Redox-based probes for protein tyrosine phosphatases

Stephen E. Leonard; Francisco J. Garcia; David S. Goodsell; Kate S. Carroll

doi:10.1002/anie.201007871

Redox-based probes for protein tyrosine phosphatases

Stephen E. Leonard, Francisco J. Garcia, David S. Goodsell, Kate S. Carroll

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

Three in one: The design strategy for redox-based probes (RBPs) that detect the reversible oxidation of protein tyrosine phosphatases (PTPs) includes a "warhead" that forms a covalent adduct with the oxidized active site cysteine of PTPs, a synthetic module that directs binding to the PTP active site, and a chemical reporter tag used for the identification, purification, or direct visualization of the probe-labeled proteins (see picture).

Original language	English (US)
Pages (from-to)	4423-4427
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	19
DOIs	https://doi.org/10.1002/anie.201007871
State	Published - May 2 2011
Externally published	Yes

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry

Keywords

chemoselectivity
cysteine oxidation
protein modifications
redox chemistry
tyrosine phosphatase

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10.1002/anie.201007871

Cite this

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AU - Garcia, Francisco J.

AU - Goodsell, David S.

AU - Carroll, Kate S.

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KW - chemoselectivity

KW - cysteine oxidation

KW - protein modifications

KW - redox chemistry

KW - tyrosine phosphatase

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Redox-based probes for protein tyrosine phosphatases

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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