Yoshitaka Bessho

3.1k total citations
92 papers, 2.1k citations indexed

About

Yoshitaka Bessho is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, Yoshitaka Bessho has authored 92 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 66 papers in Molecular Biology, 24 papers in Materials Chemistry and 13 papers in Ecology. Recurrent topics in Yoshitaka Bessho's work include RNA and protein synthesis mechanisms (36 papers), RNA modifications and cancer (25 papers) and Enzyme Structure and Function (22 papers). Yoshitaka Bessho is often cited by papers focused on RNA and protein synthesis mechanisms (36 papers), RNA modifications and cancer (25 papers) and Enzyme Structure and Function (22 papers). Yoshitaka Bessho collaborates with scholars based in Japan, Taiwan and United Kingdom. Yoshitaka Bessho's co-authors include Shigeyuki Yokoyama, Hiroshi Hori, Syozo Osawa, Mikako Shirouzu, Akihiko Koga, Hiroaki Suga, Takeshi Ohama, M. Kuratani, Hidehito Inagaki and Sakurako Goto‐Ito 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

Yoshitaka Bessho

91 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
Yoshitaka Bessho Japan 27 1.5k 301 283 248 193 92 2.1k
Maria Harkiolaki United Kingdom 20 941 0.6× 57 0.2× 135 0.5× 261 1.1× 161 0.8× 51 1.8k
Adam Round France 34 2.5k 1.7× 163 0.5× 275 1.0× 759 3.1× 159 0.8× 80 3.9k
Xing Zhu China 31 1.3k 0.9× 385 1.3× 145 0.5× 147 0.6× 18 0.1× 66 2.8k
Zhiheng Yu United States 33 1.9k 1.3× 193 0.6× 1.2k 4.2× 310 1.3× 57 0.3× 75 3.3k
D. Fellmann United States 10 1.2k 0.8× 175 0.6× 182 0.6× 234 0.9× 108 0.6× 20 2.2k
Jan Kosiński Germany 31 2.6k 1.8× 139 0.5× 269 1.0× 371 1.5× 19 0.1× 56 3.2k
Karsten Richter Germany 24 1.7k 1.2× 88 0.3× 225 0.8× 172 0.7× 81 0.4× 60 2.5k
Robert L. Shoeman Germany 37 2.5k 1.7× 294 1.0× 528 1.9× 812 3.3× 374 1.9× 98 4.0k
Naoyuki Miyazaki Japan 29 1.1k 0.8× 385 1.3× 170 0.6× 136 0.5× 21 0.1× 87 2.5k
Sascha Gutmann Switzerland 15 857 0.6× 210 0.7× 131 0.5× 281 1.1× 73 0.4× 19 1.4k

