Shintaro Sugai

3.9k total citations
98 papers, 3.4k citations indexed

About

Shintaro Sugai is a scholar working on Molecular Biology, Materials Chemistry and Physical and Theoretical Chemistry. According to data from OpenAlex, Shintaro Sugai has authored 98 papers receiving a total of 3.4k indexed citations (citations by other indexed papers that have themselves been cited), including 62 papers in Molecular Biology, 25 papers in Materials Chemistry and 16 papers in Physical and Theoretical Chemistry. Recurrent topics in Shintaro Sugai's work include Protein Structure and Dynamics (29 papers), Enzyme Structure and Function (23 papers) and Proteins in Food Systems (15 papers). Shintaro Sugai is often cited by papers focused on Protein Structure and Dynamics (29 papers), Enzyme Structure and Function (23 papers) and Proteins in Food Systems (15 papers). Shintaro Sugai collaborates with scholars based in Japan, United States and Russia. Shintaro Sugai's co-authors include Kunihiro Kuwajima, Katsutoshi Nitta, Masamichi Ikeguchi, Masahiro Mitani, Norio Murai, Michio Yoneyama, Shio Makino, Akio Shimizu, Gennady V. Semisotnov and Bryan E. Finn and has published in prestigious journals such as Nucleic Acids Research, The Journal of Chemical Physics and Journal of Molecular Biology.

In The Last Decade

Shintaro Sugai

97 papers receiving 3.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Shintaro Sugai Japan	28	2.5k	1.5k	887	482	307	98	3.4k
Katsutoshi Nitta Japan	33	1.9k 0.8×	925 0.6×	502 0.6×	226 0.5×	283 0.9×	125	3.5k
D.C. Phillips United Kingdom	20	2.1k 0.8×	1.3k 0.9×	276 0.3×	323 0.7×	237 0.8×	29	3.0k
Gennady V. Semisotnov Russia	20	3.0k 1.2×	1.6k 1.0×	554 0.6×	207 0.4×	228 0.7×	52	3.7k
Valentina E. Bychkova Russia	19	1.8k 0.7×	979 0.6×	442 0.5×	166 0.3×	190 0.6×	50	2.6k
Kozo HAMAGUCHI Japan	31	2.4k 1.0×	708 0.5×	195 0.2×	77 0.2×	328 1.1×	137	3.0k
Daizo Hamada Japan	24	1.9k 0.8×	644 0.4×	465 0.5×	103 0.2×	194 0.6×	52	2.7k
George T. Robillard Netherlands	34	2.2k 0.9×	817 0.5×	243 0.3×	90 0.2×	286 0.9×	100	3.3k
Thomas F. Kumosinski United States	27	1.1k 0.4×	300 0.2×	1.1k 1.3×	208 0.4×	209 0.7×	79	2.5k
Sabato D’Auria Italy	33	2.5k 1.0×	1.2k 0.8×	126 0.1×	221 0.5×	280 0.9×	217	4.7k
Dietrich Zirwer Germany	25	1.4k 0.5×	527 0.3×	390 0.4×	171 0.4×	173 0.6×	71	1.9k

Countries citing papers authored by Shintaro Sugai

Since Specialization

Citations

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

Fields of papers citing papers by Shintaro Sugai

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shintaro Sugai

This figure shows the co-authorship network connecting the top 25 collaborators of Shintaro Sugai. A scholar is included among the top collaborators of Shintaro Sugai 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 Shintaro Sugai. Shintaro Sugai 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

Ikeguchi, Masamichi & Shintaro Sugai. (2009). Contribution of disulfide bonds to stability of the folding intermediate of α-lactalbumin. International journal of peptide & protein research. 33(4). 289–297. 3 indexed citations

Fujiwara, Kazuo, Masamichi Ikeguchi, & Shintaro Sugai. (2001). A Partially Unfolded State of Equine β-Lactoglobulin at pH 8.7. Journal of Protein Chemistry. 20(2). 131–137. 4 indexed citations

