Kunio Yamane

2.6k total citations
92 papers, 2.1k citations indexed

About

Kunio Yamane is a scholar working on Molecular Biology, Genetics and Ecology. According to data from OpenAlex, Kunio Yamane has authored 92 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 52 papers in Genetics and 36 papers in Ecology. Recurrent topics in Kunio Yamane's work include Bacterial Genetics and Biotechnology (48 papers), Bacteriophages and microbial interactions (36 papers) and Enzyme Production and Characterization (36 papers). Kunio Yamane is often cited by papers focused on Bacterial Genetics and Biotechnology (48 papers), Bacteriophages and microbial interactions (36 papers) and Enzyme Production and Characterization (36 papers). Kunio Yamane collaborates with scholars based in Japan, United States and France. Kunio Yamane's co-authors include K. Nakamura, Keigo Bunai, Hiromu Takamatsu, Junichi Sekiguchi, Akira Nakamura, Hiroshi Kakeshita, Keiko Haga, Miyuki Kumano, Bunji Maruo and Shu Ishikawa and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Kunio Yamane

91 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kunio Yamane Japan 28 1.4k 1.0k 644 615 272 92 2.1k
Ilkka Palva Finland 22 1.3k 0.9× 881 0.9× 521 0.8× 596 1.0× 212 0.8× 41 2.0k
Junichi Sekiguchi Japan 33 1.7k 1.2× 1.2k 1.2× 820 1.3× 612 1.0× 281 1.0× 101 2.9k
Janice Pero United States 28 2.1k 1.5× 1.5k 1.5× 1.1k 1.8× 382 0.6× 384 1.4× 40 2.8k
Fujio Kawamura Japan 33 2.2k 1.5× 1.7k 1.7× 1.3k 2.0× 304 0.5× 378 1.4× 111 3.0k
Roland Freudl Germany 36 2.5k 1.7× 1.8k 1.7× 1.0k 1.6× 438 0.7× 249 0.9× 80 3.3k
Maxime Schwartz France 24 1.8k 1.2× 1.5k 1.5× 672 1.0× 210 0.3× 388 1.4× 40 2.5k
Dimitri Karamata Switzerland 31 2.0k 1.4× 1.8k 1.8× 1.3k 2.0× 368 0.6× 407 1.5× 74 2.9k
John B. Perkins United States 22 1.7k 1.1× 1.2k 1.2× 947 1.5× 149 0.2× 244 0.9× 35 2.4k
Ahmed T. Abdelal United States 25 1.1k 0.8× 432 0.4× 219 0.3× 221 0.4× 318 1.2× 60 1.7k
Sylvie Létoffé France 30 1.6k 1.1× 1.1k 1.1× 295 0.5× 158 0.3× 119 0.4× 45 2.9k

