M. Kato-Murayama

483 total citations
22 papers, 377 citations indexed

About

M. Kato-Murayama is a scholar working on Molecular Biology, Oncology and Materials Chemistry. According to data from OpenAlex, M. Kato-Murayama has authored 22 papers receiving a total of 377 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 5 papers in Oncology and 5 papers in Materials Chemistry. Recurrent topics in M. Kato-Murayama's work include Enzyme Structure and Function (5 papers), RNA and protein synthesis mechanisms (4 papers) and Biochemical and Molecular Research (3 papers). M. Kato-Murayama is often cited by papers focused on Enzyme Structure and Function (5 papers), RNA and protein synthesis mechanisms (4 papers) and Biochemical and Molecular Research (3 papers). M. Kato-Murayama collaborates with scholars based in Japan, United Kingdom and India. M. Kato-Murayama's co-authors include Mikako Shirouzu, Shigeyuki Yokoyama, Kazutaka Murayama, Takaho Terada, Yoshitaka Bessho, Toshiaki Hosaka, Ryogo Akasaka, Tetsu Akiyama, Seiki Kuramitsu and Kazunari Arima and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Journal of Virology.

In The Last Decade

M. Kato-Murayama

22 papers receiving 374 citations

Peers

M. Kato-Murayama
Dana M. Francis United States
M. Kato-Murayama
Citations per year, relative to M. Kato-Murayama M. Kato-Murayama (= 1×) peers Dana M. Francis

Countries citing papers authored by M. Kato-Murayama

Since Specialization
Citations

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

Fields of papers citing papers by M. Kato-Murayama

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M. Kato-Murayama. 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 M. Kato-Murayama. The network helps show where M. Kato-Murayama may publish in the future.

Co-authorship network of co-authors of M. Kato-Murayama

This figure shows the co-authorship network connecting the top 25 collaborators of M. Kato-Murayama. A scholar is included among the top collaborators of M. Kato-Murayama 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 M. Kato-Murayama. M. Kato-Murayama 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.
Murayama, Kazutaka, M. Kato-Murayama, Toshiaki Hosaka, et al.. (2024). Structural basis for the effects of Ser387 phosphorylation of MgcRacGAP on its GTPase-activating activities for CDC42 and RHOA. Journal of Structural Biology. 216(4). 108151–108151. 1 indexed citations
2.
Murayama, Kazutaka, et al.. (2024). Molecular basis of ligand recognition specificity of flavone glucosyltransferases in Nemophila menziesii. Archives of Biochemistry and Biophysics. 753. 109926–109926. 3 indexed citations
3.
Kimura‐Someya, Tomomi, Kazushige Katsura, M. Kato-Murayama, et al.. (2024). Structural analyses of the GI.4 norovirus by cryo-electron microscopy and X-ray crystallography revealing binding sites for human monoclonal antibodies. Journal of Virology. 98(5). e0019724–e0019724. 1 indexed citations
4.
Murayama, Kazutaka, M. Kato-Murayama, Tomohiro Sato, et al.. (2021). Anthocyanin 5,3′-aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin. Phytochemistry. 186. 112727–112727. 11 indexed citations
5.
Shimizu, Kanako, Tomonori Iyoda, Hiroshi Nakazato, et al.. (2021). Identification of TCR repertoires in functionally competent cytotoxic T cells cross-reactive to SARS-CoV-2. Communications Biology. 4(1). 1365–1365. 21 indexed citations
6.
Murayama, Kazutaka, M. Kato-Murayama, Yuka Itoh, et al.. (2020). Structural basis for inhibitory effects of Smad7 on TGF-β family signaling. Journal of Structural Biology. 212(3). 107661–107661. 18 indexed citations
7.
Dileep, K.V., Naoki Sakai, Kentaro Ihara, et al.. (2020). Piperidine-4-carboxamide as a new scaffold for designing secretory glutaminyl cyclase inhibitors. International Journal of Biological Macromolecules. 170. 415–423. 15 indexed citations
8.
Ohbayashi, Naomi, Kazutaka Murayama, M. Kato-Murayama, et al.. (2018). Structural Basis for the Inhibition of Cyclin G‐Associated Kinase by Gefitinib. ChemistryOpen. 7(9). 713–719. 13 indexed citations
9.
Kato-Murayama, M., Kazutaka Murayama, Toshiaki Hosaka, et al.. (2016). Structural basis of cucumisin protease activity regulation by its propeptide. The Journal of Biochemistry. 161(1). 45–53. 11 indexed citations
10.
Murayama, Kazutaka, M. Kato-Murayama, Toshiaki Hosaka, et al.. (2012). Crystal Structure of Cucumisin, a Subtilisin-Like Endoprotease from Cucumis melo L.. Journal of Molecular Biology. 423(3). 386–396. 26 indexed citations
11.
Murayama, Kazutaka, M. Kato-Murayama, Ryogo Akasaka, et al.. (2012). Structure of the Rho-specific guanine nucleotide-exchange factor Xpln. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(12). 1455–1459. 3 indexed citations
12.
Murayama, Kazutaka, M. Kato-Murayama, Yoshiko Ishizuka‐Katsura, et al.. (2011). Crystal Structures of the Armadillo Repeat Domain of Adenomatous Polyposis Coli and Its Complex with the Tyrosine-Rich Domain of Sam68. Structure. 19(10). 1496–1508. 31 indexed citations
13.
Sakamoto, Kensaku, Kazutaka Murayama, Kenji Oki, et al.. (2009). Genetic Encoding of 3-Iodo-l-Tyrosine in Escherichia coli for Single-Wavelength Anomalous Dispersion Phasing in Protein Crystallography. Structure. 17(3). 335–344. 56 indexed citations
14.
Hosaka, Toshiaki, Kazutaka Murayama, M. Kato-Murayama, et al.. (2009). Structure of the putative thioesterase protein TTHA1846 fromThermus thermophilusHB8 complexed with coenzyme A and a zinc ion. Acta Crystallographica Section D Biological Crystallography. 65(8). 767–776. 3 indexed citations
15.
Murayama, Kazutaka, Sanae Nakayama, M. Kato-Murayama, et al.. (2009). Crystal Structure of Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1. Journal of Biological Chemistry. 284(51). 35896–35905. 38 indexed citations
16.
Murayama, Kazutaka, M. Kato-Murayama, Ryogo Akasaka, et al.. (2008). Crystal structure of the Bruton’s tyrosine kinase PH domain with phosphatidylinositol. Biochemical and Biophysical Research Communications. 377(1). 23–28. 15 indexed citations
17.
Dong, Xuesong, M. Kato-Murayama, Tomonari Muramatsu, et al.. (2007). The crystal structure of leucyl/phenylalanyl‐tRNA‐protein transferase from Escherichia coli. Protein Science. 16(3). 528–534. 19 indexed citations
18.
Kato-Murayama, M., Yoshitaka Bessho, Mikako Shirouzu, & Shigeyuki Yokoyama. (2005). Crystal Structure of the RNA 2′-Phosphotransferase from Aeropyrum pernix K1. Journal of Molecular Biology. 348(2). 295–305. 23 indexed citations
19.
Murayama, Kazutaka, M. Kato-Murayama, Kazushige Katsura, et al.. (2004). Structure of a putativetrans-editing enzyme for prolyl-tRNA synthetase fromAeropyrum pernixK1 at 1.7 Å resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(1). 26–29. 7 indexed citations
20.
Kukimoto‐Niino, Mutsuko, Kazutaka Murayama, M. Kato-Murayama, et al.. (2004). Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8. Protein Science. 13(11). 3038–3042. 10 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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