Shimizu, Akio, et al.. (1995). The superreactive disulfide bonds in α-lactalbumin and lysozyme. Journal of Protein Chemistry. 14(8). 731–737. 17 indexed citations

Tsuge, Hideaki, Hideo Ago, Masana Noma, et al.. (1992). Crystallographic Studies of a Calcium Binding Lysozyme from Equine Milk at 2.5 ÅResolution. The Journal of Biochemistry. 111(2). 141–143. 37 indexed citations

Kuwajima, Kunihiro, Edward P. Garvey, Bryan E. Finn, C. Robert Matthews, & Shintaro Sugai. (1991). Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry. 30(31). 7693–7703. 130 indexed citations

Permyakov, Eugene A., et al.. (1991). Calcium-regulated interactions of human α-lactalbumin with bee venom melittin. Biophysical Chemistry. 39(2). 111–117. 14 indexed citations

Tsuge, Hideaki, Masashi Miyano, Tatsuji Chuman, et al.. (1991). A structural study of calcium-binding equine lysozyme by two-dimensional 1H-NMR. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078(1). 77–84. 17 indexed citations

Kuwajima, Kunihiro, et al.. (1990). Kinetics of disulfide bond reduction in .alpha.-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. Biochemistry. 29(36). 8240–8249. 113 indexed citations

Desmet, Johan, H. Van Dael, Frans Van Cauwelaert, Katsutoshi Nitta, & Shintaro Sugai. (1989). Comparison of the binding of Ca2+ and Mn2+ to bovine α-lactalbumin and equine lysozyme. Journal of Inorganic Biochemistry. 37(3). 185–191. 26 indexed citations

10.

Kuwajima, Kunihiro, Masahiro Mitani, & Shintaro Sugai. (1989). Characterization of the critical state in protein folding. Journal of Molecular Biology. 206(3). 547–561. 169 indexed citations

11.

Ikeguchi, Masamichi, Kunihiro Kuwajima, Masahiro Mitani, & Shintaro Sugai. (1986). Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozyme. Biochemistry. 25(22). 6965–6972. 231 indexed citations

12.

Kuwajima, Kunihiro, et al.. (1980). α-Lactalbumin: A calcium metalloprotein. Biochemical and Biophysical Research Communications. 95(3). 1098–1104. 256 indexed citations

13.

Kuwajima, Kunihiro & Shintaro Sugai. (1978). Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism. Biophysical Chemistry. 8(3). 247–254. 49 indexed citations

14.

Murai, Norio, Masao Miyazaki, & Shintaro Sugai. (1976). The Anion-induced Conformational Transition of Poly(L-homoarginine). NIPPON KAGAKU KAISHI. 1976(4). 659–659. 6 indexed citations

15.

Nitta, Katsutoshi, et al.. (1973). Conformational transition of the copolymer of maleic acid and styrene in aqueous solution. Journal of Polymer Science Polymer Physics Edition. 11(3). 413–425. 68 indexed citations

16.

Ishikawa, Mitsuo & Shintaro Sugai. (1971). NMR Studies of β-Coil Transitions in Synthetic Polypeptides. Kobunshi Kagaku. 28(310). 138–142. 1 indexed citations

17.

Nitta, Katsutoshi, et al.. (1971). The Conformational Transition of Maleic Acid-Styrene Copolymer in Aqueous Solutions. Kobunshi Kagaku. 28(316). 671–675,708. 7 indexed citations

18.

Sugai, Shintaro & Katsutoshi Nitta. (1969). Counterion binding in partially neutralized poly(D‐glutamic acid) and poly(DL‐glutamic acid). Biopolymers. 7(4). 495–502. 10 indexed citations

19.

Nitta, Katsutoshi & Shintaro Sugai. (1967). Potentiometric Titration and the Stability of Helical Conformation of L-Alanine-L-glutamic Acid Copolymers in Aqueous Solution. Nippon kagaku zassi. 88(4). 412–416. 9 indexed citations

20.

Sugai, Shintaro, et al.. (1965). Conformation of Poly-L-alanine and Poly-DL-alanine in the Solid State. Kobunshi Kagaku. 22(237). 84–88. 2 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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