{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15(32)"],"submitter":["Busquets-Hernandez C"],"pubmed_abstract":["Protein palmitoylation or <i>S</i>-acylation has emerged as a key regulator of cellular processes. Increasing evidence shows that this modification is not restricted to palmitate but it can include additional fatty acids, raising the possibility that differential <i>S</i>-acylation contributes to the fine-tuning of protein activity. However, methods to profile the acyl moieties attached to proteins are scarce. Herein, we report a method for the identification and quantification of lipids bound to proteins that relies on hydroxylamine treatment and mass spectrometry analysis of fatty acid hydroxamates. This method has enabled unprecedented and extensive profiling of the <i>S</i>-acylome in different cell lines and tissues and has shed light on the substrate specificity of some <i>S</i>-acyl"],"journal":["Chemical science"],"pagination":["12845-12855"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11322976"],"repository":["biostudies-literature"],"pubmed_title":["Quantitative analysis of protein lipidation and acyl-CoAs reveals substrate preferences of the <i>S</i>-acylation machinery."],"pmcid":["PMC11322976"],"pubmed_authors":["Tsiotsia A","Ribo S","Triola G","Gratacos-Batlle E","Carbajo D","Blanco-Canosa JB","Busquets-Hernandez C","Chamberlain LH"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative analysis of protein lipidation and acyl-CoAs reveals substrate preferences of the <i>S</i>-acylation machinery.","description":"Protein palmitoylation or <i>S</i>-acylation has emerged as a key regulator of cellular processes. Increasing evidence shows that this modification is not restricted to palmitate but it can include additional fatty acids, raising the possibility that differential <i>S</i>-acylation contributes to the fine-tuning of protein activity. However, methods to profile the acyl moieties attached to proteins are scarce. Herein, we report a method for the identification and quantification of lipids bound to proteins that relies on hydroxylamine treatment and mass spectrometry analysis of fatty acid hydroxamates. This method has enabled unprecedented and extensive profiling of the <i>S</i>-acylome in different cell lines and tissues and has shed light on the substrate specificity of some <i>S</i>-acyl","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2025-04-19T20:40:45.437Z","creation":"2025-04-19T20:40:45.437Z"},"accession":"S-EPMC11322976","cross_references":{"pubmed":["39148806"],"doi":["10.1039/d4sc02235a"]}}