Masaaki Komatsu

73.9k total citations · 23 hit papers
227 papers, 45.7k citations indexed

About

Masaaki Komatsu is a scholar working on Epidemiology, Molecular Biology and Cell Biology. According to data from OpenAlex, Masaaki Komatsu has authored 227 papers receiving a total of 45.7k indexed citations (citations by other indexed papers that have themselves been cited), including 162 papers in Epidemiology, 107 papers in Molecular Biology and 49 papers in Cell Biology. Recurrent topics in Masaaki Komatsu's work include Autophagy in Disease and Therapy (161 papers), Endoplasmic Reticulum Stress and Disease (44 papers) and Ubiquitin and proteasome pathways (33 papers). Masaaki Komatsu is often cited by papers focused on Autophagy in Disease and Therapy (161 papers), Endoplasmic Reticulum Stress and Disease (44 papers) and Ubiquitin and proteasome pathways (33 papers). Masaaki Komatsu collaborates with scholars based in Japan, United States and South Korea. Masaaki Komatsu's co-authors include Noboru Mizushima, Keiji Tanaka, Takashi Ueno, Yoshinobu Ichimura, Eiki Kominami, Satoshi Waguri, Isei Tanida, Yu‐shin Sou, Yasuo Uchiyama and Keiji Tanaka and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Masaaki Komatsu

224 papers receiving 45.4k citations

Hit Papers

Autophagy: Renovation of Cells and Tissues 2005 2026 2012 2019 2011 2009 2006 2010 2005 1000 2.0k 3.0k 4.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Masaaki Komatsu Japan 89 29.0k 21.8k 8.4k 5.8k 3.9k 227 45.7k
Tamotsu Yoshimori Japan 95 38.0k 1.3× 24.4k 1.1× 14.1k 1.7× 5.5k 0.9× 5.9k 1.5× 246 55.8k
Ana María Cuervo United States 112 30.4k 1.0× 21.1k 1.0× 14.0k 1.7× 12.3k 2.1× 2.8k 0.7× 252 52.5k
Yoshinori Ohsumi Japan 108 40.9k 1.4× 28.4k 1.3× 18.1k 2.2× 4.2k 0.7× 2.6k 0.7× 259 56.4k
Keiji Tanaka Japan 112 19.9k 0.7× 37.9k 1.7× 11.5k 1.4× 4.3k 0.7× 6.8k 1.7× 428 55.1k
Eiki Kominami Japan 78 15.9k 0.5× 14.9k 0.7× 8.1k 1.0× 5.0k 0.9× 2.2k 0.6× 313 31.3k
Beth Levine United States 106 55.2k 1.9× 38.4k 1.8× 13.3k 1.6× 7.3k 1.3× 9.4k 2.4× 187 83.7k
Daniel J. Klionsky United States 133 51.1k 1.8× 42.5k 1.9× 21.3k 2.5× 6.5k 1.1× 5.0k 1.3× 519 81.9k
Akitsugu Yamamoto Japan 76 15.2k 0.5× 14.1k 0.6× 7.9k 0.9× 3.6k 0.6× 3.0k 0.8× 210 29.5k
Richard J. Youle United States 103 20.3k 0.7× 43.9k 2.0× 6.6k 0.8× 7.5k 1.3× 6.7k 1.7× 239 63.1k
Andrea Ballabio Italy 98 13.0k 0.4× 20.0k 0.9× 7.9k 0.9× 8.0k 1.4× 2.9k 0.7× 377 40.3k

Countries citing papers authored by Masaaki Komatsu

Since Specialization
Citations

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

Fields of papers citing papers by Masaaki Komatsu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masaaki Komatsu

