{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shao Q"],"funding":["Mark Foundation For Cancer Research","Apple Tree Partners","National Cancer Institute","NCI NIH HHS","NIH HHS"],"pagination":["24788-24799"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12011284"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146(36)"],"pubmed_abstract":["14-3-3 proteins have a unique ability to bind and sequester a multitude of diverse phosphorylated signaling proteins and transcription factors. Many previous studies have shown that interactions of 14-3-3 with specific phosphorylated substrate proteins can be enhanced through small-molecule natural products or fully synthetic molecular glue interactions. However, enhancing 14-3-3 interactions with both therapeutically intractable transcription factor substrates and potential neo-substrates to sequester and inhibit their function remains elusive. One of the 14-3-3 proteins, 14-3-3σ or SFN, has cysteine C38 at the substrate-binding interface, near the sites where previous 14-3-3 molecular glues have been found to bind. In this study, we screen a fully synthetic cysteine-reactive covalent lig"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Targeted Protein Localization by Covalent 14-3-3 Recruitment."],"pmcid":["PMC12011284"],"funding_grant_id":["S10 OD024998","R35 CA263814","R35CA263814"],"pubmed_authors":["Nomura DK","Duong TN","Park I","Orr LM","Shao Q"],"additional_accession":[]},"is_claimable":false,"name":"Targeted Protein Localization by Covalent 14-3-3 Recruitment.","description":"14-3-3 proteins have a unique ability to bind and sequester a multitude of diverse phosphorylated signaling proteins and transcription factors. Many previous studies have shown that interactions of 14-3-3 with specific phosphorylated substrate proteins can be enhanced through small-molecule natural products or fully synthetic molecular glue interactions. However, enhancing 14-3-3 interactions with both therapeutically intractable transcription factor substrates and potential neo-substrates to sequester and inhibit their function remains elusive. One of the 14-3-3 proteins, 14-3-3σ or SFN, has cysteine C38 at the substrate-binding interface, near the sites where previous 14-3-3 molecular glues have been found to bind. In this study, we screen a fully synthetic cysteine-reactive covalent lig","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-06-02T04:15:02.79Z","creation":"2025-07-03T03:04:51.729Z"},"accession":"S-EPMC12011284","cross_references":{"pubmed":["39196545"],"doi":["10.1021/jacs.3c12389"]}}