{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Frenal K"],"funding":["Howard Hughes Medical Institute","Medical Research Council","Wellcome Trust"],"pagination":["895-911"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3813974"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(8)"],"pubmed_abstract":["The advent of techniques to study palmitoylation on a whole proteome scale has revealed that it is an important reversible modification that plays a role in regulating multiple biological processes. Palmitoylation can control the affinity of a protein for lipid membranes, which allows it to impact protein trafficking, stability, folding, signalling and interactions. The publication of the palmitome of the schizont stage of Plasmodium falciparum implicated a role for palmitoylation in host cell invasion, protein export and organelle biogenesis. However, nothing is known so far about the repertoire of protein S-acyl transferases (PATs) that catalyse this modification in Apicomplexa. We undertook a comprehensive analysis of the repertoire of Asp-His-His-Cys cysteine-rich domain (DHHC-CRD) PAT"],"journal":["Traffic (Copenhagen, Denmark)"],"pubmed_title":["Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion."],"pmcid":["PMC3813974"],"funding_grant_id":["G0501670)","G0501670","WT098051"],"pubmed_authors":["Rayner JC","Bushell ES","Frenal K","Tay CL","Jia Y","Graindorge A","Soldati-Favre D","Mueller C","Billker O"],"additional_accession":[]},"is_claimable":false,"name":"Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion.","description":"The advent of techniques to study palmitoylation on a whole proteome scale has revealed that it is an important reversible modification that plays a role in regulating multiple biological processes. Palmitoylation can control the affinity of a protein for lipid membranes, which allows it to impact protein trafficking, stability, folding, signalling and interactions. The publication of the palmitome of the schizont stage of Plasmodium falciparum implicated a role for palmitoylation in host cell invasion, protein export and organelle biogenesis. However, nothing is known so far about the repertoire of protein S-acyl transferases (PATs) that catalyse this modification in Apicomplexa. We undertook a comprehensive analysis of the repertoire of Asp-His-His-Cys cysteine-rich domain (DHHC-CRD) PAT","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Aug","modification":"2026-05-01T21:18:04.937Z","creation":"2019-03-27T01:17:53Z"},"accession":"S-EPMC3813974","cross_references":{"pubmed":["23638681"],"doi":["10.1111/tra.12081"]}}