{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Banahene N"],"funding":["Division of Chemistry","Life Sciences Research Foundation","Camille and Henry Dreyfus Foundation","Howard Hughes Medical Institute","Agilent Technologies","NHGRI NIH HHS","ACS Division of Analytical Chemistry","Helen Hay Whitney Foundation","National Human Genome Research Institute","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["12138-12154"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11066868"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146(17)"],"pubmed_abstract":["Protein lipidation dynamically controls protein localization and function within cellular membranes. A unique form of protein <i>O</i>-fatty acylation in <i>Corynebacterium</i>, termed protein <i>O</i>-mycoloylation, involves the attachment of mycolic acids─unusually large and hydrophobic fatty acids─to serine residues of proteins in these organisms' outer mycomembrane. However, as with other forms of protein lipidation, the scope and functional consequences of protein <i>O</i>-mycoloylation are challenging to investigate due to the inherent difficulties of enriching and analyzing lipidated peptides. To facilitate the analysis of protein lipidation and enable the comprehensive profiling and site mapping of protein <i>O</i>-mycoloylation, we developed a chemical proteomics strategy integrat"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Chemical Proteomics Strategies for Analyzing Protein Lipidation Reveal the Bacterial &lt;i&gt;O&lt;/i&gt;-Mycoloylome."],"pmcid":["PMC11066868"],"funding_grant_id":["1654408","T32 HG002760","TH-17-034","P41 GM108538","T32HG002760","P41GM108538"],"pubmed_authors":["Biegas KJ","Banahene N","Kambitsis NH","Johnson UG","Bernhardt TG","McKitterick AC","Peters-Clarke TM","Shishkova E","Hart EM","Coon JJ","Swarts BM"],"additional_accession":[]},"is_claimable":false,"name":"Chemical Proteomics Strategies for Analyzing Protein Lipidation Reveal the Bacterial &lt;i&gt;O&lt;/i&gt;-Mycoloylome.","description":"Protein lipidation dynamically controls protein localization and function within cellular membranes. A unique form of protein <i>O</i>-fatty acylation in <i>Corynebacterium</i>, termed protein <i>O</i>-mycoloylation, involves the attachment of mycolic acids─unusually large and hydrophobic fatty acids─to serine residues of proteins in these organisms' outer mycomembrane. However, as with other forms of protein lipidation, the scope and functional consequences of protein <i>O</i>-mycoloylation are challenging to investigate due to the inherent difficulties of enriching and analyzing lipidated peptides. To facilitate the analysis of protein lipidation and enable the comprehensive profiling and site mapping of protein <i>O</i>-mycoloylation, we developed a chemical proteomics strategy integrat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T08:37:16.408Z","creation":"2026-05-26T03:07:05.164Z"},"accession":"S-EPMC11066868","cross_references":{"pubmed":["38635392"],"doi":["10.1021/jacs.4c02278"]}}