Author

T. M. Gloster

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:structural biology· 2 Organism:bacteria (other)· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

M. F. White· 3 shared S. Graham· 2 shared S. McQuarrie· 2 shared A. Crowe· 1 shared A. Kumar· 1 shared B. Bode· 1 shared C. J. Leo· 1 shared C. M. Czekster· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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3 shared papersBiochemistry

M. F. White

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Author profile →

4 papers

Recent·Most cited

CRISPR antiphage defence mediated by the cyclic nucleotide-binding membrane protein Csx23

S. Gruschow, S. McQuarrie, K. Ackermann, S. McMahon, B. Bode, T. M. Gloster, M. F. White

This study identifies Csx23 as a CRISPR effector that uses cyclic nucleotide binding to mediate antiphage defence in Vibrio cholerae.

bioRxiv · Nov 24, 2023Microbiology

Structure, dynamics, and inhibition of Staphylococcus aureus m1A22-tRNA methyltransferase

P. Sweeney, A. Crowe, A. Kumar, D. Raju, N. B. Krishna, E. Sutherland, C. J. Leo, G. Fisher, R. Lalitha, L. Muthuraj, G. Sigamani, V. Oehler, S. Synowsky, S. L. Shirran, T. M. Gloster, , R. G. da Silva

This study characterizes the structure, dynamics, and inhibition of Staphylococcus aureus TrmK, identifying a cryptic binding pocket for drug discovery.

bioRxiv · Dec 24, 2021 · PreprintBiochemistry

Tetramerisation of the CRISPR ring nuclease Csx3 facilitates cyclic oligoadenylate cleavage

S. Graham, S. Grüschow, T. M. Gloster, S. McQuarrie, M. F. White, J. S. Athukoralage

The paper identifies Csx3 as a ring nuclease that degrades cyclic tetra-adenylate (cA4), revealing its role in removing cOA molecules after viral infection.

bioRxiv · Apr 28, 2020Biochemistry

Structure and mechanism of a Type III CRISPR defence DNA nuclease activated by cyclic oligoadenylate

S. A. McMahon, W. Zhu, S. Graham, R. Rambo, M. F. White, T. M. Gloster

This paper describes the structure and mechanism of Can1, a cOA-activated CRISPR defence DNA nuclease, showing how cA4 binding activates its DNA nicking activity.

bioRxiv · Sep 26, 2019Biochemistry