Results 1 to 10 of about 56,029 (251)

Global, site-specific analysis of neuronal protein S-acylation [PDF]

open access: yesScientific Reports, 2017
Protein S-acylation (palmitoylation) is a reversible lipid modification that is an important regulator of dynamic membrane-protein interactions. Proteomic approaches have uncovered many putative palmitoylated proteins however, methods for comprehensive ...
Mark O. Collins   +2 more
doaj   +9 more sources

Regulation of Dynamic Protein S-Acylation [PDF]

open access: yesFrontiers in Molecular Biosciences, 2021
Protein S-acylation is the reversible addition of fatty acids to the cysteine residues of target proteins. It regulates multiple aspects of protein function, including the localization to membranes, intracellular trafficking, protein interactions ...
Jessica J. Chen   +2 more
doaj   +5 more sources

Regulation of T cell function by protein S-acylation [PDF]

open access: yesFrontiers in Physiology, 2022
S-acylation, the reversible lipidation of free cysteine residues with long-chain fatty acids, is a highly dynamic post-translational protein modification that has recently emerged as an important regulator of the T cell function. The reversible nature of
Savannah J. West   +4 more
doaj   +5 more sources

Protein S-acyltransferases and acyl protein thioesterases, regulation executors of protein S-acylation in plants [PDF]

open access: yesFrontiers in Plant Science, 2022
Protein S-acylation, also known as palmitoylation, is an important lipid post-translational modification of proteins in eukaryotes. S-acylation plays critical roles in a variety of protein functions involved in plant development and responses to abiotic ...
Jincheng Li, Manqi Zhang, Lijuan Zhou
doaj   +4 more sources

Regulatory effects of protein S-acylation on insulin secretion and insulin action [PDF]

open access: yesOpen Biology, 2021
Post-translational modifications (PTMs) such as phosphorylation and ubiquitination are well-studied events with a recognized importance in all aspects of cellular function.
Luke H. Chamberlain   +2 more
doaj   +6 more sources

The physiology of protein S-acylation. [PDF]

open access: yesPhysiol 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.
Chamberlain LH, Shipston MJ.
europepmc   +7 more sources

Proteomic analysis of a poplar cell suspension culture suggests a major role of protein S-acylation in diverse cellular processes [PDF]

open access: yesFrontiers in Plant Science, 2016
S-acylation is a reversible post-translational modification (PTM) of proteins known to be involved in membrane targeting, subcellular trafficking and the determination of a great variety of functional properties of proteins.
Vaibhav eSrivastava   +5 more
doaj   +5 more sources

The landscape of renal protein S-acylation in mice with lipid-induced nephrotoxicity [PDF]

open access: yesScientific Reports
Excess 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
doaj   +5 more sources

The role of protein S-acylation in vascular injury associated with metabolic disorders [PDF]

open access: yesFrontiers in Endocrinology
Protein palmitoylation represents a prevalent form post-translational lipid modification across various organisms. This reversible and dynamic cellular process is significant in regulating the transcription and expression of downstream target genes, as ...
Yayun Wang   +8 more
doaj   +2 more sources

Sequestering sequestosome 1 via S-acylation in autophagy, Huntington disease, and beyond [PDF]

open access: yesAutophagy Reports
Protein mislocalization and aggregation are hallmark features in neurodegeneration. As proteins mislocalize, proteostasis deficiency and protein aggregation typically follow.
Y Alshehabi, F Abrar, D.D.O Martin
doaj   +2 more sources

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