Shinichi Taoka

1.4k total citations
23 papers, 1.1k citations indexed

About

Shinichi Taoka is a scholar working on Molecular Biology, Rheumatology and Clinical Biochemistry. According to data from OpenAlex, Shinichi Taoka has authored 23 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 12 papers in Rheumatology and 7 papers in Clinical Biochemistry. Recurrent topics in Shinichi Taoka's work include Porphyrin Metabolism and Disorders (12 papers), Folate and B Vitamins Research (12 papers) and Metabolism and Genetic Disorders (7 papers). Shinichi Taoka is often cited by papers focused on Porphyrin Metabolism and Disorders (12 papers), Folate and B Vitamins Research (12 papers) and Metabolism and Genetic Disorders (7 papers). Shinichi Taoka collaborates with scholars based in United States, Bulgaria and China. Shinichi Taoka's co-authors include Ruma Banerjee, Xiaoyin Shan, Warren D. Kruger, Matthew West, Ömer Kabil, Bryan W. Lepore, Sunil Ojha, Dagmar Ringe, Rugmini Padmakumar and Antony R. Crofts and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Shinichi Taoka

23 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shinichi Taoka United States 18 709 585 479 224 86 23 1.1k
Fernande Chatagner France 16 210 0.3× 171 0.3× 205 0.4× 125 0.6× 8 0.1× 59 712
Takahiro Hatanaka United States 15 535 0.8× 27 0.0× 561 1.2× 286 1.3× 12 0.1× 23 1.1k
Richard J. Guillory United States 22 943 1.3× 116 0.2× 99 0.2× 135 0.6× 5 0.1× 50 1.3k
R Aquaron France 18 503 0.7× 106 0.2× 66 0.1× 211 0.9× 5 0.1× 64 929
Giovanna Colombo United States 19 446 0.6× 45 0.1× 145 0.3× 130 0.6× 8 0.1× 37 913
Jan Lj. Miljković Germany 13 365 0.5× 38 0.1× 793 1.7× 43 0.2× 162 1.9× 20 1.1k
Mahmoud Tayeh United States 9 336 0.5× 21 0.0× 219 0.5× 112 0.5× 64 0.7× 20 1.0k
Doreen Braun Germany 16 248 0.3× 25 0.0× 101 0.2× 52 0.2× 60 0.7× 37 896
Amy L. Wiseman United States 7 261 0.4× 70 0.1× 293 0.6× 14 0.1× 11 0.1× 7 578
Guey‐Shuang Wu United States 22 329 0.5× 81 0.1× 54 0.1× 49 0.2× 16 0.2× 46 1.1k

Countries citing papers authored by Shinichi Taoka

Since Specialization
Citations

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

Fields of papers citing papers by Shinichi Taoka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shinichi Taoka

