Results 111 to 120 of about 36,153 (123)
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The emerging roles of S-acylation in autophagy

Trends in Biochemical Sciences
Autophagy is an intracellular degradation system that delivers cytoplasmic materials to the lysosome. S-acylation, a reversible post-translational modification that attaches long-chain fatty acids to cysteine residues within proteins, has recently emerged as an important regulatory mechanism for autophagy.
Jia Yao, Chunyang Xie, Aimin Yang
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Protein S‐acylation, a new panacea for plant fitness

Journal of Integrative Plant Biology
ABSTRACTProtein S‐acylation or palmitoylation is a reversible post‐translational modification that influences many proteins encoded in plant genomes. Exciting progress in the past 3 years demonstrates that S‐acylation modulates subcellular localization, interacting profiles, activity, or turnover of substrate proteins in plants, participating in ...
Fei Liu, Jin‐Yu Lu, Sha Li, Yan Zhang
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Enzymology of DHHC-mediated Protein S-Acylation

2011
Protein S-acylation is the post-translational modification of proteins with long-chain fatty acids at cysteine residues via a thioester linkage. The most commonly attached lipid is 16-carbon palmitate, thus the process is often called palmitoylation. Unlike other lipid modifications, protein S-acylation is reversible.
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S-Acylation regulates store-operated calcium entry

Biophysical Journal, 2022
Savannah J. West   +6 more
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Zur Herstellung von S‐Acyl‐pantetheinen

Angewandte Chemie, 1956
E. Felder, D. Pitré
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Role of S-acylating enzymes in ciliated cells

S-acylation is a post-translational modification that can regulate protein localization, function, and turnover by reversible attachment of fatty acid to specific cysteine residues. It affects over 20% of proteins, with membrane proteins making up the largest group, followed by cytosolic, ciliary, and nuclear proteins.
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Das Verhalten einiger S‐Acyl‐aminomercaptane

Justus Liebigs Annalen der Chemie, 1952
Theodor Wieland, Ekkehart Bokelmann
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