ArticleJournal of proteome research2018
Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites.
Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
43 citing papers in PubMed, 75 citations in OpenAlex.
- Bioorthogonal chemistry for deciphering lipid biology in living systems.RSC chemical biology · 2026Review
- Proteome-Wide Analysis of Palmitoylated Proteins in Macrophages Reveals Novel Insights Into Early Immune Signaling.Proteomics · 2026Article
- Lipid Metabolic Labeling to Study Site- and Lipid-Specific Long-ChainACS chemical biology · 2026Article
- Long-Chain S-Acylation Is a Key Modulator During the Macrophage Inflammatory Response.Molecular & cellular proteomics : MCP · 2026Article
- S-palmitoylation of the v-ATPase subunit RNAseK is necessary for Zika virus infection.Virology journal · 2026Article
- Enzyme-centric chemoproteomics reveals isomer-specific S-acylation modification networks.Nature communications · 2026Article
- Characterization of endogenous SUMOylation sites by click chemistry-based proteomics.Analytical and bioanalytical chemistry · 2025Article
- A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation.Nature biotechnology · 2024Article
- Recruitment, regulation, and release: Control of signaling enzyme localization and function by reversible S-acylation.The Journal of biological chemistry · 2024Review
- Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).Journal of proteome research · 2024Article
- Stearoylation cycle regulates the cell surface distribution of the PCP protein Vangl2.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).bioRxiv : the preprint server for biology · 2024Article
- zDHHC20-driven S-palmitoylation of CD80 is required for its costimulatory function.Acta pharmacologica Sinica · 2024Article
- Amino acid and protein specificity of protein fatty acylation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Discovery and Characterization of IFITMViruses · 2023Review
- S-acylation of p62 promotes p62 droplet recruitment into autophagosomes in mammalian autophagy.Molecular cell · 2023Article
- Article
- Lost in traffic: consequences of altered palmitoylation in neurodegeneration.Frontiers in physiology · 2023Review
- An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion.eLife · 2022Article
- Protein S-Acyl Transferase GhPAT27 Was Associated withPlants (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
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 eukaryotes and is important in mammalian physiology and human diseases. While chemical labeling methods have improved the detection and enrichment of S-fatty-acylated proteins, mapping sites of modification and characterizing the endogenously attached fatty acids are still challenging. Here, we describe the integration and optimization of fatty acid chemical reporter labeling with hydroxylamine-mediated enrichment of S-fatty-acylated proteins and direct tagging of modified Cys residues to selectively map lipid modification sites. This afforded improved enrichment and direct identification of many protein S-fatty-acylation sites compared to previously described methods. Notably, we directly identified the S-fatty-acylation sites of IFITM3, an important interferon-stimulated inhibitor of virus entry, and we further demonstrated that the highly conserved Cys residues are primarily modified by palmitic acid. The methods described here should facilitate the direct analysis of protein S-fatty-acylation sites and their endogenously attached fatty acids in diverse cell types and activation states important for mammalian physiology and diseases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.