Tsunehiro Mizushima

8.0k total citations · 3 hit papers
60 papers, 5.5k citations indexed

About

Tsunehiro Mizushima is a scholar working on Molecular Biology, Cell Biology and Oncology. According to data from OpenAlex, Tsunehiro Mizushima has authored 60 papers receiving a total of 5.5k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 15 papers in Cell Biology and 14 papers in Oncology. Recurrent topics in Tsunehiro Mizushima's work include Ubiquitin and proteasome pathways (30 papers), Glycosylation and Glycoproteins Research (17 papers) and Endoplasmic Reticulum Stress and Disease (13 papers). Tsunehiro Mizushima is often cited by papers focused on Ubiquitin and proteasome pathways (30 papers), Glycosylation and Glycoproteins Research (17 papers) and Endoplasmic Reticulum Stress and Disease (13 papers). Tsunehiro Mizushima collaborates with scholars based in Japan, United Kingdom and United States. Tsunehiro Mizushima's co-authors include Keiji Tanaka, Tomitake Tsukihara, Kenji Takagi, Masaaki Komatsu, Yu‐shin Sou, Yoshinobu Ichimura, Takashi Yamane, Eiki Yamashita, Masayuki Yamamoto and Toshiaki Fukutomi and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Tsunehiro Mizushima

59 papers receiving 5.4k citations

Hit Papers

Phosphorylation of p62 Ac... 1998 2026 2007 2016 2013 1998 2008 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tsunehiro Mizushima Japan 29 4.2k 1.5k 1.1k 539 502 60 5.5k
Frank Löhr Germany 41 4.3k 1.0× 1.2k 0.8× 768 0.7× 436 0.8× 268 0.5× 150 6.1k
Gary S. Shaw Canada 41 4.2k 1.0× 1.0k 0.7× 430 0.4× 632 1.2× 552 1.1× 153 5.5k
Bradley J. Backes United States 30 2.9k 0.7× 871 0.6× 1.4k 1.3× 588 1.1× 450 0.9× 45 5.0k
Janet Finer-Moore United States 38 4.6k 1.1× 720 0.5× 1.1k 1.0× 843 1.6× 330 0.7× 97 6.4k
Chris Meisinger Germany 63 11.3k 2.7× 1.1k 0.7× 1.4k 1.2× 383 0.7× 250 0.5× 119 12.5k
Ching‐Shih Chen United States 44 4.7k 1.1× 521 0.4× 651 0.6× 1.0k 1.9× 616 1.2× 144 6.8k
Bernard Guiard France 68 11.8k 2.8× 585 0.4× 1.4k 1.3× 237 0.4× 243 0.5× 156 12.6k
Matthieu Schapira Canada 46 8.2k 2.0× 969 0.7× 2.0k 1.8× 1.1k 2.0× 559 1.1× 114 10.4k
Xiaolan Zhao United States 38 6.0k 1.4× 466 0.3× 1.1k 1.0× 1.4k 2.6× 176 0.4× 132 7.3k
John E. Burke Canada 45 4.1k 1.0× 472 0.3× 1.2k 1.1× 500 0.9× 597 1.2× 127 5.8k

