Keizo Yuasa

2.1k total citations
58 papers, 1.6k citations indexed

About

Keizo Yuasa is a scholar working on Molecular Biology, Pharmacology and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, Keizo Yuasa has authored 58 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 44 papers in Molecular Biology, 13 papers in Pharmacology and 11 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in Keizo Yuasa's work include Phosphodiesterase function and regulation (15 papers), Cholinesterase and Neurodegenerative Diseases (9 papers) and Receptor Mechanisms and Signaling (8 papers). Keizo Yuasa is often cited by papers focused on Phosphodiesterase function and regulation (15 papers), Cholinesterase and Neurodegenerative Diseases (9 papers) and Receptor Mechanisms and Signaling (8 papers). Keizo Yuasa collaborates with scholars based in Japan, United States and Germany. Keizo Yuasa's co-authors include Kenji Omori, Jun Kotera, Kotomi Fujishige, Hideo Michibata, Akihiko Tsuji, Katsuzumi Okumura, Takashi Sasaki, Shin‐ichiro Takebayashi, Noriyuki Yanaka and Masami Nagahama and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Scientific Reports.

In The Last Decade

Keizo Yuasa

57 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Keizo Yuasa Japan 21 1.3k 422 216 177 165 58 1.6k
B Thiele Germany 21 1.3k 1.1× 176 0.4× 134 0.6× 197 1.1× 105 0.6× 57 2.0k
Young‐Kook Kim South Korea 23 851 0.7× 82 0.2× 80 0.4× 114 0.6× 95 0.6× 69 1.4k
Fabio Cattaneo Italy 26 906 0.7× 120 0.3× 75 0.3× 154 0.9× 168 1.0× 49 1.5k
Carsten Andersen United States 19 791 0.6× 113 0.3× 40 0.2× 114 0.6× 62 0.4× 25 1.4k
Tsui‐Ting Ching United States 18 822 0.6× 427 1.0× 15 0.1× 185 1.0× 139 0.8× 30 1.7k
Yong‐Sung Juhnn South Korea 25 967 0.8× 133 0.3× 32 0.1× 96 0.5× 311 1.9× 68 1.6k
Anna Markowska Poland 22 927 0.7× 54 0.1× 96 0.4× 197 1.1× 297 1.8× 146 2.0k
Alexander R. Moise United States 32 2.2k 1.7× 49 0.1× 75 0.3× 156 0.9× 139 0.8× 52 2.9k
Mari K. Haddox United States 23 980 0.8× 177 0.4× 62 0.3× 116 0.7× 77 0.5× 43 1.5k
Yung-Jin Kim South Korea 18 828 0.7× 82 0.2× 55 0.3× 157 0.9× 203 1.2× 44 1.6k

Countries citing papers authored by Keizo Yuasa

Since Specialization
Citations

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

Fields of papers citing papers by Keizo Yuasa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Keizo Yuasa

This figure shows the co-authorship network connecting the top 25 collaborators of Keizo Yuasa. A scholar is included among the top collaborators of Keizo Yuasa 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 Keizo Yuasa. Keizo Yuasa 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.
Ye, Yuxin, Hang Wang, Koji Kato, et al.. (2023). Structural basis of EHEP-mediated offense against phlorotannin-induced defense from brown algae to protect akuBGL activity. eLife. 12. 1 indexed citations
2.
Miyamoto, K., et al.. (2021). Natriuretic peptide receptor-C releases and activates guanine nucleotide-exchange factor H1 in a ligand-dependent manner. Biochemical and Biophysical Research Communications. 552. 9–16. 5 indexed citations
3.
4.
Tsuji, Akihiko & Keizo Yuasa. (2019). Identification and enzymatic characterization of clip domain serine protease in the digestive fluid of the sea hare, Aplysia kurodai. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 237. 110322–110322. 1 indexed citations
5.
Tsuji, Akihiko, et al.. (2018). Intracellular localization and binding partners of death associated protein kinase-related apoptosis-inducing protein kinase 1. Biochemical and Biophysical Research Communications. 496(4). 1222–1228. 8 indexed citations
6.
Kawamoto, Kohei, et al.. (2017). PCTK3/CDK18 regulates cell migration and adhesion by negatively modulating FAK activity. Scientific Reports. 7(1). 45545–45545. 28 indexed citations
7.
Takeda, Maki, Keisuke Oyama, Norio Kamemura, et al.. (2017). Change in plasma membrane potential of rat thymocytes by tert-butylhydroquinone, a food additive: Possible risk on lymphocytes. Food and Chemical Toxicology. 109(Pt 1). 296–301. 8 indexed citations
8.
Yuasa, Keizo, et al.. (2015). Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins. Biochemical and Biophysical Research Communications. 464(1). 70–75. 19 indexed citations
9.
Ishida, Yoichi, et al.. (2015). NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and is involved in pre-rRNA processing. Biochemical and Biophysical Research Communications. 464(3). 780–786. 23 indexed citations
10.
Reger, Albert S., Shrenik Mehta, Keizo Yuasa, et al.. (2014). Crystal Structure of the cGMP-dependent Protein Kinase II Leucine Zipper and Rab11b Protein Complex Reveals Molecular Details of G-kinase-specific Interactions. Journal of Biological Chemistry. 289(37). 25393–25403. 17 indexed citations
11.
Kim, Hye-Jin, Atsushi Tabata, Toshifumi Tomoyasu, et al.. (2014). Estrogen stimuli promote osteoblastic differentiation via the subtilisin-like proprotein convertase PACE4 in MC3T3-E1 cells. Journal of Bone and Mineral Metabolism. 33(1). 30–39. 17 indexed citations
12.
Miyamoto, K., et al.. (2014). PCTAIRE Kinase 3/Cyclin-dependent Kinase 18 Is Activated through Association with Cyclin A and/or Phosphorylation by Protein Kinase A. Journal of Biological Chemistry. 289(26). 18387–18400. 24 indexed citations
13.
14.
Tsuji, Akihiko, et al.. (2012). Purification and characterization of cellulase from North Pacific krill (Euphausia pacifica). Analysis of cleavage specificity of the enzyme. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 163(3-4). 324–333. 14 indexed citations
15.
Yuasa, Keizo, et al.. (2012). Sudachitin, a Polymethoxyflavone fromCitrus sudachi, Suppresses Lipopolysaccharide-Induced Inflammatory Responses in Mouse Macrophage-Like RAW264 Cells. Bioscience Biotechnology and Biochemistry. 76(3). 598–600. 34 indexed citations
16.
Yuasa, Keizo, et al.. (2009). Transcriptional regulation of fibrillin‐2 gene by E2F family members in chondrocyte differentiation. Journal of Cellular Biochemistry. 106(4). 580–588. 7 indexed citations
17.
Tsuji, Akihiko, et al.. (2008). Purification and characterization of cathepsin B‐like cysteine protease from cotyledons of daikon radish, Raphanus sativus. FEBS Journal. 275(21). 5429–5443. 13 indexed citations
18.
19.
Sasaki, Takashi, et al.. (2003). Molecular comparison of rat cyclic nucleotide phosphodiesterase 8 family: unique expression of PDE8B in rat brain. Gene. 319. 21–31. 35 indexed citations
20.
Yuasa, Keizo, Jun Kotera, Kotomi Fujishige, et al.. (2000). Isolation and Characterization of Two Novel Phosphodiesterase PDE11A Variants Showing Unique Structure and Tissue-specific Expression. Journal of Biological Chemistry. 275(40). 31469–31479. 118 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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