Masaki Yamamoto

25.8k total citations · 4 hit papers
394 papers, 16.6k citations indexed

About

Masaki Yamamoto is a scholar working on Molecular Biology, Materials Chemistry and Radiation. According to data from OpenAlex, Masaki Yamamoto has authored 394 papers receiving a total of 16.6k indexed citations (citations by other indexed papers that have themselves been cited), including 140 papers in Molecular Biology, 129 papers in Materials Chemistry and 74 papers in Radiation. Recurrent topics in Masaki Yamamoto's work include Enzyme Structure and Function (90 papers), Advanced X-ray Imaging Techniques (58 papers) and X-ray Spectroscopy and Fluorescence Analysis (40 papers). Masaki Yamamoto is often cited by papers focused on Enzyme Structure and Function (90 papers), Advanced X-ray Imaging Techniques (58 papers) and X-ray Spectroscopy and Fluorescence Analysis (40 papers). Masaki Yamamoto collaborates with scholars based in Japan, United States and United Kingdom. Masaki Yamamoto's co-authors include Takashi Kumasaka, Masashi Miyano, Tetsuya Hori, Tetsuji Okada, David C. Teller, Craig A. Behnke, Brian A. Fox, Ronald E. Stenkamp, Krzysztof Palczewski and Isolde Le Trong and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Masaki Yamamoto

369 papers receiving 16.2k citations

Hit Papers

Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor 1988 2026 2000 2013 2000 2000 2014 1988 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
Masaki Yamamoto Japan 53 10.2k 4.1k 2.5k 1.0k 925 394 16.6k
Yifan Cheng United States 67 16.6k 1.6× 2.5k 0.6× 2.2k 0.9× 940 0.9× 513 0.6× 213 25.5k
Martin Caffrey United States 60 11.3k 1.1× 2.6k 0.6× 2.1k 0.8× 819 0.8× 297 0.3× 210 14.4k
Sjors H. W. Scheres United Kingdom 72 19.8k 1.9× 1.8k 0.4× 2.9k 1.2× 671 0.6× 939 1.0× 143 29.4k
Richard A. Henderson United Kingdom 67 14.6k 1.4× 7.2k 1.8× 3.6k 1.4× 986 0.9× 1.4k 1.5× 320 24.5k
Nikolaus Grigorieff United States 64 12.3k 1.2× 1.5k 0.4× 2.0k 0.8× 453 0.4× 790 0.9× 134 18.6k
Yoshinori Fujiyoshi Japan 60 12.2k 1.2× 3.0k 0.7× 1.6k 0.7× 1.4k 1.4× 232 0.3× 220 16.4k
Richard D. Leapman United States 57 7.1k 0.7× 1.2k 0.3× 3.5k 1.4× 2.3k 2.2× 990 1.1× 222 16.6k
Kenneth H. Downing United States 54 10.8k 1.1× 2.5k 0.6× 1.7k 0.7× 909 0.9× 507 0.5× 179 17.2k
Thomas Walz United States 87 17.5k 1.7× 2.6k 0.6× 1.4k 0.6× 1.7k 1.6× 137 0.1× 271 28.0k
Andrew G. W. Leslie United Kingdom 57 23.9k 2.3× 2.8k 0.7× 5.7k 2.3× 743 0.7× 280 0.3× 97 30.8k

Countries citing papers authored by Masaki Yamamoto

Since Specialization
Citations

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

Fields of papers citing papers by Masaki Yamamoto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masaki Yamamoto

