Author

S. Tsukiji

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

Biochemistry· 1 Cell Biology· 1 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Assay:imaging· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. Kawasaki· 1 shared A. Miyawaki· 1 shared C. Oki· 1 shared F. Nakatsu· 1 shared H. Ichise· 1 shared K. Aoki· 1 shared K. Kuwata· 1 shared K. Sumiyama· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 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

1 shared paperCell Biology

A. Kawasaki

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

ORP9-PH domain-based fluorescent reporters for visualizing phosphatidylinositol 4-phosphate dynamics in living cells

M. Ajiki, M. Yoshikawa, T. Miyazaki, A. Kawasaki, K. Aoki, F. Nakatsu, S. Tsukiji

The paper develops fluorescent PI4P reporters based on ORP9-PH domains to visualize PI4P dynamics in living cells across multiple locations with high specificity.

bioRxiv · Dec 14, 2023Cell Biology

Metastatic Single Tumor Cells Evade NK Cell-mediated Killing by Thrombin-mediated Loss of the Activating Ligand CD155/PVR/Necl-5

H. Ichise, S. Tsukamoto, T. Hirashima, Y. Konishi, C. Oki, S. Tsukiji, S. Iwano, A. Miyawaki, K. Sumiyama, K. Terai, M. Matsuda

The paper shows metastatic tumor cells evade NK cell killing by losing CD155/PVR/Necl-5 via thrombin, allowing survival in lung capillaries.

bioRxiv · Jan 15, 2021Immunology

Improved synthetic lipidation-based protein translocation system for SNAP-tag fusion proteins

T. Yoshii, K. Tahara, S. Suzuki, Y. Hatano, K. Kuwata, S. Tsukiji

This paper improves a synthetic lipidation system for translocating SNAP-tag fusion proteins to the plasma membrane, enhancing its applicability for controlling cell-signaling molecules.

bioRxiv · Apr 9, 2020Biochemistry