Kiyoshi Yasukawa

12.5k total citations · 6 hit papers
209 papers, 10.6k citations indexed

About

Kiyoshi Yasukawa is a scholar working on Molecular Biology, Oncology and Immunology. According to data from OpenAlex, Kiyoshi Yasukawa has authored 209 papers receiving a total of 10.6k indexed citations (citations by other indexed papers that have themselves been cited), including 120 papers in Molecular Biology, 56 papers in Oncology and 38 papers in Immunology. Recurrent topics in Kiyoshi Yasukawa's work include Cytokine Signaling Pathways and Interactions (41 papers), Monoclonal and Polyclonal Antibodies Research (25 papers) and Enzyme Production and Characterization (20 papers). Kiyoshi Yasukawa is often cited by papers focused on Cytokine Signaling Pathways and Interactions (41 papers), Monoclonal and Polyclonal Antibodies Research (25 papers) and Enzyme Production and Characterization (20 papers). Kiyoshi Yasukawa collaborates with scholars based in Japan, United States and France. Kiyoshi Yasukawa's co-authors include Tetsuya Taga, Tadamitsu Kishimoto, Koichi Nakajima, Shin‐ichiro Kashiwamura, Masahiko Hibi, Masaaki Murakami, Susumu Tsunasawa, Fumio Sakiyama, Kuniyo Inouye and Toshio Hirano and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Kiyoshi Yasukawa

205 papers receiving 10.3k citations

Hit Papers

Complementary DNA for a novel human interleukin (BSF-2) t... 1985 2026 1998 2012 1986 1994 1993 1992 1985 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kiyoshi Yasukawa Japan 39 4.5k 4.3k 3.8k 1.3k 951 209 10.6k
Koichi Nakajima Japan 46 4.0k 0.9× 3.8k 0.9× 3.6k 1.0× 907 0.7× 1.2k 1.2× 95 9.4k
Massimo Gadina United States 55 4.1k 0.9× 6.4k 1.5× 3.5k 0.9× 1.0k 0.8× 794 0.8× 126 13.2k
Diane Pennica United States 46 3.1k 0.7× 3.7k 0.9× 6.1k 1.6× 884 0.7× 1.7k 1.8× 89 12.4k
Francesco Colotta Italy 52 3.6k 0.8× 6.0k 1.4× 4.0k 1.1× 667 0.5× 1.5k 1.6× 138 12.9k
S J Korsmeyer United States 50 3.5k 0.8× 4.4k 1.0× 9.1k 2.4× 1.4k 1.1× 1.4k 1.5× 74 15.8k
Alfons Billiau Belgium 66 3.3k 0.7× 6.7k 1.5× 3.3k 0.9× 1.0k 0.8× 1.1k 1.2× 267 13.4k
Sofie Struyf Belgium 67 5.5k 1.2× 6.0k 1.4× 4.2k 1.1× 540 0.4× 1.1k 1.1× 207 13.9k
Stephanie S. Watowich United States 52 3.6k 0.8× 9.6k 2.2× 3.5k 0.9× 1.1k 0.8× 1.1k 1.1× 126 14.5k
Lionel Feigenbaum United States 61 4.3k 0.9× 9.0k 2.1× 4.5k 1.2× 445 0.4× 879 0.9× 123 15.1k
Naoto Ishii Japan 51 2.4k 0.5× 7.1k 1.6× 2.3k 0.6× 541 0.4× 648 0.7× 167 10.9k

Countries citing papers authored by Kiyoshi Yasukawa

Since Specialization
Citations

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

Fields of papers citing papers by Kiyoshi Yasukawa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kiyoshi Yasukawa

