Yoshihiro Agari

881 total citations
30 papers, 717 citations indexed

About

Yoshihiro Agari is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Yoshihiro Agari has authored 30 papers receiving a total of 717 indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 18 papers in Materials Chemistry and 16 papers in Genetics. Recurrent topics in Yoshihiro Agari's work include Enzyme Structure and Function (18 papers), Bacterial Genetics and Biotechnology (15 papers) and Biochemical and Molecular Research (6 papers). Yoshihiro Agari is often cited by papers focused on Enzyme Structure and Function (18 papers), Bacterial Genetics and Biotechnology (15 papers) and Biochemical and Molecular Research (6 papers). Yoshihiro Agari collaborates with scholars based in Japan, United States and Netherlands. Yoshihiro Agari's co-authors include Akeo Shinkai, Seiki Kuramitsu, Keiko Sakamoto, Shigeyuki Yokoyama, Tairo Oshima, Masatada Tamakoshi, Akio Ebihara, Naoshi Dohmae, Koji Yonekura and Saori Maki-Yonekura and has published in prestigious journals such as Molecular Cell, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Yoshihiro Agari

30 papers receiving 711 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yoshihiro Agari Japan 15 634 202 126 100 63 30 717
P. Imbault France 14 826 1.3× 84 0.4× 92 0.7× 35 0.3× 42 0.7× 22 946
Matthias Brigulla Germany 7 445 0.7× 312 1.5× 181 1.4× 80 0.8× 15 0.2× 7 736
Christopher B. Sherrill United States 9 532 0.8× 76 0.4× 53 0.4× 76 0.8× 85 1.3× 10 748
Christopher N. Merrikh United States 9 606 1.0× 246 1.2× 57 0.5× 33 0.3× 31 0.5× 11 745
Alexandra Tsirigotaki Belgium 14 423 0.7× 284 1.4× 118 0.9× 42 0.4× 24 0.4× 16 728
Wenjie Zeng China 15 533 0.8× 169 0.8× 75 0.6× 28 0.3× 19 0.3× 26 760
Nam K. Tonthat United States 17 561 0.9× 371 1.8× 176 1.4× 79 0.8× 57 0.9× 18 762
Jan Bobek Czechia 15 367 0.6× 101 0.5× 81 0.6× 13 0.1× 44 0.7× 29 551
Mario Bumann Switzerland 8 517 0.8× 102 0.5× 32 0.3× 90 0.9× 16 0.3× 12 605

