Naohiro Kobayashi

4.5k total citations
93 papers, 2.0k citations indexed

About

Naohiro Kobayashi is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Naohiro Kobayashi has authored 93 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 13 papers in Materials Chemistry and 9 papers in Physiology. Recurrent topics in Naohiro Kobayashi's work include RNA and protein synthesis mechanisms (23 papers), RNA Research and Splicing (20 papers) and Protein Structure and Dynamics (16 papers). Naohiro Kobayashi is often cited by papers focused on RNA and protein synthesis mechanisms (23 papers), RNA Research and Splicing (20 papers) and Protein Structure and Dynamics (16 papers). Naohiro Kobayashi collaborates with scholars based in Japan, Germany and United States. Naohiro Kobayashi's co-authors include Eisuke Munekata, Shinya Honda, Shigeyuki Yokoyama, T. Kigawa, Peter Güntert, Takashi Nagata, Kengo Tsuda, Y. Muto, Toshimichi Fujiwara and Masato Katahira and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Naohiro Kobayashi

86 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Naohiro Kobayashi Japan 25 1.6k 378 145 128 104 93 2.0k
Jayashree Srinivasan United States 11 1.7k 1.1× 310 0.8× 72 0.5× 147 1.1× 170 1.6× 16 2.2k
Karim M. ElSawy United Kingdom 11 1.2k 0.8× 211 0.6× 121 0.8× 76 0.6× 166 1.6× 26 1.7k
Andrew A. Bogan United States 6 1.9k 1.2× 432 1.1× 157 1.1× 114 0.9× 139 1.3× 8 2.3k
Nilesh K. Banavali United States 23 2.3k 1.4× 413 1.1× 60 0.4× 169 1.3× 81 0.8× 53 2.9k
Ryan Brenke United States 11 1.5k 0.9× 333 0.9× 183 1.3× 54 0.4× 140 1.3× 13 1.9k
Sergey Lyskov United States 14 1.6k 1.0× 323 0.9× 215 1.5× 81 0.6× 138 1.3× 19 2.1k
Irene Luque Spain 27 1.4k 0.9× 406 1.1× 107 0.7× 82 0.6× 169 1.6× 65 2.2k
Suhail A. Islam United Kingdom 19 1.6k 1.0× 467 1.2× 103 0.7× 170 1.3× 133 1.3× 34 2.2k
Razif R. Gabdoulline Germany 23 1.7k 1.1× 433 1.1× 86 0.6× 95 0.7× 120 1.2× 37 2.2k
Gerard Kroon United States 18 1.6k 1.0× 569 1.5× 109 0.8× 305 2.4× 96 0.9× 34 2.0k

Countries citing papers authored by Naohiro Kobayashi

Since Specialization
Citations

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

Fields of papers citing papers by Naohiro Kobayashi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Naohiro Kobayashi

