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ProteomicsPrenylcysteine oxidase 1 like protein is required for neutrophil bactericidal activities
The bactericidal function of neutrophils are dependent on myriad intrinsic and extrinsic stimuli. Using systems immunology approaches we identified microbiome- and infection-induced changes in neutrophils. We focused on investigating the Prenylcysteine oxidase 1 like (Pcyox1l) protein function. Muri...
ORGANISM(S): Mus musculus (Mouse) 
2023-04-14 | PXD031115 | Pride
Neutrophil Prenylation Pcyox1l 
ProteomicsIn Vivo Metabolic Labeling with an Isoprenoid Probe Reveals APOE Allele-specific Differences in the Prenylome
Prenylation is a ubiquitous process in eukaryotes consisting of the irreversible post-translational modification of proteins through the attachment of a lipophilic isoprenoid moiety to a cysteine residue near their C-terminus. Due to the important functional roles of prenylated proteins, their parti...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-27 | PXD063356 | Pride
Prenylation Apoe3 Liver Kidney Transgenic mice Apoe4 
ProteomicsIn vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins
Dysregulated prenylation has been implicated in the many diseases, including Alzheimer’s disease (AD). Prenylomic analysis, the combination of metabolic incorporation of an isoprenoid analogue (C15AlkOPP) into prenylated proteins with a bottom-up proteomic analysis, has allowed identification of pre...
ORGANISM(S): Mus musculus (Mouse) 
2022-10-28 | PXD032350 | Pride
Altzhimer's disease Brain Prenylation Prenylomics Mice 
ProteomicsImproved synthesis and application of an alkyne-functionalized isoprenoid analogue to study the prenylomes of motor neurons, astrocytes and their stem cell progenitors
Protein prenylation is one example of a broad class of post-translational modifications where proteins are covalently linked to various hydrophobic moieties. To globally identify and monitor levels of all prenylated proteins in a cell simultaneously, our laboratory and others have developed chemical...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2024-05-21 | PXD040354 | Pride
Prenylation Astrocytes Als Chemical enrichment Neurons 
ProteomicsBroadening the Utility of Farnesyltransferase-Catalyzed Protein Labeling Using Norbornene–Tetrazine Click Chemistry
Bio-orthogonal chemistry has gained widespread use in the study of many biological systems of interest, including protein prenylation. Prenylation is a post-translational modification in which a 15 or 20 carbon isoprenoid chain is transferred onto a cysteine near the C-terminus of a target protein. ...
ORGANISM(S): Homo sapiens (Human) 
2024-05-21 | PXD045277 | Pride
Prenylation Lfq Click chemistry 
ProteomicsA chemistry-based orthogonal enzyme-substrate design strategy for discovery of substrates of protein palmitoyltransferases
Attachment of lipids to proteins is a key form of protein modification which intersects with all areas of cellular physiology 1 . Of these, the most pervasive form of protein lipidation is protein S-acylation, also commonly known as protein palmitoylation. Protein palmitoylation is a post-translatio...
ORGANISM(S): Homo sapiens (Human) 
2023-10-04 | PXD041525 | Pride
Palmitoylation Palmitoyltransferases Bump-hole 
ProteomicsThinking outside the CaaX-box: an unusual reversible prenylation on ALDH9A1
Protein lipidation is a post-translational modification that confers hydrophobicity on protein substrates to control their cellular localization, mediate protein trafficking, and regulate protein function. In particular, protein prenylation is a C-terminal modification on proteins bearing canonical ...
ORGANISM(S): Homo sapiens (Human) 
2023-11-06 | PXD036365 | Pride
Prenyaltion Lipidation Aldh9a1 Prenylomics Proteomics 
UnknownExtended pharmacological thromboprophylaxis and clinically relevant venous thromboembolism after major abdominal and pelvic surgery: international, prospective, propensity score-weighted cohort study.
Not available
S-EPMC11894929 | biostudies-literature
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