Author

M. Stacey

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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Microbiology· 2 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Organism:mouse· 2 Assay:cryo-EM· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Organism:yeast· 1

Frequent Co-Authors

D. J. Rowlands· 2 shared J. Alzahrani· 2 shared J. S. Snowden· 2 shared L. Sherry· 2 shared N. A. Ranson· 2 shared N. J. Stonehouse· 2 shared A. B. Shaw· 1 shared A. Moon-Walker· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersImmunology

D. J. Rowlands

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Lymphocytic choriomeningitis arenavirus utilises tunnelling nanotube-like intercellular connections for cell-to-cell spread

O. Byford, A. B. Shaw, H. N. Tse, A. Moon-Walker, E. O. Saphire, S. P. J. Whelan, M. Stacey, R. Hewson, J. Fontana, J. N. Barr

This paper shows LCMV spreads between cells via tunnelling nanotube-like structures, bypassing extracellular transmission.

bioRxiv · Jun 28, 2023 · PreprintMicrobiology

VelcroVax: a bolt-on vaccine platform technology improves antibody titres against a viral glycoprotein in mice

N. J. Stonehouse, N. J. Kingston, K. Grehan, J. S. Snowden, M. Hassall, J. Alzahrani, G. C. Paesen, L. Sherry, C. R. Hayward, A. Roe, S. Stephen, D. C. Tomlinson, A. Zeltina, K. J. Doores, N. A. Ranson, , D. J. Rowlands

VelcroVax is a vaccine platform that enhances antibody titres against a viral glycoprotein in mice by combining a modified VLP with a SUMO-tagged antigen.

bioRxiv · Apr 22, 2022 · PreprintImmunology

Structural insight into Pichia pastoris fatty acid synthase

J. S. Snowden, J. Alzahrani, L. Sherry, M. Stacey, D. J. Rowlands, N. A. Ranson, N. J. Stonehouse

The paper determines the structure of P. pastoris fatty acid synthase using cryoEM, identifying structural differences from S. cerevisiae FAS and resolving the mobile ACP domain.

bioRxiv · Jan 27, 2021Microbiology