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

ImmunologybioRxivDec 17, 2021

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

S. C. Trevelin, S. Pickering, K. Todd…·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.

DOI 10.3389/fimmu.2022.838328

humanspatial transcriptomics

𝕏 PostBluesky

MicrobiologybioRxivPreprintJun 22, 2021

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…·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.

DOI 10.1101/2021.06.22.449398

humanproteomics

𝕏 PostBluesky

ImmunologybioRxivPreprintFeb 3, 2021

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…·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.

DOI 10.1101/2021.02.03.429355

humanproteomics

𝕏 PostBluesky