Author

Y. Fujioka

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 Microbiology· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 6 Research Focus:cell signaling & trafficking· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:differential expression· 1

Frequent Co-Authors

Y. Ohba· 5 shared A. Yoshida· 4 shared M. Fujioka· 4 shared S. Kashiwagi· 4 shared A. O. Satoh· 3 shared H. Sasajima· 3 shared M. Amano· 3 shared A. Horii· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 34 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

5 shared papersCell Biology

Y. Ohba

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

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

Comparative pathogenicity of SARS-CoV-2 Omicron subvariants including BA.1, BA.2, and BA.5

T. Tamura, D. Yamasoba, Y. Oda, J. Ito, T. Kamasaki, N. Nao, R. Hashimoto, Y. Fujioka, R. Suzuki, L. Wang, H. Ito, I. Kimura, I. Yokota, M. Kishimoto, M. Tsuda, , T. Fukuhara

This study compares the pathogenicity of SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.5, finding BA.5 is more fusogenic and induces stronger inflammation than earlier variants.

bioRxiv · Aug 5, 2022Microbiology

A method for the generation of pseudotyped virus particles bearing SARS coronavirus spike protein in high yields

Y. Fujioka, S. Kashiwagi, A. Yoshida, A. O. Satoh, M. Fujioka, M. Amano, Y. Yamauchi, Y. Ohba

This paper describes an improved method to produce SARS-CoV and SARS-CoV-2 Spike protein pseudotyped VSV particles for coronavirus entry studies and antiviral development.

bioRxiv · Jul 30, 2021 · PreprintMicrobiology

Interaction Between Phosphoinositide 3-Kinase and the VDAC2 Channel Tethers Endosomes to Mitochondria and Promotes Endosome Maturation

A. O. Satoh, Y. Fujioka, S. Kashiwagi, A. Yoshida, M. Fujioka, H. Sasajima, A. Nanbo, M. Amano, Y. Ohba

This study identifies VDAC2 as a mitochondrial protein that binds PI3K, tethers endosomes to mitochondria, and promotes endosome maturation through both structural and pore functions.

bioRxiv · Jan 18, 2021 · PreprintCell Biology

Localization of BCR-ABL to stress granules contributes to its oncogenic function

S. Kashiwagi, Y. Fujioka, T. Kondo, A. O. Satho, A. Yoshida, M. Fujioka, H. Sasajima, M. Amano, T. Teshima, Y. Ohba

This study shows BCR-ABL localizes to stress granules, and this localization contributes to its oncogenic function in CML.

bioRxiv · Oct 20, 2019Cell Biology

Folding latency of fluorescent proteins affects the mitochondrial localization of fusion protein

S. Kashiwagi, Y. Fujioka, A. O. Satoh, A. Yoshida, M. Fujioka, P. Nepal, A. Tsuzuki, O. Aoki, S. Paudel, H. Sasajima, Y. Ohba

The paper shows that faster folding fluorescent proteins can mislocalize mitochondrial-targeted fusion proteins, and slowing their folding improves mitochondrial localization.

bioRxiv · Sep 13, 2019Cell Biology