{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Anny CA"],"funding":["H2020 Marie"],"pagination":["e202500547"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12781144"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(1)"],"pubmed_abstract":["A novel strategy based on genetic code expansion combined with click chemistry for the simultaneous visualization of distinct posttranslational modification (PTM) states of a single protein within living cells. As a model, it is focused on threonine 41 (T41) of β-catenin, a regulatory hotspot implicated in epithelial cancers and known to be phosphorylated, O-GlcNAcylated, or left unmodified. Using site-specific incorporation of the unnatural phenylselenocysteine, a β-catenin-EGFP fusion protein is engineered allowing selective installation of a S-GlcNAc moiety via oxidative elimination and thiol-Michael ligation. Additional β-catenin variants, phosphomimetic T41E-mCherry and wild-type-blue fluorescent protein fusions, are produced to represent other PTM states. All constructs are successfu"],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["Simultaneous Visualization of Distinct Posttranslational Modification States of β-Catenin Using Genetic Code Expansion and Click Chemistry."],"pmcid":["PMC12781144"],"funding_grant_id":["847568"],"pubmed_authors":["Biot C","Huvent I","Schulz C","Anny CA","Bray F","Lefebvre T","Spriet C","Nouaille S","Faure R"],"additional_accession":[]},"is_claimable":false,"name":"Simultaneous Visualization of Distinct Posttranslational Modification States of β-Catenin Using Genetic Code Expansion and Click Chemistry.","description":"A novel strategy based on genetic code expansion combined with click chemistry for the simultaneous visualization of distinct posttranslational modification (PTM) states of a single protein within living cells. As a model, it is focused on threonine 41 (T41) of β-catenin, a regulatory hotspot implicated in epithelial cancers and known to be phosphorylated, O-GlcNAcylated, or left unmodified. Using site-specific incorporation of the unnatural phenylselenocysteine, a β-catenin-EGFP fusion protein is engineered allowing selective installation of a S-GlcNAc moiety via oxidative elimination and thiol-Michael ligation. Additional β-catenin variants, phosphomimetic T41E-mCherry and wild-type-blue fluorescent protein fusions, are produced to represent other PTM states. All constructs are successfu","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-06T12:43:04.406Z","creation":"2026-05-30T03:11:16.505Z"},"accession":"S-EPMC12781144","cross_references":{"pubmed":["41387094"],"doi":["10.1002/cbic.202500547"]}}