Masashi Yokochi

2.5k total citations
17 papers, 760 citations indexed

About

Masashi Yokochi is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Masashi Yokochi has authored 17 papers receiving a total of 760 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 8 papers in Materials Chemistry and 4 papers in Cell Biology. Recurrent topics in Masashi Yokochi's work include Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (7 papers) and Protein Kinase Regulation and GTPase Signaling (5 papers). Masashi Yokochi is often cited by papers focused on Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (7 papers) and Protein Kinase Regulation and GTPase Signaling (5 papers). Masashi Yokochi collaborates with scholars based in Japan, United States and Greece. Masashi Yokochi's co-authors include Fuyuhiko Inagaki, Kenji Ogura, Tomohide Saio, Yoshihiro Kobashigawa, Hiroyuki Kumeta, Takeshi Iwata, Toshimichi Fujiwara, Genji Kurisu, Yoshinori Makino and Masato Naito and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Masashi Yokochi

17 papers receiving 754 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Masashi Yokochi Japan 13 563 253 172 103 72 17 760
Takuya Torizawa Japan 13 796 1.4× 217 0.9× 202 1.2× 149 1.4× 30 0.4× 23 1.0k
Alberto Schena Switzerland 11 804 1.4× 163 0.6× 74 0.4× 98 1.0× 139 1.9× 20 1.1k
Yoichi Takakusagi Japan 21 496 0.9× 212 0.8× 257 1.5× 281 2.7× 124 1.7× 67 1.0k
Rebecca B. Berlow United States 12 606 1.1× 197 0.8× 75 0.4× 39 0.4× 31 0.4× 19 752
Roman V. Agafonov United States 13 658 1.2× 187 0.7× 68 0.4× 49 0.5× 73 1.0× 22 839
Amy M. Ruschak Canada 11 856 1.5× 214 0.8× 161 0.9× 29 0.3× 24 0.3× 14 1.0k
Labros G. Meimetis United States 14 633 1.1× 155 0.6× 62 0.4× 203 2.0× 62 0.9× 17 1.0k
Julianne L. Kitevski-LeBlanc Canada 9 851 1.5× 100 0.4× 94 0.5× 55 0.5× 39 0.5× 9 978
Javier Ruiz‐Sanz Spain 20 741 1.3× 324 1.3× 86 0.5× 33 0.3× 18 0.3× 36 948
Kurt W. Vogel United States 17 628 1.1× 94 0.4× 44 0.3× 76 0.7× 50 0.7× 36 909

Countries citing papers authored by Masashi Yokochi

Since Specialization
Citations

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

Fields of papers citing papers by Masashi Yokochi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Masashi Yokochi

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

All Works

17 of 17 papers shown
1.
Hoch, Jeffrey C., Kumaran Baskaran, Hamid R. Eghbalnia, et al.. (2022). Biological Magnetic Resonance Data Bank. Nucleic Acids Research. 51(D1). D368–D376. 143 indexed citations
2.
Bekker, Gert‐Jan, Masashi Yokochi, Hirofumi Suzuki, et al.. (2021). Protein Data Bank Japan: Celebrating our 20th anniversary during a global pandemic as the Asian hub of three dimensional macromolecular structural data. Protein Science. 31(1). 173–186. 35 indexed citations
3.
Kinjo, Akira R., Gert‐Jan Bekker, Hiroshi Wako, et al.. (2017). New tools and functions in data‐out activities at Protein Data Bank Japan (PDBj). Protein Science. 27(1). 95–102. 65 indexed citations
4.
Yokochi, Masashi, Naohiro Kobayashi, Eldon L. Ulrich, et al.. (2016). Publication of nuclear magnetic resonance experimental data with semantic web technology and the application thereof to biomedical research of proteins. Journal of Biomedical Semantics. 7(1). 16–16. 7 indexed citations
5.
Saio, Tomohide, Kenji Ogura, Hiroyuki Kumeta, et al.. (2015). Ligand-driven conformational changes of MurD visualized by paramagnetic NMR. Scientific Reports. 5(1). 16685–16685. 28 indexed citations
6.
Kobashigawa, Yoshihiro, Tomohide Saio, Mitsuhiro Sekiguchi, et al.. (2012). Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein–protein complex structure determination. Journal of Biomolecular NMR. 53(1). 53–63. 29 indexed citations
7.
Sekiguchi, Mariko, Yoshihiro Kobashigawa, Motoji Kawasaki, et al.. (2011). An evaluation tool for FKBP12-dependent and -independent mTOR inhibitors using a combination of FKBP-mTOR fusion protein, DSC and NMR. Protein Engineering Design and Selection. 24(11). 811–817. 6 indexed citations
8.
Saio, Tomohide, Kenji Ogura, Kazumi Shimizu, et al.. (2011). An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe. Journal of Biomolecular NMR. 51(3). 395–408. 43 indexed citations
9.
Saio, Tomohide, Masashi Yokochi, Hiroyuki Kumeta, & Fuyuhiko Inagaki. (2010). PCS-based structure determination of protein–protein complexes. Journal of Biomolecular NMR. 46(4). 271–280. 64 indexed citations
10.
Saio, Tomohide, Kenji Ogura, Masashi Yokochi, Yoshihiro Kobashigawa, & Fuyuhiko Inagaki. (2009). Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect. Journal of Biomolecular NMR. 44(3). 157–166. 65 indexed citations
11.
Saio, Tomohide, Masashi Yokochi, & Fuyuhiko Inagaki. (2009). The NMR structure of the p62 PB1 domain, a key protein in autophagy and NF-κB signaling pathway. Journal of Biomolecular NMR. 45(3). 335–341. 20 indexed citations
12.
Ogura, Kenji, et al.. (2008). Solution structure of the Grb2 SH2 domain complexed with a high-affinity inhibitor. Journal of Biomolecular NMR. 42(3). 197–207. 18 indexed citations
13.
Kobashigawa, Yoshihiro, Masato Naito, Masashi Yokochi, et al.. (2007). Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nature Structural & Molecular Biology. 14(6). 503–510. 101 indexed citations
14.
Saio, Tomohide, Hiroyuki Kumeta, Kenji Ogura, et al.. (2007). The Cooperative Role of OsCnfU-1A Domain I and Domain II in the Iron Sulphur Cluster Transfer Process as Revealed by NMR. The Journal of Biochemistry. 142(1). 113–121. 10 indexed citations
15.
Hirano, Yoshinori, Sosuke Yoshinaga, Kenji Ogura, et al.. (2004). Solution Structure of Atypical Protein Kinase C PB1 Domain and Its Mode of Interaction with ZIP/p62 and MEK5. Journal of Biological Chemistry. 279(30). 31883–31890. 67 indexed citations
16.
Yuzawa, Satoru, Masashi Yokochi, Hideki Hatanaka, et al.. (2001). Solution structure of Grb2 reveals extensive flexibility necessary for target recognition. Journal of Molecular Biology. 306(3). 527–537. 57 indexed citations
17.
Homma, S., et al.. (1982). Estimation of generator potentials in primary spindle endings evoked by brief tendon taps in man. Neuroscience Letters. 32(3). 277–280. 2 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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