Countries citing papers authored by Yoshihiro Agari

Since Specialization
Citations

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

Fields of papers citing papers by Yoshihiro Agari

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yoshihiro Agari

This figure shows the co-authorship network connecting the top 25 collaborators of Yoshihiro Agari. A scholar is included among the top collaborators of Yoshihiro Agari 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 Yoshihiro Agari. Yoshihiro Agari 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.
Kanagawa, Mayumi, Kiyoshi Okada, Seiki Baba, et al.. (2016). Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, fromThermus thermophilus,Sulfolobus tokodaiiandMethanocaldococcus jannaschii. Acta Crystallographica Section F Structural Biology Communications. 72(8). 627–635. 3 indexed citations
2.
Iwanaga, Naoki, Kaori Ide, Takeshi Nagashima, et al.. (2014). Genome-wide comprehensive analysis of transcriptional regulation by ArgR in Thermus thermophilus. Extremophiles. 18(6). 995–1008. 7 indexed citations
3.
Takano, Hideaki, Yoshihiro Agari, Kenta Hagiwara, et al.. (2014). LdrP, a cAMP receptor protein/FNR family transcriptional regulator, serves as a positive regulator for the light-inducible gene cluster in the megaplasmid of Thermus thermophilus. Microbiology. 160(12). 2650–2660. 17 indexed citations
4.
Agari, Yoshihiro, Kenji Fukui, Noriko Nakagawa, et al.. (2014). The role of ribonucleases in regulating global mRNA levels in the model organism Thermus thermophilus HB8. BMC Genomics. 15(1). 386–386. 13 indexed citations
5.
Agari, Yoshihiro, Seiki Kuramitsu, & Akeo Shinkai. (2012). X‐ray crystal structure of TTHB099, a CRP/FNR superfamily transcriptional regulator from thermus thermophilus HB8, reveals a DNA‐binding protein with no required allosteric effector molecule. Proteins Structure Function and Bioinformatics. 80(5). 1490–1494. 10 indexed citations
6.
Sakamoto, Keiko, Yoshihiro Agari, Seiki Kuramitsu, & Akeo Shinkai. (2011). Phenylacetyl Coenzyme A Is an Effector Molecule of the TetR Family Transcriptional Repressor PaaR from Thermus thermophilusHB8. Journal of Bacteriology. 193(17). 4388–4395. 20 indexed citations
7.
Morita, R, Hideo Ohyama, Ryosuke Mega, et al.. (2011). An alkyltransferase-like protein from Thermus thermophilus HB8 affects the regulation of gene expression in alkylation response. The Journal of Biochemistry. 150(3). 327–339. 2 indexed citations
8.
Fukui, Kenji, Taisuke Wakamatsu, Yoshihiro Agari, Ryoji Masui, & Seiki Kuramitsu. (2011). Inactivation of the DNA Repair Genes mutS, mutL or the Anti-Recombination Gene mutS2 Leads to Activation of Vitamin B1 Biosynthesis Genes. PLoS ONE. 6(4). e19053–e19053. 18 indexed citations
9.
Agari, Yoshihiro, Seiki Kuramitsu, & Akeo Shinkai. (2010). Identification of novel genes regulated by the oxidative stress-responsive transcriptional activator SdrP in Thermus thermophilus HB8. FEMS Microbiology Letters. 313(2). 127–134. 14 indexed citations
10.
Kitamura, Yoshiaki, Akio Ebihara, Yoshihiro Agari, et al.. (2009). Structure ofD-alanine-D-alanine ligase fromThermus thermophilusHB8: cumulative conformational change and enzyme–ligand interactions. Acta Crystallographica Section D Biological Crystallography. 65(10). 1098–1106. 36 indexed citations
11.
Agari, Yoshihiro, Keiko Sakamoto, Masatada Tamakoshi, et al.. (2009). Transcription Profile of Thermus thermophilus CRISPR Systems after Phage Infection. Journal of Molecular Biology. 395(2). 270–281. 98 indexed citations
12.
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
13.
Sakamoto, Keiko, et al.. (2008). X‐ray crystal structure of a CRISPR‐associated RAMP superfamily protein, Cmr5, from Thermus thermophilus HB8. Proteins Structure Function and Bioinformatics. 75(2). 528–532. 21 indexed citations
14.
Kumarevel, Thirumananseri, Yoshihiro Agari, Akeo Shinkai, et al.. (2008). Crystal structure of ST2348, a CBS domain protein, from hyperthermophilic archaeon Sulfolobus tokodaii. Biochemical and Biophysical Research Communications. 375(1). 124–128. 12 indexed citations
15.
Sakamoto, Keiko, Yoshihiro Agari, Shigeyuki Yokoyama, Seiki Kuramitsu, & Akeo Shinkai. (2008). Functional identification of an anti-σE factor from Thermus thermophilus HB8. Gene. 423(2). 153–159. 5 indexed citations
16.
Naitow, Hisashi, Yuki Nakamura, Noriko Nakagawa, et al.. (2008). Crystallization screening test for the whole-cell project onThermus thermophilusHB8. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(6). 487–491. 27 indexed citations
17.
Agari, Yoshihiro, et al.. (2008). Global gene expression mediated by Thermus thermophilus SdrP, a CRP/FNR family transcriptional regulator. Molecular Microbiology. 70(1). 60–75. 43 indexed citations
18.
Agari, Yoshihiro, Shinya Sato, Taisuke Wakamatsu, et al.. (2007). X‐ray crystal structure of a hypothetical Sua5 protein from Sulfolobus tokodaii strain 7. Proteins Structure Function and Bioinformatics. 70(3). 1108–1111. 26 indexed citations
19.
Goto, Masaru, Yoshihiro Agari, R. Omi, I. Miyahara, & Ken Hirotsu. (2003). Expression, purification and preliminary X-ray characterization ofN-acetyl-γ-glutamyl-phosphate reductase fromThermus thermophilusHB8. Acta Crystallographica Section D Biological Crystallography. 59(2). 356–358. 4 indexed citations
20.
Ohtani, Naoto, Noriko Nakagawa, Jun Hoseki, et al.. (2002). [An exhaustive overproduction of bacterial proteins].. PubMed. 47(8 Suppl). 1009–13. 1 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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