Kazutaka Murayama

3.0k total citations
115 papers, 2.2k citations indexed

About

Kazutaka Murayama is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Kazutaka Murayama has authored 115 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 85 papers in Molecular Biology, 24 papers in Materials Chemistry and 20 papers in Oncology. Recurrent topics in Kazutaka Murayama's work include Enzyme Structure and Function (23 papers), RNA and protein synthesis mechanisms (16 papers) and Ubiquitin and proteasome pathways (10 papers). Kazutaka Murayama is often cited by papers focused on Enzyme Structure and Function (23 papers), RNA and protein synthesis mechanisms (16 papers) and Ubiquitin and proteasome pathways (10 papers). Kazutaka Murayama collaborates with scholars based in Japan, United States and Germany. Kazutaka Murayama's co-authors include Mikako Shirouzu, Shigeyuki Yokoyama, Katsuyuki Aoki, Takaho Terada, Seiki Kuramitsu, Kazuhiko Igarashi, M. Kato-Murayama, Mutsuko Kukimoto‐Niino, Miki Watanabe‐Matsui and Toshitaka Matsui and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Blood.

In The Last Decade

Kazutaka Murayama

111 papers receiving 2.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kazutaka Murayama Japan 27 1.4k 309 247 238 232 115 2.2k
Christine L. Gee United States 21 1.1k 0.8× 228 0.7× 282 1.1× 339 1.4× 267 1.2× 47 2.0k
Iban Ubarretxena‐Belandia United States 25 1.8k 1.3× 375 1.2× 230 0.9× 239 1.0× 117 0.5× 52 2.5k
Alessandro Senes United States 22 2.2k 1.6× 232 0.8× 221 0.9× 230 1.0× 91 0.4× 37 2.7k
Bjørn Dalhus Norway 34 2.2k 1.6× 219 0.7× 114 0.5× 400 1.7× 300 1.3× 94 3.4k
James Baleja United States 31 2.0k 1.5× 290 0.9× 202 0.8× 170 0.7× 99 0.4× 93 2.9k
Lanette Fee United States 10 2.9k 2.2× 330 1.1× 358 1.4× 717 3.0× 237 1.0× 12 4.0k
Pamela J. Focia United States 26 1.5k 1.1× 315 1.0× 188 0.8× 206 0.9× 148 0.6× 40 2.3k
Amir R. Khan Ireland 24 1.5k 1.1× 151 0.5× 628 2.5× 227 1.0× 241 1.0× 62 2.5k
Steven R. Jordan United States 24 2.2k 1.6× 406 1.3× 131 0.5× 280 1.2× 247 1.1× 46 3.2k
Ralph Golbik Germany 37 2.6k 1.9× 272 0.9× 431 1.7× 649 2.7× 232 1.0× 115 4.2k

Countries citing papers authored by Kazutaka Murayama

Since Specialization
Citations

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

Fields of papers citing papers by Kazutaka Murayama

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kazutaka Murayama

This figure shows the co-authorship network connecting the top 25 collaborators of Kazutaka Murayama. A scholar is included among the top collaborators of Kazutaka 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 Kazutaka Murayama. Kazutaka 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.
Hattori, Shin-ichiro, Haydar Bulut, Hironori Hayashi, et al.. (2024). Structural and virologic mechanism of the emergence of resistance to M pro inhibitors in SARS-CoV-2. Proceedings of the National Academy of Sciences. 121(37). e2404175121–e2404175121. 7 indexed citations
2.
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
3.
Kitajima, Yasuo, et al.. (2022). Little involvement of recycled-amino acids from proteasomal proteolysis in de novo protein synthesis. Biochemical and Biophysical Research Communications. 634. 40–47. 7 indexed citations
4.
Shima, Hiroki, Kazutaka Murayama, Toshitaka Matsui, et al.. (2022). Autocitrullination and Changes in the Activity of Peptidylarginine Deiminase 3 Induced by High Ca2+ Concentrations. ACS Omega. 7(32). 28378–28387. 3 indexed citations
5.
Kobayashi, Maki, Katsuhiko Kojima, Kazutaka Murayama, et al.. (2021). MK‐6, a novel not‐α IL‐2, elicits a potent antitumor activity by improving the effector to regulatory T cell balance. Cancer Science. 112(11). 4478–4489. 5 indexed citations
6.
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
7.
Kitajima, Yasuo, et al.. (2020). Puromycin‐sensitive aminopeptidase is required for C2C12 myoblast proliferation and differentiation. Journal of Cellular Physiology. 236(7). 5293–5305. 10 indexed citations
8.
Murayama, Kazutaka, et al.. (2020). The impact of intracellular aminopeptidase on C2C12 myoblast proliferation and differentiation. Biochemical and Biophysical Research Communications. 524(3). 608–613. 8 indexed citations
9.
Watanabe‐Matsui, Miki, Tamami Uejima, Hiroki Shima, et al.. (2016). Charge-state-distribution analysis of Bach2 intrinsically disordered heme binding region. The Journal of Biochemistry. 160(5). 291–298. 15 indexed citations
10.
Maéda, Hiroshi, Youhei Yamagata, Kazutaka Murayama, et al.. (2015). Synergistic Effect of Neutral Protease and Clostripain on Rat Pancreatic Islet Isolation. Transplantation. 99(7). 1349–1355. 20 indexed citations
11.
Maeda, Hiroshi, Kanako Nakagawa, Kazutaka Murayama, et al.. (2015). Cloning a neutral protease of Clostridium histolyticum, determining its substrate specificity, and designing a specific substrate. Applied Microbiology and Biotechnology. 99(24). 10489–10499. 6 indexed citations
12.
Watanabe‐Matsui, Miki, Takashi Matsumoto, Toshitaka Matsui, et al.. (2014). Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. Archives of Biochemistry and Biophysics. 565. 25–31. 35 indexed citations
13.
Murayama, Kazutaka, et al.. (2014). Characterization of glycerophosphoethanolamine ethanolaminephosphodiesterase from Streptomyces sanglieri. Journal of Bioscience and Bioengineering. 119(2). 123–130. 5 indexed citations
14.
Ohbayashi, Naomi, Takashi Matsumoto, Hiroki Shima, et al.. (2013). Solution Structure of Clostridial Collagenase H and Its Calcium-Dependent Global Conformation Change. Biophysical Journal. 104(7). 1538–1545. 19 indexed citations
15.
Murayama, Kazutaka, et al.. (2013). Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297. Journal of Structural Biology. 182(2). 192–196. 23 indexed citations
16.
Murayama, Kazutaka, Youhei Yamagata, Kimiko Watanabe, et al.. (2013). Collagenase H is Crucial for Isolation of Rat Pancreatic Islets. Cell Transplantation. 23(10). 1187–1198. 27 indexed citations
17.
Sugimori, Daisuke, et al.. (2011). Kinetic characterization and Mg2+ enhancement of Streptomyces griseocarneus sphingomyelinase C produced by recombinant Streptomyces lividans. Protein Expression and Purification. 81(2). 151–156. 6 indexed citations
18.
Murayama, Kazutaka & Kensaku Sakamoto. (2009). Site-specific Incorporation of 3-Iodo-L-tyrosine into Proteins and Single-wavelength Anomalous Dispersion Phasing with Soft X-ray in Protein Crystallography. Nihon Kessho Gakkaishi. 51(4). 251–257. 1 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.
Hashimoto, Hiroyuki, et al.. (1997). Presence of Turner stigmata in a case of dysgenetic male pseudohermaphroditism with 45,X/46,X+mar karyotype. Archives of Disease in Childhood. 76(3). 268–271. 7 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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