Kazuo Yonaha

526 total citations
34 papers, 423 citations indexed

About

Kazuo Yonaha is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, Kazuo Yonaha has authored 34 papers receiving a total of 423 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 18 papers in Biochemistry and 9 papers in Materials Chemistry. Recurrent topics in Kazuo Yonaha's work include Amino Acid Enzymes and Metabolism (18 papers), Enzyme Structure and Function (9 papers) and Biopolymer Synthesis and Applications (7 papers). Kazuo Yonaha is often cited by papers focused on Amino Acid Enzymes and Metabolism (18 papers), Enzyme Structure and Function (9 papers) and Biopolymer Synthesis and Applications (7 papers). Kazuo Yonaha collaborates with scholars based in Japan, Spain and Czechia. Kazuo Yonaha's co-authors include Seizen Toyama, Kenji Soda, Masatoshi Nozaki, Koji Suzuki, Takao Kamura, Haruo Misono, Shigeo Aibara, Yuhei Morita, Masaaki Yasuda and Nobuhisa Watanabe and has published in prestigious journals such as Nucleic Acids Research, Journal of Molecular Biology and Analytical Biochemistry.

In The Last Decade

Kazuo Yonaha

32 papers receiving 375 citations

Peers

Kazuo Yonaha

GENET

BIOCH

Roman H. Szczepanowski Poland

Mark Lunzer United States

Maria Cartenı́-Farina Italy

E.A. Pratt United States

Karina Kitzing Switzerland

Ian A. Anton United Kingdom

José Sy United States

David H. Dyer United States

J.A. Littlechild United Kingdom

V Horn United States

Roman H. Szczepanowski Poland

Kazuo Yonaha

609 ×2.3

142 ×1.0

GENET

70 ×0.5

BIOCH

99 ×0.8

23 ×0.5

Citations per year, relative to Kazuo Yonaha Kazuo Yonaha (= 1×) peers Roman H. Szczepanowski

Countries citing papers authored by Kazuo Yonaha

Since Specialization

Citations

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

Fields of papers citing papers by Kazuo Yonaha

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kazuo Yonaha

This figure shows the co-authorship network connecting the top 25 collaborators of Kazuo Yonaha. A scholar is included among the top collaborators of Kazuo Yonaha 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 Kazuo Yonaha. Kazuo Yonaha 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

Yonaha, Kazuo & Kenji Soda. (2005). Applications of stereoselectivity of enzymes: Synthesis of optically active amino acids and α-hydroxy acids, and stereospecific isotope-labeling of amino acids, amines and coenzymes. Advances in biochemical engineering, biotechnology. 33. 95–130. 3 indexed citations

Iha, Masahiko, et al.. (1995). The primary structure of a hemorrhagic factor, HR2b, from the venom of Okinawa habu ({iTrimeresurus flavoviridis}). Toxicon. 33(2). 229–239. 9 indexed citations

Yonaha, Kazuo, et al.. (1995). Isolation of peptides homologous to domains of human α 1B-glycoprotein from a mongoose antihemorrhagic factor. Toxicon. 33(2). 241–245. 20 indexed citations

Jhee, Kwang-Hwan, et al.. (1995). Thermostable Ornithine Aminotransferase from Bacillus sp. YM-2: Purification and Characterization. The Journal of Biochemistry. 118(1). 101–108. 6 indexed citations

Yonaha, Kazuo, et al.. (1994). Characterization of the antihemorrhagic factors of mongoose (Herpestes edwardsii). Toxicon. 32(11). 1459–1469. 19 indexed citations

Yonaha, Kazuo, et al.. (1991). Characterization of three hemorrhagic factors from the venom of Okinawa habu (Trimeresurus flavoviridis). Toxicon. 29(6). 703–711. 11 indexed citations

Yonaha, Kazuo, et al.. (1990). Neutralization of hemorrhagic snake venoms by sera of Trimeresurus flavoviridis (Habu), Herpestes edwardsii (mongoose) and Dinodon semicarinatus (Akamata). Toxicon. 28(8). 989–991. 17 indexed citations

Esaki, Nobuyoshi, et al.. (1990). Preparation of stereoselectively-deuterated NADH and NADPH by coupling of glutamate racemase and glutamate dehydrogenase. Biotechnology Letters. 12(2). 105–110. 2 indexed citations

Watanabe, Nobuhisa, K. Sakabe, N. Sakabe, et al.. (1989). Crystal Structure Analysis of ω-Amino Acid: Pyruvate Aminotransferase with a Newly Developed Weissenberg Camera and an Imaging Plate Using Synchrotron Radiation1. The Journal of Biochemistry. 105(1). 1–3. 54 indexed citations

10.

Kita, Keiko, Hirokazu Kotani, Nobutsugu Hiraoka, Teruya Nakamura, & Kazuo Yonaha. (1989). Overproduction and crystallization ofFokI restriction endonuclease. Nucleic Acids Research. 17(21). 8741–8753. 12 indexed citations

11.

Yonaha, Kazuo, et al.. (1988). Purification and crystallization of hemorrhagic factor, HR2b, from the venom of Trimeresurus flavoviridis (habu). Toxicon. 26(12). 1205–1208. 5 indexed citations

12.

Yonaha, Kazuo, et al.. (1988). Purification of an antihemorrhagic factor from the serum of the non-venomous snake Dinodon semicarinatus. Toxicon. 26(4). 420–423. 27 indexed citations

13.

Yonaha, Kazuo, Seizen Toyama, & Kenji Soda. (1987). ω-Amino acid-pyruvate aminotransferase. Methods in enzymology on CD-ROM/Methods in enzymology. 143. 500–504. 10 indexed citations

14.

Yonaha, Kazuo, Seizen Toyama, & Kenji Soda. (1985). [20] Taurine-glutamate transaminase. Methods in enzymology on CD-ROM/Methods in enzymology. 113. 102–108. 7 indexed citations

15.

Yonaha, Kazuo, S. D. Elliott, & Teh‐Yung Liu. (1982). Primary structure of zymogen of streptococcal proteinase. Journal of Protein Chemistry. 1(4). 317–334. 13 indexed citations

16.

Yonaha, Kazuo & Seizen Toyama. (1980). Enzymatic determination of l-alanine with ω-amino acid:pyruvate aminotransferase. Analytical Biochemistry. 101(2). 504–506. 2 indexed citations

17.

Yonaha, Kazuo & Seizen Toyama. (1979). Diamine transamination catalyzed by .OMEGA.-amino acid: pyruvate aminotransferase of Pseudomonassp. F-126.. Agricultural and Biological Chemistry. 43(5). 1043–1048. 4 indexed citations

18.

Morita, Yuhei, Shigeo Aibara, Kazuo Yonaha, Seizen Toyama, & Kenji Soda. (1979). Preliminary crystallographic study of ω-amino acid: Pyruvate aminotransferase from Pseudomonas sp. F-126. Journal of Molecular Biology. 130(2). 211–213. 6 indexed citations

19.

Yonaha, Kazuo, Seizen Toyama, Masaaki Yasuda, & Kenji Soda. (1977). Properties of Crystalline ω-Amino Acid : Pyruvate Aminotransferase ofPseudomonassp. F–126. Agricultural and Biological Chemistry. 41(9). 1701–1706. 1 indexed citations

20.

Yonaha, Kazuo, et al.. (1975). Occurrence of Kynurenine Aminotransferase in Extracts of Yeasts. Kyoto University Research Information Repository (Kyoto University). 53(3). 315–318. 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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