Results 11 to 20 of about 31,021 (196)
Mechanisms and functions of protein S-acylation [PDF]
Nature Reviews Molecular Cell BiologyOver the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty acid to a protein.
Laurence Abrami +2 more
exaly +6 more sources
Ion channel regulation by protein S-acylation [PDF]
Journal of General Physiology, 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.
Mike Shipston, Shipston Michael J
exaly +5 more sources
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
doaj +3 more sources
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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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
doaj +3 more sources
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
europepmc +4 more sources
The physiology of protein S-acylation. [PDF]
Physiol Rev, 2015 Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto ...
Chamberlain LH, Shipston MJ.
europepmc +6 more sources
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.
europepmc +4 more sources
Palmitoylation: a protein S-acylation with implications for breast cancer. [PDF]
NPJ Breast Cancer, 2016 AbstractProtein S-acylation is a reversible post-translational lipid modification that involves linkage of a fatty acid chain predominantly to a cysteine amino acid via a thioester bond. The fatty acid molecule is primarily palmitate, thus the term ‘palmitoylation’ is more commonly used.
Anderson AM, Ragan MA.
europepmc +7 more sources
FASN inhibitor TVB-3166 prevents S-acylation of the spike protein of human coronaviruses
Journal of Lipid Research, 2022 The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and other coronaviruses mediates host cell entry and is S-acylated on multiple phylogenetically conserved cysteine residues.
Katrina Mekhail +13 more
doaj +1 more source