Countries citing papers authored by Kunio Yamane

Since Specialization
Citations

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

Fields of papers citing papers by Kunio Yamane

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kunio Yamane

This figure shows the co-authorship network connecting the top 25 collaborators of Kunio Yamane. A scholar is included among the top collaborators of Kunio Yamane 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 Kunio Yamane. Kunio Yamane 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.
Kodama, Takeko, Keiji Endo, Katsutoshi Ara, et al.. (2007). Effect of Bacillus subtilis spo0A mutation on cell wall lytic enzymes and extracellular proteases, and prevention of cell lysis. Journal of Bioscience and Bioengineering. 103(1). 13–21. 41 indexed citations
2.
Ara, Katsutoshi, Katsuya Ozaki, K. Nakamura, et al.. (2007). Bacillus minimum genome factory: effective utilization of microbial genome information. Biotechnology and Applied Biochemistry. 46(3). 169–178. 96 indexed citations
3.
Kanai, R., Keiko Haga, T. Akiba, Kunio Yamane, & Kazuaki Harata. (2006). Role of Trp140 at subsite −6 on the maltohexaose production of maltohexaose‐producing amylase from alkalophilic Bacillus sp.707. Protein Science. 15(3). 468–477. 7 indexed citations
4.
Bunai, Keigo & Kunio Yamane. (2004). Effectiveness and limitation of two-dimensional gel electrophoresis in bacterial membrane protein proteomics and perspectives. Journal of Chromatography B. 815(1-2). 227–236. 84 indexed citations
5.
6.
Yamane, Kunio, et al.. (2002). Identification and characterization of theBacillus subtilisd-glucarate/galactarate utilization operonycbCDEFGHJ. FEMS Microbiology Letters. 210(2). 193–199. 10 indexed citations
7.
Nakamura, K., et al.. (2001). Minimal Functional Structure of Escherichia coli 4.5 S RNA Required for Binding to Elongation Factor G. Journal of Biological Chemistry. 276(25). 22844–22849. 15 indexed citations
8.
Ishii, Noriyuki, Keiko Haga, Kunio Yamane, & Kazuaki Harata. (2000). Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 determined at 1.9?? resolution. Journal of Molecular Recognition. 13(1). 35–43. 8 indexed citations
9.
Hayashi, Kenji, et al.. (1999). Analysis ofEscherichia coli4.5S RNA binding affinity to Ffh and EF-G. FEMS Microbiology Letters. 180(2). 271–277. 12 indexed citations
10.
Nakamura, K., et al.. (1999). Bacillus subtilis Histone-like Protein, HBsu, Is an Integral Component of a SRP-like Particle That Can Bind theAlu Domain of Small Cytoplasmic RNA. Journal of Biological Chemistry. 274(19). 13569–13576. 71 indexed citations
11.
Tjalsma, Harold, Michiel Noback, Sierd Bron, et al.. (1997). Bacillus subtilis Contains Four Closely Related Type I Signal Peptidases with Overlapping Substrate Specificities. Journal of Biological Chemistry. 272(41). 25983–25992. 104 indexed citations
12.
Oguro, Akihiro, Hiroshi Kakeshita, Hiromu Takamatsu, K. Nakamura, & Kunio Yamane. (1996). The effect of Srb, a homologue of the mammalian SRP receptor α-subunit, on Bacillus subtilis growth and protein translocation. Gene. 172(1). 17–24. 32 indexed citations
13.
Kurita, Kei, et al.. (1996). Identification of a Region of Bacillus subtilis Ffh, a Homologue of Mammalian SRP54 Protein, That Is Essential for Binding to Small Cytoplasmic RNA. Journal of Biological Chemistry. 271(22). 13140–13146. 30 indexed citations
14.
Takamatsu, Hiromu, et al.. (1994). The Rapid Degradation of Mutant Sec A Protein in theBacillus subtilis secA341(ts) Mutant Causes a Protein Translocation Defect in the Cell. Bioscience Biotechnology and Biochemistry. 58(10). 1845–1850. 9 indexed citations
15.
Nakamura, Akira, Keiko Haga, & Kunio Yamane. (1994). The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping‐Pong mechanism. FEBS Letters. 337(1). 66–70. 71 indexed citations
16.
Honda, Kiyofumi, et al.. (1993). Extracellular production of human hepatitis B virus preS2 antigen as hybrid proteins with Bacillus subtilis ?-amylases in high-salt-concentration media. Applied Microbiology and Biotechnology. 40(2-3). 341–7. 3 indexed citations
17.
Takano, Toshiya, Akira Miyauchi, Hiroaki Takagi, et al.. (1992). Expression of the Cyclodextrin Glucanotransferase Gene ofBacillus maceransinBacillus brevis. Bioscience Biotechnology and Biochemistry. 56(5). 808–809. 5 indexed citations
18.
Nakamura, K., et al.. (1990). Processing of an NH2-Terminally Extended Thermostable α-Amylase by Bacillus subtilis Alkaline Protease1. The Journal of Biochemistry. 108(6). 954–959. 2 indexed citations
19.
Tsukamoto, Akira, et al.. (1988). Nucleotide sequence of the maltohexaose-producing amylase gene from an alkalophilic sp. #707 and structural similarity to liquefying type α-amylases. Biochemical and Biophysical Research Communications. 151(1). 25–31. 27 indexed citations
20.
Nakamura, K., et al.. (1988). Enhanced Secretion of β-Lactamase on Structural Modification of the Bacillus subtilis α-Amylase Signal Peptide1. The Journal of Biochemistry. 104(2). 265–269. 5 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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