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 | |
| 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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