Junshi Sakamoto

1.6k total citations
48 papers, 1.3k citations indexed

About

Junshi Sakamoto is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Materials Chemistry. According to data from OpenAlex, Junshi Sakamoto has authored 48 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 14 papers in Cellular and Molecular Neuroscience and 10 papers in Materials Chemistry. Recurrent topics in Junshi Sakamoto's work include Photosynthetic Processes and Mechanisms (27 papers), Photoreceptor and optogenetics research (11 papers) and Enzyme Structure and Function (10 papers). Junshi Sakamoto is often cited by papers focused on Photosynthetic Processes and Mechanisms (27 papers), Photoreceptor and optogenetics research (11 papers) and Enzyme Structure and Function (10 papers). Junshi Sakamoto collaborates with scholars based in Japan, United States and Netherlands. Junshi Sakamoto's co-authors include Kevin P. Campbell, Nobuhito Sone, Marlon Pragnell, Yūji Tonomura, Shunsuke Noguchi, Derrick R. Witcher, Steven D. Kahl, Clara Franzini‐Armstrong, Michel De Waard and Tatsuki Kurokawa and has published in prestigious journals such as Science, Journal of Biological Chemistry and Scientific Reports.

In The Last Decade

Junshi Sakamoto

48 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Junshi Sakamoto Japan 18 1.1k 364 134 124 122 48 1.3k
Morten J. Buch-Pedersen Denmark 17 1.1k 1.0× 69 0.2× 56 0.4× 49 0.4× 150 1.2× 26 1.6k
Florent Guillain France 26 1.4k 1.3× 84 0.2× 331 2.5× 49 0.4× 191 1.6× 47 1.8k
Daohua Jiang China 17 755 0.7× 264 0.7× 235 1.8× 88 0.7× 24 0.2× 34 1.1k
Kwok Ki Ho United States 15 793 0.7× 61 0.2× 49 0.4× 45 0.4× 48 0.4× 27 1.1k
Patrice Hamel United States 24 1.4k 1.2× 104 0.3× 9 0.1× 96 0.8× 187 1.5× 41 1.6k
James N. Blaza United Kingdom 18 1.2k 1.1× 48 0.1× 10 0.1× 151 1.2× 59 0.5× 29 1.6k
Daijiro Ohmori Japan 18 455 0.4× 60 0.2× 13 0.1× 49 0.4× 54 0.4× 50 925
E. Kurt Dolence United States 20 410 0.4× 70 0.2× 48 0.4× 118 1.0× 41 0.3× 38 1.0k
Stefan Kerscher Germany 24 1.6k 1.4× 61 0.2× 9 0.1× 36 0.3× 45 0.4× 27 1.8k
D. E. Green United States 12 696 0.6× 77 0.2× 15 0.1× 33 0.3× 115 0.9× 15 991

Countries citing papers authored by Junshi Sakamoto

Since Specialization
Citations

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

Fields of papers citing papers by Junshi Sakamoto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Junshi Sakamoto

