F. Inagaki

688 total citations
21 papers, 590 citations indexed

About

F. Inagaki is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, F. Inagaki has authored 21 papers receiving a total of 590 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 8 papers in Materials Chemistry and 3 papers in Genetics. Recurrent topics in F. Inagaki's work include Protein Structure and Dynamics (8 papers), Enzyme Structure and Function (8 papers) and Glycosylation and Glycoproteins Research (4 papers). F. Inagaki is often cited by papers focused on Protein Structure and Dynamics (8 papers), Enzyme Structure and Function (8 papers) and Glycosylation and Glycoproteins Research (4 papers). F. Inagaki collaborates with scholars based in Japan, United States and Germany. F. Inagaki's co-authors include Daisuke Kohda, Kenji Ogura, Hiroaki Terasawa, Hideki Hatanaka, Masato Kawasaki, Valsan Mandiyan, Joseph Schlessinger, Satoru Yuzawa, Toru Fuwa and Tetsuo Miyake and has published in prestigious journals such as Journal of Molecular Biology, Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

F. Inagaki

21 papers receiving 580 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
F. Inagaki Japan 13 486 94 83 82 69 21 590
Francesco Chillemi Italy 16 462 1.0× 86 0.9× 68 0.8× 50 0.6× 104 1.5× 35 693
Kurt W. Vogel United States 17 628 1.3× 94 1.0× 168 2.0× 76 0.9× 104 1.5× 36 909
Donald K. McRorie United States 9 525 1.1× 159 1.7× 96 1.2× 69 0.8× 59 0.9× 10 735
William Close Germany 8 592 1.2× 75 0.8× 73 0.9× 34 0.4× 47 0.7× 10 902
James R. Beasley United States 12 631 1.3× 121 1.3× 28 0.3× 101 1.2× 49 0.7× 19 746
Tom L. Blundell United Kingdom 10 681 1.4× 192 2.0× 115 1.4× 27 0.3× 62 0.9× 11 770
Norbert Garnier France 14 298 0.6× 38 0.4× 79 1.0× 75 0.9× 40 0.6× 28 389
Berthold Wroblowski Belgium 14 546 1.1× 136 1.4× 98 1.2× 46 0.6× 64 0.9× 31 712
Linda Whittaker United States 13 627 1.3× 57 0.6× 76 0.9× 50 0.6× 44 0.6× 20 815
Deepti Karandur United States 11 522 1.1× 44 0.5× 86 1.0× 75 0.9× 76 1.1× 15 638

Countries citing papers authored by F. Inagaki

Since Specialization
Citations

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

Fields of papers citing papers by F. Inagaki

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of F. Inagaki

This figure shows the co-authorship network connecting the top 25 collaborators of F. Inagaki. A scholar is included among the top collaborators of F. Inagaki 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 F. Inagaki. F. Inagaki 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.
Ogura, Kenji, Yoshihiro Kobashigawa, Tomohide Saio, et al.. (2013). Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies. Protein Engineering Design and Selection. 26(6). 409–416. 8 indexed citations
2.
Takahasi, Kiyohiro, et al.. (2012). A low-cost affinity purification system using  -1,3-glucan recognition protein and curdlan beads. Protein Engineering Design and Selection. 25(8). 405–413. 9 indexed citations
3.
Sekiguchi, Mariko, Yoshihiro Kobashigawa, Motoji Kawasaki, et al.. (2011). An evaluation tool for FKBP12-dependent and -independent mTOR inhibitors using a combination of FKBP-mTOR fusion protein, DSC and NMR. Protein Engineering Design and Selection. 24(11). 811–817. 6 indexed citations
4.
Saio, Tomohide, Hiroyuki Kumeta, Kenji Ogura, et al.. (2007). The Cooperative Role of OsCnfU-1A Domain I and Domain II in the Iron Sulphur Cluster Transfer Process as Revealed by NMR. The Journal of Biochemistry. 142(1). 113–121. 10 indexed citations
5.
Kawasaki, Masato & F. Inagaki. (2001). Random PCR-Based Screening for Soluble Domains Using Green Fluorescent Protein. Biochemical and Biophysical Research Communications. 280(3). 842–844. 43 indexed citations
6.
Ogura, Kenji, Koji Nagata, Hideki Hatanaka, et al.. (1999). Solution structure of human acidic fibroblast growth factor and interaction with heparin-derived hexasaccharide. Journal of Biomolecular NMR. 13(1). 11–24. 46 indexed citations
7.
Ogura, Kenji, Shigeo Tsuchiya, Hiroaki Terasawa, et al.. (1999). Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide. Journal of Molecular Biology. 289(3). 439–445. 57 indexed citations
8.
Inagaki, F.. (1999). [Structural biology of SH2 and SH3].. PubMed. 44(4 Suppl). 355–67. 1 indexed citations
9.
Ogura, Kenji, Shigeo Tsuchiya, Hiroaki Terasawa, et al.. (1997). Conformation of an Shc-derived phosphotyrosine-containing peptide complexed with the Grb2 SH2 domain. Journal of Biomolecular NMR. 10(3). 273–278. 16 indexed citations
10.
Ogura, Kenji, Hiroaki Terasawa, & F. Inagaki. (1996). An improved double-tuned and isotope-filtered pulse scheme based on a pulsed field gradient and a wide-band inversion shaped pulse. Journal of Biomolecular NMR. 8(4). 89 indexed citations
11.
Ikura, Teikichi, N. Gō, Daisuke Kohda, et al.. (1993). Secondary structural features of modules M2 and M3 of barnase in solution by NMR experiment and distance geometry calculation. Proteins Structure Function and Bioinformatics. 16(4). 341–356. 18 indexed citations
12.
Kohda, Daisuke, Hideki Hatanaka, Masafumi Odaka, et al.. (1993). Solution Structure of the SH3 Domain of Phospholipase C-y. 3 indexed citations
13.
Wakamatsu, Kaori, Daisuke Kohda, Hideki Hatanaka, et al.. (1992). Structure-activity relationships of .mu.-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry. 31(50). 12577–12584. 71 indexed citations
14.
Tate, Shin‐ichi, Saori Ichikawa, M. Kaneko, et al.. (1992). Stable isotope aided nuclear magnetic resonance study to investigate the receptor-binding site of human interleukin 1.beta.. Biochemistry. 31(8). 2435–2442. 15 indexed citations
15.
Kohda, Daisuke & F. Inagaki. (1992). Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Biochemistry. 31(47). 11928–11939. 52 indexed citations
16.
17.
Nohara, Keiko, Minoru Suzuki, F. Inagaki, & Kunimitsu Kaya. (1991). A GM1b-Derived Disialoganglioside GD1c Is the Predominant Ganglioside of Rat Thymocytes1. The Journal of Biochemistry. 110(2). 274–278. 9 indexed citations
18.
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20.
Nagaoka, Shin‐ichi, et al.. (1987). Hydrated Dynamic Surfaces. ASAIO Journal. 33(2). 76–77. 34 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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