Results 31 to 40 of about 36,153 (123)
The role of S‐acylation in protein trafficking [PDF]
Traffic, 2017 Protein S‐acylation, also known as palmitoylation, consists of the addition of a lipid molecule to one or more cysteine residues through a thioester bond. This modification, which is widespread in eukaryotes, is thought to affect over 12% of the human proteome.
José L. Daniotti +2 more
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S-acylation in plants: an expanding field [PDF]
Biochemical Society Transactions, 2020 S-acylation is a common yet poorly understood fatty acid-based post-translational modification of proteins in all eukaryotes, including plants. While exact roles for S-acylation in protein function are largely unknown the reversibility of S-acylation indicates that it is likely able to play a regulatory role.
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Differential S-acylation of Enveloped Viruses
Protein & Peptide Letters, 2019 Post-translational modifications often regulate protein functioning. Covalent attachment of long chain fatty acids to cysteine residues via a thioester linkage (known as protein palmitoylation or S-acylation) affects protein trafficking, protein-protein and protein-membrane interactions.
Larisa V, Kordyukova +3 more
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The Physiology of ProteinS-acylation [PDF]
Physiological Reviews, 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. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto ...
Chamberlain, Luke H. +1 more
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S-acylation of Orai1 regulates store-operated Ca2+ entry. [PDF]
J Cell Sci, 2022 ABSTRACT Store-operated Ca2+ entry is a central component of intracellular Ca2+ signaling pathways. The Ca2+ release-activated channel (CRAC) mediates store-operated Ca2+ entry in many different cell types. The CRAC channel is composed of the plasma membrane (PM)-localized Orai1 channel and endoplasmic reticulum (ER)-localized STIM1 Ca2+
West SJ +6 more
europepmc +3 more sources
Detection of Heterogeneous Protein S-Acylation in Cells [PDF]
, 2019 The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(I)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly ...
Greaves, Jennifer +1 more
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Progress toward Understanding Protein S-acylation: Prospective in Plants [PDF]
Frontiers in Plant Science, 2017 S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-translational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond.
Li, Yaxiao, Qi, Baoxiu
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Frontiers in Physiology, 2014 Mechanisms that control surface expression and/or activity of large conductance calcium-activated potassium (BK) channels are important determinants of their (patho)physiological function.
Michael J Shipston
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Journal of Extracellular Vesicles, 2020 Extracellular vesicles (EVs) are membrane-enclosed particles that play an important role in cancer progression and have emerged as a promising source of circulating biomarkers. Protein S-acylation, frequently called palmitoylation, has been proposed as a
Javier Mariscal +10 more
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2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. [PDF]
PLoS ONE, 2013 S-acylation, the covalent attachment of palmitate and other fatty acids on cysteine residues, is a reversible post-translational modification that exerts diverse effects on protein functions.
Maria P Pedro +5 more
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