Results 21 to 30 of about 21,138,684 (162)
The landscape of renal protein S-acylation in mice with lipid-induced nephrotoxicity [PDF]
Scientific ReportsExcess fat intake is associated with kidney toxicity and dysfunction. Because fatty acids can also be reversibly attached onto cysteine residues and modulate the function of several membrane-bound proteins, we studied the effect of high-fat diet (HFD) on
Fangrui Xiu +5 more
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Assaying Protein S-Acylation in Plants
, 2013 S-acylation is increasingly being recognized as an important posttranslational modification of proteins controlling activity, subcellular localization, microdomain residence, and stability. Heterotrimeric G-proteins and GPCRs are particularly well studied S-acylated proteins, and fast, cheap, reliable methods are required for the analysis of S ...
Piers A. Hemsley +1 more
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Accessory proteins of the zDHHC family of S-acylation enzymes [PDF]
Journal of Cell Science, 2020 ABSTRACT Almost two decades have passed since seminal work in Saccharomyces cerevisiae identified zinc finger DHHC domain-containing (zDHHC) enzymes as S-acyltransferases. These enzymes are ubiquitous in the eukarya domain, with 23 distinct zDHHC-encoding genes in the human genome.
Christine Salaun +4 more
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Enzyme-centric chemoproteomics reveals isomer-specific S-acylation modification networks [PDF]
Nature CommunicationsProtein lipidation is a critical post-translational modification, but the relationship between the fine structure of fatty acids (FAs) and the specificity of lipidation remains largely unexplored.
Pengfei Wu +6 more
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S‐acylation: an orchestrator of the life cycle and function of membrane proteins
The FEBS Journal, 2023 S‐acylation is a covalent post‐translational modification of proteins with fatty acids, achieved by enzymatic attachment via a labile thioester bond. This modification allows for dynamic control of protein properties and functions in association with cell membranes. This lipid modification regulates a substantial portion of the human proteome and plays
Mesquita, Francisco S. +3 more
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Progress toward Understanding Protein S-acylation: Prospective in Plants [PDF]
Frontiers in Plant Science, 2017 S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-translational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond.
Li, Y, Qi, B
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Interactions and S-acylation of Sprouty and SPRED proteins [PDF]
, 2023 Sprouty (Spry)/SPRED proteins are important regulators of the MAPK/ERK signalling pathway, and dysregulation of this pathway can contribute to development of cancer.
Butler, Liam
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S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation [PDF]
EMBO ReportsSmall peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular ...
Wenliang Li +12 more
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Quantitative analysis of S-acylation
S-acylation is a protein post-translational modification that relies on the attachment of a hydrophobic fatty acid chain to a cysteine residue through the formation of a thioester bond.
Carla Busquets Hernández +2 more
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Enzymology of DHHC-mediated Protein S-Acylation [PDF]
, 2011 Protein S-acylation is the post-translational modification of proteins with long-chain fatty acids at cysteine residues via a thioester linkage. The most commonly attached lipid is 16-carbon palmitate, thus the process is often called palmitoylation. Unlike other lipid modifications, protein S-acylation is reversible.
Jennings, Benjamin
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