Katsuhide Yutani

5.2k total citations
154 papers, 4.5k citations indexed

About

Katsuhide Yutani is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Katsuhide Yutani has authored 154 papers receiving a total of 4.5k indexed citations (citations by other indexed papers that have themselves been cited), including 136 papers in Molecular Biology, 111 papers in Materials Chemistry and 16 papers in Spectroscopy. Recurrent topics in Katsuhide Yutani's work include Enzyme Structure and Function (109 papers), Protein Structure and Dynamics (92 papers) and Biochemical and Molecular Research (16 papers). Katsuhide Yutani is often cited by papers focused on Enzyme Structure and Function (109 papers), Protein Structure and Dynamics (92 papers) and Biochemical and Molecular Research (16 papers). Katsuhide Yutani collaborates with scholars based in Japan, United States and Russia. Katsuhide Yutani's co-authors include Kyoko Ogasahara, Kazufumi Takano, Yuriko Yamagata, Yoshinobu Sugino, Jun Funahashi, Edith Wilson Miles, Satoshi Fujii, Ryota Kuroki, Masakazu Kikuchi and Kouhei Tsumoto and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Katsuhide Yutani

153 papers receiving 4.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Katsuhide Yutani Japan 41 3.8k 2.1k 370 325 314 154 4.5k
Roger H. Pain United Kingdom 35 3.3k 0.9× 1.3k 0.6× 449 1.2× 194 0.6× 220 0.7× 122 4.3k
Jack F. Kirsch United States 41 4.1k 1.1× 1.7k 0.8× 287 0.8× 263 0.8× 284 0.9× 145 5.8k
Kyoko Ogasahara Japan 33 2.4k 0.6× 1.4k 0.7× 257 0.7× 254 0.8× 224 0.7× 91 2.8k
Karen N. Allen United States 43 4.0k 1.0× 1.9k 0.9× 316 0.9× 206 0.6× 309 1.0× 137 5.8k
Gennady V. Semisotnov Russia 20 3.0k 0.8× 1.6k 0.7× 477 1.3× 140 0.4× 156 0.5× 52 3.7k
Se Won Suh South Korea 40 4.2k 1.1× 906 0.4× 287 0.8× 187 0.6× 494 1.6× 196 5.7k
Lanette Fee United States 10 2.9k 0.8× 717 0.3× 358 1.0× 244 0.8× 275 0.9× 12 4.0k
A. Ducruix France 32 2.6k 0.7× 1.5k 0.7× 332 0.9× 119 0.4× 118 0.4× 103 3.8k
Louis T. J. Delbaere Canada 36 3.1k 0.8× 1.4k 0.6× 239 0.6× 258 0.8× 390 1.2× 132 4.3k
David P. Goldenberg United States 32 2.7k 0.7× 981 0.5× 556 1.5× 152 0.5× 213 0.7× 58 3.2k

