Hideyasu Okamura

479 total citations
18 papers, 392 citations indexed

About

Hideyasu Okamura is a scholar working on Molecular Biology, Biomaterials and Genetics. According to data from OpenAlex, Hideyasu Okamura has authored 18 papers receiving a total of 392 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Biomaterials and 2 papers in Genetics. Recurrent topics in Hideyasu Okamura's work include Protein Structure and Dynamics (7 papers), DNA and Nucleic Acid Chemistry (4 papers) and Silk-based biomaterials and applications (4 papers). Hideyasu Okamura is often cited by papers focused on Protein Structure and Dynamics (7 papers), DNA and Nucleic Acid Chemistry (4 papers) and Silk-based biomaterials and applications (4 papers). Hideyasu Okamura collaborates with scholars based in Japan, India and United Kingdom. Hideyasu Okamura's co-authors include Yoshifumi Nishimura, Aritaka Nagadoi, Kozo Makino, Etsuko Katoh, Tadateru Nishikawa, Peter König, Daniela Rhodes, Akinori Kidera, Masaki Nishikiori and Tsutomu Yamane and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Hideyasu Okamura

18 papers receiving 390 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hideyasu Okamura Japan 10 284 104 94 56 48 18 392
Y. Papanikolau Greece 8 391 1.4× 97 0.9× 69 0.7× 42 0.8× 24 0.5× 13 440
Jan S. Schuhmacher Germany 8 298 1.0× 172 1.7× 59 0.6× 41 0.7× 17 0.4× 10 423
Thomas Kriehuber Germany 11 608 2.1× 41 0.4× 52 0.6× 139 2.5× 65 1.4× 11 713
James T. MacDonald United Kingdom 18 871 3.1× 163 1.6× 50 0.5× 102 1.8× 15 0.3× 27 967
Ana María Fernández‐Escamilla Spain 11 226 0.8× 60 0.6× 27 0.3× 53 0.9× 19 0.4× 13 283
Lars Ferbitz Germany 5 640 2.3× 115 1.1× 50 0.5× 75 1.3× 7 0.1× 6 749
James Tolchard France 10 120 0.4× 44 0.4× 33 0.4× 22 0.4× 35 0.7× 21 249
Sung‐Hoon Jun South Korea 9 208 0.7× 49 0.5× 100 1.1× 22 0.4× 15 0.3× 14 351
Alasdair Mackenzie Norway 11 259 0.9× 27 0.3× 153 1.6× 27 0.5× 27 0.6× 15 539
Natalia Levina Russia 9 571 2.0× 106 1.0× 159 1.7× 14 0.3× 215 4.5× 10 735

