Results 251 to 260 of about 37,527 (267)

Analysis of S-Acylation of Proteins

2003
Palmitoylation 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, Evgeni, Ponimaskin, Michael F G, Schmidt   +2 more
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Assaying Protein S-Acylation in Plants

2013
S-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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Direct Analysis of Protein S-Acylation by Mass Spectrometry

2019
Dynamic 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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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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Dynamic PRDX S-acylation modulates ROS stress and signaling

Cell Chemical Biology
Peroxiredoxins (PRDXs) are a highly conserved family of peroxidases that serve as the primary scavengers of peroxides. Post-translational modifications play crucial roles modulating PRDX activities, tuning the balance between reactive oxygen species (ROS) signaling and stress. We previously reported that S-acylation occurs at the "peroxidatic" cysteine
Tian Qiu, Saara-Anne Azizi, Shubhashree Pani, Bryan C. Dickinson   +3 more
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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, Goutham Kodakandla, Qiaochu Wang, Ritika Tewari, Michael X. Zhu, Darren Boehning, Askar M. Akimzhanov   +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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