{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Azizi SA"],"funding":["Swiss National Science Foundation","NIDDK NIH HHS","National Institute of Diabetes and Digestive and Kidney Diseases","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["1648-1654"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9575173"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(10)"],"pubmed_abstract":["Protein S-acylation is a dynamic and reversible lipid post-translational modification that can affect the activity, stability, localization, and interactions of target proteins. Lipid modification occurs on cysteine residues via a thioester bond and in humans is mediated by 23 Asp-His-His-Cys domain-containing protein acyltransferases (DHHC-PATs). The DHHC-PATs have well-known roles in physiology and disease, but much remains to be discovered about their biological function and therapeutic potential. We recently developed cyanomyracrylamide (<b>CMA</b>), an acrylamide-based DHHC inhibitor with key improvements over existing inhibitors. Here we conduct a structure-activity relationship (SAR) study of <b>CMA</b> and its acrylamide derivatives against zDHHC20, the most structurally characteri"],"journal":["ACS medicinal chemistry letters"],"pubmed_title":["Charting the Chemical Space of Acrylamide-Based Inhibitors of zDHHC20."],"pmcid":["PMC9575173"],"funding_grant_id":["F30 DK125088","P2BEP2_188250","R35 GM119840","T32 GM007281"],"pubmed_authors":["Lan T","Dickinson BC","Azizi SA","Qiu T","Delalande C"],"additional_accession":[]},"is_claimable":false,"name":"Charting the Chemical Space of Acrylamide-Based Inhibitors of zDHHC20.","description":"Protein S-acylation is a dynamic and reversible lipid post-translational modification that can affect the activity, stability, localization, and interactions of target proteins. Lipid modification occurs on cysteine residues via a thioester bond and in humans is mediated by 23 Asp-His-His-Cys domain-containing protein acyltransferases (DHHC-PATs). The DHHC-PATs have well-known roles in physiology and disease, but much remains to be discovered about their biological function and therapeutic potential. We recently developed cyanomyracrylamide (<b>CMA</b>), an acrylamide-based DHHC inhibitor with key improvements over existing inhibitors. Here we conduct a structure-activity relationship (SAR) study of <b>CMA</b> and its acrylamide derivatives against zDHHC20, the most structurally characteri","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-05-28T02:15:35.398Z","creation":"2025-04-04T11:00:30.6Z"},"accession":"S-EPMC9575173","cross_references":{"pubmed":["36262404"],"doi":["10.1021/acsmedchemlett.2c00336"]}}