Mamoru Sato

3.0k total citations
96 papers, 2.4k citations indexed

About

Mamoru Sato is a scholar working on Molecular Biology, Plant Science and Computational Mechanics. According to data from OpenAlex, Mamoru Sato has authored 96 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 18 papers in Plant Science and 11 papers in Computational Mechanics. Recurrent topics in Mamoru Sato's work include DNA Repair Mechanisms (14 papers), Genomics and Chromatin Dynamics (13 papers) and Fluid Dynamics and Turbulent Flows (11 papers). Mamoru Sato is often cited by papers focused on DNA Repair Mechanisms (14 papers), Genomics and Chromatin Dynamics (13 papers) and Fluid Dynamics and Turbulent Flows (11 papers). Mamoru Sato collaborates with scholars based in Japan, United States and China. Mamoru Sato's co-authors include Hiroshi Hashimoto, Toshiyuki Shimizu, Takashi Oda, Reiji Yoshinaka, Hitoshi Kurumizaka, Hiroaki Tachiwana, Morihiko Sakaguchi, Kodai Hara, Asami Hishiki and Hiroshi Kimurâ and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Genes & Development.

In The Last Decade

Mamoru Sato

91 papers receiving 2.4k citations

Peers

Mamoru Sato

ONCOL

Nadin Neuhauser Germany

Chong Wang China

Radomir Crkvenjakov United States

Petra Langendijk-Genevaux Switzerland

Toshitaka Sato Japan

Alexandre Gattiker Switzerland

Florence Ravier Switzerland

R J DeLange United States

Feng Guo United States

W. Möller Netherlands

Nadin Neuhauser Germany

Mamoru Sato

3.4k ×1.9

291 ×0.6

521 ×2.1

111 ×0.5

379 ×1.7

ONCOL

Citations per year, relative to Mamoru Sato Mamoru Sato (= 1×) peers Nadin Neuhauser

Countries citing papers authored by Mamoru Sato

Since Specialization

Citations

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

Fields of papers citing papers by Mamoru Sato

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mamoru Sato

This figure shows the co-authorship network connecting the top 25 collaborators of Mamoru Sato. A scholar is included among the top collaborators of Mamoru Sato 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 Mamoru Sato. Mamoru Sato is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Karasawa, S., Taka‐aki Nakada, Mamoru Sato, et al.. (2021). Early Elevation of Cell-Free DNA After Acute Mesenteric Ischemia in Rats. Journal of Surgical Research. 269. 28–35. 1 indexed citations

Nakano, Ryohei, Takashi Kawai, Yosuke Fukamatsu, et al.. (2020). Postharvest Properties of Ultra-Late Maturing Peach Cultivars and Their Attributions to Melting Flesh (M) Locus: Re-evaluation of M Locus in Association With Flesh Texture. Frontiers in Plant Science. 11. 554158–554158. 9 indexed citations

Hishiki, Asami, Mamoru Sato, & Hiroshi Hashimoto. (2020). Structure of the HLTF HIRAN domain and its functional implications in regression of a stalled replication fork. Acta Crystallographica Section D Structural Biology. 76(8). 729–735. 5 indexed citations

Kuroda, Masashi, Mamoru Sato, Yuji Ohishi, et al.. (2019). Biosynthesis of bismuth selenide nanoparticles using chalcogen-metabolizing bacteria. Applied Microbiology and Biotechnology. 103(21-22). 8853–8861. 7 indexed citations

Oda, Takashi, Satoshi Omori, Kei Moritsugu, et al.. (2016). Extended string-like binding of the phosphorylated HP1α N-terminal tail to the lysine 9-methylated histone H3 tail. Scientific Reports. 6(1). 22527–22527. 24 indexed citations

Hishiki, Asami, Kodai Hara, Hideshi Yokoyama, et al.. (2015). Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance. Journal of Biological Chemistry. 290(21). 13215–13223. 60 indexed citations