This figure shows the co-authorship network connecting the top 25 collaborators of Kiyoshi Yasukawa. A scholar is included among the top collaborators of Kiyoshi Yasukawa 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 Kiyoshi Yasukawa. Kiyoshi Yasukawa 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.
Takita, Teisuke, Kazumichi M. Nishida, Masaaki Ito, et al.. (2025). Expression in HEK293 cells, purification, and characterization of recombinant human α-glucosidases. Bioscience Biotechnology and Biochemistry. 89(7). 990–994.
2.
Takita, Teisuke, et al.. (2024). Unveiling the reaction mechanism of arginine decarboxylase in Aspergillus oryzae: Insights from crystal structure analysis. Biochemical and Biophysical Research Communications. 733. 150728–150728. 1 indexed citations
3.
Kuramochi, Masahiro, Hiroto Takahashi, Tomoe Komoriya, et al.. (2024). Adenosine triphosphate induces amorphous aggregation of amyloid β by increasing Aβ dynamics. Scientific Reports. 14(1). 8134–8134. 8 indexed citations
4.
Ikeda, Yuki, Ying Qiao, Masaaki Ito, et al.. (2024). Use of human Caco-2 cells and HPAE-PAD for α-glucosidase assay. Journal of Pharmacological and Toxicological Methods. 127. 107508–107508. 1 indexed citations
5.
Fukuda, Wakao, et al.. (2023). Expression of a recombinant protein by an acetic acid bacterial host. Journal of Biotechnology. 380. 38–50.
6.
Inoue, Eisuke, Kengo Asada, Wakao Fukuda, et al.. (2023). Recombinase polymerase amplification using novel thermostable strand-displacing DNA polymerases from Aeribacillus pallidus and Geobacillus zalihae. Journal of Bioscience and Bioengineering. 135(4). 282–290. 7 indexed citations
7.
Ikeda, Yuki, Ying Qiao, Masaaki Ito, et al.. (2023). Inhibition of α-glucosidase activity by Morus australis fruit food. 23(1). 19–27. 1 indexed citations
8.
Kitagawa, Y., Teisuke Takita, Keisuke Tanaka, et al.. (2023). Insights into the catalytic mechanism of Grimontia hollisae collagenase through structural and mutational analyses. FEBS Letters. 597(19). 2473–2483. 1 indexed citations
9.
Kojima, Kenji K., Teisuke Takita, Kazuki Saito, et al.. (2023). Application of recombinant human pyruvate kinase in recombinase polymerase amplification. Journal of Bioscience and Bioengineering. 136(5). 341–346. 2 indexed citations
10.
Qiao, Ying, Masaaki Ito, Toshiyuki Kimura, et al.. (2020). Kinetic analysis of inhibition of α-glucosidase by leaf powder from Morus australis and its component iminosugars. Bioscience Biotechnology and Biochemistry. 84(10). 2149–2156. 17 indexed citations
11.
Okano, Hiroyuki, et al.. (2016). Expression of moloney murine leukemia virus reverse transcriptase in a cell-free protein expression system. Biotechnology Letters. 38(7). 1203–1211. 7 indexed citations
12.
Konishi, Atsushi, et al.. (2014). Amino acid substitutions away from the RNase H catalytic site increase the thermal stability of Moloney murine leukemia virus reverse transcriptase through RNase H inactivation. Biochemical and Biophysical Research Communications. 454(2). 269–274. 7 indexed citations
13.
Yasukawa, Kiyoshi, et al.. (2011). Thermodynamic analysis of ionizable groups involved in the catalytic mechanism of human matrix metalloproteinase 7 (MMP-7). Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814(12). 1940–1946. 10 indexed citations
14.
Mizuno, Masaki, Kiyoshi Yasukawa, & Kuniyo Inouye. (2010). Insight into the Mechanism of the Stabilization of Moloney Murine Leukaemia Virus Reverse Transcriptase by Eliminating RNase H Activity. Bioscience Biotechnology and Biochemistry. 74(2). 440–442. 25 indexed citations
15.
Yasukawa, Kiyoshi, et al.. (2007). Effects of Site-directed Mutagenesis of the Surface Residues Gln128 and Gln225 of Thermolysin on its Catalytic Activity. The Journal of Biochemistry. 141(6). 835–842. 15 indexed citations
16.
Montero‐Julian, Félix A., Hervé Brailly, I Joyeux, et al.. (1997). Characterization of soluble gp130 released by melanoma cell lines: A polyvalent antagonist of cytokines from the interleukin 6 family.. PubMed. 3(8). 1443–51. 33 indexed citations
17.
Hallek, Michael, Carola A. Neumann, Moshe Schaffer, et al.. (1997). Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines.. PubMed. 25(13). 1367–77. 63 indexed citations
18.
Lu, Zhao‐Yang, Kiyoshi Yasukawa, George D. Yancopoulos, et al.. (1994). Ciliary neurotropic factor, interleukin 11, leukemia inhibitory factor, and oncostatin M are growth factors for human myeloma cell lines using the interleukin 6 signal transducer gp130.. The Journal of Experimental Medicine. 179(4). 1337–1342. 193 indexed citations
19.
Lütticken, Claudia, Ursula Maria Wegenka, Juping Yuan, et al.. (1994). Association of Transcription Factor APRF and Protein Kinase Jak1 with the Interleukin-6 Signal Transducer gp130. Science. 263(5143). 89–92. 695 indexed citations breakdown →
20.
Suzuki, Hiroshi, Kiyoshi Yasukawa, Takashi Saito, et al.. (1992). Anti‐human interleukin‐6 receptor antibody inhibits human myeloma growth in vivo. European Journal of Immunology. 22(8). 1989–1993. 87 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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