Author

S. Yasumasu

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· 2 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:development & morphogenesis· 1 Organism:human· 1

Frequent Co-Authors

A. Stsiapanava· 2 shared L. Han· 2 shared L. Jovine· 2 shared S. Zamora-Caballero· 2 shared A. E. Carlson· 1 shared B. Wiseman· 1 shared B. Wu· 1 shared C. Emori· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiophysics

A. Stsiapanava

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Author profile →

3 papers

Recent·Most cited

Effect of Light and Water Agitation on Hatching Processes in Clown Anemonefish Amphiprion ocellaris

S. Yamanaka, M. Kawaguchi, S. Yasumasu, K. Sato, M. Kinoshita

This study shows that darkness and water agitation regulate hatching enzyme secretion and chorion digestion in clown anemonefish, enabling synchronized hatching.

bioRxiv · Feb 14, 2024 · PreprintPhysiology

Architecture of the Vertebrate Egg Coat and Structural Basis of the ZP2 Block to Polyspermy

S. Nishio, C. Emori, B. Wiseman, D. Fahrenkamp, E. Dioguardi, S. Zamora-Caballero, M. Bokhove, L. Han, A. Stsiapanava, Y. Lu, M. Kodani, R. E. Bainbridge, K. M. Komondor, A. E. Carlson, M. Landreh, , L. Jovine

This study investigates how cleavage of ZP2 in the egg zona pellucida leads to oligomerization and structural changes that block polyspermy.

bioRxiv · Jun 21, 2023Biophysics

Cryo-EM Structure of Native Human Uromodulin, a Zona Pellucida Module Polymer

A. Stsiapanava, C. Xu, M. Brunati, S. Zamora-Caballero, C. Schaeffer, L. Han, M. Carroni, S. Yasumasu, L. Rampoldi, B. Wu, L. Jovine

The paper reports the cryo-EM structure of native human uromodulin, revealing its filamentous conformation and mechanism of bacterial binding.

bioRxiv · May 28, 2020Biophysics