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Elsie M. Williams

Researcher at Victoria University of Wellington

Publications -  26
Citations -  464

Elsie M. Williams is an academic researcher from Victoria University of Wellington. The author has contributed to research in topics: Nitroreductase & Prodrug. The author has an hindex of 9, co-authored 23 publications receiving 332 citations. Previous affiliations of Elsie M. Williams include Emory University & Wellington Management Company.

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Nitroreductase gene-directed enzyme prodrug therapy: insights and advances toward clinical utility

TL;DR: This review examines the vast catalytic and therapeutic potential offered by type I nitroreductase enzymes in partnership with nitroaromatic prodrugs, with particular focus on gene-directed enzyme prodrug therapy (GDEPT; a form of cancer gene therapy).
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Engineering a Multifunctional Nitroreductase for Improved Activation of Prodrugs and PET Probes for Cancer Gene Therapy.

TL;DR: Evidence is provided that the dominant contribution to improved PR-104A activity was enhanced affinity for the prodrug over-competing intracellular substrates, suggesting optimal usefulness in bacterial rather than viral GDEPT vectors.
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Creation and screening of a multi-family bacterial oxidoreductase library to discover novel nitroreductases that efficiently activate the bioreductive prodrugs CB1954 and PR-104A

TL;DR: The utility of a flexible screening system based on the Escherichia coli SOS response to evaluate novel nitroreductase enzymes and prodrugs in concert is demonstrated, and a library of 47 candidate genes representing 11 different oxidoreductase families was created and screened to identify the most efficient activators of two different nitroaromatic pro drugs.
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Pore Engineering for Enhanced Mass Transport in Encapsulin Nanocompartments.

TL;DR: This study demonstrates the high tolerance of encapsulin for protein engineering and has created a set of novel, functionally improved scaffolds for applications as bionanoreactors.
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Reduction of quinones and nitroaromatic compounds by Escherichia coli nitroreductase A (NfsA): Characterization of kinetics and substrate specificity.

TL;DR: Evidence is presented that the reduction of quinones by NfsA is most consistent with a single-step (H-) hydride transfer mechanism, and this step is much faster than the steady-state turnover number.