Y. Morimoto

3.7k total citations
113 papers, 3.0k citations indexed

About

Y. Morimoto is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Y. Morimoto has authored 113 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 37 papers in Materials Chemistry and 13 papers in Organic Chemistry. Recurrent topics in Y. Morimoto's work include Enzyme Structure and Function (29 papers), Protein Structure and Dynamics (13 papers) and Ubiquitin and proteasome pathways (10 papers). Y. Morimoto is often cited by papers focused on Enzyme Structure and Function (29 papers), Protein Structure and Dynamics (13 papers) and Ubiquitin and proteasome pathways (10 papers). Y. Morimoto collaborates with scholars based in Japan, United States and Canada. Y. Morimoto's co-authors include Noritake Yasuoka, Tomitake Tsukihara, Naoki Shibata, N Kitamura, Keiji Miyazawa, Takeshi Shimomura, J. Kondo, Tetsuo Toraya, Tsunehiro Mizushima and Masaki Unno and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and SHILAP Revista de lepidopterología.

In The Last Decade

Y. Morimoto

111 papers receiving 3.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Y. Morimoto Japan 25 1.9k 380 369 339 324 113 3.0k
Hideki Morimoto Japan 33 1.3k 0.7× 166 0.4× 760 2.1× 1.5k 4.5× 91 0.3× 121 3.8k
Sven Klußmann Germany 37 2.6k 1.4× 121 0.3× 273 0.7× 122 0.4× 140 0.4× 80 4.7k
Stefan Walenta Germany 31 2.5k 1.3× 94 0.2× 65 0.2× 226 0.7× 28 0.1× 71 4.7k
Elias Lolis United States 42 2.0k 1.0× 439 1.2× 40 0.1× 258 0.8× 116 0.4× 108 6.9k
Kurt Deshayes United States 34 4.2k 2.2× 339 0.9× 48 0.1× 287 0.8× 51 0.2× 57 5.5k
Láśzló Révész Sweden 35 1.9k 1.0× 103 0.3× 81 0.2× 117 0.3× 35 0.1× 203 4.4k
Judith Murray‐Rust United Kingdom 29 1.7k 0.9× 177 0.5× 25 0.1× 316 0.9× 42 0.1× 83 3.4k
Jianming Xie United States 30 2.6k 1.4× 365 1.0× 34 0.1× 220 0.6× 25 0.1× 51 4.4k
Toru Kawanishi Japan 31 2.1k 1.1× 349 0.9× 75 0.2× 243 0.7× 30 0.1× 173 3.6k
George D. Hartman United States 40 2.5k 1.3× 120 0.3× 466 1.3× 347 1.0× 24 0.1× 183 5.4k

Countries citing papers authored by Y. Morimoto

Since Specialization
Citations

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

Fields of papers citing papers by Y. Morimoto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Y. Morimoto

