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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 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 
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 
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 
ProteomicsStress-induced changes in the S-palmitoylation and S-nitrosylation of proteins involved in synaptic plasticity
Summary The precise regulation of synaptic integrity is critical for neuronal network connectivity and proper brain function. Essential aspects of the activity and localization of synaptic proteins are regulated by posttranslational modifications. S-palmitoylation is a reversible covalent modificati...
ORGANISM(S): Mus musculus (Mouse) 
2019-07-16 | PXD010822 | Pride
Ptm's interplay Cell signaling Mass spectrometry Postsynaptic density synapse Nitrosylation palmitoylation 
GenomicsZDHHC20-Mediated S-Palmitoylation of YTHDF3 Stabilizes MYC mRNA to Promote Pancreatic Cancer Progression
ZDHHC20-Mediated S-Palmitoylation of YTHDF3 Stabilizes MYC mRNA to Promote Pancreatic Cancer Progression
PRJNA986177 | ENA
UnknownTemporal Profiling Establishes a Dynamic S-Palmitoylation Cycle.
Not available
S-EPMC6192522 | biostudies-literature
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