Countries citing papers authored by Hideyasu Okamura

Since Specialization
Citations

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

Fields of papers citing papers by Hideyasu Okamura

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hideyasu Okamura

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

All Works

18 of 18 papers shown
1.
Okamura, Hideyasu, et al.. (2024). Influence of Initial Secondary Structure on Conformation and Mechanical Properties of Spider Silk Protein Gels. ACS Biomaterials Science & Engineering. 10(10). 6135–6143. 1 indexed citations
2.
Okamura, Hideyasu, et al.. (2023). Real-Time Monitoring of the Structural Transition of Bombyx mori Liquid Silk under Pressure by Solid-State NMR. Journal of the American Chemical Society. 145(42). 22925–22933. 5 indexed citations
3.
Suzuki, Yu, et al.. (2022). Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR. Molecules. 27(2). 511–511. 5 indexed citations
4.
Asakura, Tetsuo, et al.. (2022). Recombinant Spider Silk Fiber with High Dimensional Stability in Water and Its NMR Characterization. Molecules. 27(23). 8479–8479. 3 indexed citations
5.
Xiang, Hongyu, Hideyasu Okamura, Yuichiro Kezuka, & Etsuko Katoh. (2018). Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. Scientific Reports. 8(1). 17719–17719. 8 indexed citations
6.
Okamura, Hideyasu, Hiroshi Nishimura, Takashi Nagata, et al.. (2016). Accurate and molecular-size-tolerant NMR quantitation of diverse components in solution. Scientific Reports. 6(1). 21742–21742. 2 indexed citations
7.
Ogura, Kenji & Hideyasu Okamura. (2013). Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR. Scientific Reports. 3(1). 2913–2913. 8 indexed citations
8.
Ogura, Kenji, Hideyasu Okamura, Masato Katahira, Etsuko Katoh, & Fuyuhiko Inagaki. (2012). Conformational dynamics of yeast calmodulin in the Ca2+‐bound state probed using NMR relaxation dispersion. FEBS Letters. 586(16). 2548–2554. 3 indexed citations
9.
Okamura, Hideyasu, Masaki Nishikiori, Hongyu Xiang, Masayuki Ishikawa, & Etsuko Katoh. (2011). Interconversion of Two GDP-Bound Conformations and Their Selection in an Arf-Family Small G Protein. Structure. 19(7). 988–998. 9 indexed citations
10.
Nishikiori, Masaki, Masashi Mori, Koji Dohi, et al.. (2011). A Host Small GTP-binding Protein ARL8 Plays Crucial Roles in Tobamovirus RNA Replication. PLoS Pathogens. 7(12). e1002409–e1002409. 61 indexed citations
11.
Yamane, Tsutomu, Hideyasu Okamura, Yoshifumi Nishimura, Akinori Kidera, & Mitsunori Ikeguchi. (2010). Side-Chain Conformational Changes of Transcription Factor PhoB upon DNA Binding: A Population-Shift Mechanism. Journal of the American Chemical Society. 132(36). 12653–12659. 13 indexed citations
12.
Yamane, Tsutomu, Hideyasu Okamura, Mitsunori Ikeguchi, Yoshifumi Nishimura, & Akinori Kidera. (2008). Water‐mediated interactions between DNA and PhoB DNA‐binding/transactivation domain: NMR‐restrained molecular dynamics in explicit water environment. Proteins Structure Function and Bioinformatics. 71(4). 1970–1983. 33 indexed citations
13.
Kawashima, Tsuyoshi, Hironori Aramaki, Kozo Makino, et al.. (2008). Transcription Regulation by Feast/Famine Regulatory Proteins, FFRPs, in Archaea and Eubacteria. Biological and Pharmaceutical Bulletin. 31(2). 173–186. 22 indexed citations
14.
Okamura, Hideyasu, Katsushi Yokoyama, Hideaki Koike, et al.. (2007). A Structural Code for Discriminating between Transcription Signals Revealed by the Feast/Famine Regulatory Protein DM1 in Complex with Ligands. Structure. 15(10). 1325–1338. 29 indexed citations
15.
Okamura, Hideyasu, Kozo Makino, & Yoshifumi Nishimura. (2007). NMR Dynamics Distinguish Between Hard and Soft Hydrophobic Cores in the DNA-binding Domain of PhoB and Demonstrate Different Roles of the Cores in Binding to DNA. Journal of Molecular Biology. 367(4). 1093–1117. 9 indexed citations
16.
Okuda, Masahiko, Aki Tanaka, Yoko Arai, et al.. (2004). A Novel Zinc Finger Structure in the Large Subunit of Human General Transcription Factor TFIIE. Journal of Biological Chemistry. 279(49). 51395–51403. 30 indexed citations
17.
Nishikawa, Tadateru, Hideyasu Okamura, Aritaka Nagadoi, et al.. (2001). Solution Structure of a Telomeric DNA Complex of Human TRF1. Structure. 9(12). 1237–1251. 68 indexed citations
18.
Okamura, Hideyasu, et al.. (2000). Structural comparison of the PhoB and OmpR DNA-binding/transactivation domains and the arrangement of PhoB molecules on the phosphate box. Journal of Molecular Biology. 295(5). 1225–1236. 83 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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