Countries citing papers authored by Tsunehiro Mizushima

Since Specialization
Citations

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

Fields of papers citing papers by Tsunehiro Mizushima

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tsunehiro Mizushima

This figure shows the co-authorship network connecting the top 25 collaborators of Tsunehiro Mizushima. A scholar is included among the top collaborators of Tsunehiro Mizushima 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 Tsunehiro Mizushima. Tsunehiro Mizushima 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.
Suzuki, Takafumi, Kenji Takagi, Tatsuro Iso, et al.. (2025). Bidirectional regulation of KEAP1 BTB domain-based sensor activity. Redox Biology. 87. 103885–103885.
2.
Satoh, Tadashi, Maho Yagi‐Utsumi, Nozomi Ishii, et al.. (2024). Structural basis of sugar recognition by SCF FBS2 ubiquitin ligase involved in NGLY1 deficiency. FEBS Letters. 598(18). 2259–2268. 2 indexed citations
3.
Sugiura, Yuki, Shunsuke Matsumoto, Yuki Takano, et al.. (2023). Defective import of mitochondrial metabolic enzyme elicits ectopic metabolic stress. Science Advances. 9(15). eadf1956–eadf1956. 7 indexed citations
4.
Suzuki, Takafumi, Jin Inoue, Tatsuro Iso, et al.. (2021). Molecular basis for the disruption of Keap1–Nrf2 interaction via Hinge & Latch mechanism. Communications Biology. 4(1). 576–576. 135 indexed citations
5.
Satoh, Tadashi, et al.. (2020). Crystallographic snapshots of the EF-hand protein MCFD2 complexed with the intracellular lectin ERGIC-53 involved in glycoprotein transport. Acta Crystallographica Section F Structural Biology Communications. 76(5). 216–221. 6 indexed citations
6.
Tezuka, Tohru, Minsoo Kim, Jung-Mi Choi, et al.. (2020). Moyamoya disease patient mutations in the RING domain of RNF213 reduce its ubiquitin ligase activity and enhance NFκB activation and apoptosis in an AAA+ domain-dependent manner. Biochemical and Biophysical Research Communications. 525(3). 668–674. 37 indexed citations
7.
Matsuda, Noriyuki, Mayumi Kimura, Bruno B. Queliconi, et al.. (2017). Parkinson’s disease-related DJ-1 functions in thiol quality control against aldehyde attack in vitro. Scientific Reports. 7(1). 12816–12816. 47 indexed citations
8.
Takagi, Kenji, Minsoo Kim, Chihiro Sasakawa, & Tsunehiro Mizushima. (2016). Crystal structure of the substrate-recognition domain of theShigellaE3 ligase IpaH9.8. Acta Crystallographica Section F Structural Biology Communications. 72(4). 269–275. 11 indexed citations
9.
Kumanomidou, Taichi, Kenji Takagi, Tomomi Nakagawa, et al.. (2015). The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3. PLoS ONE. 10(10). e0140366–e0140366. 14 indexed citations
10.
Satoh, Tadashi, Yasushi Saeki, Takeshi Hiromoto, et al.. (2014). Structural Basis for Proteasome Formation Controlled by an Assembly Chaperone Nas2. Structure. 22(5). 731–743. 25 indexed citations
11.
Uekusa, Yoshinori, Keisuke Okawa, Maho Yagi‐Utsumi, et al.. (2013). Backbone 1H, 13C, and 15N assignments of yeast Ump1, an intrinsically disordered protein that functions as a proteasome assembly chaperone. Biomolecular NMR Assignments. 8(2). 383–386. 15 indexed citations
12.
Kobayashi, T., Michinaga Ogawa, Takahito Sanada, et al.. (2013). The Shigella OspC3 Effector Inhibits Caspase-4, Antagonizes Inflammatory Cell Death, and Promotes Epithelial Infection. Cell Host & Microbe. 13(5). 570–583. 158 indexed citations
13.
Kim, Minsoo, et al.. (2013). Structural Basis for the Recognition of Ubc13 by the Shigella flexneri Effector OspI. Journal of Molecular Biology. 425(15). 2623–2631. 24 indexed citations
14.
Takagi, Kenji, Sangwoo Kim, Ryo Morishita, et al.. (2012). Structural Basis for Specific Recognition of Rpt1p, an ATPase Subunit of 26 S Proteasome, by Proteasome-dedicated Chaperone Hsm3p. Journal of Biological Chemistry. 287(15). 12172–12182. 29 indexed citations
15.
Mizushima, Tsunehiro, Hirokazu Yagi, Shigeru Iida, et al.. (2011). Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes to Cells. 16(11). 1071–1080. 179 indexed citations
16.
Kim, Sangwoo, Yasushi Saeki, Keisuke Fukunaga, et al.. (2010). Crystal Structure of Yeast Rpn14, a Chaperone of the 19 S Regulatory Particle of the Proteasome. Journal of Biological Chemistry. 285(20). 15159–15166. 20 indexed citations
17.
Ichimura, Yoshinobu, Taichi Kumanomidou, Yu‐shin Sou, et al.. (2008). Structural Basis for Sorting Mechanism of p62 in Selective Autophagy. Journal of Biological Chemistry. 283(33). 22847–22857. 642 indexed citations breakdown →
18.
Kumanomidou, Taichi, Tsunehiro Mizushima, Masaaki Komatsu, et al.. (2005). The Crystal Structure of Human Atg4b, a Processing and De-conjugating Enzyme for Autophagosome-forming Modifiers. Journal of Molecular Biology. 355(4). 612–618. 72 indexed citations
19.
Unno, Masaki, Tsunehiro Mizushima, Y. Morimoto, et al.. (2002). The Structure of the Mammalian 20S Proteasome at 2.75 Å Resolution. Structure. 10(5). 609–618. 413 indexed citations
20.
Mitsuhashi, Satoshi, Tsunehiro Mizushima, Eiki Yamashita, et al.. (2000). X-ray Structure of β-Carbonic Anhydrase from the Red Alga,Porphyridium purpureum, Reveals a Novel Catalytic Site for CO2 Hydration. Journal of Biological Chemistry. 275(8). 5521–5526. 117 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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