Yuichi Hanada

826 total citations
16 papers, 540 citations indexed

About

Yuichi Hanada is a scholar working on Ecology, Molecular Biology and Immunology. According to data from OpenAlex, Yuichi Hanada has authored 16 papers receiving a total of 540 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Ecology, 7 papers in Molecular Biology and 4 papers in Immunology. Recurrent topics in Yuichi Hanada's work include Physiological and biochemical adaptations (6 papers), Polar Research and Ecology (3 papers) and Marine Bivalve and Aquaculture Studies (2 papers). Yuichi Hanada is often cited by papers focused on Physiological and biochemical adaptations (6 papers), Polar Research and Ecology (3 papers) and Marine Bivalve and Aquaculture Studies (2 papers). Yuichi Hanada collaborates with scholars based in Japan and Canada. Yuichi Hanada's co-authors include Sakae Tsuda, Hidemasa Kondo, Kazuhisa Sekimizu, Chikara Kaito, Ai Miura, Tamotsu Hoshino, Yoshiyuki Nishimiya, Peter L. Davies, Yosuke Omae and Hiroshi Sugimoto and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Scientific Reports.

In The Last Decade

Yuichi Hanada

14 papers receiving 533 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Yuichi Hanada Japan	11	247	215	94	93	55	16	540
Qi Lin China	7	156 0.6×	129 0.6×	57 0.6×	42 0.5×	31 0.6×	15	433
Chris Hemmerich United States	12	85 0.3×	206 1.0×	46 0.5×	50 0.5×	43 0.8×	14	440
A Peek United States	7	185 0.7×	331 1.5×	25 0.3×	25 0.3×	103 1.9×	7	707
Sriram G. Garg Germany	18	327 1.3×	879 4.1×	28 0.3×	19 0.2×	140 2.5×	24	1.1k
Michelle M. Leger Canada	10	155 0.6×	403 1.9×	22 0.2×	15 0.2×	39 0.7×	18	536
Christopher P. Stefan United States	11	45 0.2×	218 1.0×	111 1.2×	15 0.2×	34 0.6×	18	497
F. C. Thomas Allnutt United States	17	155 0.6×	229 1.1×	15 0.2×	37 0.4×	25 0.5×	30	742
Vassiliki Lila Koumandou Greece	16	198 0.8×	706 3.3×	18 0.2×	11 0.1×	75 1.4×	29	1.1k
Étienne Kornobis France	14	104 0.4×	253 1.2×	70 0.7×	6 0.1×	74 1.3×	32	502
Patricia O. Wainright United States	8	270 1.1×	526 2.4×	45 0.5×	12 0.1×	57 1.0×	9	838

Countries citing papers authored by Yuichi Hanada

Since Specialization

Citations

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

Fields of papers citing papers by Yuichi Hanada

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yuichi Hanada

This figure shows the co-authorship network connecting the top 25 collaborators of Yuichi Hanada. A scholar is included among the top collaborators of Yuichi Hanada 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 Yuichi Hanada. Yuichi Hanada is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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16 of 16 papers shown

Nakamura, Koji, Yuichi Hanada, Satoshi Kubo, et al.. (2022). Preclinical Characterization of ASP2713, a Novel Igβ and FcγRIIB Cross-Linking Antibody, for Prediction of Human Pharmacokinetics and Clinically Effective Dose. Journal of Pharmaceutical Sciences. 111(9). 2630–2638.

Nakamura, Koji, et al.. (2022). Potential benefit of the cathepsin S inhibitor, ASP1617, as a treatment for systemic lupus erythematosus. European Journal of Pharmacology. 919. 174826–174826. 7 indexed citations

Ito, Masanobu, et al.. (2021). Basidiomycetous Yeast, Glaciozyma antarctica, Forming Frost-Columnar Colonies on Frozen Medium. Microorganisms. 9(8). 1679–1679. 2 indexed citations

Hanada, Yuichi, Yoshiyuki Nishimiya, Ai Miura, et al.. (2017). Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive. Scientific Reports. 7(1). 42501–42501. 39 indexed citations

Fujita, Yuji, et al.. (2016). Translational research in drug discovery — current issues and perspectives. Folia Pharmacologica Japonica. 148(6). 296–301.

Cheng, Jing, Yuichi Hanada, Ai Miura, Sakae Tsuda, & Hidemasa Kondo. (2016). Hydrophobic ice-binding sites confer hyperactivity of an antifreeze protein from a snow mold fungus. Biochemical Journal. 473(21). 4011–4026. 44 indexed citations

Kimura, Satoshi, et al.. (2015). Ribosomal RNA methyltransferases contribute to Staphylococcus aureus virulence. FEBS Journal. 282(13). 2570–2584. 34 indexed citations

Hanada, Yuichi, Yoshiyuki Nishimiya, Ai Miura, Sakae Tsuda, & Hidemasa Kondo. (2014). Hyperactive antifreeze protein from an Antarctic sea ice bacterium Colwellia sp. has a compound ice‐binding site without repetitive sequences. FEBS Journal. 281(16). 3576–3590. 55 indexed citations

Xiao, Nan, et al.. (2013). Annealing condition influences thermal hysteresis of fungal type ice-binding proteins. Cryobiology. 68(1). 159–161. 15 indexed citations

10.

Omae, Yosuke, Yuichi Hanada, Kazuhisa Sekimizu, & Chikara Kaito. (2013). Silkworm Apolipophorin Protein Inhibits Hemolysin Gene Expression of Staphylococcus aureus via Binding to Cell Surface Lipoteichoic Acids. Journal of Biological Chemistry. 288(35). 25542–25550. 25 indexed citations

11.

Tsuji, Masaharu, Nan Xiao, Yuichi Hanada, et al.. (2013). Cold adaptation of fungi obtained from soil and lake sediment in the Skarvsnes ice-free area, Antarctica. FEMS Microbiology Letters. 346(2). 121–130. 55 indexed citations

12.

Hanada, Yuichi, M. Sakashita, Yoshiyuki Nishimiya, et al.. (2013). Dependence of freeze-concentration inhibition on antifreeze protein. Hokkaido University Collection of Scholarly and Academic Papers (Hokkaido University). 71. 91–96. 2 indexed citations

13.

Matsunaga, Naoya, Miki Inoue, Naoki Kusunose, et al.. (2012). Time-Dependent Interaction between Differentiated Embryo Chondrocyte-2 and CCAAT/Enhancer-Binding Protein α Underlies the Circadian Expression of CYP2D6 in Serum-Shocked HepG2 Cells. Molecular Pharmacology. 81(5). 739–747. 29 indexed citations

14.

Kondo, Hidemasa, Yuichi Hanada, Hiroshi Sugimoto, et al.. (2012). Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation. Proceedings of the National Academy of Sciences. 109(24). 9360–9365. 82 indexed citations

15.

Hanada, Yuichi, Kazuhisa Sekimizu, & Chikara Kaito. (2011). Silkworm Apolipophorin Protein Inhibits Staphylococcus aureus Virulence. Journal of Biological Chemistry. 286(45). 39360–39369. 46 indexed citations

16.

Kaito, Chikara, Yuki Saito, Mariko Ikuo, et al.. (2011). Transcription and Translation Products of the Cytolysin Gene psm-mec on the Mobile Genetic Element SCCmec Regulate Staphylococcus aureus Virulence. PLoS Pathogens. 7(2). e1001267–e1001267. 105 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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