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Activation of an atypical plant NLR with an N-terminal deletion initiates cell death at the vacuole.
EMBO Rep
October 2024
Centre for Plant Molecular Biology, University of Tübingen, 72076, Tübingen, Germany.
Plants evolve nucleotide-binding leucine-rich repeat receptors (NLRs) to induce immunity. Activated coiled-coil (CC) domain containing NLRs (CNLs) oligomerize and form apparent cation channels promoting calcium influx and cell death, with the alpha-1 helix of the individual CC domains penetrating the plasma membranes. Some CNLs are characterized by putative N-myristoylation and S-acylation sites in their CC domain, potentially mediating permanent membrane association.
View Article and Find Full Text PDFQuantitative analysis of protein lipidation and acyl-CoAs reveals substrate preferences of the -acylation machinery.
Chem Sci
August 2024
Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC) Barcelona Spain
Protein palmitoylation or -acylation has emerged as a key regulator of cellular processes. Increasing evidence shows that this modification is not restricted to palmitate but it can include additional fatty acids, raising the possibility that differential -acylation contributes to the fine-tuning of protein activity. However, methods to profile the acyl moieties attached to proteins are scarce.
View Article and Find Full Text PDFAnalysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).
J Proteome Res
August 2024
Division of Pulmonary, Allergy and Critical Care Medicine, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Proteins undergo reversible -acylation via a thioester linkage in vivo. -palmitoylation, modification by C16:0 fatty acid, is a common -acylation that mediates critical protein-membrane and protein-protein interactions. The most widely used -acylation assays, including acyl-biotin exchange and acyl resin-assisted capture, utilize blocking of free Cys thiols, hydroxylamine-dependent cleavage of the thioester and subsequent labeling of nascent thiol.
View Article and Find Full Text PDFA rapid and convenient sample treatment method based on the dissolvable polyacrylamide gel for -acylation proteomics.
Anal Methods
July 2024
Department of Chemistry and Liver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai, 200438, People's Republic of China.
Protein -acylation is an important lipid modification and plays a series of biological functions. As a classic proteomic method for -acylated proteome analysis, the acyl-biotin exchange and its derivative methods are known to be very labour-intensive and time-consuming all the time, and will result in significant sample loss. Multiple methanol-chloroform precipitations are involved in order to remove the substances that would interfere with enrichment and identification including detergents, the residual reduction and alkylation reagents.
View Article and Find Full Text PDFProtocol to identify S-acylated proteins in hippocampal neurons using ω-alkynyl fatty acid analogs and click chemistry.
STAR Protoc
June 2024
Department of Molecular and Cellular Biology, College of Biological Sciences, University of Guelph, 50 Stone Road E, Guelph, ON N1G 2W1, Canada. Electronic address:
S-acylation, commonly palmitoylation, is the addition of fatty acids to cysteines to regulate protein localization and function. S-acylation detection has been hampered by limited sensitivity and selectivity in low-protein, costly samples like cultured neurons. Here, we present a protocol for sensitive and selective bioorthogonal labeling and click-chemistry-based detection of S-acylated proteins in primary hippocampal neurons.
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