Author

T. Ikeya

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1 Assay:structural biology· 1 Organism:yeast· 1

Frequent Co-Authors

Y. Ito· 3 shared T. Mikawa· 2 shared A. Hasan· 1 shared A. J. Hudson· 1 shared B. Romartinez-Alonso· 1 shared C. Bueno-Alejo· 1 shared C. Dominguez· 1 shared E. Nojiri· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiophysics

Y. Ito

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Different molecular recognition by three domains of the full-length GRB2 to SOS1 proline-rich motifs and EGFR phosphorylated sites

K. Tateno, T. Ando, M. Tabata, H. Sugasawa, T. Hayashi, P. M. Sayeesh, K. Inomata, T. Mikawa, Y. Ito, T. Ikeya

This study uses NMR to show that GRB2's SH3 domains bind PRMs with different affinities and that phosphorylated EGFR binding affects GRB2's structure and domain interactions.

bioRxiv · Apr 20, 2024Biophysics

Structural insights into the complex of oncogenic K-Ras4BG12V and Rgl2, a RalA/B activator

M. Tariq, T. Ikeya, N. Togashi, L. Fairall, S. Kamei, S. Mayooramurugan, L. R. Abbott, A. Hasan, C. Bueno-Alejo, S. Sukegawa, B. Romartinez-Alonso, M. A. Muro Campillo, A. J. Hudson, Y. Ito, J. W. Schwabe, , K. Tanaka

This study investigates the structural interaction between oncogenic KRas4BG12V and Rgl2RA, revealing a unique tetrameric complex formation that explains its hyperactivation of the RalA/B pathway.

bioRxiv · Oct 10, 2022Biochemistry

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