Kazuhiko Igarashi

31.0k total citations · 7 hit papers
269 papers, 24.5k citations indexed

About

Kazuhiko Igarashi is a scholar working on Molecular Biology, Immunology and Oncology. According to data from OpenAlex, Kazuhiko Igarashi has authored 269 papers receiving a total of 24.5k indexed citations (citations by other indexed papers that have themselves been cited), including 190 papers in Molecular Biology, 56 papers in Immunology and 27 papers in Oncology. Recurrent topics in Kazuhiko Igarashi's work include Heme Oxygenase-1 and Carbon Monoxide (56 papers), Immune Cell Function and Interaction (27 papers) and Epigenetics and DNA Methylation (27 papers). Kazuhiko Igarashi is often cited by papers focused on Heme Oxygenase-1 and Carbon Monoxide (56 papers), Immune Cell Function and Interaction (27 papers) and Epigenetics and DNA Methylation (27 papers). Kazuhiko Igarashi collaborates with scholars based in Japan, United States and United Kingdom. Kazuhiko Igarashi's co-authors include Masayuki Yamamoto, Ken Itoh, Yasutake Katoh, Tetsuro Ishii, Norio Hayashi, Tomoki Chiba, James Douglas Engel, Nobunao Wakabayashi, Akihiko Muto and Satoru Takahashi and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Kazuhiko Igarashi

262 papers receiving 24.2k citations

Hit Papers

An Nrf2/Small Maf Heterodimer Mediates the Induction of P... 1993 2026 2004 2015 1997 1999 2004 1999 1993 1000 2.0k 3.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kazuhiko Igarashi Japan 69 18.3k 3.6k 2.1k 2.1k 1.8k 269 24.5k
Makoto Suematsu Japan 77 10.6k 0.6× 3.0k 0.8× 1.3k 0.6× 2.2k 1.1× 3.3k 1.8× 474 22.6k
Makoto Murakami Japan 72 9.2k 0.5× 3.3k 0.9× 3.0k 1.4× 2.1k 1.0× 2.4k 1.3× 429 19.0k
Shinya Toyokuni Japan 80 11.0k 0.6× 1.8k 0.5× 2.2k 1.0× 2.6k 1.3× 1.5k 0.8× 435 23.9k
Akiyoshi Fukamizu Japan 75 10.8k 0.6× 1.6k 0.4× 1.8k 0.8× 1.1k 0.6× 2.3k 1.3× 365 20.9k
John D. Hayes United Kingdom 84 27.9k 1.5× 1.7k 0.5× 1.8k 0.9× 3.2k 1.5× 2.2k 1.2× 262 37.1k
Stephen M. Prescott United States 89 9.1k 0.5× 6.1k 1.7× 2.5k 1.2× 2.7k 1.3× 2.4k 1.3× 233 25.6k
Santos A. Susín France 74 21.6k 1.2× 4.4k 1.2× 858 0.4× 2.3k 1.1× 1.8k 1.0× 142 29.0k
Hozumi Motohashi Japan 61 16.4k 0.9× 2.3k 0.6× 682 0.3× 2.2k 1.1× 1.8k 1.0× 175 22.9k
Naoufal Zamzami France 67 20.9k 1.1× 4.2k 1.2× 913 0.4× 2.3k 1.1× 1.8k 1.0× 92 28.2k
Shaker A. Mousa United States 73 9.6k 0.5× 1.8k 0.5× 1.2k 0.5× 2.7k 1.3× 1.2k 0.7× 665 24.6k

Countries citing papers authored by Kazuhiko Igarashi

Since Specialization
Citations

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

Fields of papers citing papers by Kazuhiko Igarashi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kazuhiko Igarashi

