Results 51 to 60 of about 37,335 (238)

Kinetically Stable Boron‐Heteroatom Bonds

open access: yesAngewandte Chemie, EarlyView.
This study investigates the kinetic stability of boron‐heteroatom bonds in N‐methyliminodiacetic acid (MIDA) boronates. The hemilabile nature of the ligand enables the synthesis of molecules that would otherwise be considered too hydrolytically labile. Depending on the structure, acid‐promoted migration of the boryl group was found to produce compounds
Alina Trofimova   +8 more
wiley   +2 more sources

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, Aurelie, Hueber, Anne-Odile
openaire   +2 more sources

Therapeutic targeting of protein S-acylation for the treatment of disease [PDF]

open access: yesBiochemical 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
openaire   +3 more sources

CEBPG‐Mediated Palmitic Acid Adaptation of Cancer‐Associated Fibroblasts Drives Metastasis of Oral Squamous Cell Carcinoma

open access: yesAdvanced Science, EarlyView.
This study reveals a metabolic signaling axis in the OSCC microenvironment where palmitic acid (PA) drives the activation of CAFs. PA uptake triggers CEBPG‐dependent epigenetic remodeling to upregulate ERN1 and TMBIM6, thereby mitigating ER stress. This adaptive program sustains CAF survival and the pro‐metastatic phenotype, establishing this pathway ...
Yiling Duan   +6 more
wiley   +1 more source

Glutathione‐Responsive Acyl‐Modifications for Targeted RNA Decaging and Prolonged Protein Synthesis

open access: yesAngewandte Chemie, EarlyView.
The self‐immolation of disulfide‐based mRNA modifications in response to endogenous glutathione (GSH) promotes a gradual release of translatable mRNA within the cell, leading to improved nuclease resistance, tunable release properties, and a significant increase (up to 600%) of target protein production over time. This strategy offers an exciting proof
Mary E. Flood   +6 more
wiley   +2 more sources

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

NIR‐II‐Trackable LYTACs Phyto‐Nanotheranostics for Source‐Microenvironment Dual‐Track ROS Regulation in Acute Gouty Arthritis

open access: yesAdvanced Science, EarlyView.
The TPR‐LYTACs nanomaterial offers a dual‐pathway strategy for precise gouty arthritis treatment by targeting and degrading the ROS‐producing enzyme NOX2 inside macrophages while its antioxidant core clears accumulated ROS outside. This “source inhibition and microenvironment scavenging” approach, guided by NIR‐II imaging, effectively controls local ...
Jian Zhang   +15 more
wiley   +1 more source

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

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