Author

Yoshiaki Kise

The University of TokyoORCID 0000-0002-1840-5028Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Assay:cryo-EM· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Organism:human· 1 Approach:statistical model· 1

Frequent Co-Authors

Osamu NurekiiD· 2 shared Asako Oguni· 1 shared Chikako Okada· 1 shared Daichi Yamanouchi· 1 shared Fumiya K. SanoiD· 1 shared Go KasuyaiD· 1 shared Hidetoshi KonoiD· 1 shared Hisashi IshidaiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiochemistry

Osamu NurekiORCID

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2 papers

Recent·Most cited

Structural insights into inhibition mechanism of the helicase-primase complex from human herpesvirus 1

Ko Sato, Hisashi Ishida, Toma Miyagishi, Shunsuke Kobayashi, Yoshiaki Kise, Keisuke Hamada, Chikako Okada, Asako Oguni, Osamu Nureki, Hidetoshi Kono, Kaori Fukuzawa, Toru Sengoku

This paper reports cryo-EM structures of the HHV1 helicase-primase complex bound to DNA and inhibitors, revealing how these drugs block viral DNA replication by locking the helicase in an inactive conformation.

Cell chemical biology · Apr 15, 2026Peer-reviewedBiochemistry

Structural basis of lipid-mediated gating in a two-pore domain potassium channel

Fumiya K. Sano, Go Kasuya, Kohei Yamaguchi, Takehiro Suzuki, Daichi Yamanouchi, Kanehisa HASHIMOTO, Masataka Inoue, Kazuhiro Sawada, Ryuichiro Ishitani, Kenjiro Yoshimura, Hisato Hirano, Yuzuru Itoh, Koichi Nakajo, Naoshi Dohmae, Yoshiaki Kise, Osamu Nureki

This study presents the cryo-EM structure of TOK1, revealing its unique domain architecture and lipid-mediated gating mechanism through structural and functional analyses.

bioRxiv · Nov 12, 2025 · PreprintMolecular Biology