Site-specific analysis of protein S-acylation by resin-assisted capture[S]
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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2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. [PDF]
S-acylation, the covalent attachment of palmitate and other fatty acids on cysteine residues, is a reversible post-translational modification that exerts diverse effects on protein functions.
Maria P Pedro +5 more
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Open Biology: overview for special issue on dynamics of protein fatty acylation
Fatty acylation is a widespread form of protein modification that occurs on specific intracellular and secreted proteins. Beyond increasing hydrophobicity and the affinity of the modified protein for lipid bilayers, covalent attachment of a fatty acid ...
Marilyn D. Resh
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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
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Versatility of Acyl-Acyl Carrier Protein Synthetases
The acyl carrier protein (ACP) requires posttranslational modification with a 4'-phosphopantetheine arm for activity, and this thiol-terminated modification carries cargo between enzymes in ACP-dependent metabolic pathways. We show that acyl-ACP synthetases (AasSs) from different organisms are able to load even, odd, and unnatural fatty acids onto E ...
Beld, Joris +2 more
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Research Progress on Acylation Modification and Application of Animal and Vegetable Proteins [PDF]
Acylation is a common method for chemical modification of proteins, which can effectively improve the functional properties of proteins and has been widely used in food processing in recent years.
YAO Xuan, LÜ Xiaohui, JIN Yongguo, HU Gan
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Protein acyl thioesterases (Review)
Many proteins are S-acylated, affecting their localization and function. Dynamic S-acylation in response to various stimuli has been seen for several proteins in vivo. The regulation of S-acylation is beginning to be elucidated. Proteins can autoacylate or be S-acylated by protein acyl transferases (PATs).
Zeidman, R, Jackson, CS, Magee, AI
openaire +4 more sources
A broad inhibitor of acyl-acyl carrier protein synthetases
The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development.
Magdalena Todorinova +2 more
openaire +3 more sources
SIRT2 and lysine fatty acylation regulate the transforming activity of K-Ras4a
Ras proteins play vital roles in numerous biological processes and Ras mutations are found in many human tumors. Understanding how Ras proteins are regulated is important for elucidating cell signaling pathways and identifying new targets for treating ...
Hui Jing +6 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
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