Akimasa Miyanaga

2.7k total citations
80 papers, 2.0k citations indexed

About

Akimasa Miyanaga is a scholar working on Molecular Biology, Pharmacology and Biotechnology. According to data from OpenAlex, Akimasa Miyanaga has authored 80 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 41 papers in Pharmacology and 31 papers in Biotechnology. Recurrent topics in Akimasa Miyanaga's work include Microbial Natural Products and Biosynthesis (41 papers), Enzyme Production and Characterization (23 papers) and Enzyme Structure and Function (17 papers). Akimasa Miyanaga is often cited by papers focused on Microbial Natural Products and Biosynthesis (41 papers), Enzyme Production and Characterization (23 papers) and Enzyme Structure and Function (17 papers). Akimasa Miyanaga collaborates with scholars based in Japan, United States and Australia. Akimasa Miyanaga's co-authors include Tadashi Eguchi, Fumitaka Kudo, Shinya Fushinobu, Takayoshi Wakagi, Kiyoshi Ito, Bradley S. Moore, Hirofumi Shoun, Hayao Taguchi, Yuji Shinohara and Takuya Koseki and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Akimasa Miyanaga

78 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
Akimasa Miyanaga Japan 24 1.2k 776 535 515 244 80 2.0k
Jiahai Zhou China 31 2.2k 1.9× 504 0.6× 516 1.0× 284 0.6× 231 0.9× 104 3.3k
Fumitaka Kudo Japan 31 1.8k 1.5× 1.4k 1.8× 816 1.5× 410 0.8× 156 0.6× 110 2.6k
Christopher J. Thibodeaux Canada 17 1.1k 1.0× 481 0.6× 685 1.3× 198 0.4× 123 0.5× 44 1.7k
Steven G. Van Lanen United States 32 2.2k 1.8× 1.5k 1.9× 1.1k 2.0× 397 0.8× 145 0.6× 80 3.3k
Jörg Pietruszka Germany 35 2.0k 1.7× 431 0.6× 2.4k 4.5× 530 1.0× 259 1.1× 216 4.2k
Cheng‐Shi Jiang China 26 958 0.8× 582 0.8× 841 1.6× 301 0.6× 171 0.7× 108 2.7k
Yi Yu China 27 1.4k 1.2× 1.0k 1.3× 441 0.8× 253 0.5× 172 0.7× 65 2.1k
Yasushi Ogasawara Japan 24 937 0.8× 566 0.7× 427 0.8× 154 0.3× 103 0.4× 74 1.5k
Marta Ferraroni Italy 32 1.8k 1.5× 544 0.7× 1.1k 2.1× 168 0.3× 290 1.2× 110 2.6k
Zhoutong Sun China 28 2.4k 2.0× 161 0.2× 535 1.0× 289 0.6× 133 0.5× 100 3.1k

