Author

M. L. Halls

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 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

A. M. Ellisdon· 2 shared C. Huang· 2 shared J. C. Whisstock· 2 shared L. D'Andrea· 2 shared R. B. Schittenhelm· 2 shared A. Giganti· 1 shared B. Liu· 1 shared C. A. Mitchell· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersBiochemistry

A. M. Ellisdon

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Fatty acid binding proteins shape the cellular response to activation of the glucocorticoid receptor

B. Liu, I. R. Chandrashekaran, O. Ilyichova, D. Valour, F. Melchiore, C. Bourrier, A. Giganti, J.-P. Stephan, C. Dacquet, P. Genissel, W. Gosgnach, R. J. Weaver, C. J. Porter, M. J. Scanlon, M. L. Halls

This study shows that certain fatty acid binding proteins (FABPs) modulate glucocorticoid receptor (GR) transcriptional activity in a ligand-dependent manner, potentially enabling more targeted GR-based therapies.

bioRxiv · Jul 2, 2021 · PreprintPharmacology & Toxicology

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