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OtherAnalysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.
PRIDE ID: 17889. Data published as part of Cell Host Microbe. 2012 Aug 16;12(2):246-58 [[http://www.ncbi.nlm.nih.gov/pubmed/22901544 PubMed]]. From the Abstract: {{i}} ... sing complementary palmitoyl protein purification approaches and quantitative mass spectrometry, we examined protein palmitoylat...
ORGANISM(S): Human, Plasmodium_falciparum_refseq 
GPM11210004611 | GPMDB
Resource Reanalysis 
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 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 
GenomicsPalmitoylation negatively regulates AEG-1 function
Palmitoylation negatively regulates AEG-1 function
PRJNA888790 | ENA
ProteomicsEnrichment of Cysteine S-palmitoylated peptides using Sodium Deoxycholate Acid Precipitation - SDC-ACE
S-palmitoylation is a poorly understood post-translational modification that is gaining more attention as an essential regulator of cellular processes. The reversible nature of S-palmitoylation allows for fine-tuned control of cellular events and adaptation to stimuli. The enrichment of S-palmitoyla...
ORGANISM(S): Mus musculus (Mouse) Acyrthosiphon pisum (Pea aphid) 
2026-02-16 | PXD054682 | Pride
Cysteine palmitoylation  mouse brain palmitoylome  dbdb mice  mouse tissue specific palmitoylation 
ProteomicsDynamic Palmitoylation Events Following T-Cell Receptor Signaling
Palmitoylation is the reversible addition of palmitate to cysteine via a thioester linkage. The reversible nature of this modification makes it a prime candidate as a mechanism for regulating signal transduction in T-cell receptor signaling. Following stimulation of the T-cell receptor we find a num...
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD018703 | Pride
Lat Dhhc20 Palmitoylation S-acylation Ti-vamp Palmitome Vamp7 Dhhc pats Tcr signaling In vitro palmitoylation T-cell activation Dhhc18 
ProteomicsPharmacological Targeting of DHHC9-Mediated STRN4 Palmitoylation to Suppress YAP-Driven Cancer Metastasis
Protein S-palmitoylation, a dynamic and reversible post-translational modification involving the attachment of palmitate to cysteine residues, is a key regulator of protein functionality and cellular signaling. Dysregulation of this modification has emerged as a critical driver of cancer progression...
ORGANISM(S): Homo sapiens (Human) 
2025-09-15 | PXD060045 | Pride
Human Proteomics Protein s-palmitoylation 
TranscriptomicsPalmitoylation negatively regulates AEG-1 function
In vitro studies revealed that AEG-1 is palmitoylated at cysteine at a.a. 75 position. In order to check how palmitoylation regulates AEG-1 function in vivo we generated a knockin moue using CRISPR/Cas9 taking in which cysteine 75 was mutated to serine (AEG-1-C75S). Hepatocytes were isolated from AE...
ORGANISM(S): Mus musculus 
2023-01-25 | GSE215113 | GEO
ProteomicsDynamic Palmitoylation Events Following T-Cell Receptor Signaling
Palmitoylation is the reversible addition of palmitate to cysteine via a thioester linkage. The reversible nature of this modification makes it a prime candidate as a mechanism for regulating signal transduction in T-cell receptor signaling. Following stimulation of the T-cell receptor we find a num...
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD018710 | Pride
Lat Dhhc20 Palmitoylation S-acylation Ti-vamp Palmitome Vamp7 Dhhc pats Tcr signaling In vitro palmitoylation T-cell activation Dhhc18 
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