Author

S. Kanegasaki

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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Immunology· 2

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Approach:statistical model· 1

Frequent Co-Authors

J. E. Pease· 2 shared T. Tsuchiya· 2 shared D. P. Dyer· 1 shared H. L. Birchenough· 1 shared J. Goldblatt· 1 shared K. T. Mincham· 1 shared L. Muir· 1 shared R. A. Lawrenson· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersImmunology

J. E. Pease

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Author profile →

2 papers

Recent·Most cited

CXCL17 binds efficaciously to glycosaminoglycans with the potential to modulate chemokine signalling

S. P. Giblin, S. Ranawana, S. Hassibi, H. L. Birchenough, K. T. Mincham, R. J. Snelgrove, T. Tsuchiya, S. Kanegasaki, D. P. Dyer, J. E. Pease

This study investigates CXCL17's structural and functional properties, finding it does not act as a chemokine but binds glycosaminoglycans and modulates chemotaxis.

bioRxiv · Jul 7, 2023 · PreprintImmunology

A requirement for neutrophil glycosaminoglycans in chemokine:receptor interactions is revealed by the streptococcal protease SpyCEP

J. Goldblatt, R. A. Lawrenson, L. Muir, S. Dattani, T. Tsuchiya, S. Kanegasaki, S. Sriskandan, J. E. Pease

This study shows that SpyCEP cleavage of CXCL8 impairs chemokine-receptor interactions by disrupting glycosaminoglycan binding, affecting neutrophil migration.

bioRxiv · Dec 18, 2018Immunology