Yuji Kado

571 total citations
23 papers, 460 citations indexed

About

Yuji Kado is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Biotechnology. According to data from OpenAlex, Yuji Kado has authored 23 papers receiving a total of 460 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 4 papers in Radiology, Nuclear Medicine and Imaging and 4 papers in Biotechnology. Recurrent topics in Yuji Kado's work include Glycosylation and Glycoproteins Research (4 papers), Monoclonal and Polyclonal Antibodies Research (4 papers) and Enzyme Production and Characterization (4 papers). Yuji Kado is often cited by papers focused on Glycosylation and Glycoproteins Research (4 papers), Monoclonal and Polyclonal Antibodies Research (4 papers) and Enzyme Production and Characterization (4 papers). Yuji Kado collaborates with scholars based in Japan, United States and South Korea. Yuji Kado's co-authors include Tsuyoshi Inoue, Kazuhiko Ishikawa, Kosuke Aritake, Yoshihiro Urade, Masashi Miyano, Dmitry Kuklev, M. Wada, William L. Smith, Ranjinder S. Sidhu and Chong Yuan and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

Yuji Kado

20 papers receiving 447 citations

Peers

Yuji Kado

PHARM

BIOTE

BIOCH

RNMI

Uwe Knüpfer Germany

Gilles Cauet France

Jennifer L. Walker United States

Taiki Nishioka Japan

Dorothy L. Sentz United States

Ryszard Szyszka Poland

Alexander S. McColl United States

Takashi Tojo Japan

A. Ferretti Italy

Emily Golden Australia

Uwe Knüpfer Germany

Yuji Kado

399 ×1.5

108 ×0.9

PHARM

47 ×0.8

BIOTE

16 ×0.3

BIOCH

162 ×3.3

RNMI

Citations per year, relative to Yuji Kado Yuji Kado (= 1×) peers Uwe Knüpfer

Countries citing papers authored by Yuji Kado

Since Specialization

Citations

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

Fields of papers citing papers by Yuji Kado

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yuji Kado

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

All Works

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20 of 20 papers shown

Yuasa, Akira, Hikaru Matsuda, Yoshitaka Fujii, et al.. (2024). EE180 Cost-effectiveness Analysis of Nirmatrelvir/Ritonavir Compared With Molnupiravir in Patients at High Risk for Progression to Severe COVID-19 in Japan. Value in Health. 27(12). S89–S89. 1 indexed citations

Yamashita, Takefumi, Eiichi Mizohata, Satoru Nagatoishi, et al.. (2018). Affinity Improvement of a Cancer-Targeted Antibody through Alanine-Induced Adjustment of Antigen-Antibody Interface. Structure. 27(3). 519–527.e5. 31 indexed citations

Inoue, Masaki, Haruhiko Kamada, Yohei Mukai, et al.. (2017). A trimeric structural fusion of an antagonistic tumor necrosis factor-α mutant enhances molecular stability and enables facile modification. Journal of Biological Chemistry. 292(16). 6438–6451. 13 indexed citations

Okano, Hiroyuki, Clement Angkawidjaja, Masato Akutsu, et al.. (2017). Structural Basis for the Serratia marcescens Lipase Secretion System: Crystal Structures of the Membrane Fusion Protein and Nucleotide-Binding Domain. Biochemistry. 56(47). 6281–6291. 9 indexed citations

Fukuda, Yohta, et al.. (2015). Insights into unknown foreign ligand in copper nitrite reductase. Biochemical and Biophysical Research Communications. 464(2). 622–628. 8 indexed citations

Kado, Yuji, Eiichi Mizohata, Satoru Nagatoishi, et al.. (2015). Epiregulin Recognition Mechanisms by Anti-epiregulin Antibody 9E5. Journal of Biological Chemistry. 291(5). 2319–2330. 14 indexed citations

Nakayama, Taisuke, Eiichi Mizohata, Takefumi Yamashita, et al.. (2014). Structural features of interfacial tyrosine residue in ROBO1 fibronectin domain‐antibody complex: Crystallographic, thermodynamic, and molecular dynamic analyses. Protein Science. 24(3). 328–340. 18 indexed citations

Mine, Shouhei, Yuji Kado, Masahiro Watanabe, et al.. (2014). The structure of hyperthermophilic β‐N‐acetylglucosaminidase reveals a novel dimer architecture associated with the active site. FEBS Journal. 281(22). 5092–5103. 3 indexed citations

Kado, Yuji, Eiichi Mizohata, Tsuyoshi Inoue, et al.. (2013). Construction and characterization of functional anti-epiregulin humanized monoclonal antibodies. Biochemical and Biophysical Research Communications. 441(4). 1011–1017. 11 indexed citations

10.

Kado, Yuji, Kosuke Aritake, Nobuko Uodome, et al.. (2012). Human hematopoietic prostaglandin D synthase inhibitor complex structures. The Journal of Biochemistry. 151(4). 447–455. 7 indexed citations

11.

Kado, Yuji, Tsuyoshi Inoue, & Kazuhiko Ishikawa. (2011). Structure of hyperthermophilic β-glucosidase from Pyrococcus furiosus. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(12). 1473–1479. 36 indexed citations

12.

Tsuji, Hiroaki, Shigenori Nishimura, Takashi Inui, et al.. (2010). Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site. FEBS Journal. 277(12). 2683–2695. 9 indexed citations

13.

Nakamura, T., Yuji Kado, Takafumi N. Yamaguchi, et al.. (2009). Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed with its substrate, hydrogen peroxide. The Journal of Biochemistry. 147(1). 109–115. 51 indexed citations

14.

Yuan, Chong, Ranjinder S. Sidhu, Dmitry Kuklev, et al.. (2009). Cyclooxygenase Allosterism, Fatty Acid-mediated Cross-talk between Monomers of Cyclooxygenase Homodimers. Journal of Biological Chemistry. 284(15). 10046–10055. 108 indexed citations

15.

Aritake, Kosuke, Yuji Kado, Tsuyoshi Inoue, Masashi Miyano, & Yoshihiro Urade. (2006). Structural and Functional Characterization of HQL-79, an Orally Selective Inhibitor of Human Hematopoietic Prostaglandin D Synthase. Journal of Biological Chemistry. 281(22). 15277–15286. 86 indexed citations

16.

Morimoto, Tetsuo, et al.. (1987). Clinical study of patients with fatty liver diagnosed by computed tomography.. JOURNAL OF THE JAPANESE ASSOCIATION OF RURAL MEDICINE. 36(4). 928–932. 1 indexed citations

17.

Ogino, Keiki, Isao Sakaida, Keisuke Hino, et al.. (1986). Immunohistochemical study of glutathione S-transferase (GST-.PI.) on hepatocellular carcinoma.. Kanzo. 27(10). 1439–1443.

18.

Murata, Makoto, et al.. (1985). Two cases of acute liver injury caused by ingesting small dose of acetoaminophen.. Kanzo. 26(4). 493–499. 3 indexed citations

19.

Takashima, Tsuyoshi, et al.. (1972). Pharmacological investigations of benzothiazoline derivatives.. PubMed. 22(4). 711–5. 13 indexed citations

20.

Yoshida, Tomoharu, Nobuhiro Sakaki, Yuji Kado, et al.. (1960). [Trial biological and clinical study of achlorhydria].. PubMed. 23. 775–802. 2 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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