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John C. Jewett

Researcher at University of Arizona

Publications -  46
Citations -  3226

John C. Jewett is an academic researcher from University of Arizona. The author has contributed to research in topics: Click chemistry & Bioorthogonal chemistry. The author has an hindex of 14, co-authored 43 publications receiving 2837 citations. Previous affiliations of John C. Jewett include Dartmouth College & Lawrence Berkeley National Laboratory.

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Cu-free click cycloaddition reactions in chemical biology

TL;DR: This tutorial review will summarize the history of this emerging field, as well as recent progress in the development and application of bioorthogonal copper-free click cycloaddition reactions.
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Rapid Cu-free click chemistry with readily synthesized biarylazacyclooctynones

TL;DR: A biarylazacyclooctynone (BARAC) that has exceptional reaction kinetics and whose synthesis is designed to be both modular and scalable is described and employed for live cell fluorescence imaging of azide-labeled glycans.
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Reactivity of biarylazacyclooctynones in copper-free click chemistry

TL;DR: A systematic analysis of the effects of strain and electronics on the reactivity of cyclooctynes with azides through both experimental measurements and computational studies using a density functional theory (DFT) distortion/interaction transition state model suggests a correlation between decreased alkyne bond angle and increasedcyclooctyne reactivity.
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(D)-Amino acid chemical reporters reveal peptidoglycan dynamics of an intracellular pathogen.

TL;DR: A chemical approach for probing PG in vivo via metabolic labeling and bioorthogonal chemistry and click chemistry detection constitute a facile, modular platform that facilitates unprecedented spatial and temporal resolution of PG dynamics in vivo.
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Probing the mycobacterial trehalome with bioorthogonal chemistry.

TL;DR: A strategy for exploitingtrehalose metabolic pathways to label glycolipids in mycobacteria with azide-modified trehalose (TreAz) analogues is described and unique labeling routes that can be harnessed for pathway-targeted investigation of theMycobacterial trehalome are identified.