Mitsuru Tashiro

3.5k total citations · 2 hit papers
77 papers, 3.0k citations indexed

About

Mitsuru Tashiro is a scholar working on Molecular Biology, Spectroscopy and Organic Chemistry. According to data from OpenAlex, Mitsuru Tashiro has authored 77 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 27 papers in Spectroscopy and 16 papers in Organic Chemistry. Recurrent topics in Mitsuru Tashiro's work include Protein Structure and Dynamics (15 papers), Advanced NMR Techniques and Applications (15 papers) and Molecular spectroscopy and chirality (11 papers). Mitsuru Tashiro is often cited by papers focused on Protein Structure and Dynamics (15 papers), Advanced NMR Techniques and Applications (15 papers) and Molecular spectroscopy and chirality (11 papers). Mitsuru Tashiro collaborates with scholars based in Japan, United States and Spain. Mitsuru Tashiro's co-authors include G.T. Montelione, Takashi Fujimoto, Tomoya Machinami, Yoshiyuki Tanaka, Yoko Miyake, Akira Ono, Shuji Oda, Barbara A. Lyons, Hiroshi Yamaguchi and Yoshinori Kondo and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Mitsuru Tashiro

73 papers receiving 3.0k citations

Hit Papers

MercuryII-Mediated Formation of Thymine−HgII−Thymine Base... 2006 2026 2012 2019 2006 2008 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mitsuru Tashiro Japan 17 2.3k 809 808 377 268 77 3.0k
Michael R. Shortreed United States 31 2.3k 1.0× 717 0.9× 1.7k 2.0× 520 1.4× 140 0.5× 91 4.0k
Hong‐Zhang He Hong Kong 31 2.1k 0.9× 933 1.2× 671 0.8× 641 1.7× 116 0.4× 59 3.2k
Éric Peyrin France 32 2.1k 0.9× 310 0.4× 1.1k 1.4× 1.4k 3.8× 110 0.4× 127 3.0k
Saburo Neya Japan 31 1.7k 0.7× 1.4k 1.7× 691 0.9× 241 0.6× 68 0.3× 219 3.6k
Yelena V. Grinkova United States 28 2.9k 1.2× 525 0.6× 516 0.6× 915 2.4× 61 0.2× 42 4.6k
Danilo Roccatano Germany 37 2.3k 1.0× 756 0.9× 337 0.4× 446 1.2× 69 0.3× 97 3.7k
Yuqing Deng China 23 1.7k 0.7× 594 0.7× 259 0.3× 199 0.5× 68 0.3× 40 2.6k
Seiichi Nishizawa Japan 33 2.0k 0.9× 1.2k 1.4× 1.6k 1.9× 334 0.9× 479 1.8× 133 4.0k
Daisuke Miyoshi Japan 39 4.6k 2.0× 751 0.9× 311 0.4× 891 2.4× 114 0.4× 123 5.4k

Countries citing papers authored by Mitsuru Tashiro

Since Specialization
Citations

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

Fields of papers citing papers by Mitsuru Tashiro

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mitsuru Tashiro

This figure shows the co-authorship network connecting the top 25 collaborators of Mitsuru Tashiro. A scholar is included among the top collaborators of Mitsuru Tashiro 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 Mitsuru Tashiro. Mitsuru Tashiro 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
2.
Furihata, Kazuo & Mitsuru Tashiro. (2024). Optimization of reverse NOE pumping experiments in the analysis of complex systems with densely crowded NMR spectra. Analytical Sciences. 40(6). 1203–1207.
3.
Furihata, Kazuo & Mitsuru Tashiro. (2023). NMR screening method based on 19F spin–spin relaxation time for analyses of fluorinated compound bound to proteins. Analytical Sciences. 40(1). 219–223.
4.
Tashiro, Mitsuru, et al.. (2017). Chemoenzymatic synthesis of sucuronic acid using d -glucurono-6,3-lactone and sucrose as raw materials, and properties of the product. Enzyme and Microbial Technology. 110. 53–60. 1 indexed citations
5.
Kobayashi, Hidetomo, Toru Yoshida, Takuya Miyakawa, et al.. (2015). Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Journal of Biological Chemistry. 290(17). 11130–11143. 7 indexed citations
7.
Furihata, Kazuo, Sakurako Shimotakahara, Yōichi Shibusawa, & Mitsuru Tashiro. (2009). Application of WET sequence for the detection of the ligand signals resonating close to water. Magnetic Resonance in Chemistry. 47(11). 971–976. 4 indexed citations
8.
Tsuchiya, Hiroyuki, Mamoru Imanari, Shinji Ishihara, et al.. (2008). NMR Study for Self-aggregation of 1-Butyl-3-methylimidazolium Bromide in Aqueous Solution. Analytical Sciences. 24(10). 1369–1371. 1 indexed citations
9.
Tashiro, Mitsuru, et al.. (2008). Characterization of fibrillation process of α-synuclein at the initial stage. Biochemical and Biophysical Research Communications. 369(3). 910–914. 31 indexed citations
10.
Furihata, Kazuo, Sakurako Shimotakahara, & Mitsuru Tashiro. (2008). An efficient use of the WATERGATE W5 sequence for observing a ligand binding with a protein receptor. Magnetic Resonance in Chemistry. 46(9). 799–802. 12 indexed citations
11.
Tamura, Shun, et al.. (2007). Reduction of Aluminum Toxicity by 2-Isopropylmalic Acid in the Budding Yeast Saccharomyces cerevisiae. Biological Trace Element Research. 120(1-3). 257–263. 14 indexed citations
12.
Kojima, Masaki, et al.. (2007). Observation of multiple intermediates in α-synuclein fibril formation by singular value decomposition analysis. Biochemical and Biophysical Research Communications. 355(2). 398–403. 27 indexed citations
13.
14.
Tashiro, Mitsuru, et al.. (2005). Spectroscopic characterization of 2-isopropylmalic acid–aluminum(III) complex. Journal of Inorganic Biochemistry. 100(2). 201–205. 10 indexed citations
15.
Sei, Yoshihisa, Sakurako Shimotakahara, Heisaburo Shindo, et al.. (2005). Observation of Water Molecules Bound to a Protein Using Cold-Spray Ionization Mass Spectrometry. Analytical Sciences. 21(4). 449–451. 6 indexed citations
16.
Seki, Hiroko, Yoshihisa Sei, Sakurako Shimotakahara, et al.. (2004). Application of Difference NOE-pumping NMR Technique and Cold-Spray Ionization Mass Spectrometry to Identify a Ligand Binding with a Protein Receptor. Analytical Sciences. 20(10). 1467–1470. 8 indexed citations
17.
Tashiro, Mitsuru, Sakurako Shimotakahara, Hideki Hatanaka, et al.. (2003). Letter to the Editor: NMR structure of ubiquitin-like domain in PARKIN: Gene product of familial Parkinson's disease. Journal of Biomolecular NMR. 25(2). 153–156. 14 indexed citations
18.
Tashiro, Mitsuru, Nobuaki Ishida, Sakurako Shimotakahara, Soichi Tanabe, & Akira Ōkubo. (2003). Ontogenetic Changes of the Water Status in the Heated Quail’s Egg as Studied by Nuclear Magnetic Resonance Imaging. Analytical Sciences. 19(6). 933–936. 1 indexed citations
19.
Tashiro, Mitsuru, Roberto Tejero, Diane E. Zimmerman, et al.. (1997). High-resolution solution NMR structure of the Z domain of staphylococcal protein A. Journal of Molecular Biology. 272(4). 573–590. 129 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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