Results 41 to 50 of about 36,153 (123)

Ion channel regulation by protein S-acylation [PDF]

open access: yesJournal 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.
openaire   +2 more sources

Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei

open access: yesFrontiers in Microbiology, 2022
Syntrophomonas wolfei is an anaerobic syntrophic microbe that degrades short-chain fatty acids to acetate, hydrogen, and/or formate. This thermodynamically unfavorable process proceeds through a series of reactive acyl-Coenzyme A species (RACS). In other
Janine Y. Fu   +15 more
doaj   +1 more source

Metabolically controlled histone H4K5 acylation/acetylation ratio drives BRD4 genomic distribution

open access: yesCell Reports, 2021
Summary: In addition to acetylation, histones are modified by a series of competing longer-chain acylations. Most of these acylation marks are enriched and co-exist with acetylation on active gene regulatory elements.
Mengqing Gao   +23 more
doaj   +1 more source

Synthesis and Characterization of 2-Decenoic Acid Modified Chitosan for Infection Prevention and Tissue Engineering

open access: yesMarine 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
doaj   +1 more source

Polyglutamine Tract Expansion Increases S-Nitrosylation of Huntingtin and Ataxin-1. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins

open access: yesNature 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
doaj   +1 more source

5-Chloroisoxazoles: A Versatile Starting Material for the Preparation of Amides, Anhydrides, Esters, and Thioesters of 2H-Azirine-2-carboxylic Acids

open access: yesMolecules, 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
doaj   +1 more source

Detection of S-Acylated CD95 by Acyl-Biotin Exchange [PDF]

open access: yes, 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, Aurélie, Hueber, Anne-Odile
openaire   +2 more sources

Acylation – A New Means to Control Traffic Through the Golgi

open access: yesFrontiers 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
doaj   +1 more source

Transition-metal-free trifluoromethylthiolation–acylation of arynes by insertion into the C–S bonds

open access: yesGreen Synthesis and Catalysis, 2021
An efficient procedure to access to ortho-SCF3 substituted benzophenones from arynes and trifluoromethylthioesters has been developed under transition-metal free conditions. This difunctionalization process involves the first insertion of arynes into the
Chengyao Kimmy Cao   +2 more
doaj   +1 more source

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