Author

Naotaka Sekiyama

Kyoto UniversityORCID 0000-0003-4537-6565Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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

Frequent Co-Authors

Hidehito TochioiD· 2 shared Kayo ImamuraiD· 2 shared Akihiro NaritaiD· 1 shared Emi Sakamoto· 1 shared Fumiaki MakinoiD· 1 shared Hideki NakamuraiD· 1 shared Hidenori OhnishiiD· 1 shared Hiroki KonnoiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersBiophysics

Hidehito TochioORCID

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2 papers

Recent·Most cited

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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