Countries citing papers authored by Katsuhide Yutani

Since Specialization
Citations

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

Fields of papers citing papers by Katsuhide Yutani

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Katsuhide Yutani

This figure shows the co-authorship network connecting the top 25 collaborators of Katsuhide Yutani. A scholar is included among the top collaborators of Katsuhide Yutani 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 Katsuhide Yutani. Katsuhide Yutani 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.
Chiba, Kaori, Toshiyuki Chatake, Takashi Ohhara, et al.. (2023). Site‐specific relaxation of peptide bond planarity induced by electrically attracted proton/deuteron observed by neutron crystallography. Protein Science. 32(10). e4765–e4765. 2 indexed citations
2.
Yutani, Katsuhide, Yoshinori Matsuura, Hisashi Naitow, & Yasumasa Joti. (2018). Ion–ion interactions in the denatured state contribute to the stabilization of CutA1 proteins. Scientific Reports. 8(1). 7613–7613. 8 indexed citations
3.
Bagautdinov, B. & Katsuhide Yutani. (2011). Structure of indole-3-glycerol phosphate synthase fromThermus thermophilusHB8: implications for thermal stability. Acta Crystallographica Section D Biological Crystallography. 67(12). 1054–1064. 15 indexed citations
4.
Bagautdinov, B., et al.. (2008). Structure of putative CutA1 fromHomo sapiensdetermined at 2.05 Å resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(5). 351–357. 3 indexed citations
5.
Tanaka, Tomoyuki, Kyoko Ogasahara, Yasushi Sakaguchi, et al.. (2006). Hyper‐thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C. FEBS Letters. 580(17). 4224–4230. 53 indexed citations
6.
Jeyakanthan, Jeyaraman, et al.. (2005). Purification, crystallization and preliminary X-ray crystallographic study of theL-fuculose-1-phosphate aldolase (FucA) fromThermus thermophilusHB8. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(12). 1075–1077. 9 indexed citations
7.
Hioki, Yusaku, Kyoko Ogasahara, Soo Jae Lee, et al.. (2004). The crystal structure of the tryptophan synthase β2 subunit from the hyperthermophile Pyrococcus furiosus. European Journal of Biochemistry. 271(13). 2624–2635. 16 indexed citations
8.
Ishida, Masami, Tairo Oshima, & Katsuhide Yutani. (2002). Overexpression inEscherichia coliof the AT-richtrpAandtrpBgenes from the hyperthermophilic archaeonPyrococcus furiosus. FEMS Microbiology Letters. 216(2). 179–183. 12 indexed citations
9.
Funahashi, Jun, Kazufumi Takano, Yuriko Yamagata, & Katsuhide Yutani. (2002). Positive Contribution of Hydration Structure on the Surface of Human Lysozyme to the Conformational Stability. Journal of Biological Chemistry. 277(24). 21792–21800. 16 indexed citations
10.
Ogasahara, Kyoko, et al.. (2001). Thermal stability of pyrrolidone carboxyl peptidases from the hyperthermophilic Archaeon, Pyrococcus furiosus. European Journal of Biochemistry. 268(11). 3233–3242. 28 indexed citations
11.
Kato, Akio, et al.. (2000). Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1481(1). 88–96. 14 indexed citations
12.
Takano, Kazufumi, et al.. (1999). Effect of foreign N‐terminal residues on the conformational stability of human lysozyme. European Journal of Biochemistry. 266(2). 675–682. 35 indexed citations
13.
Tahirov, T.H., Hideyuki Oki, Tomitake Tsukihara, et al.. (1998). Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus. Journal of Molecular Biology. 284(1). 101–124. 111 indexed citations
14.
Yamasaki, Kazuhiko, Kyoko Ogasahara, Katsuhide Yutani, Motohisa Oobatake, & Shigenori Kanaya. (1995). Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR Study. Biochemistry. 34(51). 16552–16562. 53 indexed citations
15.
Yutani, Katsuhide, Kyoko Ogasahara, & Kunihiro Kuwajima. (1992). Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. Journal of Molecular Biology. 228(2). 347–350. 107 indexed citations
16.
17.
18.
Matsumura, Masazumi, et al.. (1988). Role of tyrosine‐80 in the stability of kanamycin nucleotidyltransferase analyzed by site‐directed mutagenesis. European Journal of Biochemistry. 171(3). 715–720. 25 indexed citations
19.
Yutani, Katsuhide, et al.. (1987). Proton nuclear magnetic resonance studies on the wild-type and single amino acid substituted tryptophan synthase .alpha.-subunits. Biochemistry. 26(18). 5666–5671. 11 indexed citations
20.
Ono, Tomotada, et al.. (1974). Conformation of bovind .ALPHA.--casein. III. Conformation of .ALPHA.s-casein in various concentrations.. Agricultural and Biological Chemistry. 38(9). 1609–1616. 3 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Roger H. Pain Breakdown of academic impact, for papers by Jack F. Kirsch Breakdown of academic impact, for papers by Kyoko Ogasahara Breakdown of academic impact, for papers by Karen N. Allen Breakdown of academic impact, for papers by Gennady V. Semisotnov Breakdown of academic impact, for papers by Se Won Suh Breakdown of academic impact, for papers by Lanette Fee Breakdown of academic impact, for papers by A. Ducruix Breakdown of academic impact, for papers by Louis T. J. Delbaere Breakdown of academic impact, for papers by David P. Goldenberg
Rankless by CCL
2026