ArticleACS chemical biology2013
Thiol-ene enabled detection of thiophosphorylated kinase substrates.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Allelic variation in UVR8 modulates thermotolerance-yield tradeoffs in plants.Cell research · 2026Article
- MLX phosphorylation stabilizes the ChREBP-MLX heterotetramer on tandem E-boxes to control carbohydrate and lipid metabolism.Science advances · 2025Article
- MLX phosphorylation stabilizes the ChREBP-MLX heterotetramer on tandem E-boxes to control carbohydrate and lipid metabolism.bioRxiv : the preprint server for biology · 2024Article
- Applications of Thiol-Ene Chemistry for Peptide Science.Frontiers in chemistry · 2020Review
- Auto-thiophosphorylation activity of Src tyrosine kinase.BMC biochemistry · 2016Article
- The photochemical thiol-ene reaction as a versatile method for the synthesis of glutathioneOrganic chemistry frontiers : an international journal of organic chemistry · 2016Article
- Chemical Methods for Encoding and Decoding of Posttranslational Modifications.Cell chemical biology · 2016Review
- A crosslinker based on a tethered electrophile for mapping kinase-substrate networks.Chemistry & biology · 2014Article
- Synthesis of non-linear protein dimers through a genetically encoded Thiol-ene reaction.PloS one · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein phosphorylation is a ubiquitous posttranslational modification that regulates cell signaling in both prokaryotes and eukaryotes. Although the study of phosphorylation has made great progress, several major hurdles remain, including the difficulty of the assignment of endogenous substrates to a discrete kinase and of global phosphoproteomics investigations. We have developed a novel chemical strategy for detecting phosphorylated proteins. This method utilizes adenosine 5'-O-(3-thiotriphosphate) (ATPγS), which results in the transfer of a thiophosphate moiety by a kinase to its substrate(s). This group can subsequently be employed as a nucleophilic handle to promote protein detection. To selectively label thiophosphorylated proteins, cellular thiols (e.g., cysteine-containing proteins) must first be blocked. Most common cysteine-capping strategies rely upon the nucleophilicity of the sulfur group and would therefore also modify the thiophosphate moiety. We hypothesized that the radical-mediated thiol-ene reaction, however, would be selective for cysteine over thiophosphorylated amino acids due to the differences in the electronics and pKa values between these groups. Here, we report rapid and specific tagging of thiophosphorylated proteins in vitro following chemoselective thiol capping using the thiol-ene reaction.
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