Countries citing papers authored by Yoshitaka Bessho

Since Specialization
Citations

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

Fields of papers citing papers by Yoshitaka Bessho

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshitaka Bessho

This figure shows the co-authorship network connecting the top 25 collaborators of Yoshitaka Bessho. A scholar is included among the top collaborators of Yoshitaka Bessho 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 Yoshitaka Bessho. Yoshitaka Bessho 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.
Hijikata, Atsushi, Tairo Oshima, Kei Yura, & Yoshitaka Bessho. (2023). ThermusQ: Toward the cell simulation platform for <i>Thermus thermophilus</i>. The Journal of General and Applied Microbiology. 69(2). 59–67. 2 indexed citations
2.
Kawai, Gota, G. Sampei, Makoto Nishiyama, & Yoshitaka Bessho. (2023). Non-coding RNAs and functional RNA elements in <i>Thermus thermophilus</i><i> </i>. The Journal of General and Applied Microbiology. 69(2). 131–134. 2 indexed citations
3.
Yumoto, Hirokatsu, Takahisa Koyama, Akihiro Suzuki, et al.. (2022). High-fluence and high-gain multilayer focusing optics to enhance spatial resolution in femtosecond X-ray laser imaging. Nature Communications. 13(1). 5300–5300. 13 indexed citations
4.
Nemoto, Naoki, Masahiko Kawaguchi, Kei Yura, Haruo Shimada, & Yoshitaka Bessho. (2022). PGLN: A newly identified amino phosphoglycolipid species in Thermus thermophilus HB8. Biochemistry and Biophysics Reports. 32. 101377–101377. 3 indexed citations
5.
Miyazaki, Kentaro, et al.. (2021). Complete Genome Sequences of Thermus thermophilus Strains HB5002 and HB5008, Isolated from Mine Hot Spring in Japan. Microbiology Resource Announcements. 10(16). 4 indexed citations
6.
Miyazaki, Kentaro, Toshiyuki Moriya, Naoki Nemoto, et al.. (2021). Complete Genome Sequence of Thermus thermophilus Strain HB5018, Isolated from Mine Hot Spring in Japan. Microbiology Resource Announcements. 10(10). 6 indexed citations
7.
Maestre‐Reyna, Manuel, Wei‐Cheng Huang, Wen‐Jin Wu, et al.. (2020). Vibrio cholerae biofilm scaffolding protein RbmA shows an intrinsic, phosphate‐dependent autoproteolysis activity. IUBMB Life. 73(2). 418–431. 4 indexed citations
8.
Maestre‐Reyna, Manuel, Junpei Yamamoto, Wei‐Cheng Huang, et al.. (2018). Twist and turn: a revised structural view on the unpaired bubble of class II CPD photolyase in complex with damaged DNA. IUCrJ. 5(5). 608–618. 6 indexed citations
9.
Yamashige, Hisao, Takashi Kimura, Yasumasa Joti, et al.. (2015). Extending the potential of x-ray free-electron lasers to industrial applications—an initiatory attempt at coherent diffractive imaging on car-related nanomaterials. Journal of Physics B Atomic Molecular and Optical Physics. 48(24). 244008–244008. 3 indexed citations
10.
Yokobori, Shin‐ichi, Aya Kitamura, Henri Grosjean, & Yoshitaka Bessho. (2013). Life without tRNAArg–adenosine deaminase TadA: evolutionary consequences of decoding the four CGN codons as arginine in Mycoplasmas and other Mollicutes. Nucleic Acids Research. 41(13). 6531–6543. 26 indexed citations
11.
Ueta, Masami, Chieko Wada, Yoshihiko Sako, et al.. (2013). Conservation of two distinct types of 100S ribosome in bacteria. Genes to Cells. 18(7). 554–574. 54 indexed citations
12.
Kimura, Satoshi, Chie Tomikawa, Anna Ochi, et al.. (2009). Aquifex aeolicus tRNA (N2,N2-Guanine)-dimethyltransferase (Trm1) Catalyzes Transfer of Methyl Groups Not Only to Guanine 26 but Also to Guanine 27 in tRNA. Journal of Biological Chemistry. 284(31). 20467–20478. 55 indexed citations
13.
Goto‐Ito, Sakurako, Takuhiro Ito, M. Kuratani, Yoshitaka Bessho, & Shigeyuki Yokoyama. (2009). Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation. Nature Structural & Molecular Biology. 16(10). 1109–1115. 84 indexed citations
14.
Strange, Richard W., S.V. Antonyuk, Mark J. Ellis, et al.. (2009). Structure of a putative β-phosphoglucomutase (TM1254) fromThermotoga maritima. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(12). 1218–1221. 2 indexed citations
15.
Agari, Yoshihiro, Shizuo Sato, Yoshitaka Bessho, et al.. (2008). X-ray crystal structure of a hypothetical Sua5 protein fromSulfolobus tokodaiistrain 7. Acta Crystallographica Section A Foundations of Crystallography. 64(a1). C361–C361. 1 indexed citations
16.
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
17.
Arai, Ryoichi, Kaori Ito, Tetsuo Ohnishi, et al.. (2007). Crystal structure of human myo‐inositol monophosphatase 2, the product of the putative susceptibility gene for bipolar disorder, schizophrenia, and febrile seizures. Proteins Structure Function and Bioinformatics. 67(3). 732–742. 17 indexed citations
18.
Tanaka, Hiroaki, Takashi Umehara, Koji Inaka, et al.. (2007). Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(2). 69–73. 9 indexed citations
19.
Bessho, Yoshitaka, Satoru Tamura, Hidetaka Hori, et al.. (1997). Planarian mitochondria sequence heterogeneity: relationships between the type of cytochrome c oxidase subunit I gene sequence, karyotype and genital organ. Molecular Ecology. 6(2). 129–136. 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026