Author

E. M. Williams

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:drug response / drug discovery· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Assay:metagenomics· 1

Frequent Co-Authors

D. F. Ackerley· 3 shared A. V. Sharrock· 2 shared F. Matthews· 2 shared J. S. Mumm· 2 shared K. R. Hall· 2 shared M. H. Rich· 2 shared M. T. Saxena· 2 shared R. F. Little· 2 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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3 shared papersBiochemistry

D. F. Ackerley

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Author profile →

3 papers

Recent·Most cited

A metagenomic library cloning strategy that promotes high-level expression of captured genes to enable efficient functional screening

M. H. Rich, A. V. Sharrock, T. S. Mulligan, F. Matthews, A. S. Brown, H. R. Lee-Harwood, E. M. Williams, J. N. Copp, R. F. Little, J. J. Francis, C. N. Horvat, L. J. Stevenson, J. G. Owen, M. T. Saxena, J. S. Mumm, D. F. Ackerley

This paper introduces a metagenomic library cloning strategy using partial digestion with Fatl to enhance gene expression, enabling the discovery of nitroreductases with novel functions.

Cell Chemical Biology · Dec 1, 2023Peer-reviewedBiochemistry

A giant leap in sequence space reveals the intracellular complexities of evolving a new function

K. R. Hall, K. J. Robins, M. H. Rich, M. J. Calcott, J. Copp, E. M. Williams, R. F. Little, R. Schwörer, G. B. Evans, W. M. Patrick, D. F. Ackerley

The paper evolves an enzyme to detoxify chloramphenicol, revealing that endogenous substrates significantly influence evolutionary trajectories through epistatic interactions.

bioRxiv · May 27, 2020 · PreprintBiochemistry

NTR 2.0: a rationally-engineered prodrug converting enzyme with substantially enhanced efficacy for targeted cell ablation

A. v. Sharrock, T. S. Mulligan, K. R. Hall, E. M. Williams, D. T. White, L. Zhang, F. Matthews, S. Nimmagadda, S. Washington, K. Le, D. Meir-Levi, O. L. Cox, M. T. Saxena, A. Calof, M. E. Lopez-Burks, , J. S. Mumm

This paper describes the development of NTR 2.0, a modified nitroreductase with significantly improved efficacy for targeted cell ablation using metronidazole.

bioRxiv · May 22, 2020Cell Biology