Results 171 to 180 of about 31,021 (196)
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S-acylation by the DHHC protein family
Biochemical Society Transactions, 2010A family of 23 DHHC (Asp-His-His-Cys) proteins that function as mammalian S-acyltransferases has been identified, reinvigorating the study of protein S-acylation. Recent studies have continued to reveal how S-acylation affects target proteins, and have provided glimpses of how DHHC-substrate specificity might be achieved.
Greaves, Jennifer, Chamberlain, Luke H
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2019
Palmitoylation or S-acylation is the posttranslational attachment of fatty acids to cysteine residues and is common among integral and peripheral membrane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells.
Larisa, Kordyukova +3 more
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Palmitoylation or S-acylation is the posttranslational attachment of fatty acids to cysteine residues and is common among integral and peripheral membrane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells.
Larisa, Kordyukova +3 more
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Analysis of S-Acylation of Proteins
2003Palmitoylation or S-acylation is the post-translational attachment of fatty acids to cysteine residues and is common among integral and peripheral mem brane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells.
Michael, Veit +2 more
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Protein S-Acylation in Pulmonary Disease
Free Radical Biology and Medicine, 2016Obesity is a major risk factor for asthma. Obese asthmatics exhibit poor symptom control, frequent exacerbation, and increased levels of reactive oxygen species (ROS). The consumption of a western diet, high in fat and carbohydrates, can both induce obesity and increase ROS.
Matthew J Randall +4 more
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Protein S-acylation in plants (Review)
Molecular Membrane Biology, 2009Membrane resident proteins are a common feature of biology yet many of these proteins are not integral to the membrane. These peripheral membrane proteins are often bound to the membrane by the addition of fatty acyl chains to the protein. This modification, known as S-acylation or palmitoylation, promotes very strong membrane association but is also ...
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Direct Analysis of Protein S-Acylation by Mass Spectrometry
2019Dynamic and reversible protein S-acylation, most commonly occurring as S-palmitoylation, plays an important role in protein/membrane association and the regulation of intracellular signaling via cycles of palmitoylation and depalmitoylation. Direct analysis of protein S-acylation by mass spectrometry (MS) offers several benefits over indirect detection
Yuhuan, Ji, Cheng, Lin
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Assaying Protein S-Acylation in Plants
2013S-acylation is increasingly being recognized as an important posttranslational modification of proteins controlling activity, subcellular localization, microdomain residence, and stability. Heterotrimeric G-proteins and GPCRs are particularly well studied S-acylated proteins, and fast, cheap, reliable methods are required for the analysis of S ...
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Protein S‐acylation, a new panacea for plant fitness
Journal of Integrative Plant BiologyABSTRACTProtein 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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Peptide and protein thioester synthesis via N→S acyl transfer
Organic & Biomolecular Chemistry, 2010Peptide and protein thioesters are playing an increasingly prominent role in the chemical toolbox for protein assembly and modification through Native Chemical Ligation (NCL). In this Emerging Area we highlight recent developments in a somewhat surprising route to thioesters: selective disruption of amides, the more stable carboxylic acid derivatives.
Jaskiranjit, Kang, Derek, Macmillan
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Enzymology of DHHC-mediated Protein S-Acylation
2011Protein 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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