This figure shows the co-authorship network connecting the top 25 collaborators of Junshi Sakamoto. A scholar is included among the top collaborators of Junshi Sakamoto 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 Junshi Sakamoto. Junshi Sakamoto 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.
2.
Yasunaga, Takuo, et al.. (2021). Extended supercomplex contains type-II NADH dehydrogenase, cytochrome bcc complex, and aa3 oxidase in the respiratory chain of Corynebacterium glutamicum. Journal of Bioscience and Bioengineering. 133(1). 76–82. 1 indexed citations
3.
Asseri, Amer H., et al.. (2021). Cardiolipin enhances the enzymatic activity of cytochrome bd and cytochrome bo3 solubilized in dodecyl-maltoside. Scientific Reports. 11(1). 8006–8006. 10 indexed citations
4.
Hakvoort, Henk W. J., Sangjin Hong, Robert B. Gennis, et al.. (2020). The carboxy-terminal insert in the Q-loop is needed for functionality of Escherichia coli cytochrome bd-I. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1861(5-6). 148175–148175. 19 indexed citations
5.
Arutyunyan, Alexander M., et al.. (2012). Optical and magneto-optical activity of cytochrome bd from Geobacillus thermodenitrificans. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(11). 2087–2094. 31 indexed citations
6.
Sakamoto, Junshi, et al.. (2011). Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix. BMC Microbiology. 11(1). 52–52. 7 indexed citations
7.
Yoshimune, Kazuaki, Hajime Morimoto, Yu Hirano, et al.. (2010). The obligate alkaliphile Bacillus clarkii K24-1U retains extruded protons at the beginning of respiration. Journal of Bioenergetics and Biomembranes. 42(2). 111–116. 10 indexed citations
8.
Noguchi, Shunsuke, et al.. (2002). Importance of Hydrophobic Interaction between a SoxB-Type Cytochrome c Oxidase with Its Natural Substrate Cytochrome c-551 and Its Mutants. The Journal of Biochemistry. 132(2). 189–195. 1 indexed citations
9.
Sakamoto, Junshi, et al.. (2002). Improved H+/O ratio and cell yield of Escherichia coli with genetically altered terminal quinol oxidases. Journal of Bioscience and Bioengineering. 93(5). 464–469. 9 indexed citations
10.
11.
Uchida, Takeshi, Motonari Tsubaki, Tatsuki Kurokawa, et al.. (2000). Active site structure of SoxB-type cytochrome bo3 oxidase from thermophilic Bacillus. Journal of Inorganic Biochemistry. 82(1-4). 65–72. 1 indexed citations
12.
Sakamoto, Junshi, et al.. (2000). Menaquinol oxidase activity and primary structure of cytochrome bd from the amino-acid fermenting bacterium Corynebacterium glutamicum. Archives of Microbiology. 173(5-6). 390–397. 53 indexed citations
13.
Sone, Nobuhito, Satoru Koyanagi, & Junshi Sakamoto. (2000). Energy-Yielding Properties of SoxB-Type Cytochrome bo3 Terminal Oxidase: Analyses Involving Bacillus stearothermophilus K1041 and Its Mutant Strains. The Journal of Biochemistry. 127(4). 551–557. 8 indexed citations
14.
Sakamoto, Junshi, et al.. (1999). Gene structure and quinol oxidase activity of a cytochrome bd-type oxidase from Bacillus stearothermophilus. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1411(1). 147–158. 46 indexed citations
15.
Sakamoto, Junshi, et al.. (1999). Cloning ofBacillus stearothermophilus ctaAand Heme A Synthesis with the CtaA Protein Produced inEscherichia coli. Bioscience Biotechnology and Biochemistry. 63(1). 96–103. 13 indexed citations
16.
Noguchi, Shunsuke, et al.. (1998). The cbaAB genes for bo3-type cytochrome c oxidase in Bacillus stearothermophilus. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1397(3). 262–267. 16 indexed citations
17.
Sakamoto, Junshi, Yutaka Handa, & Nobuhito Sone. (1997). A Novel Cytochrome b(o/aaa)3-Type Oxidase from Bacillus stearothermophilus Catalyzes Cytochrome c-551 Oxidation. The Journal of Biochemistry. 122(4). 764–771. 21 indexed citations
18.
Tanaka, Toshiyuki, M. Inoue, Junshi Sakamoto, & Nobuhito Sone. (1996). Intra- and Inter-Complex Cross-Linking of Subunits in the Quinol Oxidase Super-Complex from Thermophilic Bacillus PS3. The Journal of Biochemistry. 119(3). 482–486. 17 indexed citations
19.
Noguchi, Shunsuke, et al.. (1996). Identification of peptide fragments chemically cross-linked in cytochrome c oxidase from thermophilic Bacillus PS3.. PubMed. 38(1). 181–8. 2 indexed citations
20.
Noguchi, Shunsuke, et al.. (1994). Over-expression of membrane-bound cytochrome c-551 from thermophilic Bacillus PS3 in Bacillus stearothermophilus K1041. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1188(3). 302–310. 13 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 Morten J. Buch-Pedersen Breakdown of academic impact, for papers by Florent Guillain Breakdown of academic impact, for papers by Daohua Jiang Breakdown of academic impact, for papers by Kwok Ki Ho Breakdown of academic impact, for papers by Patrice Hamel Breakdown of academic impact, for papers by James N. Blaza Breakdown of academic impact, for papers by Daijiro Ohmori Breakdown of academic impact, for papers by E. Kurt Dolence Breakdown of academic impact, for papers by Stefan Kerscher Breakdown of academic impact, for papers by D. E. Green
Rankless by CCL
2026