Toru Nishinaka

1.8k total citations
62 papers, 1.5k citations indexed

About

Toru Nishinaka is a scholar working on Cell Biology, Molecular Biology and Physiology. According to data from OpenAlex, Toru Nishinaka has authored 62 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Cell Biology, 28 papers in Molecular Biology and 15 papers in Physiology. Recurrent topics in Toru Nishinaka's work include Aldose Reductase and Taurine (33 papers), Prenatal Substance Exposure Effects (12 papers) and Genomics, phytochemicals, and oxidative stress (9 papers). Toru Nishinaka is often cited by papers focused on Aldose Reductase and Taurine (33 papers), Prenatal Substance Exposure Effects (12 papers) and Genomics, phytochemicals, and oxidative stress (9 papers). Toru Nishinaka collaborates with scholars based in Japan, United States and South Korea. Toru Nishinaka's co-authors include Chihiro Yabe‐Nishimura, Tomoyuki Terada, Takeshi Miura, Masato Katsuyama, K Iwata, Han Geuk Seo, Robert Chiu, Kazunari K. Yokoyama, Chunyuan Fan and Toshiyuki Matsunaga and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and The Journal of Immunology.

In The Last Decade

Toru Nishinaka

61 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
Toru Nishinaka Japan 22 769 444 282 176 125 62 1.5k
Ravinder Tammali United States 19 637 0.8× 611 1.4× 129 0.5× 80 0.5× 82 0.7× 34 1.2k
Doina Popov Romania 25 785 1.0× 265 0.6× 495 1.8× 240 1.4× 90 0.7× 65 2.1k
Toshiaki Fukutomi Japan 11 1.3k 1.7× 209 0.5× 184 0.7× 124 0.7× 105 0.8× 34 2.0k
Shaogui Wang China 28 1.0k 1.3× 207 0.5× 220 0.8× 190 1.1× 411 3.3× 45 2.3k
Sang Mi Shin South Korea 23 932 1.2× 149 0.3× 156 0.6× 90 0.5× 77 0.6× 35 1.6k
Elaine M. Khan United States 16 643 0.8× 196 0.4× 183 0.6× 148 0.8× 88 0.7× 18 1.4k
Hae‐Young Chung South Korea 20 1.3k 1.7× 122 0.3× 392 1.4× 162 0.9× 99 0.8× 34 2.1k
Soona Shin United States 20 1.6k 2.1× 161 0.4× 292 1.0× 177 1.0× 80 0.6× 27 2.3k
Kuo Du United States 23 646 0.8× 206 0.5× 122 0.4× 93 0.5× 196 1.6× 36 2.3k
Sudhir Chowdhry United Kingdom 14 2.4k 3.1× 214 0.5× 271 1.0× 194 1.1× 123 1.0× 16 3.1k

Countries citing papers authored by Toru Nishinaka

Since Specialization
Citations

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

Fields of papers citing papers by Toru Nishinaka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Toru Nishinaka

