Akira Wadano

1.3k total citations
58 papers, 1.0k citations indexed

About

Akira Wadano is a scholar working on Molecular Biology, Plant Science and Insect Science. According to data from OpenAlex, Akira Wadano has authored 58 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 16 papers in Plant Science and 15 papers in Insect Science. Recurrent topics in Akira Wadano's work include Photosynthetic Processes and Mechanisms (19 papers), Insect and Pesticide Research (9 papers) and Neurobiology and Insect Physiology Research (7 papers). Akira Wadano is often cited by papers focused on Photosynthetic Processes and Mechanisms (19 papers), Insect and Pesticide Research (9 papers) and Neurobiology and Insect Physiology Research (7 papers). Akira Wadano collaborates with scholars based in Japan, United States and Belize. Akira Wadano's co-authors include Toshio Iwaki, Kenji Kano, Tokuji Ikeda, Shigeru Shigeoka, Michio Himeno, Akiho Yokota, Hideshi Ihara, Seiya Tsujimura, Masahiro Tamoi and Norio Murata and has published in prestigious journals such as Journal of Biological Chemistry, The Plant Cell and Biochemistry.

In The Last Decade

Akira Wadano

55 papers receiving 987 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Akira Wadano Japan 18 655 310 172 140 109 58 1.0k
Donald L. Keister United States 23 801 1.2× 778 2.5× 124 0.7× 21 0.1× 41 0.4× 48 1.5k
Y. I. Shethna India 12 393 0.6× 133 0.4× 175 1.0× 132 0.9× 35 0.3× 25 607
Shoji Ida Japan 19 502 0.8× 631 2.0× 91 0.5× 60 0.4× 21 0.2× 60 964
Roderich Brandsch Germany 26 1.4k 2.1× 157 0.5× 128 0.7× 26 0.2× 35 0.3× 79 1.9k
Terence A. Walsh United States 23 1000 1.5× 845 2.7× 62 0.4× 138 1.0× 16 0.1× 31 1.7k
John Gorton Davis United States 12 486 0.7× 89 0.3× 74 0.4× 31 0.2× 30 0.3× 17 840
J.W. Newton United States 14 293 0.4× 180 0.6× 206 1.2× 65 0.5× 37 0.3× 36 675
Hans Leif Germany 7 893 1.4× 65 0.2× 267 1.6× 20 0.1× 57 0.5× 8 1.1k
Tatas Hardo Panintingjati Brotosudarmo Indonesia 19 487 0.7× 179 0.6× 165 1.0× 15 0.1× 25 0.2× 86 1.2k
Roy Powls United Kingdom 18 553 0.8× 97 0.3× 198 1.2× 47 0.3× 7 0.1× 48 762

