Author

A. E. Burgess

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

P. D. Mace· 3 shared J. L. Brewster· 2 shared A. D. Axtman· 1 shared A. K. Dunbier· 1 shared A. L. Cadell· 1 shared B. L. Parker· 1 shared D. R. Croucher· 1 shared H. D. McMillan· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersBiochemistry

P. D. Mace

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3 papers

Recent·Most cited

Oncogenic truncations of ASXL1 enhance a motif for BRD4 ET-domain binding

A. E. Burgess, T. Kleffmann, P. D. Mace

This study identifies a molecular mechanism by which ASXL1 truncations enhance BRD4 binding through an ET-domain motif, potentially altering transcriptional regulation and offering therapeutic insights.

bioRxiv · Jul 15, 2021Biochemistry

Mechanism of preferential complex formation by Apoptosis Signal-regulating Kinases

S. J. Trevelyan, J. L. Brewster, A. E. Burgess, J. M. Crowther, A. L. Cadell, B. L. Parker, D. R. Croucher, R. C. Dobson, J. M. Murphy, P. D. Mace

This study identifies the mechanism by which ASK1-3 kinases form preferential heterocomplexes through their SAM domains, revealing structural insights into their role in inflammatory signaling.

bioRxiv · Jul 5, 2019Biochemistry

Substrate binding allosterically relieves autoinhibition of the TRIB1 pseudokinase

S. A. Jamieson, Z. Ruan, A. E. Burgess, J. R. Curry, H. D. McMillan, J. L. Brewster, A. K. Dunbier, A. D. Axtman, K. Natarajan, P. D. Mace

The paper shows that substrate binding to TRIB1 pseudokinase induces allosteric changes enabling complex formation with COP1 ubiquitin ligase.

bioRxiv · May 3, 2018Biochemistry