Author

Shin‐ichi Hisanaga

Tokyo Metropolitan Institute of Medical ScienceORCID 0000-0002-7572-472XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Neuroscience· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

Takashi NonakaiD· 2 shared Genjiro SuzukiiD· 1 shared Kanae AndoiD· 1 shared Masami Masuda‐SuzukakeiD· 1 shared Masato HasegawaiD· 1 shared Masato HosokawaiD· 1 shared Masato KawasakiiD· 1 shared Miki SendaiD· 1 shared

Activity by Year

2020-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersNeuroscience

Takashi NonakaORCID

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2 papers

Recent·Most cited

The 329HHK331 motif is essential for Alzheimer's disease tau filament fold

Yuta Sato, Masato Kawasaki, Toshio Moriya, Miki Senda, Masami Masuda‐Suzukake, Kanae Ando, Shin‐ichi Hisanaga, Toshiya Senda, Takashi Nonaka

The paper investigates the role of the 329HHK331 motif in Alzheimer's disease tau filament formation and shows that mutations in this region affect filament structure and seeding activity.

bioRxiv · Jul 3, 2026 · PreprintNeuroscience

α-Synuclein strains that cause distinct pathologies differentially inhibit proteasome

Genjiro Suzuki, Sei Imura, Masato Hosokawa, Ryu Katsumata, Takashi Nonaka, Shin‐ichi Hisanaga, Yasushi Saeki, Masato Hasegawa

The paper shows that different α-synuclein strains cause distinct pathologies by differentially inhibiting proteasome activity through structural differences in their C-terminal regions.

eLife · Jul 22, 2020Peer-reviewedNeuroscience