Results 61 to 70 of about 21,138,684 (162)
Marine Drugs, 2021 Chitosan nanofiber membranes are recognized as functional antimicrobial materials, as they can effectively provide a barrier that guides tissue growth and supports healing. Methods to stabilize nanofibers in aqueous solutions include acylation with fatty
Carlos Montez Wells +8 more
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Detection of S-Acylated CD95 by Acyl-Biotin Exchange [PDF]
, 2017 S-acylation is the covalent addition of a fatty acid, most generally palmitate onto cysteine residues of proteins through a labile thioester linkage. The death receptor CD95 is S-palmitoylated and this post-translational modification plays a crucial role on CD95 organization in cellular membranes and thus on CD95-mediated signaling.
Rossin, Aurelie, Hueber, Anne-Odile
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Polyglutamine Tract Expansion Increases S-Nitrosylation of Huntingtin and Ataxin-1. [PDF]
PLoS ONE, 2016 Expansion of the polyglutamine (polyQ) tract in the huntingtin (Htt) protein causes Huntington's disease (HD), a fatal inherited movement disorder linked to neurodegeneration in the striatum and cortex.
Chun-Lun Ni +8 more
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Therapeutic targeting of protein S-acylation for the treatment of disease [PDF]
Biochemical Society Transactions, 2019 The post-translational modification protein S-acylation (commonly known as palmitoylation) plays a critical role in regulating a wide range of biological processes including cell growth, cardiac contractility, synaptic plasticity, endocytosis, vesicle trafficking, membrane transport and biased-receptor signalling.
Niall J. Fraser +3 more
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Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins
Nature Communications, 2021 S-acylation is the post-translational covalent attachment of fatty acids (FA) onto cysteines. Nuskova et al. find that exposure of cells to different FAs affects which FA is used to S-acylate GNAI proteins, thereby altering GNAI function and EGFR pathway
Hana Nůsková +8 more
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Molecules, 2022 Amides, anhydrides, esters, and thioesters of 2H-azirine-2-carboxylic acids were prepared by a rapid procedure at room temperature involving FeCl2-catalyzed isomerization of 5-chloroisoxazoles to 2H-azirine-2-carbonyl chlorides, followed by reaction with
Anastasiya V. Agafonova +2 more
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Acylation – A New Means to Control Traffic Through the Golgi
Frontiers in Cell and Developmental Biology, 2019 The Golgi is well known to act as center for modification and sorting of proteins for secretion and delivery to other organelles. A key sorting step occurs at the trans-Golgi network and is mediated by protein adapters. However, recent data indicate that
Andreas M. Ernst +3 more
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Ion channel regulation by protein S-acylation [PDF]
Journal of General Physiology, 2014 Protein S-acylation, the reversible covalent fatty-acid modification of cysteine residues, has emerged as a dynamic posttranslational modification (PTM) that controls the diversity, life cycle, and physiological function of numerous ligand- and voltage-gated ion channels.
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A novel pathway for lipid biosynthesis: the direct acylation of glycerol
Journal of Lipid Research, 2001 The acylation of glycerol-3-phosphate by acyl-CoA is regarded as the first committed step for the synthesis of the lipoidal moiety in glycerolipids. The direct acylation of glycerol in mammalian tissues has not been demonstrated.
Douglas P. Lee +6 more
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mBio, 2020 Bacterial lipoproteins (Lpps) are a class of membrane-associated proteins universally distributed among all bacteria. A characteristic N-terminal cysteine residue that is variably acylated anchors C-terminal globular domains to the extracellular surface,
John H. Gardiner +5 more
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