Yoshiko Tampo

944 total citations
36 papers, 842 citations indexed

About

Yoshiko Tampo is a scholar working on Molecular Biology, Physiology and Surgery. According to data from OpenAlex, Yoshiko Tampo has authored 36 papers receiving a total of 842 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 8 papers in Physiology and 6 papers in Surgery. Recurrent topics in Yoshiko Tampo's work include Heme Oxygenase-1 and Carbon Monoxide (8 papers), Advanced Glycation End Products research (6 papers) and Paraquat toxicity studies and treatments (5 papers). Yoshiko Tampo is often cited by papers focused on Heme Oxygenase-1 and Carbon Monoxide (8 papers), Advanced Glycation End Products research (6 papers) and Paraquat toxicity studies and treatments (5 papers). Yoshiko Tampo collaborates with scholars based in Japan, United States and China. Yoshiko Tampo's co-authors include Masanori Yonaha, Ryosuke Tatsunami, Balaraman Kalyanaraman, Christopher R. Chitambar, Joy Joseph, Srigiridhar Kotamraju, Ágnes Keszler, Keisuke Sato, Shasi V. Kalivendi and Minoru Sawada and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Circulation Research and FEBS Letters.

In The Last Decade

Yoshiko Tampo

36 papers receiving 827 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yoshiko Tampo Japan 18 370 165 105 99 87 36 842
Gabriele Hakim Italy 17 503 1.4× 140 0.8× 66 0.6× 145 1.5× 54 0.6× 43 928
Lucia Cavallini Italy 23 743 2.0× 329 2.0× 105 1.0× 110 1.1× 81 0.9× 71 1.5k
Gunilla Ekström Sweden 17 463 1.3× 163 1.0× 141 1.3× 56 0.6× 227 2.6× 30 1.5k
Jeroen Frijhoff Sweden 12 781 2.1× 227 1.4× 71 0.7× 172 1.7× 100 1.1× 13 1.5k
Julia Watson United States 11 675 1.8× 221 1.3× 65 0.6× 113 1.1× 77 0.9× 19 1.5k
Munekazu Gemba Japan 20 497 1.3× 90 0.5× 92 0.9× 138 1.4× 149 1.7× 93 1.4k
Ajay Madan United States 20 364 1.0× 96 0.6× 104 1.0× 108 1.1× 103 1.2× 62 1.6k
Asjad Visnagri United Kingdom 11 285 0.8× 148 0.9× 67 0.6× 75 0.8× 50 0.6× 15 886
Bashir M. Rezk United States 15 555 1.5× 186 1.1× 53 0.5× 58 0.6× 41 0.5× 26 1.2k
Johanna Lång Austria 9 282 0.8× 107 0.6× 77 0.7× 153 1.5× 72 0.8× 20 865

Countries citing papers authored by Yoshiko Tampo

Since Specialization
Citations

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

Fields of papers citing papers by Yoshiko Tampo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshiko Tampo

