Shigeru Endo

1.2k total citations
50 papers, 912 citations indexed

About

Shigeru Endo is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Shigeru Endo has authored 50 papers receiving a total of 912 indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 19 papers in Materials Chemistry and 10 papers in Spectroscopy. Recurrent topics in Shigeru Endo's work include Protein Structure and Dynamics (24 papers), Enzyme Structure and Function (18 papers) and Spectroscopy and Quantum Chemical Studies (8 papers). Shigeru Endo is often cited by papers focused on Protein Structure and Dynamics (24 papers), Enzyme Structure and Function (18 papers) and Spectroscopy and Quantum Chemical Studies (8 papers). Shigeru Endo collaborates with scholars based in Japan and Canada. Shigeru Endo's co-authors include Hiroshi Wako, Kuniaki Nagayama, Akiyoshi Wada, Keiko Tanaka, Tsuguhiro Hoshino, Toshiki Nakamura, Katsuyuki Hayakawa, Hideaki� Yoshimura, Masaki Kato and Hideyuki Yoshimura and has published in prestigious journals such as Bioinformatics, Journal of Molecular Biology and Cancer.

In The Last Decade

Shigeru Endo

47 papers receiving 866 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shigeru Endo Japan 17 434 270 222 141 111 50 912
Kazuhiro Fukada Japan 19 253 0.6× 127 0.5× 45 0.2× 33 0.2× 122 1.1× 75 1.1k
Michel Juy France 17 486 1.1× 202 0.7× 114 0.5× 180 1.3× 33 0.3× 23 957
Kenji Sasahara Japan 22 914 2.1× 281 1.0× 64 0.3× 26 0.2× 165 1.5× 46 1.3k
Corey J. Wilson United States 24 915 2.1× 265 1.0× 53 0.2× 58 0.4× 34 0.3× 49 1.3k
Daiana A. Capdevila Argentina 20 745 1.7× 177 0.7× 245 1.1× 65 0.5× 12 0.1× 31 1.2k
Toon H. Evers Netherlands 11 648 1.5× 97 0.4× 107 0.5× 57 0.4× 25 0.2× 15 1.0k
Kira A. Markossian Russia 21 827 1.9× 234 0.9× 50 0.2× 43 0.3× 112 1.0× 35 1.1k
Ronald Gebhardt Germany 21 251 0.6× 297 1.1× 64 0.3× 88 0.6× 609 5.5× 69 1.1k
Andrew N. Round United Kingdom 17 234 0.5× 67 0.2× 101 0.5× 415 2.9× 302 2.7× 24 1.0k
S. Abe Japan 17 570 1.3× 334 1.2× 54 0.2× 63 0.4× 43 0.4× 95 1.3k

Countries citing papers authored by Shigeru Endo

Since Specialization
Citations

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

Fields of papers citing papers by Shigeru Endo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shigeru Endo

This figure shows the co-authorship network connecting the top 25 collaborators of Shigeru Endo. A scholar is included among the top collaborators of Shigeru Endo 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 Shigeru Endo. Shigeru Endo 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.
Matsuki, Hitoshi, et al.. (2017). Thermotropic and barotropic phase transitions on diacylphosphatidylethanolamine bilayer membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1859(7). 1222–1232. 12 indexed citations
2.
Wako, Hiroshi & Shigeru Endo. (2017). Normal mode analysis as a method to derive protein dynamics information from the Protein Data Bank. Biophysical Reviews. 9(6). 877–893. 46 indexed citations
3.
Kinjo, Akira R., Gert‐Jan Bekker, Hiroshi Wako, et al.. (2017). New tools and functions in data‐out activities at Protein Data Bank Japan (PDBj). Protein Science. 27(1). 95–102. 65 indexed citations
4.
Wako, Hiroshi & Shigeru Endo. (2013). Normal mode analysis based on an elastic network model for biomolecules in the Protein Data Bank, which uses dihedral angles as independent variables. Computational Biology and Chemistry. 44. 22–30. 29 indexed citations
5.
Tsuchiya, Yuko, Kengo Kinoshita, Shigeru Endo, & Hiroshi Wako. (2012). Dynamic features of homodimer interfaces calculated by normal‐mode analysis. Protein Science. 21(10). 1503–1513. 4 indexed citations
6.
7.
Sugiyama, Junichi, et al.. (2011). A Method of Visualizing Three-Dimensional Distribution of Yeast in Bread Dough. Revista Trace. 23(3). 313–320.
8.
Hirose, Shuichi, Yutaka Kuroda, Hiroshi Wako, et al.. (2010). Prediction of protein motions from amino acid sequence and its application to protein-protein interaction. BMC Structural Biology. 10(1). 20–20. 14 indexed citations
9.
Wako, Hiroshi, Masaki Kato, & Shigeru Endo. (2004). ProMode: a database of normal mode analyses on protein molecules with a full-atom model. Bioinformatics. 20(13). 2035–2043. 48 indexed citations
10.
Wako, Hiroshi, et al.. (2003). Improvements in ProMode (a Database of Normal Mode Analyses of Proteins). Proceedings Genome Informatics Workshop/Genome informatics. 14. 663–664. 1 indexed citations
11.
Wako, Hiroshi & Shigeru Endo. (2002). ProMode: A Database of Normal Mode Analysis of Proteins. Proceedings Genome Informatics Workshop/Genome informatics. 13(13). 519–520. 4 indexed citations
12.
13.
Wako, Hiroshi, Shigeru Endo, Kuniaki Nagayama, & Nobuhiro Gō. (1995). FEDER/2: program for static and dynamic conformational energy analysis of macro-molecules in dihedral angle space. Computer Physics Communications. 91(1-3). 233–251. 16 indexed citations
14.
Takahashi, Takuya, Shigeru Endo, & Kuniaki Nagayama. (1993). Stabilization of Protein Crystals by Electrostatic Interactions as Revealed by a Numerical Approach. Journal of Molecular Biology. 234(2). 421–432. 22 indexed citations
15.
Endo, Shigeru, et al.. (1993). Oxytocin solution structure changes upon protonation of the N-terminus in dimethyl sulfoxide. Journal of Biomolecular NMR. 3(6). 653–73. 18 indexed citations
16.
Yoshimura, Hideaki�, et al.. (1990). Two-dimensional crystallization of proteins on mercury. Ultramicroscopy. 32(3). 265–274. 65 indexed citations
17.
Yoshimura, Hideyuki, et al.. (1989). Hexagonal Structure of Two-Dimensional Crystals of the α3β3 Complex of Thermophilic ATP Synthase1. The Journal of Biochemistry. 106(6). 958–960. 41 indexed citations
18.
Endo, Shigeru, et al.. (1988). Probing Stability and Dynamics of Proteins by Protease Digestion II: Identification of the Initial Chymotryptic Cleavage Sites of Homologous Cytochromesc. Journal of Biomolecular Structure and Dynamics. 6(1). 1–21. 31 indexed citations
19.
Endo, Shigeru, Yoshio Saitō, & Akiyoshi Wada. (1983). Denaturant-gradient chromatography for the study of protein denaturation: Principle and procedure. Analytical Biochemistry. 131(1). 108–120. 29 indexed citations
20.
Endo, Shigeru, et al.. (1981). Scanning electron microscopy studies of wheat protein fractions from doughs mixed with oxidants at high temperature. Journal of the Science of Food and Agriculture. 32(3). 235–242. 5 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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