This figure shows the co-authorship network connecting the top 25 collaborators of Masaki Yamamoto. A scholar is included among the top collaborators of Masaki Yamamoto 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 Masaki Yamamoto. Masaki Yamamoto 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
2.
Fujimura, Akiko, Takuma Shibata, Hideki Shigematsu, et al.. (2023). TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction. Nature Communications. 14(1). 164–164. 28 indexed citations
3.
Ando, Ryoko, Satoshi Shimozono, Hideo Ago, et al.. (2023). StayGold variants for molecular fusion and membrane-targeting applications. Nature Methods. 21(4). 648–656. 52 indexed citations
4.
Abe, Takashi, et al.. (2023). Surrogate Modeling and Application of Half-Wave Rectified Brushless Synchronous Motor for Model-Based Design. IEEJ Journal of Industry Applications. 13(1). 81–90. 1 indexed citations
5.
Sakai, Naoki, Sachiko Toma-Fukai, Norifumi Muraki, et al.. (2023). Elucidating polymorphs of crystal structures by intensity-based hierarchical clustering analysis of multiple diffraction data sets. Acta Crystallographica Section D Structural Biology. 79(10). 909–924. 4 indexed citations
6.
Baba, Seiki, Hideo Okumura, S.V. Antonyuk, et al.. (2022). Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases. Proceedings of the National Academy of Sciences. 119(30). e2205664119–e2205664119. 7 indexed citations
7.
Okumura, Hideo, Naoki Sakai, Hironori Murakami, et al.. (2022). In situ crystal data-collection and ligand-screening system at SPring-8. Acta Crystallographica Section F Structural Biology Communications. 78(6). 241–251. 7 indexed citations
8.
Yamamoto, Satoru, Masaki Yamamoto, Kazuki Goto, et al.. (2021). Evaluation of degradation behavior in quantum dot light-emitting diode with different hole transport materials via transient electroluminescence. Applied Physics Letters. 118(20). 18 indexed citations
9.
Antonyuk, S.V., Daisuke Sasaki, Keitaro Yamashita, et al.. (2021). An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures. Science Advances. 7(1). 33 indexed citations
10.
Baba, Seiki, Takashi Kawamura, Naoki Sakai, et al.. (2021). Guidelines for de novo phasing using multiple small-wedge data collection. Journal of Synchrotron Radiation. 28(5). 1284–1295. 5 indexed citations
11.
Maestre‐Reyna, Manuel, Wei‐Cheng Huang, Wen‐Jin Wu, et al.. (2020). Vibrio cholerae biofilm scaffolding protein RbmA shows an intrinsic, phosphate‐dependent autoproteolysis activity. IUBMB Life. 73(2). 418–431. 4 indexed citations
12.
Murai, Masahito, Masaki Yamamoto, & Kazuhiko Takai. (2019). Mechanistic Insights into Rhenium‐Catalyzed Regioselective C‐Alkenylation of Phenols with Internal Alkynes. Chemistry - A European Journal. 25(66). 15189–15197. 6 indexed citations
13.
Murai, Masahito, Masaki Yamamoto, & Kazuhiko Takai. (2019). Rhenium-Catalyzed Regioselective ortho-Alkenylation and [3 + 2 + 1] Cycloaddition of Phenols with Internal Alkynes. Organic Letters. 21(9). 3441–3445. 14 indexed citations
14.
Murakawa, T., Seiki Baba, Yoshiaki Kawano, et al.. (2018). In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase. Proceedings of the National Academy of Sciences. 116(1). 135–140. 9 indexed citations
15.
Kameda, Hiroshi, Naoya Fukui, Kunihiro Hongo, et al.. (2016). Common structural features of toxic intermediates from α-synuclein and GroES fibrillogenesis detected using cryogenic coherent X-ray diffraction imaging. The Journal of Biochemistry. 161(1). 55–65. 6 indexed citations
16.
Hiruma, Junichiro, Masashi Muramatsu, Masaki Yamamoto, et al.. (2016). 496 NLRC4 inflammasome is involved in the pathophysiology of psoriasis. Journal of Investigative Dermatology. 136(5). S87–S87.
17.
Padmanabhan, Balasundaram, Kit I. Tong, Yoshihiro Nakamura, et al.. (2004). Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(1). 153–155. 15 indexed citations
18.
Yamamoto, Masaki, Takashi Kumasaka, Go Ueno, et al.. (2002). RIKEN structural genomics beamlines at SPring-8. Acta Crystallographica Section A Foundations of Crystallography. 58(s1). c302–c302. 6 indexed citations
19.
Sugahara, Mitsuaki, Tsutomu Mikawa, Takashi Kumasaka, et al.. (2000). Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8. The EMBO Journal. 19(15). 3857–3869. 128 indexed citations
20.
Palczewski, Krzysztof, Takashi Kumasaka, Tetsuya Hori, et al.. (2000). Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor. Science. 289(5480). 739–745. 4567 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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