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Published in 2022 at "ACS medicinal chemistry letters"
DOI: 10.1021/acsmedchemlett.2c00174
Abstract: Acyl protein thioesterases hydrolyze fatty acid thioesters on cysteine residues of proteins. The two protein depalmitoylases APT1 and APT2 have a very high degree of similarity and show substantial overlap in substrate utility. Potent, selective,…
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Keywords:
based probes;
activity based;
acyl protein;
protein thioesterases ... See more keywords
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Published in 2018 at "Critical Reviews in Biochemistry and Molecular Biology"
DOI: 10.1080/10409238.2017.1409191
Abstract: Abstract Protein depalmitoylation describes the removal of thioester-linked long chain fatty acids from cysteine residues in proteins. For many S-palmitoylated proteins, this process is promoted by acyl protein thioesterase enzymes, which catalyze thioester hydrolysis to…
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Keywords:
protein;
protein depalmitoylases;
protein thioesterase;
depalmitoylation ... See more keywords
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Published in 2018 at "PLoS ONE"
DOI: 10.1371/journal.pone.0190255
Abstract: Protein palmitoylation is a dynamic post-translational modification (PTM) important for cellular functions such as protein stability, trafficking, localization, and protein-protein interactions. S-palmitoylation occurs via the addition of palmitate to cysteine residues via a thioester linkage,…
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Keywords:
protein;
probe;
activity based;
protein thioesterases ... See more keywords
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1
Published in 2022 at "Frontiers in Plant Science"
DOI: 10.3389/fpls.2022.956231
Abstract: 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 and…
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Keywords:
protein acylation;
acylation;
acyl protein;
protein thioesterases ... See more keywords