Author

C. L. Tooke

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Assay:structural biology· 2 Approach:deep learning· 1 Assay:DNA methylation· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Research Focus:gene regulatory network inference· 1

Frequent Co-Authors

J. Spencer· 3 shared A. J. Mulholland· 2 shared A. R. Mack· 1 shared A. S. F. Oliveira· 1 shared C. J. Schofield· 1 shared C. K. Colenso· 1 shared C. Reding· 1 shared E. Olehnovics· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersMicrobiology

J. Spencer

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Harvesting and amplifying gene cassettes confers cross-resistance to critically important antibiotics

P. Dulyayangkul, T. Beavis, W. W. Lee, R. Ardagh, F. Edwards, F. Hamilton, I. Head, K. J. Heesom, O. Mounsey, M. Murarik, C. Reding, N. Satapoomin, J. M. Shaw, Y. Takebayashi, C. L. Tooke, , M. B. Avison

The paper shows that gene cassettes in an integron, amplified by IS26, confer resistance to amikacin and piperacillin/tazobactam, often leaving meropenem as the last-resort antibiotic.

bioRxiv · Dec 2, 2023 · PreprintMicrobiology

Tautomer-specific deacylation and {Omega}-loop flexibility explain carbapenem-hydrolyzing, broad-spectrum activity of the KPC-2 β-lactamase

C. L. Tooke, P. Hinchliffe, M. Beer, K. Zinovjev, C. K. Colenso, C. J. Schofield, A. J. Mulholland, J. Spencer

This study identifies how tautomer-specific deacylation and {Omega}-loop flexibility enable KPC-2 β-lactamase to efficiently hydrolyze carbapenems, revealing structural and energetic mechanisms for its broad-spectrum activity.

bioRxiv · Nov 11, 2022Biochemistry

Allosteric communication in Class A β-lactamases occurs via Cooperative Coupling of Loop Dynamics

I. Galdadas, S. Qu, A. S. F. Oliveira, E. Olehnovics, A. R. Mack, M. F. Mojica, P. K. Agarwal, C. L. Tooke, F. L. Gervasio, J. Spencer, R. A. Bonomo, A. J. Mulholland, S. Haider

This study identifies allosteric communication pathways in Class A β-lactamases using molecular dynamics simulations, showing how amino acid substitutions affect enzyme activity and antibiotic resistance.

bioRxiv · Dec 30, 2020Biophysics