Countries citing papers authored by Akira Wadano

Since Specialization
Citations

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

Fields of papers citing papers by Akira Wadano

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Akira Wadano

This figure shows the co-authorship network connecting the top 25 collaborators of Akira Wadano. A scholar is included among the top collaborators of Akira Wadano 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 Akira Wadano. Akira Wadano 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.
Matsumura, Hiroyoshi, Takayuki Maeda, Masahiro Tamoi, et al.. (2011). Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12. Structure. 19(12). 1846–1854. 44 indexed citations
2.
Iwaki, Toshio, Daisuke Kobayashi, Atsushi Kobayashi, et al.. (2008). Inhibition of RuBisCO cloned from Thermosynechococcus vulcanus and expressed in Escherichia coli with compounds predicted by Molecular Operation Environment (MOE). Journal of Bioscience and Bioengineering. 105(1). 26–33.
3.
Iwaki, Toshio, Naoki Inoue, Shigeo Wada, et al.. (2006). Expression of foreign type I ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) stimulates photosynthesis in cyanobacterium Synechococcus PCC7942 cells. Photosynthesis Research. 88(3). 287–297. 50 indexed citations
4.
5.
Ishida, H., et al.. (2003). Regulation of the expression of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) in a cyanobacterium, Synechococcus PCC7942. Photosynthesis Research. 78(1). 59–65. 10 indexed citations
6.
Ihara, Hideshi, et al.. (1998). Purification and partial amino acid sequences of the binding protein from Bombyx mori for CryIAa δ-endotoxin of Bacillus thuringiensis. Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology. 120(1). 197–204. 34 indexed citations
7.
Himeno, Michio, et al.. (1997). Carboxysomal Diffusion Resistance to Ribulose 1,5-Bisphosphate and 3-Phosphoglycerate in the Cyanobacterium Synechococcus PCC7942. Plant and Cell Physiology. 38(7). 769–775. 13 indexed citations
8.
Nishikawa, Keisuke, Tomohiro Hirahashi, Michio Himeno, & Akira Wadano. (1996). REGULATION MECHANISM OF PHOSPHORIBULOKINASE FROM THE CYANOBACTERIUM SYNECHOCCOCUS POC7942. Plant and Cell Physiology. 37. 45. 1 indexed citations
9.
Fujita, Naoko, et al.. (1996). Comparison of the primary structure ofwaxy proteins (granule-bound starch synthase) between polyploid wheats and related diploid species. Biochemical Genetics. 34(11-12). 403–413. 22 indexed citations
10.
Yokota, Akiho, Akira Wadano, & Hiroshi Murayama. (1996). Modeling of Continuously and Directly Analyzed Biphasic Reaction Courses of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase. The Journal of Biochemistry. 119(3). 487–499. 13 indexed citations
11.
Fujita, Naoko, et al.. (1995). Variation in the primary structure ofwaxy proteins (granule-bound starch synthase) in diploid cereals. Biochemical Genetics. 33(7-8). 269–281. 16 indexed citations
12.
Fujita, Naoko, et al.. (1995). Variation in the primary structure ofwaxy proteins (granule-bound starch synthase) in diploid cereals. Biochemical Genetics. 33(7-8). 269–281. 2 indexed citations
13.
Ihara, Hideshi, et al.. (1993). Specific Toxicity of δ-Endotoxins fromBacillus thuringiensistoBombyx mori. Bioscience Biotechnology and Biochemistry. 57(2). 200–204. 45 indexed citations
14.
Yokota, Akiho, et al.. (1991). Cooperative Binding of Carboxyarabinitol Bisphosphate to the Regulatory Sites of Ribulose Bisphosphate Carboxylase/Oxygenase from Spinach. The Journal of Biochemistry. 110(2). 253–256. 12 indexed citations
15.
Wadano, Akira, et al.. (1989). Purification and some properties of isocitrate dehydrogenase of a blowfly Aldrichina grahami. Comparative Biochemistry and Physiology Part B Comparative Biochemistry. 94(1). 189–194. 3 indexed citations
16.
17.
Goshima, Naoki, et al.. (1986). 3-hydroxykynurenine as O2⨪ scavenger in the blowfly, Aldrichina grahami. Biochemical and Biophysical Research Communications. 139(2). 666–672. 18 indexed citations
18.
Goshima, Naoki, et al.. (1985). Superoxide Dismutase in a Blowfly, Aldrichina grahami I. Interference of the Enzyme Assay by the Insect Homogenate. Osaka Prefecture University Repository (Osaka Prefecture University). 37. 75–80. 1 indexed citations
19.
Uemura, Takashi, et al.. (1985). Purification of Clostridium perfringens enterotoxins by high performance liquid chromatography. FEMS Microbiology Letters. 29(3). 293–297. 6 indexed citations
20.
Wadano, Akira, et al.. (1975). Changes in the Concentration of Free Amino Acids and Related Compounds in a Blowfly, Aldrichina Grahami, during Metamorphosis. Osaka Prefecture University Repository (Osaka Prefecture University). 27. 51–56. 3 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Donald L. Keister Breakdown of academic impact, for papers by Y. I. Shethna Breakdown of academic impact, for papers by Shoji Ida Breakdown of academic impact, for papers by Roderich Brandsch Breakdown of academic impact, for papers by Terence A. Walsh Breakdown of academic impact, for papers by John Gorton Davis Breakdown of academic impact, for papers by J.W. Newton Breakdown of academic impact, for papers by Hans Leif Breakdown of academic impact, for papers by Tatas Hardo Panintingjati Brotosudarmo Breakdown of academic impact, for papers by Roy Powls
Rankless by CCL
2026