Author

Hidehito Tochio

Kyoto UniversityORCID 0000-0003-3843-3330Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:cryo-EM· 1 Organism:Drosophila· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Assay:protein sequence· 1

Frequent Co-Authors

Kayo ImamuraiD· 2 shared Naotaka SekiyamaiD· 2 shared Akihiro NaritaiD· 1 shared Chioko NagaoiD· 1 shared Emi Sakamoto· 1 shared Esha ChawlaiD· 1 shared Fumiaki MakinoiD· 1 shared Gal BitaniD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

Kayo ImamuraORCID

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3 papers

Recent·Most cited

NeuroscienceNature CommunicationsPeer-reviewedJul 15, 2026

Development of an RNA Aptamer as a Therapeutic Agent for Synucleinopathies

Kazuma Murakami, Thi Hong Van Nguyen, Leo Tsuda…·Gal Bitan

This paper develops an RNA aptamer, 1R6, that targets synuclein and shows therapeutic potential in synucleinopathies by inhibiting aggregation and promoting disaggregation.

DOI 10.1038/s41467-026-75209-z

Drosophilaexperimental assay

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BiophysicsNature CommunicationsPeer-reviewedApr 17, 2026

From Monomers to Oligomers: Structural Mechanism of Receptor-Triggered MyD88 Assembly in Innate Immune Signaling

Kazuki Kasai, Kayo Imamura, Masatoshi Uno…·Hidehito Tochio

This study reveals the structural mechanism of MyD88 oligomerization in innate immune signaling using cryo-EM and high-speed AFM.

6 citationstop 2%

cryo-EMfluorescence / live-cell microscopy

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BiophysicsbioRxivPreprintOct 27, 2025

Sequence-encoded conformational biases shape self-assembly modes of intrinsically disordered proteins

Ryoga Kobayashi, Norio Yoshida, Yohei Miyanoiri…·Naotaka Sekiyama

This study shows that sequence-encoded conformational biases in intrinsically disordered proteins influence their self-assembly modes, affecting condensate properties and amyloid fibril formation.

1 citation

protein structureprotein sequence

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