Author

T. Inada

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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Biochemistry· 3 Ecology· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Assay:proteomics· 3 Organism:plant (other)· 2 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Research Focus:ecology & biodiversity· 1 Assay:field survey / ecological data· 1

Frequent Co-Authors

Y. Matsuo· 2 shared D. M. Best· 1 shared G. Mao· 1 shared H. Yoshioka· 1 shared J. Musial· 1 shared K. Ikeuchi· 1 shared K. M. Best· 1 shared L. Kater· 1 shared

Activity by Year

2022-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

Y. Matsuo

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

NADPH oxidase-mediated sulfenylation of cysteine derivatives is key regulatory events for plant immune responses

Y. Hino, T. Inada, M. Yoshioka, H. Yoshioka

This study shows that NADPH oxidase-generated ROS sulfenylates cysteine residues in ROS sensor proteins, regulating plant immune responses like cell death and pathogen defense.

bioRxiv · Nov 24, 2023Immunology

Elevation and topography shape the diversity of mesoscale landscape-level woody plant species found in temperate evergreen forests

S. Watanabe, Y. Maesako, T. Inada

The paper examines how elevation and topography influence woody plant species diversity at the mesoscale landscape level in temperate evergreen forests, finding they drive species richness and composition differently.

bioRxiv · Mar 29, 2023 · PreprintEcology

Mechanistic insights into the UFM1 E3 ligase complex in ufmylation and ribosome-associated protein quality control

R. Ishimura, S. Ito, G. Mao, S. Komatsu-Hirota, T. Inada, N. N. Noda, M. Komatsu

This study elucidates the mechanism of the UFM1 E3 ligase complex in ufmylation and its role in ER-RQC by showing its interaction with CDK5RAP3 and ufmylated RPL26.

bioRxiv · Feb 16, 2023 · PreprintBiochemistry

Decoding of the ubiquitin code for clearance of colliding ribosomes by the RQT complex

Y. Matsuo, T. Inada, T. Uchihashi

The paper investigates how the RQT complex decodes ubiquitin signals to clear colliding ribosomes, showing that Cue3 and Rqt4 interact with K63-linked ubiquitin chains.

Nature Communications · Jan 10, 2023Peer-reviewedBiochemistry

Clearing of ribosome collisions by the ribosome quality control trigger complex RQT

K. M. Best, K. Ikeuchi, L. Kater, D. M. Best, J. Musial, Y. Matsuo, O. Berninghausen, T. Becker, T. Inada, R. Beckmann

The paper shows RQT clears collided ribosomes by pulling mRNA to trigger destabilizing conformational transitions for subunit dissociation.

bioRxiv · Apr 19, 2022 · PreprintBiochemistry