Hidehiko Hirakawa

737 total citations
33 papers, 620 citations indexed

About

Hidehiko Hirakawa is a scholar working on Molecular Biology, Pharmacology and Oncology. According to data from OpenAlex, Hidehiko Hirakawa has authored 33 papers receiving a total of 620 indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 12 papers in Pharmacology and 5 papers in Oncology. Recurrent topics in Hidehiko Hirakawa's work include Pharmacogenetics and Drug Metabolism (12 papers), Enzyme Catalysis and Immobilization (11 papers) and Biochemical and Structural Characterization (5 papers). Hidehiko Hirakawa is often cited by papers focused on Pharmacogenetics and Drug Metabolism (12 papers), Enzyme Catalysis and Immobilization (11 papers) and Biochemical and Structural Characterization (5 papers). Hidehiko Hirakawa collaborates with scholars based in Japan, South Korea and United States. Hidehiko Hirakawa's co-authors include Teruyuki Nagamune, Noriho Kamiya, Satoshi Yamaguchi, Yûichi Yamamura, Tsutomu Tanaka, Hiroshi Watanabe, Jing Zhang, Youichi Ishii, Minae Mure and Emily E. Scott and has published in prestigious journals such as Journal of Biological Chemistry, Angewandte Chemie International Edition and PLoS ONE.

In The Last Decade

Hidehiko Hirakawa

32 papers receiving 618 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hidehiko Hirakawa Japan 14 523 109 77 75 61 33 620
Loleta Chung United States 8 831 1.6× 36 0.3× 189 2.5× 100 1.3× 121 2.0× 8 1.1k
Andreas Eipper Germany 7 416 0.8× 50 0.5× 52 0.7× 8 0.1× 83 1.4× 8 465
Marie Bérubé Canada 11 331 0.6× 33 0.3× 298 3.9× 23 0.3× 63 1.0× 15 614
Mandy K. S. Vink Netherlands 10 413 0.8× 28 0.3× 440 5.7× 35 0.5× 22 0.4× 12 630
Bert‐Jan Baas Netherlands 14 481 0.9× 25 0.2× 330 4.3× 28 0.4× 60 1.0× 24 745
Kaori Hiraga United States 11 503 1.0× 42 0.4× 20 0.3× 25 0.3× 53 0.9× 16 566
Robert J. Floor Netherlands 9 639 1.2× 38 0.3× 58 0.8× 11 0.1× 137 2.2× 10 710
Akihiro Ogura Japan 14 337 0.6× 17 0.2× 424 5.5× 60 0.8× 29 0.5× 41 631
Ivana Drienovská Netherlands 13 601 1.1× 12 0.1× 349 4.5× 76 1.0× 54 0.9× 23 818
Rebecca Blomberg Switzerland 4 658 1.3× 11 0.1× 109 1.4× 22 0.3× 77 1.3× 4 753

Countries citing papers authored by Hidehiko Hirakawa

Since Specialization
Citations

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

Fields of papers citing papers by Hidehiko Hirakawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hidehiko Hirakawa