This figure shows the co-authorship network connecting the top 25 collaborators of Yoshiko Tampo. A scholar is included among the top collaborators of Yoshiko Tampo 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 Yoshiko Tampo. Yoshiko Tampo 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.
Kimura, Junpei, et al.. (2018). Low concentrations of clarithromycin upregulate cellular antioxidant enzymes and phosphorylation of extracellular signal-regulated kinase in human small airway epithelial cells. Journal of Pharmaceutical Health Care and Sciences. 4(1). 23–23. 2 indexed citations
2.
Sato, Keisuke, et al.. (2016). Epalrestat Upregulates Heme Oxygenase-1, Superoxide Dismutase, and Catalase in Cells of the Nervous System. Biological and Pharmaceutical Bulletin. 39(9). 1523–1530. 24 indexed citations
3.
Sato, Keisuke, et al.. (2015). Glycolaldehyde induces endoplasmic reticulum stress and apoptosis in Schwann cells. Toxicology Reports. 2. 1454–1462. 10 indexed citations
4.
Sato, Keisuke, et al.. (2014). Epalrestat increases glutathione, thioredoxin, and heme oxygenase-1 by stimulating Nrf2 pathway in endothelial cells. Redox Biology. 4. 87–96. 32 indexed citations
5.
Sato, Keisuke, et al.. (2013). Glycolaldehyde Induces Cytotoxicity and Increases Glutathione and Multidrug-Resistance-Associated Protein Levels in Schwann Cells. Biological and Pharmaceutical Bulletin. 36(7). 1111–1117. 18 indexed citations
6.
Sato, Keisuke, et al.. (2013). Epalrestat increases intracellular glutathione levels in Schwann cells through transcription regulation. Redox Biology. 2. 15–21. 28 indexed citations
7.
8.
Tatsunami, Ryosuke, et al.. (2012). Methylglyoxal has deleterious effects on thioredoxin in human aortic endothelial cells. Environmental Toxicology and Pharmacology. 34(2). 117–126. 19 indexed citations
9.
Ohtaki, Ko‐ichi, et al.. (2012). Protective Effects of Clarithromycin, a Lipophilic 14-membered Macrolide, on Hemolysis Induced by Lysophosphatidylcholine in Human Erythrocytes. Iryo Yakugaku (Japanese Journal of Pharmaceutical Health Care and Sciences). 38(10). 617–627. 1 indexed citations
10.
Tatsunami, Ryosuke, et al.. (2009). Methylglyoxal Causes Dysfunction of Thioredoxin and Thioredoxin Reductase in Endothelial Cells. Journal of Pharmacological Sciences. 111(4). 426–432. 16 indexed citations
11.
Kotamraju, Srigiridhar, Yoshiko Tampo, Shasi V. Kalivendi, et al.. (2004). Nitric oxide mitigates peroxide-induced iron-signaling, oxidative damage, and apoptosis in endothelial cells: role of proteasomal function?. Archives of Biochemistry and Biophysics. 423(1). 74–80. 20 indexed citations
12.
Tampo, Yoshiko, Srigiridhar Kotamraju, Christopher R. Chitambar, et al.. (2003). Oxidative Stress–Induced Iron Signaling Is Responsible for Peroxide-Dependent Oxidation of Dichlorodihydrofluorescein in Endothelial Cells. Circulation Research. 92(1). 56–63. 137 indexed citations
13.
Tampo, Yoshiko, et al.. (2002). Paraquat-Induced Oxidative Stress and Dysfunction of the Glutathione Redox Cycle in Pulmonary Microvascular Endothelial Cells. Toxicology and Applied Pharmacology. 178(2). 82–92. 69 indexed citations
14.
Tampo, Yoshiko, et al.. (1999). Superoxide production from paraquat evoked by exogenous NADPH in pulmonary endothelial cells. Free Radical Biology and Medicine. 27(5-6). 588–595. 47 indexed citations
15.
16.
Tampo, Yoshiko, et al.. (1998). Lucigenin reduction by nadph‐cytochrome P450 reductase and the effect of phospholipids and albumin on chemiluminescence. IUBMB Life. 45(1). 115–123. 5 indexed citations
17.
Tampo, Yoshiko & Masanori Yonaha. (1996). Enzymatic and Molecular Aspects of the Antioxidant Effect of Menadione in Hepatic Microsomes. Archives of Biochemistry and Biophysics. 334(1). 163–174. 23 indexed citations
18.
Tampo, Yoshiko, Sukeo Onodera, & Masanori Yonaha. (1994). Mechanism of the biphasic effect of ethylenediaminetetraacetate on lipid peroxidation in iron-supported and reconstituted enzymatic system. Free Radical Biology and Medicine. 17(1). 27–34. 12 indexed citations
19.
Tampo, Yoshiko & Masanori Yonaha. (1991). Mechanism of cobalt (II) ion inhibition of iron-supported phospholipid peroxidation. Archives of Biochemistry and Biophysics. 289(1). 26–32. 16 indexed citations
20.
Tampo, Yoshiko & Masanori Yonaha. (1990). Vitamin E and Glutathione are Required for Preservation of Microsomal Glutathione S‐Transferase from Oxidative Stress in Microsomes. Pharmacology & Toxicology. 66(4). 259–265. 16 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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