Author

S.-i. Koda

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Approach:statistical model· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

S. Saito· 4 shared A. Mukaiyama· 1 shared D. Ouyang· 1 shared D. Simon· 1 shared E. Yamashita· 1 shared K. Ito-Miwa· 1 shared K. Terauchi· 1 shared S. Akiyama· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiophysics

S. Saito

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Regulation Mechanisms of the Dual ATPase in KaiC

Y. Furuike, A. Mukaiyama, S.-i. Koda, D. Simon, D. Ouyang, K. Ito-Miwa, S. Saito, E. Yamashita, T. Nishiwaki-Ohkawa, K. Terauchi, T. Kondo, S. Akiyama

This study investigates how the dual ATPase activities in KaiC coordinate to regulate the cyanobacterial circadian clock through structural and biochemical analysis.

bioRxiv · Oct 28, 2021Biochemistry

Ring-shaped multimeric structure enables the acceleration of KaiB-KaiC complex formation induced by the ADP/ATP exchange inhibition

S.-i. Koda, S. Saito

This paper investigates how the ring-shaped hexameric structure of KaiC enables acceleration of KaiB-KaiC complex formation through cooperative binding, despite ADP/ATP exchange inhibition typically slowing processes.

bioRxiv · Jul 6, 2021 · PreprintBiophysics

An alternative interpretation of the slow KaiB-KaiC binding of the cyanobacterial clock proteins

S.-i. Koda, S. Saito

This study proposes a new binding mechanism for KaiB-KaiC in cyanobacteria that explains the slowness of the circadian rhythm without requiring conformational changes in KaiB.

bioRxiv · Apr 21, 2020Biophysics

Sufficiency of unidirectional allostery in KaiC in generating the cyanobacterial circadian rhythm

S.-i. Koda, S. Saito

This study shows that unidirectional allostery from C2 to C1 in KaiC is sufficient to generate the cyanobacterial circadian rhythm, as demonstrated by matching experimental data on phosphorylation and ATPase activity.

bioRxiv · Apr 1, 2020 · PreprintBiophysics