Mr Michael Oliver
- Research Associate (Virology)
The University of Glasgow uses cookies for analytics. Find out more about our Privacy policy.
Necessary cookies enable core functionality. The website cannot function properly without these cookies, and can only be disabled by changing your browser preferences.
Analytical cookies help us improve our website. We use Google Analytics. All data is anonymised.
Hotjar and Clarity help us to understand our users’ behaviour by visually representing their clicks, taps and scrolling. All data is anonymised.
Oliver, M. R. , Toon, K. , Lewis, C. B., Devlin, S., Gifford, R. J. and Grove, J. (2023) Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism. PLoS Biology, 21(7), e3002174. (doi: 10.1371/journal.pbio.3002174) (PMID:37432947) (PMCID:PMC10335668)
Oliver, M. R. et al. (2021) Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix. Nature Communications, 12(1), 1002. (doi: 10.1038/s41467-021-21191-7) (PMID:33579933) (PMCID:PMC7881018)
Oliver, M. R. , Toon, K. , Lewis, C. B., Devlin, S., Gifford, R. J. and Grove, J. (2023) Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism. PLoS Biology, 21(7), e3002174. (doi: 10.1371/journal.pbio.3002174) (PMID:37432947) (PMCID:PMC10335668)
Oliver, M. R. et al. (2021) Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix. Nature Communications, 12(1), 1002. (doi: 10.1038/s41467-021-21191-7) (PMID:33579933) (PMCID:PMC7881018)
https://orcid.org/0000-0002-1838-8416