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ProteomicsDirect identification of protein S-palmitoylation sites
S-fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryot...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008399 | Pride
S-palmitoylation Site identification S-fatty-acylation 
ProteomicsTLR9-Driven S-Palmitoylation in Dendritic Cells Reveals Immune and Metabolic Protein Targets
Dendritic cells (DCs) rely on Toll-like receptor 9 (TLR9) to detect unmethylated CpG motifs in microbial DNA, triggering essential immune responses. While the downstream signaling pathways of TLR9 activation are well characterized, their impact on S-palmitoylation is unknown. S-palmitoylation, invol...
ORGANISM(S): Mus musculus (Mouse) 
2025-08-25 | PXD066223 | Pride
Tlr9 Dendritic cells. S-palmitoylation 
ProteomicsS-palmitoylation of synaptic proteins in rat synaptoneurosomes
Temporal and target-specific S-palmitoylation of synaptic proteins supports synapse and neural network plasticity: Synaptic plasticity is a phenomenon essential for learning and memory, which relies on activity-dependent changes in neural connectivity. S-palmitoylation, a reversible posttranslation...
ORGANISM(S): Rattus norvegicus (Rat) 
2025-10-20 | PXD058417 | Pride
Ltp stimulation Synaptoneurosomes Acyl-biotin exchange S-palmitoylation 
ProteomicsS-palmitoylation of MAP kinase is essential for fungal virulence
acylation also called S-palmitoylation is an important reversible protein post-translational modification in organisms. However, its function remains unknown in pathogenic fungi. Here, we found treatment of rice false fungus Ustilaginoidea virens with S-palmitoylation inhibitor 2-BP resulted in a si...
ORGANISM(S): Ustilaginoidea virens 
2024-10-14 | PXD054433 | Pride
S-palmitoylation  biotin  ustilaginoidea virens  virulence 
ProteomicsS-palmitoylation of MAP kinase is essential for fungal virulence
acylation also called S-palmitoylation is an important reversible protein post-translational modification in organisms. However, its function remains unknown in pathogenic fungi. Here, we found treatment of rice false fungus Ustilaginoidea virens with S-palmitoylation inhibitor 2-BP resulted in a si...
ORGANISM(S): Ustilaginoidea virens 
2024-10-14 | PXD048216 | Pride
S-palmitoylation  biotin  ustilaginoidea virens  virulence 
ProteomicsS-palmitoylation during retinoic acid induced neuronal differentiation of SH-SY5Y neuroblastoma cells
S-palmitoylation is the covalent attachment of palmitic acid to cysteine residues through a thioester bond. S-palmitoylation is highly abundant in neurons, where it plays a fundamental role in neuronal development. In addition, S-palmitoylation is associated with many neurodegenerative diseases, inc...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD040613 | Pride
Acyl-biotin exchange Lipid metabolic labelling Protein s-palmitoylation Sh-sy5y differentiation Retinoic acid Mass spectrometry-based proteomics 
ProteomicsMouse Liver S-Palmitoylation ZDHHC13 LC-MS/MS
Protein S-palmitoylation is a reversible post-translational modification which adding 16-carbon palmitate to specific cysteines and contributes to variable biological functions such as protein trafficking, scaffolding and signaling. ZDHHC13 is one of the members of DHHC-containing palmitoyl-acyltran...
ORGANISM(S): Mus musculus (Mouse) 
2017-09-29 | PXD003039 | Pride
Zdhhc13 Mouse S-palmitoylation Liver Lc-ms/ms 
UnknownTopology-driven discovery of transmembrane protein S-palmitoylation.
Not available
S-EPMC11923826 | biostudies-literature
UnknownProtein S-palmitoylation modification: implications in tumor and tumor immune microenvironment.
Not available
S-EPMC10896991 | biostudies-literature
UnknownPRDX6: A protein bridging S-palmitoylation and diabetic neuropathy.
Not available
S-EPMC9478578 | biostudies-literature
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