Author

Gosuke Hayashi

Nagoya UniversityORCID 0000-0001-6853-2706Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Molecular Biology· 1 Synthetic Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Assay:ChIP-seq· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

Ami Hirano· 1 shared C. Kim· 1 shared Fumiaki OhtakeiD· 1 shared Fumika KoyanoiD· 1 shared Haruhiko EharaiD· 1 shared Hiroshi MurakamiiD· 1 shared Hitoshi KurumizakaiD· 1 shared Junko Kato· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperBiochemistry

Ami Hirano

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Molecular BiologybioRxivPreprintMay 5, 2026

Structural basis for site-specific histone H3 acetylation-dependent regulation of RNAPII transcription through nucleosomes

Takumi Oishi, Suguru Hatazawa, Tomoya Kujirai…·Hitoshi Kurumizaka

The paper investigates how specific acetylation sites on histone H3 affect RNAPII transcription through nucleosomes using cryo-EM structures.

DOI 10.64898/2026.05.02.722397

ChIP-seqexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivPreprintMar 16, 2026

UFD1 Recognition of Initiator and Proximal Ubiquitin Drives p97-Mediated Substrate Unfolding enhanced by FAF1, FAF2, and UBXD7

Shunki Miyauchi, Ami Hirano, Nanako Yasumoto…·Yusuke Sato

The paper elucidates how UFD1 recognizes initiator and proximal ubiquitin to drive p97-mediated substrate unfolding, with accessory adaptors enhancing this process.

1 citation

humanstructural biology

𝕏 PostBluesky

Synthetic BiologybioRxivPreprintApr 10, 2025

De novo chemo-optogenetics through rational small-molecule design and TRAP display

Tomoki Miyazaki, Tomoshige Fujino, Tatsuyuki Yoshii…·Shinya Tsukiji

This paper introduces a method to create synthetic chemo-optogenetic tools by combining rational small-molecule design with TRAP display to generate light-controlled protein binders.

DOI 10.1101/2025.04.10.648175

experimental assay

𝕏 PostBluesky