Author

M. Yagi-Utsumi

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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Approach:experimental assay· 4 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Organism:non-human primate· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

K. Kato· 4 shared C. Song· 2 shared K. Murata· 2 shared S. Yanaka· 2 shared T. Satoh· 2 shared C. Ganser· 1 shared C. Yamazaki· 1 shared E. W. Goh· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersBiophysics

K. Kato

Mutual co-authors in cluster

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4 papers

Recent·Most cited

The double-layered structure of amyloid-β assemblage on GM1-containing membranes catalytically promotes fibrillization

M. Yagi-Utsumi, S. G. Itoh, H. Okumura, K. Yanagisawa, K. Kato, K. Nishimura

This study identifies a double-layered Aβ structure on GM1 membranes that catalyzes fibril formation without becoming fibrils itself.

bioRxiv · Jun 26, 2022Biophysics

Desiccation-induced fibrous condensation of CAHS protein from an anhydrobiotic tardigrade

M. Yagi-Utsumi, K. Aoki, H. Watanabe, C. Song, S. Nishimura, T. Satoh, S. Yanaka, C. Ganser, S. Tanaka, V. Schnapka, E. W. Goh, Y. Furutani, K. Murata, T. Uchihashi, K. Arakawa, K. Kato

This study investigates the self-assembling properties of CAHS1 protein from tardigrades under desiccation conditions, showing it forms hydrogels and condensates that may contribute to desiccation tolerance.

bioRxiv · Jun 22, 2021Biochemistry

Characterization of amyloid β fibril formation under microgravity conditions

M. Yagi-Utsumi, S. Yanaka, C. Song, T. Satoh, C. Yamazaki, H. Kasahara, T. Shimazu, K. Murata, K. Kato

This study examines amyloid β fibril formation under microgravity conditions on the ISS, finding slower progression and distinct morphologies compared to ground-based experiments.

npj Microgravity · Jun 12, 2020Peer-reviewedBiophysics

Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR

M. S. Chandak, T. Nakamura, M. Yagi-Utsumi, T. Yamaguchi, K. Kato, K. Kuwajima

This study investigates the residual structure of unfolded ubiquitin using H/D-exchange 2D NMR, identifying protected amide groups that suggest partial native β-hairpin structure in the unfolded state.

bioRxiv · Sep 27, 2018Biophysics