This figure shows the co-authorship network connecting the top 25 collaborators of Y. Morimoto. A scholar is included among the top collaborators of Y. Morimoto 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 Y. Morimoto. Y. Morimoto 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.
Jiko, Chimari, Y. Morimoto, Tomitake Tsukihara, & Christoph Gerle. (2023). Large-scale column-free purification of bovine F-ATP synthase. Journal of Biological Chemistry. 300(2). 105603–105603. 3 indexed citations
2.
Kita, Akiko & Y. Morimoto. (2022). Hydrogen/Deuterium Exchange Behavior During Denaturing/Refolding Processes Determined in Tetragonal Hen Egg-White Lysozyme Crystals. Molecular Biotechnology. 64(5). 590–597. 1 indexed citations
3.
Kita, Akiko & Y. Morimoto. (2020). Hydrogen/deuterium exchange behavior in tetragonal hen egg-white lysozyme crystals affected by solution state. Journal of Applied Crystallography. 53(3). 837–840. 7 indexed citations
4.
Kita, Akiko & Y. Morimoto. (2015). An Effective Deuterium Exchange Method for Neutron Crystal Structure Analysis with Unfolding–Refolding Processes. Molecular Biotechnology. 58(2). 130–136. 5 indexed citations
5.
Morimoto, Y., et al.. (2015). Crystal structure of (2-{[3,5-bis(1,1-dimethylethyl)-4-hydroxyphenyl](5-methyl-2H-pyrrol-2-ylidene)methyl}-5-methyl-1H-pyrrolido-κ2N,N′)difluoridoboron. SHILAP Revista de lepidopterología. 71(9). o694–o695. 1 indexed citations
6.
Uemura, Takuya, Akiko Kita, Yoshihiko Watanabe, et al.. (2015). The catalytic mechanism of decarboxylative hydroxylation of salicylate hydroxylase revealed by crystal structure analysis at 2.5 Å resolution. Biochemical and Biophysical Research Communications. 469(2). 158–163. 20 indexed citations
7.
Ozawa, Yukiko, Yuko Ueno, Y. Morimoto, et al.. (2011). Cyanidioschyzon merolae ferredoxin: A high resolution crystal structure analysis and its thermal stability. FEBS Letters. 585(9). 1299–1302. 6 indexed citations
8.
Kovalevsky, Andrey, Toshiyuki Chatake, Naoya Shibayama, et al.. (2010). Direct Determination of Protonation States of Histidine Residues in a 2 Å Neutron Structure of Deoxy-Human Normal Adult Hemoglobin and Implications for the Bohr Effect. Journal of Molecular Biology. 398(2). 276–291. 29 indexed citations
9.
Kovalevsky, Andrey, Toshiyuki Chatake, Naoya Shibayama, et al.. (2008). Preliminary time-of-flight neutron diffraction study of human deoxyhemoglobin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(4). 270–273. 9 indexed citations
10.
Fujii, Noriko, Yoshiari Shimmyo, Yutaka Sadakane, et al.. (2006). Age-related changes of alpha-crystallin aggregate in human lens. Amino Acids. 32(1). 87–94. 40 indexed citations
11.
Umena, Yasufumi, Kazuko Yorita, Takeshi Matsuoka, et al.. (2005). Crystallization and preliminary X-ray diffraction study ofL-lactate oxidase (LOX), R181M mutant, fromAerococcus viridans. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(4). 439–441. 5 indexed citations
12.
Unno, Masaki, Tsunehiro Mizushima, Y. Morimoto, et al.. (2002). The Structure of the Mammalian 20S Proteasome at 2.75 Å Resolution. Structure. 10(5). 609–618. 413 indexed citations
13.
Misaki, S., et al.. (1999). Structure determination of rubredoxin from Desulfovibrio vulgaris Miyazaki F in two crystal forms. Acta Crystallographica Section D Biological Crystallography. 55(2). 408–413. 8 indexed citations
14.
Bando, Mai, Y. Morimoto, Tetsuro Sato, et al.. (1994). Crystal structural analysis of tobacco necrosis virus at 5 Å resolution. Acta Crystallographica Section D Biological Crystallography. 50(6). 878–883. 4 indexed citations
15.
Fujii, Isao, Y. Morimoto, Yoshiki Higuchi, & Noritake Yasuoka. (1992). New programs. Journal of Molecular Graphics. 10(3). 185–189. 2 indexed citations
16.
Morimoto, Y., et al.. (1991). Evalution of X-ray diffraction data from protein crystals by use of an imaging plate. Acta Crystallographica Section B Structural Science. 47(1). 137–144. 19 indexed citations
17.
Park, Jang-Su, Y. Morimoto, Yoshiki Higuchi, et al.. (1991). 1H NMR studies on ferricytochromec 3 fromDesulfovibrio vulgaris Miyazaki F and its interaction with ferredoxin I. Journal of Biomolecular NMR. 1(3). 271–282. 19 indexed citations
18.
19.
Morimoto, Y., Toshiki Tani, Hirokazu Okumura, Yoshiki Higuchi, & Noritake Yasuoka. (1991). Effects of Amino Acid Substitution on Three-Dimensional Structure: An X-Ray Analysis of Cytochrome c3, from Desulfovibrio vulgaris Hildenborough at 2 Å Resolution1. The Journal of Biochemistry. 110(4). 532–540. 56 indexed citations
20.
Takeda, Kazuo, et al.. (1986). Effect of iodination on the purple membrane structure. Photobiochemistry and photobiophysics.. 13(1-2). 187–196. 1 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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