This figure shows the co-authorship network connecting the top 25 collaborators of Masaaki Komatsu. A scholar is included among the top collaborators of Masaaki Komatsu 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 Masaaki Komatsu. Masaaki Komatsu 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.
Park, Semin, Sang-Won Park, Ssang‐Goo Cho, et al.. (2024). NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination. Nature Communications. 15(1). 10925–10925. 4 indexed citations
2.
Ishimura, Ryosuke, et al.. (2023). Mechanistic insights into the roles of the UFM1 E3 ligase complex in ufmylation and ribosome-associated protein quality control. Science Advances. 9(33). eadh3635–eadh3635. 27 indexed citations
3.
Takahashi, Masahiko, Hiroki Kitaura, Akiyoshi Kakita, et al.. (2022). USP10 Inhibits Aberrant Cytoplasmic Aggregation of TDP-43 by Promoting Stress Granule Clearance. Molecular and Cellular Biology. 42(3). e0039321–e0039321. 15 indexed citations
4.
Ishimura, Ryosuke, Daisuke Noshiro, Yasuko Ono, et al.. (2022). The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3. Nature Communications. 13(1). 7857–7857. 50 indexed citations
5.
Sánchez‐Martín, Pablo, Yu‐shin Sou, Shun Kageyama, et al.. (2020). NBR 1‐mediated p62‐liquid droplets enhance the Keap1‐Nrf2 system. EMBO Reports. 21(3). e48902–e48902. 94 indexed citations
6.
Yasuda, Daisuke, Tomoyuki Ohe, Kyôko Takahashi, et al.. (2020). Inhibitors of the protein–protein interaction between phosphorylated p62 and Keap1 attenuate chemoresistance in a human hepatocellular carcinoma cell line. Free Radical Research. 54(11-12). 859–871. 28 indexed citations
7.
Sou, Yu‐shin, Tetsuya Saito, Akiko Kuma, et al.. (2019). Loss of autophagy impairs physiological steatosis by accumulation of NCoR1. Life Science Alliance. 3(1). e201900513–e201900513. 23 indexed citations
8.
Wijk, Sjoerd J. L. van, Franziska Fricke, Lina Herhaus, et al.. (2017). Linear ubiquitination of cytosolic Salmonella Typhimurium activates NF-κB and restricts bacterial proliferation. Nature Microbiology. 2(7). 17066–17066. 138 indexed citations
9.
Dragich, Joanna M., Takaaki Kuwajima, Evelien Eenjes, et al.. (2016). Autophagy linked FYVE (Alfy/WDFY3) is required for establishing neuronal connectivity in the mammalian brain. eLife. 5. 82 indexed citations
10.
Haldar, Arun Kumar, Clémence Foltz, Ryan Finethy, et al.. (2015). Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins. Proceedings of the National Academy of Sciences. 112(41). E5628–37. 131 indexed citations
11.
Ezaki, Junji, Naomi Matsumoto, Mitsue Takeda‐Ezaki, et al.. (2011). Liver autophagy contributes to the maintenance of blood glucose and amino acid levels. Autophagy. 7(7). 727–736. 225 indexed citations
12.
Tatsumi, K., Ritsuko Shimizu, Satoshi Waguri, et al.. (2011). The Ufm1-activating enzyme Uba5 is indispensable for erythroid differentiation in mice. Nature Communications. 2(1). 181–181. 130 indexed citations
13.
Matsuda, Noriyuki, Shigeto Sato, Kahori Shiba, et al.. (2010). PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. The Journal of Cell Biology. 189(2). 211–221. 1542 indexed citations breakdown →
14.
Zhang, Yong, et al.. (2009). Adipose-specific deletion of autophagy-related gene 7 ( atg7 ) in mice reveals a role in adipogenesis. Proceedings of the National Academy of Sciences. 106(47). 19860–19865. 527 indexed citations breakdown →
15.
Tatsumi, K., Yu‐shin Sou, Norihiro Tada, et al.. (2009). A Novel Type of E3 Ligase for the Ufm1 Conjugation System. Journal of Biological Chemistry. 285(8). 5417–5427. 191 indexed citations
16.
Kirkin, Vladimir, Trond Lamark, Yu‐shin Sou, et al.. (2009). A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates. Molecular Cell. 33(4). 505–516. 908 indexed citations breakdown →
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.
Sasakawa, Hiroaki, Eri Sakata, Yoshiki Yamaguchi, et al.. (2006). Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier 1. Biochemical and Biophysical Research Communications. 343(1). 21–26. 57 indexed citations
19.
Komatsu, Masaaki, Satoshi Waguri, Takashi Ueno, et al.. (2005). Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice. The Journal of Cell Biology. 169(3). 425–434. 1941 indexed citations breakdown →
20.
Komatsu, Masaaki, Eiki Kominami, Kiichi Arahata, & Toshifumi Tsukahara. (1999). Cloning and characterization of two neural‐salient serine/arginine‐rich (NSSR) proteins involved in the regulation of alternative splicing in neurones. Genes to Cells. 4(10). 593–606. 42 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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