Results 41 to 50 of about 21,138,684 (162)
The physiology of protein S-acylation [PDF]
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.
Chamberlain, Luke H. +1 more
core +3 more sources
Assaying protein palmitoylation in plants
Background Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes.
Taylor Laura +2 more
doaj +1 more source
Distinct Roles of N-Terminal Fatty Acid Acylation of the Salinity-Sensor Protein SOS3
The Salt-Overly-Sensitive (SOS) pathway controls the net uptake of sodium by roots and the xylematic transfer to shoots in vascular plants. SOS3/CBL4 is a core component of the SOS pathway that senses calcium signaling of salinity stress to activate and ...
Irene Villalta +10 more
doaj +1 more source
Development of an Acrylamide-Based Inhibitor of Protein S-Acylation [PDF]
Protein S-acylation is a dynamic lipid post-translational modification that can modulate the localization and activity of target proteins. In humans, the installation of the lipid onto target proteins is catalyzed by a family of 23 Asp-His-His-Cys domain-
Noah, Brookes +8 more
core +2 more sources
In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases
Protein S-acylation, more commonly known as protein palmitoylation, is a biological process defined by the covalent attachment of long chain fatty acids onto cysteine residues of a protein, effectively altering the local hydrophobicity and influencing ...
R. Elliot Murphy, Anirban Banerjee
doaj +1 more source
S-acylation regulates the membrane association and activity of Calpain-5 [PDF]
Abstract Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. CAPN5 is partly membrane associated, despite its lack of a transmembrane domain. Unlike classical calpains, CAPN5 contains a C-terminal C2 domain. C2 domains often have affinity to lipids, mediating membrane association.
Jozsef, Gal +5 more
openaire +2 more sources
Differential S-acylation of Enveloped Viruses
Post-translational modifications often regulate protein functioning. Covalent attachment of long chain fatty acids to cysteine residues via a thioester linkage (known as protein palmitoylation or S-acylation) affects protein trafficking, protein-protein and protein-membrane interactions.
Larisa V, Kordyukova +3 more
openaire +2 more sources
S-Acyl Glutathione Thioesterase of Plant Tissue [PDF]
The enzymic hydrolysis of S-acyl glutathione has been observed in extracts of various plant tissues. The richest source found in this study was avocado mesocarp. No enzymic activity was observed with acetyl coenzyme A or acetylthiocholine as substrates. Hydrolytic activity was essentially constant in the pH range 7 to 9.
L K, Winberry, J B, Mudd
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Detection of Heterogeneous Protein S-Acylation in Cells [PDF]
The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(I)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly ...
Greaves, Jennifer +1 more
openaire +4 more sources
Palmitoylation: a protein S-acylation with implications for breast cancer [PDF]
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, Alison M., Ragan, Mark A.
openaire +5 more sources

