Author

A. M. Ellisdon

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· 2 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:cancer & tumor microenvironment· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Research Focus:differential expression· 1

Frequent Co-Authors

C. Bayly-Jones· 2 shared C. Huang· 2 shared J. C. Whisstock· 2 shared L. D'Andrea· 2 shared M. L. Halls· 2 shared R. B. Schittenhelm· 2 shared A. C. Chueh· 1 shared C. A. Mitchell· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersCancer Biology

C. Bayly-Jones

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Feed-forward stimulation of CAMK2 by the oncogenic pseudokinase PEAK1 generates a therapeutically "actionable" signalling axis in triple negative breast cancer

X. Yang, X. Ma, T. Zhao, D. R. Croucher, E. V. Nguyen, K. C. Clark, C. Hu, S. L. Latham, C. Bayly-Jones, V. C. B. Nguyen, S. Budnar, S. Shin, L. K. Nguyen, T. R. Cotton, A. C. Chueh, , R. J. Daly

This study identifies a novel feed-forward signalling axis between PEAK1 and CAMK2 in TNBC, showing that targeting CAMK2 can inhibit PEAK1-driven oncogenic processes.

bioRxiv · Feb 14, 2024Cancer Biology

The cryo-EM structure of the neurofibromin dimer reveals the molecular basis for von Recklinghausen disease

C. J. Lupton, C. Bayly-Jones, L. D'Andrea, C. Huang, R. B. Schittenhelm, H. Venugopal, J. C. Whisstock, M. L. Halls, A. M. Ellisdon

This paper determines the cryo-EM structure of full-length NF1, revealing its autoinhibited conformation and providing insights into disease mechanisms and therapeutic strategies.

bioRxiv · Feb 18, 2021 · PreprintBiochemistry

Structural analysis of the PTEN:P-Rex2 signalling node reveals how cancer-associated mutations coordinate to hyperactivate Rac1

L. D'Andrea, C. M. Lucato, E. A. Marquez, Y.-G. Chang, S. Civciristov, C. Huang, H. Elmlund, R. B. Schittenhelm, C. A. Mitchell, J. C. Whisstock, M. L. Halls, A. M. Ellisdon

The paper investigates the PTEN:P-Rex2 complex, identifying how cancer mutations disrupt its inhibitory function and hyperactivate Rac1 signaling.

bioRxiv · Apr 11, 2020Biochemistry