Author

Harry Wilson

King's College LondonORCID 0000-0002-3185-1073Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Assay:structural biology· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

Chad M. SwansoniD· 2 shared Clément R. BoutoniD· 2 shared María José ListaiD· 2 shared Stuart J. D. NeiliD· 2 shared Andrew G. PurkissiD· 1 shared Anob M. ChakrabartiiD· 1 shared Elizabeth R. MorrisiD· 1 shared Grega Gimpelj Domjanič· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersImmunology

Chad M. SwansonORCID

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2 papers

Recent·Most cited

The long isoform of ZAP coordinates multiple enzymes to mediate complete decay of target transcripts

Clément R. Bouton, Grega Gimpelj Domjanič, María José Lista, Rui Pedro Galão, Thomas Courty, Piotr Kwiatkowski, Harry Wilson, Peter W. S. Hill, Hannah E. Mischo, Anob M. Chakrabarti, Mario Poljak, Jernej Ule, Stuart J. D. Neil, Chad M. Swanson

This study identifies how the long ZAP isoform recruits enzymes to degrade viral RNA through a coordinated decay pathway.

Cell Reports · May 1, 2026Peer-reviewedImmunology

Structural and functional characterization of the KHNYN extended-diKH domain for mediating ZAP antiviral activity

Rebecca L Youle, María José Lista, Clément R. Bouton, Simone Kunzelmann, Harry Wilson, M.A. Cottee, Andrew G. Purkiss, Elizabeth R. Morris, Stuart J. D. Neil, Ian A. Taylor, Chad M. Swanson

This study characterizes the KHNYN ex-diKH domain's role in ZAP antiviral activity, revealing its structural features and identifying a potential protein-protein interaction site.

Journal of Biological Chemistry · Feb 19, 2025Peer-reviewedMicrobiology