This figure shows the co-authorship network connecting the top 25 collaborators of Hidehiko Hirakawa. A scholar is included among the top collaborators of Hidehiko Hirakawa 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 Hidehiko Hirakawa. Hidehiko Hirakawa 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.
2.
Hirakawa, Hidehiko, et al.. (2016). Three proliferating cell nuclear antigen homologues from Metallosphaera sedula form a head-to-tail heterotrimer. Scientific Reports. 6(1). 26588–26588. 5 indexed citations
3.
Hirakawa, Hidehiko, et al.. (2015). Supramolecular protein assembly supports immobilization of a cytochrome P450 monooxygenase system as water-insoluble gel. Scientific Reports. 5(1). 8648–8648. 26 indexed citations
4.
Hirakawa, Hidehiko, et al.. (2015). Ca2+‐independent sortase‐A exhibits high selective protein ligation activity in the cytoplasm of Escherichia coli. Biotechnology Journal. 10(9). 1487–1492. 64 indexed citations
5.
Hirakawa, Hidehiko, et al.. (2014). Electron donation to an archaeal cytochrome P450 is enhanced by PCNA‐mediated selective complex formation with foreign redox proteins. Biotechnology Journal. 9(12). 1573–1581. 15 indexed citations
6.
Min, Junhong, et al.. (2014). Fusion protein bilayer fabrication composed of recombinant azurin/cytochrome P450 by the sortase-mediated ligation method. Colloids and Surfaces B Biointerfaces. 120. 215–221. 3 indexed citations
7.
Hirakawa, Hidehiko, et al.. (2013). Introduction of selective intersubunit disulfide bonds into self‐assembly protein scaffold to enhance an artificial multienzyme complex's activity. Biotechnology and Bioengineering. 110(7). 1858–1864. 21 indexed citations
8.
Hirakawa, Hidehiko & Teruyuki Nagamune. (2013). Use of Sulfolobus solfataricus PCNA Subunit Proteins to Direct the Assembly of Multimeric Enzyme Complexes. Methods in molecular biology. 978. 149–163. 3 indexed citations
9.
Hirakawa, Hidehiko, et al.. (2013). Fine Tuning of Spatial Arrangement of Enzymes in a PCNA-Mediated Multienzyme Complex Using a Rigid Poly-L-Proline Linker. PLoS ONE. 8(9). e75114–e75114. 36 indexed citations
10.
Zhang, Jing, Satoshi Yamaguchi, Hidehiko Hirakawa, & Teruyuki Nagamune. (2013). Intracellular protein cyclization catalyzed by exogenously transduced Streptococcus pyogenes sortase A. Journal of Bioscience and Bioengineering. 116(3). 298–301. 11 indexed citations
11.
Tamaki, Takanori, Hidenori Ohashi, Hidehiko Hirakawa, et al.. (2013). Molecular recognition moiety and its target biomolecule interact in switching enzyme activity. Journal of Bioscience and Bioengineering. 115(6). 639–644. 2 indexed citations
12.
Hirakawa, Hidehiko & Teruyuki Nagamune. (2011). Nanoscale-Engineered Cytochrome P450 System with a Branch Structure. Methods in molecular biology. 743. 1–16. 3 indexed citations
13.
Yamamura, Yûichi, Hidehiko Hirakawa, Satoshi Yamaguchi, & Teruyuki Nagamune. (2011). Enhancement of sortase A-mediated protein ligation by inducing a β-hairpin structure around the ligation site. Chemical Communications. 47(16). 4742–4742. 59 indexed citations
14.
Reed, Timothy M., Gerald H. Lushington, Hidehiko Hirakawa, et al.. (2010). Crystal Structure of Histamine Dehydrogenase from Nocardioides simplex. Journal of Biological Chemistry. 285(33). 25782–25791. 18 indexed citations
15.
Hirakawa, Hidehiko & Teruyuki Nagamune. (2010). Molecular Assembly of P450 with Ferredoxin and Ferredoxin Reductase by Fusion to PCNA. ChemBioChem. 11(11). 1517–1520. 74 indexed citations
16.
Hirakawa, Hidehiko & Teruyuki Nagamune. (2009). A branched fusion P450 system containing CYP119. Journal of Bioscience and Bioengineering. 108. S100–S101. 2 indexed citations
17.
Reed, Timothy M., Hidehiko Hirakawa, Minae Mure, Emily E. Scott, & Julian Limburg. (2008). Expression, purification, crystallization and preliminary X-ray studies of histamine dehydrogenase fromNocardioides simplex. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(9). 785–787. 1 indexed citations
18.
Hirakawa, Hidehiko, et al.. (2007). Intramolecular electron transfer in a cytochrome P450cam system with a site-specific branched structure. Protein Engineering Design and Selection. 20(9). 453–459. 39 indexed citations
19.
Hirakawa, Hidehiko, et al.. (2005). Log P effect of organic solvents on a thermophilic alcohol dehydrogenase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1748(1). 94–99. 22 indexed citations
20.

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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