This figure shows the co-authorship network connecting the top 25 collaborators of Kazuhiko Igarashi. A scholar is included among the top collaborators of Kazuhiko Igarashi 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 Kazuhiko Igarashi. Kazuhiko Igarashi 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.
Matsumoto, Mitsuyo, Miki Watanabe‐Matsui, Tadashi Nakagawa, et al.. (2024). TANK Binding Kinase 1 Promotes BACH1 Degradation through Both Phosphorylation-Dependent and -Independent Mechanisms without Relying on Heme and FBXO22. International Journal of Molecular Sciences. 25(8). 4141–4141. 2 indexed citations
2.
Nishizawa, Hironari, Guan Chen, Mitsuyo Matsumoto, et al.. (2024). Intracellular biliverdin dynamics during ferroptosis. The Journal of Biochemistry. 176(6). 472–483.
3.
Niihori, Tetsuya, Akihiko Muto, Yoshikazu Hayashi, et al.. (2023). Mecom mutation related to radioulnar synostosis with amegakaryocytic thrombocytopenia reduces HSPCs in mice. Blood Advances. 7(18). 5409–5420. 2 indexed citations
4.
Alam, Mahabub, Hiroki Shima, Yoshitaka Matsuo, et al.. (2022). mTORC1-independent translation control in mammalian cells by methionine adenosyltransferase 2A and S-adenosylmethionine. Journal of Biological Chemistry. 298(7). 102084–102084. 8 indexed citations
5.
Cai, Lun, Ali S. Arbab, Tae Jin Lee, et al.. (2022). BACH1-Hemoxygenase-1 axis regulates cellular energetics and survival following sepsis. Free Radical Biology and Medicine. 188. 134–145. 19 indexed citations
6.
Satō, Masaki, Mitsuyo Matsumoto, Yuriko Saiki, et al.. (2020). BACH1 Promotes Pancreatic Cancer Metastasis by Repressing Epithelial Genes and Enhancing Epithelial–Mesenchymal Transition. Cancer Research. 80(6). 1279–1292. 82 indexed citations
7.
Shima, Hiroki, et al.. (2019). Haploinsufficient tumor suppressor Tip60 negatively regulates oncogenic Aurora B kinase. Journal of Biosciences. 44(6). 9 indexed citations
8.
Kishimoto, Daiga, Yohei Kirino, Maasa Tamura, et al.. (2018). Dysregulated heme oxygenase-1low M2-like macrophages augment lupus nephritis via Bach1 induced by type I interferons. Arthritis Research & Therapy. 20(1). 64–64. 39 indexed citations
9.
Nar, Rukiye, Álex Pérez, Masatoshi Ikeda, et al.. (2018). Identification of a Novel Enhancer/Chromatin Opening Element Associated with High-Level γ -Globin Gene Expression. Molecular and Cellular Biology. 38(19). 4 indexed citations
10.
Ito, Masato, Nobuhiko Nagano, Ryo Ogawa, et al.. (2017). Genetic ablation of Bach1 gene enhances recovery from hyperoxic lung injury in newborn mice via transient upregulation of inflammatory genes. Pediatric Research. 81(6). 926–931. 17 indexed citations
11.
Kasuga, Kie, Yasutake Katoh, Keisuke Nagase, & Kazuhiko Igarashi. (2017). Microproteomics with microfluidic‐based cell sorting: Application to 1000 and 100 immune cells. PROTEOMICS. 17(13-14). 23 indexed citations
12.
Kobayashi, Masahiro, Hiroki Kato, Ari Itoh‐Nakadai, et al.. (2016). Iron-heme-Bach1 axis is involved in erythroblast adaptation to iron deficiency. Haematologica. 102(3). 454–465. 23 indexed citations
13.
Watanabe‐Matsui, Miki, Tamami Uejima, Hiroki Shima, et al.. (2016). Charge-state-distribution analysis of Bach2 intrinsically disordered heme binding region. The Journal of Biochemistry. 160(5). 291–298. 15 indexed citations
14.
Maéda, Hiroshi, Youhei Yamagata, Kazutaka Murayama, et al.. (2015). Synergistic Effect of Neutral Protease and Clostripain on Rat Pancreatic Islet Isolation. Transplantation. 99(7). 1349–1355. 20 indexed citations
15.
Takada, Tsuyoshi, Shigeru Miyaki, Hiroyuki Ishitobi, et al.. (2015). Bach1 deficiency reduces severity of osteoarthritis through upregulation of heme oxygenase-1. Arthritis Research & Therapy. 17(1). 285–285. 68 indexed citations
16.
Brydun, Andrey, et al.. (2014). Bach1Deficiency and Accompanying Overexpression of Heme Oxygenase-1 Do Not Influence Aging or Tumorigenesis in Mice. Oxidative Medicine and Cellular Longevity. 2014. 1–12. 23 indexed citations
17.
Watanabe‐Matsui, Miki, Takashi Matsumoto, Toshitaka Matsui, et al.. (2014). Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. Archives of Biochemistry and Biophysics. 565. 25–31. 35 indexed citations
18.
Ohbayashi, Naomi, Takashi Matsumoto, Hiroki Shima, et al.. (2013). Solution Structure of Clostridial Collagenase H and Its Calcium-Dependent Global Conformation Change. Biophysical Journal. 104(7). 1538–1545. 19 indexed citations
19.
Inoue, Motoki, Susumu Tazuma, Keishi Kanno, et al.. (2010). Bach1 gene ablation reduces steatohepatitis in mouse MCD diet model. Journal of Clinical Biochemistry and Nutrition. 48(2). 161–166. 40 indexed citations
20.
Itoh, Ken, Hozumi Motohashi, Norio Hayashi, et al.. (1996). Bach Proteins Belong to a Novel Family of BTB-Basic Leucine Zipper Transcription Factors That Interact with MafK and Regulate Transcription through the NF-E2 Site. Molecular and Cellular Biology. 16(11). 6083–6095. 548 indexed citations breakdown →

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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