Site-specific analysis of protein S-acylation by resin-assisted capture[S] [PDF]
Journal of Lipid Research, 2011 Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain ...
Michael T. Forrester +6 more
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Protein acylation in inflammatory diseases: from mechanisms to therapeutic strategies [PDF]
Cell Communication and SignalingProtein acylation, a critical subset of post-translational modifications (PTMs), serves as a dynamic regulatory mechanism linking cellular metabolism, epigenetic regulation, and inflammatory responses.
Jiayi Ding +4 more
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Improvement of plant resistance to geminiviruses via protein de-S-acylation
Stress BiologyGeminiviruses are an important group of viruses that infect a variety of plants and result in heavy agricultural losses worldwide. The homologs of C4 (or L4) in monopartite geminiviruses and AC4 (or AL4) in bipartite geminiviruses are critical viral ...
Yawen Zhao +11 more
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Dynamic Protein S-Acylation in Plants. [PDF]
Int J Mol Sci, 2019 Lipid modification is an important post-translational modification. S-acylation is unique among lipid modifications, as it is reversible and has thus attracted much attention. We summarize some proteins that have been shown experimentally to be S-acylated in plants. Two of these S-acylated proteins have been matched to the S-acyl transferase.
Zheng L, Liu P, Liu Q, Wang T, Dong J.
europepmc +4 more sources
Protocol for evaluating S-acylated protein membrane affinity using protein-lipid conjugates
STAR ProtocolsSummary: S-acylation of proteins allows their association with membranes. Here, we present a protocol for establishing a platform for membrane affinity evaluation of S-acylated proteins in vitro. We describe steps for preparing lipid-maleimide compounds,
Chunyang Xie +5 more
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Ion channel regulation by protein S-acylation. [PDF]
J Gen Physiol, 2014 Protein S-acylation, the reversible covalent fatty-acid modification of cysteine residues, has emerged as a dynamic posttranslational modification (PTM) that controls the diversity, life cycle, and physiological function of numerous ligand- and voltage-gated ion channels.
Shipston MJ.
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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture. [PDF]
J Vis Exp, 2020 Protein S-acylation, also referred to as S-palmitoylation, is a reversible post-translational modification of cysteine residues with long-chain fatty acids via a labile thioester bond. S-acylation, which is emerging as a widespread regulatory mechanism, can modulate almost all aspects of the biological activity of proteins, from complex formation to ...
Tewari R +3 more
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Progress toward Understanding Protein S-acylation: Prospective in Plants. [PDF]
Front Plant Sci, 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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A composite motif in calcimembrin/C16orf74 dictates multimeric dephosphorylation by calcineurin [PDF]
Nature CommunicationsCalcineurin, the Ca2+/calmodulin-activated protein phosphatase, recognizes substrates and regulators via short linear motifs, PxIxIT and LxVP, which dock to distinct sites on calcineurin to determine enzyme distribution and catalysis, respectively ...
Devin A. Bradburn +6 more
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Correction: The role of protein S-acylation in vascular injury associated with metabolic disorders [PDF]
Frontiers in EndocrinologyYayun Wang +8 more
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