M. Fujihashi

1.2k total citations
42 papers, 937 citations indexed

About

M. Fujihashi is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, M. Fujihashi has authored 42 papers receiving a total of 937 indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 26 papers in Materials Chemistry and 9 papers in Pharmacology. Recurrent topics in M. Fujihashi's work include Enzyme Structure and Function (26 papers), Plant biochemistry and biosynthesis (11 papers) and Microbial Natural Products and Biosynthesis (9 papers). M. Fujihashi is often cited by papers focused on Enzyme Structure and Function (26 papers), Plant biochemistry and biosynthesis (11 papers) and Microbial Natural Products and Biosynthesis (9 papers). M. Fujihashi collaborates with scholars based in Japan, Canada and United States. M. Fujihashi's co-authors include Kunio Miki, E.F. Pai, Tanetoshi Koyama, Yuan‐Wei Zhang, Lakshmi P. Kotra, Yoshiki Higuchi, Yukio Kobayashi, Angélica M. Bello, Yoshiho Nagata and Nobuo Kamiya and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

M. Fujihashi

41 papers receiving 931 citations

Peers

M. Fujihashi

PHARM

BIOTE

R.D. Seidel United States

Peter A. Jekel Netherlands

T. Lundqvist Sweden

Massimiliano Perduca Italy

Eyal Akiva United States

Zhengding Su China

Lisa Wen United States

Erick Strauss South Africa

Erica Frare Italy

David J. Aceti United States

R.D. Seidel United States

M. Fujihashi

1.1k ×1.4

230 ×1.0

156 ×0.8

PHARM

197 ×1.9

BIOTE

132 ×1.3

Citations per year, relative to M. Fujihashi M. Fujihashi (= 1×) peers R.D. Seidel

Countries citing papers authored by M. Fujihashi

Since Specialization

Citations

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

Fields of papers citing papers by M. Fujihashi

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Fujihashi

This figure shows the co-authorship network connecting the top 25 collaborators of M. Fujihashi. A scholar is included among the top collaborators of M. Fujihashi 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 M. Fujihashi. M. Fujihashi is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Abe, Tohru, et al.. (2024). Identification and functional/structural analyses of large terpene synthases. Methods in enzymology on CD-ROM/Methods in enzymology. 699. 477–512. 2 indexed citations

Tachibana, M., Shigeo Toya, Hiroyoshi Matsumura, et al.. (2024). Heat‐sterilizable antibody mimics designed on the cold shock protein scaffold from hyperthermophile Thermotoga maritima. Protein Science. 34(1). e70018–e70018.

Sato, Takaaki, et al.. (2021). Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure. ACS Chemical Biology. 16(5). 794–799. 2 indexed citations

Fujihashi, M., et al.. (2018). Identification of a pyrophosphate-dependent kinase and its donor selectivity determinants. Nature Communications. 9(1). 1765–1765. 18 indexed citations

Fujihashi, M., et al.. (2015). Orotidine Monophosphate Decarboxylase – A Fascinating Workhorse Enzyme with Therapeutic Potential. Journal of genetics and genomics. 42(5). 221–234. 7 indexed citations

Fujihashi, M.. (2014). Investigation of the Reaction Mechanism of Enzymes Based on their Crystal Structures. Nihon Kessho Gakkaishi. 56(4). 236–240. 1 indexed citations

Sato, Takaaki, et al.. (2013). An Uncharacterized Member of the Ribokinase Family in Thermococcus kodakarensis Exhibits myo-Inositol Kinase Activity. Journal of Biological Chemistry. 288(29). 20856–20867. 9 indexed citations

Fujihashi, M., et al.. (2013). Atomic Resolution Structure of the Orotidine 5′-Monophosphate Decarboxylase Product Complex Combined with Surface Plasmon Resonance Analysis. Journal of Biological Chemistry. 288(13). 9011–9016. 9 indexed citations

Fujihashi, M., Toyokazu Ishida, Shingo Kuroda, et al.. (2013). Substrate Distortion Contributes to the Catalysis of Orotidine 5′-Monophosphate Decarboxylase. Journal of the American Chemical Society. 135(46). 17432–17443. 25 indexed citations

10.

Nakamura, Akira, M. Fujihashi, Takaaki Sato, et al.. (2012). Dynamic, Ligand-dependent Conformational Change Triggers Reaction of Ribose-1,5-bisphosphate Isomerase from Thermococcus kodakarensis KOD1. Journal of Biological Chemistry. 287(25). 20784–20796. 21 indexed citations

11.

Sasaki, Daisuke, M. Fujihashi, Yuki Iwata, et al.. (2011). Structure and Mutation Analysis of Archaeal Geranylgeranyl Reductase. Journal of Molecular Biology. 409(4). 543–557. 33 indexed citations

12.

Yoshida, Shosuke, M. Fujihashi, Kazuya Kitagawa, et al.. (2010). Structure-based Catalytic Optimization of a Type III Rubisco from a Hyperthermophile. Journal of Biological Chemistry. 285(50). 39339–39347. 24 indexed citations

13.

Fujihashi, M., et al.. (2007). Crystal structure of human cyclophilin D in complex with its inhibitor, cyclosporin A at 0.96‐Å resolution. Proteins Structure Function and Bioinformatics. 70(4). 1635–1639. 52 indexed citations

14.

Bello, Angélica M., M. Fujihashi, Yan Li, et al.. (2007). A Potent, Covalent Inhibitor of Orotidine 5‘-Monophosphate Decarboxylase with Antimalarial Activity.. Journal of Medicinal Chemistry. 50(10). 2541–2541. 1 indexed citations

15.

Fujihashi, M., Nobutaka Numoto, Yukio Kobayashi, et al.. (2006). Crystal Structure of Archaeal Photolyase from Sulfolobus tokodaii with Two FAD Molecules: Implication of a Novel Light-harvesting Cofactor. Journal of Molecular Biology. 365(4). 903–910. 64 indexed citations

16.

Payandeh, Jian, M. Fujihashi, W. Gillon, & E.F. Pai. (2005). The Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase Reveals an Ancient Fold for an Ancient Enzyme. Journal of Biological Chemistry. 281(9). 6070–6078. 41 indexed citations

17.

Amano, Koh, M. Fujihashi, Akikazu Ando, Kunio Miki, & Yoshiho Nagata. (2004). Involvement of Tyrosines at Fucose-binding Sites ofAleuria aurantiaLectin: Non-equal Response to Site-directed Mutagenesis among Five Sites. Bioscience Biotechnology and Biochemistry. 68(4). 841–847. 9 indexed citations

18.

Nonaka, Tsuyoshi, M. Fujihashi, Akiko Kita, et al.. (2004). The Crystal Structure of an Oxidatively Stable Subtilisin-like Alkaline Serine Protease, KP-43, with a C-terminal β-Barrel Domain. Journal of Biological Chemistry. 279(45). 47344–47351. 34 indexed citations

19.

Kharel, Yugesh, Yuan‐Wei Zhang, M. Fujihashi, Kunio Miki, & Tanetoshi Koyama. (2001). Identification of Significant Residues for Homoallylic Substrate Binding of Micrococcus luteus B-P 26 Undecaprenyl Diphosphate Synthase. Journal of Biological Chemistry. 276(30). 28459–28464. 32 indexed citations

20.

Fujihashi, M., Naoto Shimizu, Yuan‐Wei Zhang, Tanetoshi Koyama, & Kunio Miki. (1999). Crystallization and preliminary X-ray diffraction studies of undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26. Acta Crystallographica Section D Biological Crystallography. 55(9). 1606–1607. 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.

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