K. Izui

1.0k total citations
26 papers, 815 citations indexed

About

K. Izui is a scholar working on Molecular Biology, Cell Biology and Plant Science. According to data from OpenAlex, K. Izui has authored 26 papers receiving a total of 815 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 8 papers in Cell Biology and 6 papers in Plant Science. Recurrent topics in K. Izui's work include Photosynthetic Processes and Mechanisms (8 papers), Mitochondrial Function and Pathology (7 papers) and Biotin and Related Studies (7 papers). K. Izui is often cited by papers focused on Photosynthetic Processes and Mechanisms (8 papers), Mitochondrial Function and Pathology (7 papers) and Biotin and Related Studies (7 papers). K. Izui collaborates with scholars based in Japan, United States and India. K. Izui's co-authors include Shuichi Yanagisawa, Shingo Hata, Takeshi Kawamura, Hiroshi Kouchi, Hidehiro Toh, Jennifer Nielsen, J. O. Lampen, Hiroyuki Katsuki, Natsumi Kanzaki and Kazuyoshi Futai and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

K. Izui

25 papers receiving 766 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
K. Izui Japan 17 507 394 128 89 67 26 815
Bénédicte Purnelle Belgium 13 816 1.6× 331 0.8× 56 0.4× 36 0.4× 86 1.3× 25 1.0k
Karen Broglie United States 15 748 1.5× 717 1.8× 92 0.7× 61 0.7× 31 0.5× 21 1.2k
F. Van Vliet Belgium 12 554 1.1× 438 1.1× 34 0.3× 64 0.7× 99 1.5× 16 765
Robyn van Heeswijck Australia 11 396 0.8× 261 0.7× 51 0.4× 32 0.4× 28 0.4× 17 591
Annamaria Merico Italy 14 789 1.6× 298 0.8× 35 0.3× 21 0.2× 66 1.0× 19 1.1k
Johan A. van den Berg Netherlands 16 1.1k 2.1× 271 0.7× 69 0.5× 49 0.6× 49 0.7× 23 1.2k
Ryuji Tsugeki Japan 16 942 1.9× 841 2.1× 21 0.2× 68 0.8× 30 0.4× 22 1.2k
Chantal Vergnolle France 16 769 1.5× 703 1.8× 100 0.8× 252 2.8× 26 0.4× 22 1.1k
Frank P. Wolter Germany 14 761 1.5× 418 1.1× 24 0.2× 418 4.7× 80 1.2× 23 976
Benoît Lefebvre France 22 610 1.2× 1.3k 3.3× 109 0.9× 47 0.5× 31 0.5× 40 1.6k

Countries citing papers authored by K. Izui

Since Specialization
Citations

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

Fields of papers citing papers by K. Izui

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K. Izui

This figure shows the co-authorship network connecting the top 25 collaborators of K. Izui. A scholar is included among the top collaborators of K. Izui 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 K. Izui. K. Izui 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.
Banba, Mari, Yoshikazu Shimoda, Svetlana A. Chechetka, et al.. (2007). Transcriptome Profiling of Lotus japonicus Roots During Arbuscular Mycorrhiza Development and Comparison with that of Nodulation. DNA Research. 14(3). 117–133. 52 indexed citations
3.
Nakagawa, Tomomi, Takane Katayama, T Sugimoto, et al.. (2003). Regulatory regions and nuclear factors involved in nodule-enhanced expression of a soybean phosphoenolpyruvate carboxylase gene: implications for molecular evolution. Molecular Genetics and Genomics. 269(2). 163–172. 14 indexed citations
4.
Takabatake, Reona, et al.. (2001). Characterization of a Saccharomyces cerevisiae Gene That Encodes a Mitochondrial Phosphate Transporter--Like Protein. The Journal of Biochemistry. 129(5). 827–833. 21 indexed citations
5.
Banba, Mari, et al.. (2001). Lotus japonicus Forms Early Senescent Root Nodules with Rhizobium etli. Molecular Plant-Microbe Interactions. 14(2). 173–180. 53 indexed citations
6.
Izui, K., et al.. (2000). Illumination Increases the Affinity of Phosphoenolpyruvate Carboxylase to Bicarbonate in Leaves of a C4 Plant, Amaranthus hypochondriacus. Plant and Cell Physiology. 41(8). 905–910. 19 indexed citations
7.
Kanzaki, Natsumi, et al.. (1998). PCR-RFLP and sequencing analysis of ribosomal DNA of Bursaphelenchus nematodes related to pine wilt disease. Fundamental & applied nematology. 21(6). 655–666. 76 indexed citations
8.
Masuda, Tetsuya, et al.. (1998). Cloning, Expression, and Characterization of a Root-Form Phosphoenolpyruvate Carboxylase from Zea mays: Comparison with the C4-Form Enzyme. Plant and Cell Physiology. 39(8). 865–873. 68 indexed citations
9.
Ogawa, Nanayo, et al.. (1998). Characterization of a Maize Ca2+-Dependent Protein Kinase Phosphorylating Phosphoenolpyruvate Carboxylase. Plant and Cell Physiology. 39(10). 1010–1019. 26 indexed citations
10.
Hata, Shingo, et al.. (1997). cDNA Cloning of Squalene Synthase Genes from Mono- and Dicotyledonous Plants, and Expression of the Gene in Rice. Plant and Cell Physiology. 38(12). 1409–1413. 32 indexed citations
11.
Hata, Shingo, et al.. (1997). Effects of Site-directed Mutagenesis of Conserved Lys606 Residue on Catalytic and Regulatory Functions of Maize C4-form Phosphoenolpyruvate Carboxylase. Plant and Cell Physiology. 38(12). 1340–1345. 10 indexed citations
13.
Nakamura, T., Shigeru Minoguchi, & K. Izui. (1996). Purification and Characterization of Recombinant Phosphoenolpyruvate Carboxylase of Thermus sp.. The Journal of Biochemistry. 120(3). 518–524. 9 indexed citations
14.
Toh, Hidehiro, Takeshi Kawamura, & K. Izui. (1994). Molecular evolution of phosphoeno/pyruvate carboxylase. Plant Cell & Environment. 17(1). 31–43. 58 indexed citations
16.
Chang, Chung Nan, Jennifer Nielsen, K. Izui, Günter Blobel, & J. O. Lampen. (1982). Identification of the signal peptidase cleavage site in Bacillus licheniformis prepenicillinase.. Journal of Biological Chemistry. 257(8). 4340–4344. 34 indexed citations
17.
Lampen, J. O., Jennifer Nielsen, K. Izui, & Michael P. Caulfield. (1980). Bacillus licheniformis β-lactamases: multiple forms and their roles. Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 289(1036). 345–348. 8 indexed citations
18.
Izui, K.. (1980). [Mechanism of enzyme secretion in bacteria. Studies on penicillinase of Bacillus licheniformis and alkaline phosphatase of Escherichia coli (author's transl)].. PubMed. 52(5). 285–304. 1 indexed citations
19.
Izui, K., Jennifer Nielsen, Michael P. Caulfield, & J. O. Lampen. (1980). Large exopenicillinase, initial extracellular form detected in cultures of Bacillus licheniformis. Biochemistry. 19(9). 1882–1886. 41 indexed citations
20.
Izui, K., et al.. (1967). Regulation of phosphoenolpyruvate carboxylase activity in Escherichia coli. Biochimica et Biophysica Acta (BBA) - Enzymology. 139(1). 188–190. 17 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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