiroki, et al.. (2015). Simple model of pH-induced protein denaturation. Physical Review E. 92(1). 12709–12709. 3 indexed citations
5.
Hopf, Thomas A., et al.. (2015). Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors. Nature Communications. 6(1). 6077–6077. 96 indexed citations
6.
Kato, Aya, Johannes Reisert, Sayoko Ihara, Keiichi Yoshikawa, & Kazushige Touhara. (2014). Evaluation of the Role of G Protein-Coupled Receptor Kinase 3 in Desensitization of Mouse Odorant Receptors in a Mammalian Cell Line and in Olfactory Sensory Neurons. Chemical Senses. 39(9). 771–780. 10 indexed citations
7.
Ihara, Sayoko, Keiichi Yoshikawa, & Kazushige Touhara. (2013). Chemosensory signals and their receptors in the olfactory neural system. Neuroscience. 254. 45–60. 53 indexed citations
8.
Murugan, Avaniyapuram Kannan, Sayoko Ihara, Emi Tokuda, et al.. (2008). SWAP‐70 is important for invasive phenotypes of mouse embryo fibroblasts transformed by v‐Src. IUBMB Life. 60(4). 236–240. 12 indexed citations
9.
Ihara, Sayoko, et al.. (2007). Pleckstrin-2 selectively interacts with phosphatidylinositol 3-kinase lipid products and regulates actin organization and cell spreading. Biochemical and Biophysical Research Communications. 361(2). 270–275. 28 indexed citations
10.
Fukui, Yasuhisa, et al.. (2007). Activity of β3‐β4 loop of the PH domain is required for the membrane targeting of SWAP‐70. IUBMB Life. 59(2). 99–103. 3 indexed citations
11.
Konishi, Hiroaki, et al.. (2006). Mutation of the PI3′ Kinase Gene in a Human Colon Carcinoma Cell Line, HCC2998. DNA and Cell Biology. 25(7). 399–405. 6 indexed citations
12.
Oka, Tsutomu, Sayoko Ihara, & Yasuhisa Fukui. (2006). Cooperation of DEF6 with Activated Rac in Regulating Cell Morphology. Journal of Biological Chemistry. 282(3). 2011–2018. 32 indexed citations
13.
Ihara, Sayoko, et al.. (2006). Mutational analysis on the function of the SWAP-70 PH domain. Molecular and Cellular Biochemistry. 293(1-2). 137–145. 20 indexed citations
14.
Kobayashi, Michimoto, et al.. (2003). Activation of ErbB3–PI3-kinase pathway is correlated with malignant phenotypes of adenocarcinomas. Oncogene. 22(9). 1294–1301. 38 indexed citations
15.
Shinohara, Azusa, et al.. (2002). Identification of ribosomal protein S3a as a candidate for a novel PI 3-kinase target in the nucleus. Cytotechnology. 40(1-3). 85–92. 2 indexed citations
16.
Shinohara, Masahiro, Yoh Terada, Akihiro Iwamatsu, et al.. (2002). SWAP-70 is a guanine-nucleotide-exchange factor that mediates signalling of membrane ruffling. Nature. 416(6882). 759–763. 182 indexed citations
17.
Nagata, Satoshi, et al.. (2000). Quantification of Phosphatidylinositol 3,4,5-Trisphosphate by Liposome Lysis Assay with Specific Monoclonal Antibodies. Analytical Biochemistry. 285(2). 270–273. 3 indexed citations
18.
Yokogawa, Tohei, Satoshi Nagata, Tomoaki Tsutsumi, et al.. (2000). Evidence that 3′‐phosphorylated polyphosphoinositides are generated at the nuclear surface: use of immunostaining technique with monoclonal antibodies specific for PI 3,4‐P2. FEBS Letters. 473(2). 222–226. 48 indexed citations
19.
Ihara, Sayoko. (1997). Dual control of neurite outgrowth by STAT3 and MAP kinase in PC12 cells stimulated with interleukin-6. The EMBO Journal. 16(17). 5345–5352. 132 indexed citations
20.
Ihara, Sayoko, et al.. (1996). A Novel Differentiation Factor for PC12 Cells from Culture Supernatant of Mouse Hepatocyte Cell Line MLE-15A2. Bioscience Biotechnology and Biochemistry. 60(8). 1339–1345. 1 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

Breakdown of academic impact, for papers by Nicolas Bourmeyster Breakdown of academic impact, for papers by Sascha E. Dho Breakdown of academic impact, for papers by Nobuhiko Yokoyama Breakdown of academic impact, for papers by Hiroshi Ueda Breakdown of academic impact, for papers by Ilia A. Yamboliev Breakdown of academic impact, for papers by Michael F. Crouch Breakdown of academic impact, for papers by Sheryl P. Denker Breakdown of academic impact, for papers by Paschal A. Oude Weernink Breakdown of academic impact, for papers by Felicity M. Davis Breakdown of academic impact, for papers by Steve Stippec
Rankless by CCL
2026