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Article

Optimized allosteric inhibition of engineered protein tyrosine phosphatases with an expanded palette of biarsenical small molecules.

Bioorganic & medicinal chemistry - 15 May 2018

Korntner Samuel, Pomorski Adam, Krężel Artur, Bishop Anthony C

Abstract excerpt

Protein tyrosine phosphatases (PTPs), which catalyze the dephosphorylation of phosphotyrosine in protein substrates, are important cell-signaling regulators, as well as potential drug targets for a range of human diseases. Chemical tools for selectively targeting the activities of individual PTPs would help to elucidate PTP signaling roles and potentially expedite the validation of PTPs as therapeutic targets. We...

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Identifiers

PMID: 29673715
DOI: 10.1016/j.bmc.2018.04.026
PMCID: PMC5935566

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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