Soh, Young‐Min, Frank Bürmann, Ho‐Chul Shin, et al.. (2014). Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding. Molecular Cell. 57(2). 290–303. 107 indexed citations

Kuwabara, N., Yasuto Murayama, Hiroshi Hashimoto, et al.. (2012). Mechanistic Insights into the Activation of Rad51-Mediated Strand Exchange from the Structure of a Recombination Activator, the Swi5-Sfr1 Complex. Structure. 20(3). 440–449. 38 indexed citations

Kikuchi, Sotaro, Kodai Hara, Toshiyuki Shimizu, Mamoru Sato, & Hiroshi Hashimoto. (2012). Structural Basis of Recruitment of DNA Polymerase ζ by Interaction between REV1 and REV7 Proteins. Journal of Biological Chemistry. 287(40). 33847–33852. 84 indexed citations

10.

Tachiwana, Hiroaki, Wataru Kagawa, Akihisa Osakabe, et al.. (2011). Crystal structure of the human centromeric nucleosome containing CENP-A. Nature. 476(7359). 232–235. 306 indexed citations

11.

Hara, Kodai, Hiroshi Hashimoto, Yoshiki Murakumo, et al.. (2010). Crystal Structure of Human REV7 in Complex with a Human REV3 Fragment and Structural Implication of the Interaction between DNA Polymerase ζ and REV1. Journal of Biological Chemistry. 285(16). 12299–12307. 104 indexed citations

12.

Hishiki, Asami, Hiroshi Hashimoto, Tomo Hanafusa, et al.. (2009). Structural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear Antigen. Journal of Biological Chemistry. 284(16). 10552–10560. 124 indexed citations

13.

Imasaki, Tsuyoshi, et al.. (2004). Crystallization and preliminary X-ray crystallographic analyses ofEcoO109I and its complex with DNA. Acta Crystallographica Section D Biological Crystallography. 60(6). 1165–1166. 4 indexed citations

14.

Sato, Mamoru, et al.. (2001). Cloning, Sequencing, and Phylogenetic Analysis of Complementary DNA of Novel Cytochrome P-450 CYP1A in Japanese Eel (Anguilla japonica). Marine Biotechnology. 3(3). 218–223. 5 indexed citations

15.

Sato, Kazuo, et al.. (1999). Detection of Driver Gas Contamination in High-Enthalpy Shock Tunnels.. JOURNAL OF THE JAPAN SOCIETY FOR AERONAUTICAL AND SPACE SCIENCES. 47(551). 470–473. 5 indexed citations

16.

Terai, Tadamasa, et al.. (1996). Transformation of Grayanotoxin III to 10-epi-Grayanotoxin III. Its X-Ray Crystallographic Analysis and Acute Toxicity in Mice.. Chemical and Pharmaceutical Bulletin. 44(6). 1245–1247. 4 indexed citations

17.

Kumasaka, Takashi, Hiroyuki Takeya, Masaki Yamamoto, et al.. (1995). Crystallization and Preliminary X-Ray Study of H2-Proteinase from the Venom of Trimeresurus flavoviridis. The Journal of Biochemistry. 117(5). 929–930. 1 indexed citations

18.

Mikami, Bunzo, Edward J. Hehre, Mamoru Sato, et al.. (1993). The 2.0-.ANG. resolution structure of soybean .beta.-amylase complexed with .alpha.-cyclodextrin. Biochemistry. 32(27). 6836–6845. 95 indexed citations

19.

Mikami, Bunzo, Mamoru Sato, Takumi Shibata, et al.. (1992). Three-Dimensional Structure of Soybean β-Amylase Determined at 3.0 Å Resolution: Preliminary Chain Tracing of the Complex with α-Cyclodextrin. The Journal of Biochemistry. 112(4). 541–546. 23 indexed citations

20.

Kanda, Hiroshi, et al.. (1991). NACA0012 Airfoil Data Corrected for Sidewall Boundary-layer Effects in the NAL Two-Dimensional Transonic Wind Tunnel. JAXA Repository (JAXA). 640. 1–72. 3 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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