Satoshi Sogabe

2.8k total citations
44 papers, 2.2k citations indexed

About

Satoshi Sogabe is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Satoshi Sogabe has authored 44 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 13 papers in Oncology and 12 papers in Organic Chemistry. Recurrent topics in Satoshi Sogabe's work include Cancer therapeutics and mechanisms (9 papers), Photosynthetic Processes and Mechanisms (5 papers) and HER2/EGFR in Cancer Research (4 papers). Satoshi Sogabe is often cited by papers focused on Cancer therapeutics and mechanisms (9 papers), Photosynthetic Processes and Mechanisms (5 papers) and HER2/EGFR in Cancer Research (4 papers). Satoshi Sogabe collaborates with scholars based in Japan, United States and Switzerland. Satoshi Sogabe's co-authors include Tomoyasu Ishikawa, Toshimasa Tanaka, Yoshikazu Ohta, Hiroshi Miki, Noriyuki Habuka, Yasuhiko Shiratori, Hirosato Ebiike, Yuko Aoki, Miyako Masubuchi and Kiyoaki Sakata and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Satoshi Sogabe

43 papers receiving 2.2k citations

Peers

Satoshi Sogabe
Chuan Shih United States
Hai‐Bing Zhou China
Khaled A. M. Abouzid Egypt
Martin Rowlands United Kingdom
Juan Sun China
James R. Kiefer United States
Shilong Zheng United States
Giuseppe Giannini Italy
Bing Xiong China
Chuan Shih United States
Satoshi Sogabe
Citations per year, relative to Satoshi Sogabe Satoshi Sogabe (= 1×) peers Chuan Shih

Countries citing papers authored by Satoshi Sogabe

Since Specialization
Citations

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

Fields of papers citing papers by Satoshi Sogabe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Satoshi Sogabe

This figure shows the co-authorship network connecting the top 25 collaborators of Satoshi Sogabe. A scholar is included among the top collaborators of Satoshi Sogabe 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 Satoshi Sogabe. Satoshi Sogabe 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.
2.
Shibata, Sachio, Satoshi Sogabe, Masanori Miwa, et al.. (2021). Identification of the first highly selective inhibitor of human lactate dehydrogenase B. Scientific Reports. 11(1). 21353–21353. 37 indexed citations
3.
Kunugi, Akiyoshi, et al.. (2018). HBT1, a Novel AMPA Receptor Potentiator with Lower Agonistic Effect, Avoided Bell-Shaped Response in In Vitro BDNF Production. Journal of Pharmacology and Experimental Therapeutics. 364(3). 377–389. 23 indexed citations
4.
Yasui, Takeshi, Takeshi Yamamoto, Nozomu Sakai, et al.. (2017). Discovery of a novel B-cell lymphoma 6 (BCL6)–corepressor interaction inhibitor by utilizing structure-based drug design. Bioorganic & Medicinal Chemistry. 25(17). 4876–4886. 21 indexed citations
5.
Sakamoto, Kotaro, Yoshihiro Ishibashi, Ryutaro Adachi, et al.. (2017). Identification of cytidine-5-triphosphate synthase1-selective inhibitory peptide from random peptide library displayed on T7 phage. Peptides. 94. 56–63. 6 indexed citations
6.
Sogabe, Satoshi, et al.. (2017). Discovery of a Kelch-like ECH-associated protein 1-inhibitory tetrapeptide and its structural characterization. Biochemical and Biophysical Research Communications. 486(3). 620–625. 11 indexed citations
7.
Sakamoto, Kotaro, Satoshi Sogabe, Yusuke Kamada, et al.. (2016). Discovery of high-affinity BCL6-binding peptide and its structure-activity relationship. Biochemical and Biophysical Research Communications. 482(2). 310–316. 26 indexed citations
8.
Sakamoto, Kotaro, Satoshi Sogabe, Yusuke Kamada, et al.. (2016). Discovery of GPX4 inhibitory peptides from random peptide T7 phage display and subsequent structural analysis. Biochemical and Biophysical Research Communications. 482(2). 195–201. 46 indexed citations
9.
Hasui, Tomoaki, Norio Ohyabu, Hideki Matsui, et al.. (2013). Design, synthesis, and structure–activity relationships of dihydrofuran-2-one and dihydropyrrol-2-one derivatives as novel benzoxazin-3-one-based mineralocorticoid receptor antagonists. Bioorganic & Medicinal Chemistry. 21(19). 5983–5994. 23 indexed citations
10.
Ishikawa, Tomoyasu, Masaki Seto, Hiroshi Banno, et al.. (2011). Design and Synthesis of Novel Human Epidermal Growth Factor Receptor 2 (HER2)/Epidermal Growth Factor Receptor (EGFR) Dual Inhibitors Bearing a Pyrrolo[3,2-d]pyrimidine Scaffold. Journal of Medicinal Chemistry. 54(23). 8030–8050. 180 indexed citations
11.
Aertgeerts, Kathleen, R.J. Skene, Jason K. Yano, et al.. (2011). Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. Journal of Biological Chemistry. 286(21). 18756–18765. 310 indexed citations
12.
Asano, Yasutomi, Shuji Kitamura, Kazuyoshi Aso, et al.. (2008). Discovery, synthesis and biological evaluation of isoquinolones as novel and highly selective JNK inhibitors (1). Bioorganic & Medicinal Chemistry. 16(8). 4715–4732. 24 indexed citations
13.
Asano, Yasutomi, Shuji Kitamura, Fumio Itoh, et al.. (2008). Discovery, synthesis and biological evaluation of isoquinolones as novel and highly selective JNK inhibitors (2). Bioorganic & Medicinal Chemistry. 16(8). 4699–4714. 75 indexed citations
14.
Kawasaki, Ken‐ichi, Miyako Masubuchi, Kenji Morikami, et al.. (2003). Design and synthesis of novel benzofurans as a new class of antifungal agents targeting fungal N-myristoyltransferase. Part 3. Bioorganic & Medicinal Chemistry Letters. 13(1). 87–91. 90 indexed citations
15.
Sogabe, Satoshi, Miyako Masubuchi, Kiyoaki Sakata, et al.. (2002). Crystal Structures of Candida albicans N-Myristoyltransferase with Two Distinct Inhibitors. Chemistry & Biology. 9(10). 1119–1128. 107 indexed citations
16.
Ebiike, Hirosato, Miyako Masubuchi, Pingli Liu, et al.. (2002). Design and synthesis of novel benzofurans as a new class of antifungal agents targeting fungal N-myristoyltransferase. Part 2. Bioorganic & Medicinal Chemistry Letters. 12(4). 607–610. 66 indexed citations
17.
18.
Sogabe, Satoshi & Kunio Miki. (1995). Refined Crystal Structure of Ferrocytochromec2fromRhodopseudomonas viridisat 1.6 Å Resolution. Journal of Molecular Biology. 252(2). 235–247. 24 indexed citations
19.
Miki, Kunio, et al.. (1994). Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis. Acta Crystallographica Section D Biological Crystallography. 50(3). 271–275. 2 indexed citations
20.

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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