Riku Aono

講師(任期付)

  • 84 Citations
  • 4 h-Index
20122018
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Isomerases Medicine & Life Sciences
Phosphorylases Medicine & Life Sciences
Adenosine Monophosphate Medicine & Life Sciences
Oxygenases Medicine & Life Sciences
Archaea Medicine & Life Sciences
Metabolic Networks and Pathways Medicine & Life Sciences
Pyrobaculum Medicine & Life Sciences
Nucleosides Medicine & Life Sciences

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Research Output 2012 2018

  • 84 Citations
  • 4 h-Index
  • 6 Article
2 Citations (Scopus)

A phosphofructokinase homolog from Pyrobaculum calidifontis displays kinase activity towards pyrimidine nucleosides and ribose 1-phosphate

Aziz, I., Bibi, T., Rashid, N., Aono, R., Atomi, H. & Akhtar, M., 2018 Aug 1, In : Journal of Bacteriology. 200, 16, e00284-18.

Research output: Contribution to journalArticle

Open Access
Pyrobaculum
Pyrimidine Nucleosides
Phosphofructokinases
Phosphotransferases
Nucleosides
3 Citations (Scopus)

Mutation design of a thermophilic Rubisco based on three-dimensional structure enhances its activity at ambient temperature

Fujihashi, M., Nishitani, Y., Kiriyama, T., Aono, R., Sato, T., Takai, T., Tagashira, K., Fukuda, W., Atomi, H., Imanaka, T. & Miki, K., 2016 Oct 1, In : Proteins: Structure, Function and Bioinformatics. 84, 10, p. 1339-1346 8 p.

Research output: Contribution to journalArticle

Oxygenases
Mutation
Temperature
Mutant Proteins
Enzymes
28 Citations (Scopus)

A pentose bisphosphate pathway for nucleoside degradation in Archaea

Aono, R., Sato, T., Imanaka, T. & Atomi, H., 2015 May 1, In : Nature Chemical Biology. 11, 5, p. 355-360 6 p.

Research output: Contribution to journalArticle

Pentoses
Archaea
Nucleosides
Thermococcus
Pentose Phosphate Pathway
4 Citations (Scopus)

Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization

Nishitani, Y., Aono, R., Nakamura, A., Sato, T., Atomi, H., Imanaka, T. & Miki, K., 2013 Aug 9, In : Journal of Molecular Biology. 425, 15, p. 2709-2721 13 p.

Research output: Contribution to journalArticle

Phosphorylases
Dimerization
Adenosine Monophosphate
Thermococcus
Archaea
18 Citations (Scopus)

Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1

Nakamura, A., Fujihashi, M., Aono, R., Sato, T., Nishiba, Y., Yoshida, S., Yano, A., Atomi, H., Imanaka, T. & Miki, K., 2012 Jun 15, In : Journal of Biological Chemistry. 287, 25, p. 20784-20796 13 p.

Research output: Contribution to journalArticle

Open Access
Isomerases
Ligands
Substrates
Ribose
Catalytic Domain