Toshihide Kimura

669 total citations
20 papers, 570 citations indexed

About

Toshihide Kimura is a scholar working on Surgery, Molecular Biology and Cell Biology. According to data from OpenAlex, Toshihide Kimura has authored 20 papers receiving a total of 570 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Surgery, 7 papers in Molecular Biology and 7 papers in Cell Biology. Recurrent topics in Toshihide Kimura's work include Pancreatic function and diabetes (10 papers), Sulfur Compounds in Biology (6 papers) and Cellular transport and secretion (5 papers). Toshihide Kimura is often cited by papers focused on Pancreatic function and diabetes (10 papers), Sulfur Compounds in Biology (6 papers) and Cellular transport and secretion (5 papers). Toshihide Kimura collaborates with scholars based in Japan and United States. Toshihide Kimura's co-authors include Ichiro Niki, Shigeki Taniguchi, Yukiko Kaneko, Lin Kang, Toshimasa Ishizaki, Mitsuhiro Okamoto, Yumiko Kojima, Yuka Kimura, Hideo Kimura and Akihiro Iwamatsu and has published in prestigious journals such as Biochemical and Biophysical Research Communications, Journal of Cell Science and FEBS Letters.

In The Last Decade

Toshihide Kimura

19 papers receiving 563 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Toshihide Kimura Japan 11 281 182 175 115 106 20 570
Tianluo Lei China 12 113 0.4× 307 1.7× 85 0.5× 128 1.1× 146 1.4× 16 622
So Nagai Japan 13 116 0.4× 275 1.5× 107 0.6× 62 0.5× 200 1.9× 53 713
Britta M. Stenson Sweden 11 187 0.7× 220 1.2× 131 0.7× 34 0.3× 304 2.9× 11 546
Srijana Ranjit Nepal 4 349 1.2× 259 1.4× 81 0.5× 83 0.7× 406 3.8× 6 644
Mark A. Duerr United States 6 81 0.3× 202 1.1× 132 0.8× 67 0.6× 83 0.8× 8 459
Sharmila Adhikari Singapore 12 127 0.5× 163 0.9× 118 0.7× 33 0.3× 60 0.6× 18 415
T. Nakai Japan 13 90 0.3× 158 0.9× 172 1.0× 27 0.2× 126 1.2× 27 560
C Pacot France 9 152 0.5× 707 3.9× 312 1.8× 64 0.6× 196 1.8× 14 968
Samantha L. Hoopes United States 14 270 1.0× 183 1.0× 42 0.2× 26 0.2× 71 0.7× 14 599
Maija Vaittinen Finland 15 72 0.3× 224 1.2× 98 0.6× 23 0.2× 173 1.6× 23 567

