Author

Karen E. Marshall

University of SussexORCID 0000-0001-5056-2317Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Cell Biology· 1 Neuroscience· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell-cell communication· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1

Frequent Co-Authors

Louise C. SerpelliD· 3 shared Alice C. Copsey· 2 shared Charles R. HarringtoniD· 2 shared Claude M. Wischik· 2 shared Mahmoud Bukar MainaiD· 2 shared Sebastian Scott Oakley· 2 shared Devkee M. VadukuliD· 1 shared Georg MeisliD· 1 shared

Activity by Year

2019-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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3 shared papersCell Biology

Louise C. SerpellORCID

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3 papers

Recent·Most cited

Cell BiologyBioscience ReportsPeer-reviewedAug 21, 2026

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…·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.

DOI 10.1042/bsr20260349

humanproteomics

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BiochemistrybioRxivPreprintFeb 5, 2025

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…·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.

DOI 10.1101/2025.02.05.636249

proteomicsexperimental assay

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NeurosciencebioRxivPreprintApr 15, 2019

Misfolded Amyloid β-42 induced impairment of the endo-lysosomal pathway revealed by real-time optical monitoring

Karen E. Marshall, Devkee M. Vadukul, Kevin Staras, Louise C. Serpell

The paper uses optical reporters to show that Aβ42 oligomers disrupt the endo-lysosomal pathway by impairing protein uptake and causing lysosomal accumulation.

1 citation

imagingexperimental assay

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