This figure shows the co-authorship network connecting the top 25 collaborators of Naohiro Kobayashi. A scholar is included among the top collaborators of Naohiro Kobayashi 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 Naohiro Kobayashi. Naohiro Kobayashi 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.
Wu, Nan, Zhichao Xu, Shen Huang, et al.. (2025). A Structural Model of Truncated Gaussia princeps Luciferase Elucidating the Crucial Catalytic Function of No.76 Arginine towards Coelenterazine Oxidation. PLoS Computational Biology. 21(1). e1012722–e1012722.
2.
Kobayashi, Naohiro, Weihua Qin, Yoshie Chiba, et al.. (2022). Structural basis for the unique multifaceted interaction of DPPA3 with the UHRF1 PHD finger. Nucleic Acids Research. 50(21). 12527–12542. 15 indexed citations
3.
Furuita, Kyoko, et al.. (2022). 1H, 13C, and 15N resonance assignments of human glutathione peroxidase 4. Biomolecular NMR Assignments. 16(2). 267–271. 1 indexed citations
4.
Kobayashi, Naohiro, Tomoyuki Kawamura, Shinji Kikuchi, et al.. (2022). Rapid enlargement of pulmonary benign metastasizing leiomyoma with fluid-containing cystic change: a case report. SHILAP Revista de lepidopterología. 8(1). 84–84. 2 indexed citations
5.
Huang, Yuanpeng J., Ning Zhang, Beate Bersch, et al.. (2021). Assessment of prediction methods for protein structures determined by NMR in CASP14 : Impact of AlphaFold2. Proteins Structure Function and Bioinformatics. 89(12). 1959–1976. 32 indexed citations
6.
Koga, Rie, Mami Yamamoto, Takahiro Kosugi, et al.. (2020). Robust folding of a de novo designed ideal protein even with most of the core mutated to valine. Proceedings of the National Academy of Sciences. 117(49). 31149–31156. 20 indexed citations
7.
He, Fahu, Kanako Kuwasako, Mari Takahashi, et al.. (2020). 1H, 13C and 15N resonance assignment of the YTH domain of YTHDC2. Biomolecular NMR Assignments. 15(1). 1–7. 1 indexed citations
8.
Nakayama, Naomi, Gyosuke Sakashita, Takashi Nagata, et al.. (2020). Nucleus Accumbens-Associated Protein 1 Binds DNA Directly through the BEN Domain in a Sequence-Specific Manner. Biomedicines. 8(12). 608–608. 13 indexed citations
9.
Yamada, Tatsuya, Tomohiko Hayashi, Naohiro Kobayashi, et al.. (2019). How Does the Recently Discovered Peptide MIP Exhibit Much Higher Binding Affinity than an Anticancer Protein p53 for an Oncoprotein MDM2?. Journal of Chemical Information and Modeling. 59(8). 3533–3544. 8 indexed citations
10.
Kobayashi, Naohiro, et al.. (2018). Synthesis of alkyne-tagged and biotin-tagged Sortin1 as novel photoaffinity probes. Bioorganic & Medicinal Chemistry Letters. 28(9). 1562–1565. 6 indexed citations
11.
Kondo, Keiko, Tsukasa Mashima, Takanori Oyoshi, et al.. (2018). Plastic roles of phenylalanine and tyrosine residues of TLS/FUS in complex formation with the G-quadruplexes of telomeric DNA and TERRA. Scientific Reports. 8(1). 2864–2864. 31 indexed citations
12.
Nagata, Takashi, Kengo Tsuda, Takao Imai, et al.. (2017). Backbone and side chain assignments of the second RNA-binding domain of Musashi-1 in its free form and in complex with 5-mer RNA. Biomolecular NMR Assignments. 11(2). 265–268. 4 indexed citations
13.
Wang, Jing, et al.. (2013). Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA. Biochemical and Biophysical Research Communications. 441(4). 701–706. 26 indexed citations
14.
Furukawa, Ayako, Takashi Nagata, Akimasa Matsugami, et al.. (2009). Structure, interaction and real‐time monitoring of the enzymatic reaction of wild‐type APOBEC3G. The EMBO Journal. 28(4). 440–451. 108 indexed citations
15.
He, Fahu, Kohei Saito, Satoru Watanabe, et al.. (2009). Solution structure of the cysteine‐rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily. Protein Science. 18(3). 650–656. 23 indexed citations
16.
Wei, Yufeng, Shaohua Liu, Jörn Lausen, et al.. (2007). A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription. Nature Structural & Molecular Biology. 14(7). 653–661. 30 indexed citations
17.
Tochio, N., S. Koshiba, Naohiro Kobayashi, et al.. (2006). Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3. Protein Science. 15(11). 2534–2543. 33 indexed citations
18.
Nakajima, Jun, et al.. (2002). Motion vector re-estimation for fast video transcoding from MPEG-2 to MPEG-4. 4. 87–90. 2 indexed citations
19.
Kobayashi, Naohiro, et al.. (2000). Role of Side-chains in the Cooperative β-Hairpin Folding of the Short C−Terminal Fragment Derived from Streptococcal Protein G. Biochemistry. 39(21). 6564–6571. 81 indexed citations
20.
Zanotti, Giancarlo, et al.. (1999). d-Configuration of Serine Is Crucial in Maintaining the Phalloidin-like Conformation of Viroisin. Biochemistry. 38(33). 10723–10729. 4 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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