Author

J. L. Brewster

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1

Frequent Co-Authors

P. D. Mace· 3 shared A. E. Burgess· 2 shared S. A. Jamieson· 2 shared A. D. Axtman· 1 shared A. K. Dunbier· 1 shared A. L. Cadell· 1 shared B. L. Parker· 1 shared C. S. Lentz· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersBiochemistry

P. D. Mace

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Author profile →

4 papers

Recent·Most cited

Structure of phage lambda Red-beta(177) annealase shows how it anneals DNA strands during single-strand annealing homologous DNA recombination

T. P. Newing, J. L. Brewster, H. Yu, N. Johnston, L. J. Fitschen, G. Tolun

This paper determines the structure of Red-beta annealase using cryo-EM and proposes a mechanism for DNA strand annealing during homologous recombination.

bioRxiv · Apr 9, 2022Biochemistry

Structural basis for active-site probes targeting Staphylococcus aureus serine hydrolase virulence factors

M. Fellner, C. S. Lentz, S. A. Jamieson, J. L. Brewster, L. Chen, M. Bogyo, P. D. Mace

The paper reports structures of Staphylococcus aureus serine hydrolases and their interactions with inhibitors, revealing functional insights and potential targets for therapeutic development.

bioRxiv · Apr 21, 2020 · PreprintBiochemistry

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