Author

I. Shimada

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Approach:microscopy & imaging analysis· 1 Assay:structural biology· 1 Organism:yeast· 1

Frequent Co-Authors

A. Watanabe· 1 shared E. Nojiri· 1 shared H. Ogasa· 1 shared H. Yagi· 1 shared M. Kikkawa· 1 shared M. Okada· 1 shared N. Nishida· 1 shared O. Takarada· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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1 shared paperBiophysics

A. Watanabe

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2 papers

Recent·Most cited

Multi-state structure determination and dynamics analysis reveals a new ubiquitin-recognition mechanism in yeast ubiquitin C-terminal hydrolase

M. Okada, Y. Tateishi, E. Nojiri, T. Mikawa, S. Rajesh, H. Ogasa, T. Ueda, H. Yagi, T. Kohno, T. Kigawa, I. Shimada, P. Guentert, Y. Ito, T. Ikeya

The paper develops an NMR method to determine multi-state structures of proteins and applies it to yeast ubiquitin hydrolase 1, revealing dynamic motions critical for ubiquitin recognition and proteolysis.

bioRxiv · Apr 22, 2021 · PreprintBiophysics

Structural basis for two-way communication between dynein and microtubules

N. Nishida, Y. Komori, O. Takarada, A. Watanabe, S. Tamura, S. Kubo, I. Shimada, M. Kikkawa

This study investigates the structural basis of two-way communication between dynein and microtubules using NMR and cryo-EM, revealing conformational changes in the MTBD and their implications for dynein movement.

bioRxiv · Sep 18, 2019Biophysics