This figure shows the co-authorship network connecting the top 25 collaborators of Toru Nishinaka. A scholar is included among the top collaborators of Toru Nishinaka 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 Toru Nishinaka. Toru Nishinaka 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.
Shimizu, Kahori, Hideo Shindou, Koji Tomita, & Toru Nishinaka. (2025). Approaches to the Treatment of Lifestyle-related Diseases Through the Regulation of Phospholipid Biosynthesis in the Liver. YAKUGAKU ZASSHI. 145(3). 171–176. 1 indexed citations
2.
Shimizu, Kahori, Shotaro Michinaga, Hiroki Nakanishi, et al.. (2024). Overexpression of lysophospholipid acyltransferase, LPLAT10 / LPCAT4 / LPEAT2 , in the mouse liver increases glucose‐stimulated insulin secretion. The FASEB Journal. 38(2). e23425–e23425. 2 indexed citations
3.
Ikejiri, Masahiro, Takuya Ito, Katsuhito Nagai, et al.. (2023). Impact of Different Attitudes toward Face-to-Face and Online Classes on Learning Outcomes in Japan. SHILAP Revista de lepidopterología. 11(1). 16–16. 1 indexed citations
4.
Shimizu, Kahori, Shotaro Michinaga, Tomoyuki Terada, et al.. (2022). Liver-specific overexpression of lipoprotein lipase improves glucose metabolism in high-fat diet-fed mice. PLoS ONE. 17(9). e0274297–e0274297. 18 indexed citations
5.
Endo, Satoshi, et al.. (2021). Loxoprofen enhances intestinal barrier function via generation of its active metabolite by carbonyl reductase 1 in differentiated Caco-2 cells. Chemico-Biological Interactions. 348. 109634–109634. 5 indexed citations
6.
Tsutsui, Hidenobu, Takeshi Miura, Kohei Hayashi, et al.. (2018). Post-treatment with JP-1302 protects against renal ischemia/reperfusion-induced acute kidney injury in rats. Journal of Pharmacological Sciences. 139(3). 137–142. 10 indexed citations
7.
Tsutsui, Hidenobu, Takeshi Miura, Toru Nishinaka, et al.. (2018). Inhibition of α2C-adrenoceptors ameliorates cisplatin-induced acute renal failure in rats. European Journal of Pharmacology. 838. 113–119. 5 indexed citations
8.
Arai, Yuki, Satoshi Endo, Naohito Abe, et al.. (2014). Structure–activity relationship of flavonoids as potent inhibitors of carbonyl reductase 1 (CBR1). Fitoterapia. 101. 51–56. 30 indexed citations
9.
Nishinaka, Toru, et al.. (2011). Regulation of aldo–keto reductase AKR1B10 gene expression: Involvement of transcription factor Nrf2. Chemico-Biological Interactions. 191(1-3). 185–191. 61 indexed citations
10.
Terada, Tomoyuki, et al.. (2010). Site‐directed mutagenesis of rat thioltransferase: Effects of essential cysteine residues for the protection against oxidative stress. Journal of Biochemical and Molecular Toxicology. 24(1). 60–65. 3 indexed citations
11.
Miura, Takeshi, Toru Nishinaka, & Tomoyuki Terada. (2009). Importance of the substrate-binding loop region of human monomeric carbonyl reductases in catalysis and coenzyme binding. Life Sciences. 85(7-8). 303–308. 6 indexed citations
12.
Miura, Takeshi, Toru Nishinaka, Tomoyuki Terada, & Kazuya Yonezawa. (2009). Relationship between aging and dosage of warfarin: The current status of warfarin anticoagulant therapy for Japanese outpatients in a department of cardiovascular medicine. Journal of Cardiology. 53(3). 355–360. 16 indexed citations
13.
Miura, Takeshi, et al.. (2008). Investigation of the role of the amino acid residue at position 230 for catalysis in monomeric carbonyl reductase 3. Chemico-Biological Interactions. 178(1-3). 211–214. 4 indexed citations
14.
15.
Kang, Eun Sil, Im Sun Woo, Hyo Jung Kim, et al.. (2007). Up-regulation of aldose reductase expression mediated by phosphatidylinositol 3-kinase/Akt and Nrf2 is involved in the protective effect of curcumin against oxidative damage. Free Radical Biology and Medicine. 43(4). 535–545. 89 indexed citations
16.
Nishinaka, Toru, Shinzo Kimura, Masato Katsuyama, et al.. (2007). Curcumin activates human glutathione S-transferase P1 expression through antioxidant response element. Toxicology Letters. 170(3). 238–247. 105 indexed citations
17.
Paek, Kyung Shin, et al.. (2005). Phorbol ester up-regulates aldose reductase expression in A549 cells: a potential role for aldose reductase in cell cycle modulation. Cellular and Molecular Life Sciences. 62(10). 1146–1155. 14 indexed citations
18.
Yabe‐Nishimura, Chihiro, Toru Nishinaka, K Iwata, & Han Geuk Seo. (2003). Up-regulation of aldose reductase by the substrate, methylglyoxal. Chemico-Biological Interactions. 143-144. 317–323. 17 indexed citations
19.
Nishitani, Junko, et al.. (1999). Recruitment of the Retinoblastoma Protein to c-Jun Enhances Transcription Activity Mediated through the AP-1 Binding Site. Journal of Biological Chemistry. 274(9). 5454–5461. 36 indexed citations
20.
Nishinaka, Toru, et al.. (1997). A unique cathepsin-like protease isolated from CV-1 cells is involved in rapid degradation of retinoblastoma susceptibility gene product, RB, and transcription factor SP1. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1351(3). 274–286. 35 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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