Author

R. A. Lawrenson

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· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

J. E. Pease· 2 shared S. Sriskandan· 2 shared A. Fosberry· 1 shared C. Haslam· 1 shared D. Mossakowska· 1 shared E. J. Jones· 1 shared J. C. Brown· 1 shared J. Goldblatt· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersMicrobiology

J. E. Pease

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Author profile →

2 papers

Recent·Most cited

Structure-activity studies of Streptococcus pyogenes enzyme SpyCEP reveal high affinity for CXCL8 in the SpyCEP C-terminal

M. Pearson, C. Haslam, A. Fosberry, E. J. Jones, M. Reglinski, R. J. Edwards, R. A. Lawrenson, J. C. Brown, D. Mossakowska, J. E. Pease, S. Sriskandan

This study investigates SpyCEP's enzymatic function, revealing the C-terminal's role in substrate binding and the N-terminal's necessity for full catalytic activity.

bioRxiv · Nov 14, 2021 · PreprintMicrobiology

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