T. Murakawa

468 total citations
33 papers, 337 citations indexed

About

T. Murakawa is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, T. Murakawa has authored 33 papers receiving a total of 337 indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 12 papers in Biochemistry and 8 papers in Materials Chemistry. Recurrent topics in T. Murakawa's work include Microbial metabolism and enzyme function (15 papers), Porphyrin Metabolism and Disorders (14 papers) and Biochemical Acid Research Studies (8 papers). T. Murakawa is often cited by papers focused on Microbial metabolism and enzyme function (15 papers), Porphyrin Metabolism and Disorders (14 papers) and Biochemical Acid Research Studies (8 papers). T. Murakawa collaborates with scholars based in Japan, France and United States. T. Murakawa's co-authors include Toshihide Okajima, Hideyuki Hayashi, Katsuyuki Tanizawa, Shun Hirota, Yukio Yamamoto, Masayasu Taki, Shun’ichi Kuroda, Hiromi Hayashi, Yoshiaki Kawano and T. Yano and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

T. Murakawa

31 papers receiving 334 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. Murakawa Japan 12 253 84 81 51 38 33 337
Fabian Rabe von Pappenheim Germany 6 155 0.6× 77 0.9× 55 0.7× 21 0.4× 12 0.3× 10 294
Kerstin Nordstrand Sweden 7 441 1.7× 62 0.7× 157 1.9× 84 1.6× 73 1.9× 8 521
Lisa-Marie Funk Germany 6 142 0.6× 50 0.6× 55 0.7× 25 0.5× 9 0.2× 6 273
S. Kirk Wright United States 8 185 0.7× 45 0.5× 77 1.0× 57 1.1× 21 0.6× 10 311
Thomas Kleinschroth Germany 8 441 1.7× 20 0.2× 33 0.4× 31 0.6× 40 1.1× 11 517
Natalia Kulminskaya Denmark 11 108 0.4× 40 0.5× 71 0.9× 61 1.2× 20 0.5× 14 280
Russell R. Poyner United States 13 379 1.5× 32 0.4× 190 2.3× 49 1.0× 23 0.6× 18 502
Sudhir C. Sharma United States 10 234 0.9× 19 0.2× 88 1.1× 45 0.9× 28 0.7× 12 367
Markandeswar Panda United States 11 259 1.0× 26 0.3× 84 1.0× 22 0.4× 41 1.1× 24 429
Kirill Zinovjev Spain 15 327 1.3× 22 0.3× 134 1.7× 21 0.4× 22 0.6× 38 505

Countries citing papers authored by T. Murakawa

Since Specialization
Citations

This map shows the geographic impact of T. Murakawa'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 T. Murakawa with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. Murakawa more than expected).

Fields of papers citing papers by T. Murakawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of T. Murakawa

This figure shows the co-authorship network connecting the top 25 collaborators of T. Murakawa. A scholar is included among the top collaborators of T. Murakawa 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 T. Murakawa. T. Murakawa 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.
Fukui, Kenji, T. Murakawa, Seiki Baba, Takashi Kumasaka, & T. Yano. (2025). KH–R3H domain cooperation in RNA recognition by the global RNA-binding protein KhpB. Nature Communications. 16(1). 8028–8028.
2.
3.
Fukui, Kenji, Tatsuya Yamamoto, T. Murakawa, et al.. (2023). Catalytic mechanism of the zinc-dependent MutL endonuclease reaction. Life Science Alliance. 6(10). e202302001–e202302001. 2 indexed citations
4.
Fukui, Kenji, Yuki Fujii, T. Murakawa, et al.. (2022). Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8. Journal of Structural Biology. 214(4). 107904–107904. 1 indexed citations
5.
Suzuki, Youichi & T. Murakawa. (2022). Restriction of Flaviviruses by an Interferon-Stimulated Gene SHFL/C19orf66. International Journal of Molecular Sciences. 23(20). 12619–12619. 6 indexed citations
6.
Murakawa, T., Mamoru Suzuki, Kenji Fukui, et al.. (2022). Serial femtosecond X-ray crystallography of an anaerobically formed catalytic intermediate of copper amine oxidase. Acta Crystallographica Section D Structural Biology. 78(12). 1428–1438. 5 indexed citations
7.
Shoji, Mitsuo, T. Murakawa, Mauro Boero, et al.. (2022). Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase. Chemical Science. 13(36). 10923–10938. 12 indexed citations
8.
Watanabe, Yasuo, Youichi Suzuki, T. Murakawa, et al.. (2022). Identification of the corticotropin-releasing factor receptor 1 antagonists as inhibitors of Chikungunya virus replication using a Gaussia luciferase–expressing subgenomic replicon. Biochemical and Biophysical Research Communications. 637. 181–188. 2 indexed citations
9.
Murakawa, T., et al.. (2022). Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement. IUCrJ. 9(3). 342–348. 2 indexed citations
10.
Fukui, Kenji, Masao Inoue, T. Murakawa, et al.. (2022). Structural and functional insights into the mechanism by which MutS2 recognizes a DNA junction. Structure. 30(7). 973–982.e4. 3 indexed citations
11.
Murakawa, T., Mamoru Suzuki, Toshi Arima, et al.. (2021). Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase. Acta Crystallographica Section F Structural Biology Communications. 77(10). 356–363. 2 indexed citations
12.
Murakawa, T., Kazuo Kurihara, Mitsuo Shoji, et al.. (2020). Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing. Proceedings of the National Academy of Sciences. 117(20). 10818–10824. 10 indexed citations
13.
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
14.
Murakawa, T., Tadashi Nakai, Yoshiaki Kawano, et al.. (2015). Probing the Catalytic Mechanism of Copper Amine Oxidase from Arthrobacter globiformis with Halide Ions. Journal of Biological Chemistry. 290(38). 23094–23109. 14 indexed citations
15.
Ishii, Seiji, T. Yano, Akihiro Okamoto, T. Murakawa, & Hideyuki Hayashi. (2013). Boundary of the Nucleotide-Binding Domain of Streptococcus ComA Based on Functional and Structural Analysis. Biochemistry. 52(15). 2545–2555. 11 indexed citations
16.
Murakawa, T., Hiromi Hayashi, Masayasu Taki, et al.. (2011). Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors. The Journal of Biochemistry. 151(2). 167–178. 9 indexed citations
17.
Murakawa, T., et al.. (2010). Product-assisted Catalysis as the Basis of the Reaction Specificity of Threonine Synthase. Journal of Biological Chemistry. 286(4). 2774–2784. 10 indexed citations
18.
Ikushiro, Hiroko, Jun Hoseki, T. Murakawa, et al.. (2009). Structural Insights into the Enzymatic Mechanism of Serine Palmitoyltransferase from Sphingobacterium multivorum. The Journal of Biochemistry. 146(4). 549–562. 43 indexed citations
19.
Higashiya, A., S. Imada, T. Murakawa, et al.. (2007). Compact Resonant Inelastic X-Ray Scattering Equipment at BL19LXU in SPring-8. AIP conference proceedings. 879. 1415–1418. 1 indexed citations
20.
Okajima, Toshihide, T. Murakawa, Mayumi Uchida, et al.. (2006). Kinetic and Structural Studies on the Catalytic Role of the Aspartic Acid Residue Conserved in Copper Amine Oxidase,. Biochemistry. 45(13). 4105–4120. 40 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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