Countries citing papers authored by Toshihide Kimura

Since Specialization
Citations

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

Fields of papers citing papers by Toshihide Kimura

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Toshihide Kimura

This figure shows the co-authorship network connecting the top 25 collaborators of Toshihide Kimura. A scholar is included among the top collaborators of Toshihide Kimura 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 Toshihide Kimura. Toshihide Kimura 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.
Watanabe, Naoya, Yukiko Kaneko, Hisamitsu Ishihara, et al.. (2024). Diacylglycerol kinase ζ is a positive insulin secretion regulator in pancreatic β-cell line MIN6. Biochemical and Biophysical Research Communications. 742. 151109–151109.
2.
Ihim, Stella Amarachi, et al.. (2023). Apigenin Alleviates Endoplasmic Reticulum Stress-Mediated Apoptosis in INS-1 β-Cells. Biological and Pharmaceutical Bulletin. 46(4). 630–635. 10 indexed citations
3.
Kaneko, Yukiko, Naoya Watanabe, Akira Minami, et al.. (2022). Asymmetric dimethylarginine accumulation under hyperglycemia facilitates β-cell apoptosis via inhibiting nitric oxide production. Biochemical and Biophysical Research Communications. 637. 108–116. 1 indexed citations
4.
Yamaguchi, Momoka, et al.. (2022). Harmine suppresses collagen production in hepatic stellate cells by inhibiting DYRK1B. Biochemical and Biophysical Research Communications. 600. 136–141. 7 indexed citations
5.
Terabayashi, Takeshi, Tomoki Nishioka, Kozo Kaibuchi, et al.. (2019). IRR is involved in glucose-induced endocytosis after insulin secretion. Journal of Pharmacological Sciences. 140(3). 300–304. 2 indexed citations
6.
Kimura, Toshihide, et al.. (2019). GDP-Bound Rab27a Dissociates from the Endocytic Machinery in a Phosphorylation-Dependent Manner after Insulin Secretion. Biological and Pharmaceutical Bulletin. 42(9). 1532–1537. 1 indexed citations
7.
Terabayashi, Takeshi, Katsuhiro Hanada, Kou Motani, et al.. (2018). Baicalein disturbs the morphological plasticity and motility of breast adenocarcinoma cells depending on the tumor microenvironment. Genes to Cells. 23(6). 466–479. 11 indexed citations
8.
Sato, Yuka, Takeshi Ikeda, Koh Yamashita, et al.. (2018). Pharmacokinetics of insulin disappearance after massive overdosing. Endocrine Journal. 65(11). 1147–1153. 4 indexed citations
9.
Okamoto, Mitsuhiro, Toshimasa Ishizaki, & Toshihide Kimura. (2014). Protective effect of hydrogen sulfide on pancreatic beta-cells. Nitric Oxide. 46. 32–36. 27 indexed citations
10.
Okamoto, Mitsuhiro, Masahiro Takei, Tomomi Ando, et al.. (2013). Endogenous hydrogen sulfide protects pancreatic beta-cells from a high-fat diet-induced glucotoxicity and prevents the development of type 2 diabetes. Biochemical and Biophysical Research Communications. 442(3-4). 227–233. 50 indexed citations
11.
Okamoto, Mitsuhiro, et al.. (2013). [Hydrogen sulfide and its effect on pancreatic beta-cells].. PubMed. 71(1). 175–80. 2 indexed citations
12.
Yamamoto, Junichiro, Waichi Sato, Tomoki Kosugi, et al.. (2012). Distribution of hydrogen sulfide (H2S)-producing enzymes and the roles of the H2S donor sodium hydrosulfide in diabetic nephropathy. Clinical and Experimental Nephrology. 17(1). 32–40. 83 indexed citations
14.
Taniguchi, Shigeki, Lin Kang, Toshihide Kimura, & Ichiro Niki. (2010). Hydrogen sulphide protects mouse pancreatic β‐cells from cell death induced by oxidative stress, but not by endoplasmic reticulum stress. British Journal of Pharmacology. 162(5). 1171–1178. 92 indexed citations
15.
Kimura, Toshihide & Ichiro Niki. (2010). Rab27a, actin and beta-cell endocytosis [Review]. Endocrine Journal. 58(1). 1–6. 17 indexed citations
16.
Kimura, Toshihide, et al.. (2010). Glucose-induced translocation of coronin 3 regulates the retrograde transport of the secretory membrane in the pancreatic β-cells. Biochemical and Biophysical Research Communications. 395(3). 318–323. 13 indexed citations
17.
Yuzawa, Yukio, Ichiro Niki, Tomoki Kosugi, et al.. (2008). Overexpression of Calmodulin in Pancreatic β Cells Induces Diabetic Nephropathy. Journal of the American Society of Nephrology. 19(9). 1701–1711. 16 indexed citations
18.
Kaneko, Yukiko, Toshihide Kimura, Shigeki Taniguchi, et al.. (2008). Glucose‐induced production of hydrogen sulfide may protect the pancreatic beta‐cells from apoptotic cell death by high glucose. FEBS Letters. 583(2). 377–382. 82 indexed citations
19.
Kimura, Toshihide, Yukiko Kaneko, Hisamitsu Ishihara, et al.. (2008). The GDP-dependent Rab27a effector coronin 3 controls endocytosis of secretory membrane in insulin-secreting cell lines. Journal of Cell Science. 121(18). 3092–3098. 61 indexed citations
20.
Tsunekawa, Shin, Naoki Yamamoto, Katsura Tsukamoto, et al.. (2007). Protection of pancreatic β-cells by exendin-4 may involve the reduction of endoplasmic reticulum stress; in vivo and in vitro studies. Journal of Endocrinology. 193(1). 65–74. 90 indexed citations

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