Author

N. N. Noda

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

Biology Disciplines

Click to filter author papers

Cell Biology· 4 Biochemistry· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 6 Assay:proteomics· 4 Research Focus:cell signaling & trafficking· 3 Organism:mouse· 3 Research Focus:cell type annotation· 2 Research Focus:differential expression· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2

Frequent Co-Authors

M. Komatsu· 3 shared K. Matoba· 2 shared S. Kageyama· 2 shared S. Komatsu-Hirota· 2 shared Y. Ichimura· 2 shared A. H. El-Gowily· 1 shared A. Horii· 1 shared A. Yamasaki· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 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

3 shared papersCell Biology

M. Komatsu

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

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

Phosphorylation of phase-separated p62 bodies by ULK1 activates a redox-independent stress response

M. Komatsu, R. Ikeda, D. Noshiro, H. Morishita, S. Takada, S. Kageyama, Y. Fujioka, T. Funakoshi, S. Komatsu-Hirota, R. Arai, E. Ryzhii, M. Abe, T. Koga, M. Nakao, K. Sakimura, , N. N. Noda

This study identifies ULK1 as the kinase responsible for phosphorylating p62, which activates NRF2 in a redox-independent manner through retention of KEAP1 in p62 bodies.

bioRxiv · Dec 21, 2022Cell Biology

Phosphorylation by casein kinase 2 ensures ER-phagy receptor TEX264 binding to ATG8 proteins

H. Chino, A. Yamasaki, K. L. Ode, H. R. Ueda, N. N. Noda, N. Mizushima

The paper shows phosphorylation of TEX264's LIR by casein kinase 2 enhances its binding to ATG8 proteins, crucial for ER-phagy, through hydrogen bonds not achievable with acidic residues.

bioRxiv · Feb 11, 2022 · PreprintCell Biology

Droplets of amyotrophic lateral sclerosis-associated p62/SQSTM1 mutants show slower inner fluidity

F. M. Omar, Y. Ichimura, S. Kageyama, A. H. El-Gowily, Y.-s. Sou, M. Koike, N. N. Noda, M. Komatsu

This study investigates how ALS/FTD-related p62 mutations affect liquid droplet properties, finding that some mutants show reduced Nrf2 activation and delayed turnover, while all exhibit slower inner fluidity.

bioRxiv · Jun 7, 2021Cell Biology

Mutagenesis and homology modeling reveal a predicted pocket of lysophosphatidylcholine acyltransferase 2 to catch Acyl-CoA.

F. Hamano, K. Matoba, T. Hashidate, T. Suzuki, K. Miura, D. Hishikawa, T. Harayama, K. Yuki, Y. Kita, N. N. Noda, T. Shimizu, H. Shindou

The paper identifies key residues and an acyl-CoA-binding pocket in mouse LPCAT2 using homology modeling, providing structural insights for drug development against PAF-related diseases.

bioRxiv · Oct 31, 2020Biochemistry

Lysosomal microautophagic pathway links proteostasis to protein aggregation disease

Y. Fujiwara, C. Kabuta, V. R. Contu, M. Ogawa, H. Fujita, H. Kikuchi, R. Sakai, M. Suzuki, I. Koyama-Honda, M. Inoue, Y. Oya, Y. U. Inoue, T. Inoue, R. Takahashi, G. Matsumoto, , T. Kabuta

This study identifies SIDT2 as a mediator of microautophagy that delivers cytosolic proteins into lysosomes, linking proteostasis to protein aggregation disease.

bioRxiv · Aug 11, 2020 · PreprintCell Biology