{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fan AT"],"funding":["NCI NIH HHS","NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["e202417272"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11890178"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["64(5)"],"pubmed_abstract":["Bifunctional molecules such as targeted protein degraders induce proximity to promote gain-of-function pharmacology. These powerful approaches have gained broad traction across academia and the pharmaceutical industry, leading to an intensive focus on strategies that can accelerate their identification and optimization. We and others have previously used chemical proteomics to map degradable target space, and these datasets have been used to develop and train multiparameter models to extend degradability predictions across the proteome. In this study, we now turn our attention to develop generalizable chemistry strategies to accelerate the development of new bifunctional degraders. We implement lysine-targeted reversible-covalent chemistry to rationally tune the binding kinetics at the pro"],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["A Kinetic Scout Approach Accelerates Targeted Protein Degrader Development."],"pmcid":["PMC11890178"],"funding_grant_id":["T32 CA009523","T32 GM007198","T32 GM139795","DP2 NS132610","T32 GM146648"],"pubmed_authors":["Jiang J","Smith ER","Chaudhry C","Sellers WR","Poirier GJ","Dunne-Dombrink K","Tao AJ","Ferguson FM","Huang HT","Sigua LH","Gadbois GE","Goyal P","Donovan KA","Wu S","Fan AT","Fischer ES"],"additional_accession":[]},"is_claimable":false,"name":"A Kinetic Scout Approach Accelerates Targeted Protein Degrader Development.","description":"Bifunctional molecules such as targeted protein degraders induce proximity to promote gain-of-function pharmacology. These powerful approaches have gained broad traction across academia and the pharmaceutical industry, leading to an intensive focus on strategies that can accelerate their identification and optimization. We and others have previously used chemical proteomics to map degradable target space, and these datasets have been used to develop and train multiparameter models to extend degradability predictions across the proteome. In this study, we now turn our attention to develop generalizable chemistry strategies to accelerate the development of new bifunctional degraders. We implement lysine-targeted reversible-covalent chemistry to rationally tune the binding kinetics at the pro","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-06T22:33:20.826Z","creation":"2026-06-06T03:10:41.673Z"},"accession":"S-EPMC11890178","cross_references":{"pubmed":["39602499"],"doi":["10.1002/anie.202417272"]}}