Countries citing papers authored by Akimasa Miyanaga

Since Specialization
Citations

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

Fields of papers citing papers by Akimasa Miyanaga

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Akimasa Miyanaga

This figure shows the co-authorship network connecting the top 25 collaborators of Akimasa Miyanaga. A scholar is included among the top collaborators of Akimasa Miyanaga 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 Akimasa Miyanaga. Akimasa Miyanaga 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.
Adachi, Naruhiko, Masato Kawasaki, Toshio Moriya, et al.. (2025). Ancestral sequence reconstruction as a tool for structural analysis of modular polyketide synthases. Nature Communications. 16(1). 6847–6847. 1 indexed citations
2.
Wang, Dawei, et al.. (2024). Engineering the Substrate Specificity of (S)‐β‐Phenylalanine Adenylation Enzyme HitB. ChemBioChem. 25(15). e202400383–e202400383. 3 indexed citations
3.
Miyanaga, Akimasa, et al.. (2023). Substrate Specificity of Chondroitinase ABC-I Based on Analyses of Biochemical Reactions and Crystal Structure. Trends in Glycoscience and Glycotechnology. 35(208). E94–E99.
4.
5.
Tanaka, Nobukiyo, Masahiro Nakajima, Shinji Kamisuki, et al.. (2019). Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family. Journal of Biological Chemistry. 294(19). 7942–7965. 15 indexed citations
6.
Miyanaga, Akimasa, et al.. (2018). Structural Basis of Sequential Allosteric Transitions in Tetrameric d-Lactate Dehydrogenases from Three Gram-Negative Bacteria. Biochemistry. 57(37). 5388–5406. 12 indexed citations
7.
Kudo, Fumitaka, Akimasa Miyanaga, & Tadashi Eguchi. (2018). Structural basis of the nonribosomal codes for nonproteinogenic amino acid selective adenylation enzymes in the biosynthesis of natural products. Journal of Industrial Microbiology & Biotechnology. 46(3-4). 515–536. 48 indexed citations
8.
Miyanaga, Akimasa, Fumitaka Kudo, & Tadashi Eguchi. (2018). Protein–protein interactions in polyketide synthase–nonribosomal peptide synthetase hybrid assembly lines. Natural Product Reports. 35(11). 1185–1209. 76 indexed citations
9.
Tanaka, Nobukiyo, Koichi Abe, Masahiro Nakajima, et al.. (2017). Function and structure relationships of a β‐1,2‐glucooligosaccharide‐degrading β‐glucosidase. FEBS Letters. 591(23). 3926–3936. 26 indexed citations
10.
Miyanaga, Akimasa, et al.. (2017). Structural analysis of the dual-function thioesterase SAV606 unravels the mechanism of Michael addition of glycine to an α,β-unsaturated thioester. Journal of Biological Chemistry. 292(26). 10926–10937. 21 indexed citations
11.
Miyanaga, Akimasa, Fumitaka Kudo, & Tadashi Eguchi. (2016). Mechanisms of β-amino acid incorporation in polyketide macrolactam biosynthesis. Current Opinion in Chemical Biology. 35. 58–64. 32 indexed citations
12.
Nakajima, Masahiro, Akimasa Miyanaga, Koichi Abe, et al.. (2016). Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua. PLoS ONE. 11(2). e0148870–e0148870. 31 indexed citations
13.
Shinohara, Yuji, Akimasa Miyanaga, Fumitaka Kudo, & Tadashi Eguchi. (2014). The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates. FEBS Letters. 588(6). 995–1000. 10 indexed citations
14.
Nakajima, Masahiro, et al.. (2014). Crystallization and preliminary X-ray diffraction analysis of Lin1840, a putative β-glucosidase fromListeria innocua. Acta Crystallographica Section F Structural Biology Communications. 70(10). 1398–1401. 2 indexed citations
15.
Miyanaga, Akimasa, et al.. (2014). Diverse allosteric and catalytic functions of tetrameric d-lactate dehydrogenases from three Gram-negative bacteria. AMB Express. 4(1). 76–76. 16 indexed citations
16.
Miyanaga, Akimasa, et al.. (2013). The crystal structure of d-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochemical and Biophysical Research Communications. 439(1). 109–114. 8 indexed citations
17.
Miyanaga, Akimasa & Sueharu Horinouchi. (2009). Enzymatic synthesis of bis-5-alkylresorcinols by resorcinol-producing type III polyketide synthases. The Journal of Antibiotics. 62(7). 371–376. 12 indexed citations
18.
Miyanaga, Akimasa, Takuya Koseki, Hiroshi Matsuzawa, et al.. (2006). Crystal Structure of GH54 (.ALPHA.-L-Arabinofuranosidase and Unique Function of CBM42 Attached to It. Journal of Applied Glycoscience. 53(2). 143–148. 1 indexed citations
19.
Miyanaga, Akimasa, Takuya Koseki, Sachiko Nakamura, et al.. (2006). The family 42 carbohydrate-binding module of family 54 α-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose. Biochemical Journal. 399(3). 503–511. 38 indexed citations
20.
Miyanaga, Akimasa, Shinya Fushinobu, Kiyoshi Ito, Hirofumi Shoun, & Takayoshi Wakagi. (2003). Mutational and structural analysis of cobalt‐containing nitrile hydratase on substrate and metal binding. European Journal of Biochemistry. 271(2). 429–438. 71 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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