Author

K. Wilkinson

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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Cell Biology· 4

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 4 Approach:experimental assay· 4 Research Focus:cancer & tumor microenvironment· 2 Research Focus:cell type annotation· 2 Research Focus:development & morphogenesis· 2 Assay:bulk RNA-seq· 1 Research Focus:differential expression· 1 Organism:human· 1

Frequent Co-Authors

J. Henley· 4 shared L. Lee· 2 shared R. Seager· 2 shared Y. Nakamura· 2 shared C. Guo· 1 shared H. I. Needs· 1 shared I. Collinson· 1 shared N. Rawlings· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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4 shared papersCell Biology

J. Henley

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4 papers

Recent·Most cited

SUMOylation of MFF is required for stress-induced mitochondrial fission

R. Seager, N. Shree Ramesh, S. Cross, C. Guo, K. Wilkinson, J. Henley

The paper shows that SUMOylation of MFF at Lys151, induced by AMPK phosphorylation under stress, promotes mitochondrial fission by altering the DRP1-MiD-MFF complex.

bioRxiv · May 5, 2023 · PreprintCell Biology

Perturbation of the mitochondrial import machinery by aggregation prone Tau affects organelle morphology and reduces neuronal complexity

H. I. Needs, K. Wilkinson, J. Henley, I. Collinson

This study investigates how TauP301L affects mitochondrial import, morphology, and function in neurons, revealing a link between aggregation-prone proteins and neurodegeneration.

bioRxiv · Nov 30, 2022 · PreprintCell Biology

Parkin-mediated ubiquitination contributes to the constitutive turnover of mitochondrial fission factor (Mff)

L. Lee, R. Seager, Y. Nakamura, K. Wilkinson, J. Henley

This study shows Parkin ubiquitinates Mff under basal conditions to regulate its constitutive turnover, independent of PINK1 and stress.

bioRxiv · Apr 4, 2019Cell Biology

Protective role of the deSUMOylating enzyme SENP3 in myocardial ischaemia-reperfusion injury

N. Rawlings, L. Lee, Y. Nakamura, K. Wilkinson, J. Henley

This study shows that SENP3 levels decrease during cardiac ischaemia and reperfusion, and its loss increases cell death, suggesting a protective role in myocardial injury.

bioRxiv · Feb 21, 2019Cell Biology