Author

S. J. D. Neil

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

Immunology· 2 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:human· 3 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Assay:imaging· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

M. Shankar-Hari· 2 shared S. Pickering· 2 shared A. C. Hayday· 1 shared A. G. Laing· 1 shared A. Green· 1 shared A. Rosa· 1 shared C. Bishop· 1 shared C. Graham· 1 shared

Activity by Year

2021-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 21 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

2 shared papersImmunology

M. Shankar-Hari

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Disrupted Peyer's patch microanatomy in COVID-19 including germinal centre atrophy independent of local virus

S. C. Trevelin, S. Pickering, K. Todd, C. Bishop, M. Pitcher, J. G. Mesa, L. Montorsi, F. Spada, N. Petrov, A. Green, M. Shankar-Hari, S. J. D. Neil, J. Spencer

This study examines the impact of COVID-19 on ileal Peyer's patches, finding disrupted microanatomy and germinal centre atrophy independent of local viral load.

bioRxiv · Dec 17, 2021Immunology

The C-terminal PARP domain of the long ZAP isoform contributes essential effector functions for CpG-directed antiviral activity

D. Kmiec, M. J. Lista, M. Ficarelli, C. Swanson, S. J. D. Neil

This study identifies the C-terminal PARP domain and CaaX box of ZAP-L as essential for CpG-directed antiviral activity by modulating cofactor interactions and subcellular localization.

bioRxiv · Jun 22, 2021 · PreprintMicrobiology

Impact of the B.1.1.7 variant on neutralizing monoclonal antibodies recognizing diverse epitopes on SARS-CoV-2 Spike

C. Graham, J. Seow, I. Huettner, H. Khan, N. Kouphou, S. Acors, H. Winstone, S. Pickering, R. Pedro Galao, M. Jose Lista, J. M. Jimenez-Guardeno, A. G. Laing, Y. Wu, M. Joseph, L. Muir, , K. J. Doores

This study examines how mutations in the B.1.1.7 variant of SARS-CoV-2 affect neutralization by monoclonal antibodies targeting non-RBD epitopes.

bioRxiv · Feb 3, 2021 · PreprintImmunology