This figure shows the co-authorship network connecting the top 25 collaborators of Shinichi Taoka. A scholar is included among the top collaborators of Shinichi Taoka 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 Shinichi Taoka. Shinichi Taoka 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.
Puranik, Mrinalini, Colin L. Weeks, Dorothée Lahaye, et al.. (2006). Dynamics of Carbon Monoxide Binding to Cystathionine β-Synthase. Journal of Biological Chemistry. 281(19). 13433–13438. 72 indexed citations
2.
3.
Taoka, Shinichi & Ruma Banerjee. (2002). Stopped-flow Kinetic Analysis of the Reaction Catalyzed by the Full-length Yeast Cystathionine β-Synthase. Journal of Biological Chemistry. 277(25). 22421–22425. 27 indexed citations
5.
Taoka, Shinichi, Edward L. Green, Thomas M. Loehr, & Ruma Banerjee. (2001). Mercuric chloride-induced spin or ligation state changes in ferric or ferrous human cystathionine β-synthase inhibit enzyme activity. Journal of Inorganic Biochemistry. 87(4). 253–259. 23 indexed citations
6.
Taoka, Shinichi & Ruma Banerjee. (2001). Characterization of NO binding to human cystathionine β-synthase:. Journal of Inorganic Biochemistry. 87(4). 245–251. 163 indexed citations
7.
Green, Edward L., Shinichi Taoka, Ruma Banerjee, & Thomas M. Loehr. (2000). Resonance Raman Characterization of the Heme Cofactor in Cystathionine β-Synthase. Identification of the Fe−S(Cys) Vibration in the Six-Coordinate Low-Spin Heme. Biochemistry. 40(2). 459–463. 38 indexed citations
8.
Taoka, Shinichi, Matthew West, & Ruma Banerjee. (1999). Characterization of the Heme and Pyridoxal Phosphate Cofactors of Human Cystathionine β-Synthase Reveals Nonequivalent Active Sites. Biochemistry. 38(22). 7406–7406. 16 indexed citations
9.
Taoka, Shinichi, Matthew West, & Ruma Banerjee. (1999). Characterization of the Heme and Pyridoxal Phosphate Cofactors of Human Cystathionine β-Synthase Reveals Nonequivalent Active Sites. Biochemistry. 38(9). 2738–2744. 92 indexed citations
10.
Taoka, Shinichi, et al.. (1999). Assignment of Enzymatic Functions to Specific Regions of the PLP-Dependent Heme Protein Cystathionine β-Synthase. Biochemistry. 38(40). 13155–13161. 70 indexed citations
11.
Taoka, Shinichi, et al.. (1998). Evidence for Heme-mediated Redox Regulation of Human Cystathionine β-Synthase Activity. Journal of Biological Chemistry. 273(39). 25179–25184. 209 indexed citations
12.
Taoka, Shinichi, Raghavakaimal Padmakumar, Charles B. Grissom, & Ruma Banerjee. (1997). Magnetic field effects on coenzyme B12-dependent enzymes: Validation of ethanolamine ammonia lyase results and extension to human methylmalonyl CoA mutase. Bioelectromagnetics. 18(7). 506–513. 21 indexed citations
13.
Calafat, Antonia M., Shinichi Taoka, James M. Puckett, et al.. (1995). Structural and electronic similarity but functional difference in methylmalonyl-CoA mutase between coenzyme B12 and the analog 2,'5'-dideoxyadenosylcobalamin. Biochemistry. 34(43). 14125–14130. 29 indexed citations
14.
Taoka, Shinichi, Chia‐Ling Tu, Kurt A. Kistler, & David N. Silverman. (1994). Comparison of intra- and intermolecular proton transfer in human carbonic anhydrase II.. Journal of Biological Chemistry. 269(27). 17988–17992. 26 indexed citations
15.
Taoka, Shinichi, et al.. (1994). Inhibition of the human methylmalonyl-CoA mutase by various CoA-esters.. Journal of Biological Chemistry. 269(50). 31630–31634. 42 indexed citations
16.
LoGrasso, Philip V., et al.. (1993). Influence of amino acid replacement at position 198 on catalytic properties of zinc-bound water in human carbonic anhydrase III. Biochemistry. 32(22). 5786–5791. 21 indexed citations
17.
Taoka, Shinichi, Paul A. Jursinic, & M. Seibert. (1993). Slow oxygen release on the first two flashes in chemically stressed Photosystem II membrane fragments results from hydrogen peroxide oxidation. Photosynthesis Research. 38(3). 425–431. 10 indexed citations
18.
Taoka, Shinichi, et al.. (1992). Catalysis by mutants of human carbonic anhydrase II: effects of replacing hydrophobic residues 198 and 204. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1159(3). 274–278. 5 indexed citations
19.
Taoka, Shinichi. (1989). Kinetics of electron transfer and binding of inhibitors in the two-electron gate of chloroplasts. 1 indexed citations
20.
Tsuruya, Shigeru, et al.. (1970). Polymerization of 2, 4, 6‐tribromophenol by copper (II) ‐ acetonitrile complex. Journal of Polymer Science Part B Polymer Letters. 8(4). 275–279. 4 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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