Author

Alice C. Copsey

University of Sussex

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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Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1

Frequent Co-Authors

Charles R. HarringtoniD· 2 shared Claude M. Wischik· 2 shared Karen E. MarshalliD· 2 shared Louise C. SerpelliD· 2 shared Mahmoud Bukar MainaiD· 2 shared Sebastian Scott Oakley· 2 shared Georg MeisliD· 1 shared John M. D. StoreyiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 42 mutual co-author links

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2 shared papersCell Biology

Charles R. HarringtonORCID

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2 papers

Recent·Most cited

A proteomic analysis of the PHF-forming tau fragment (tau297-391) following uptake into differentiated human neuronal SHSY5Y cells

Alice C. Copsey, Sebastian Scott Oakley, Mahmoud Bukar Maina, Robert Parker, Karen E. Marshall, Charles R. Harrington, John M.D. Storey, Claude M. Wischik, Louise C. Serpell

The paper investigates the proteomic response in neuronal cells after exposure to a tau fragment, identifying pathways linked to tau pathology development.

Bioscience Reports · Aug 21, 2026Peer-reviewedCell Biology

Inhibiting disulphide bonding in truncated tau297-391 results in enhanced self-assembly of tau into seed-competent assemblies.

Sebastian Scott Oakley, Karen E. Marshall, Georg Meisl, Alice C. Copsey, Mahmoud Bukar Maina, Robert Milton, Thomas Vorley, John M. D. Storey, Charles R. Harrington, Claude M. Wischik, Wei‐Feng Xue, Louise C. Serpell

This study investigates how inhibiting disulphide bonding in truncated tau affects its self-assembly into seed-competent structures, revealing enhanced aggregation rates and implications for tauopathy research.

bioRxiv · Feb 5, 2025 · PreprintBiochemistry