Results 61 to 70 of about 32,516 (204)

Palmitoyl Acyltransferase Zdhhc17 Promotes Functional Recovery After Spinal Cord Injury by Targeting the Nuclear Transport Factors Kpna2 and Ipo9

open access: yesAdvanced Science, EarlyView.
In this study, we demonstrate that Zdhhc17, acting as a PAT, suppresses neuronal apoptosis and promotes axon regeneration after injury, thereby enhancing functional recovery following SCI. In this context, Kpna2 and Ipo9 serve as novel palmitoylation substrates of Zdhhc17, whose palmitoylation prevents the injury‐induced degradation of their proteins ...
Meixuan Chen   +12 more
wiley   +1 more source

Pseudo-enzymatic S-acylation of a myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo [PDF]

open access: yesBiochemical Journal, 1998
Covalent attachment of a variety of lipid groups to proteins is now recognized as a major group of post-translational modifications. S-acylation of proteins at cysteine residues is the only modification considered dynamic and thus has the potential for regulating protein function and/or localization.
M C, Bañó, C S, Jackson, A I, Magee
openaire   +2 more sources

Trypanosoma brucei Acyl-Protein Thioesterase-like (TbAPT-L) Is a Lipase with Esterase Activity for Short and Medium-Chain Fatty Acids but Has No Depalmitoylation Activity

open access: yesPathogens, 2022
Dynamic post-translational modifications allow the rapid, specific, and tunable regulation of protein functions in eukaryotic cells. S-acylation is the only reversible lipid modification of proteins, in which a fatty acid, usually palmitate, is ...
Robert W. B. Brown   +15 more
doaj   +1 more source

Lactylation‐Driven PROS1‐TYRO3‐CARF Signaling Promotes Therapy‐Induced Senescence Escape and Radioresistance in Meningioma

open access: yesAdvanced Science, EarlyView.
A glycolysis‐driven epigenetic switch promotes therapy resistance in meningioma. Increased lactate production enhances histone H3K27 lactylation, which activates PROS1 secretion. Secreted PROS1 engages TYRO3 signaling to degrade the senescence regulator CARF, allowing cancer cells to escape growth arrest.
Zhuohang Wang   +12 more
wiley   +1 more source

Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein [PDF]

open access: yesScientific Reports, 2017
AbstractMembrane-bound sialidase Neu3 is involved in the catabolism of glycoconjugates, and plays crucial roles in numerous biological processes. Since the mechanism of its association with membranes is still not completely understood, the aim of this work was to provide further information regarding this aspect.
Macarena Rodríguez‐Walker   +1 more
openaire   +4 more sources

Aspirin‐Derived Salicyl‐CoA Drives Histone Lysine Salicylation Regulated by CBP and SIRT2

open access: yesAdvanced Science, EarlyView.
Aspirin‐derived salicyl‐CoA serves as a previously unrecognized acyl donor for protein lysine salicylation. This study identifies histone lysine salicylation as a reversible epigenetic modification regulated by CBP and SIRT2, expanding the biochemical actions of aspirin beyond its canonical acetylation‐dependent mechanisms and providing a new framework
Facai Zhang   +15 more
wiley   +1 more source

S‐acylation of Ca2+ transport proteins in cancer

open access: yesChronic Diseases and Translational Medicine
AbstractAlterations in cellular calcium (Ca2+) signals have been causally associated with the development and progression of human cancers. Cellular Ca2+ signals are generated by channels, pumps, and exchangers that move Ca2+ ions across membranes and are decoded by effector proteins in the cytosol or in organelles. S‐acylation, the reversible addition
Kouba, Sana, Demaurex, Nicolas
openaire   +3 more sources

Protocol to identify S-acylated proteins in hippocampal neurons using ω-alkynyl fatty acid analogs and click chemistry

open access: yesSTAR Protocols
Summary: S-acylation, commonly palmitoylation, is the addition of fatty acids to cysteines to regulate protein localization and function. S-acylation detection has been hampered by limited sensitivity and selectivity in low-protein, costly samples like ...
Charlotte A. Townsend   +4 more
doaj   +1 more source

Protein acylation in inflammatory diseases: from mechanisms to therapeutic strategies

open access: yesCell Communication and Signaling
Protein acylation, a critical subset of post-translational modifications (PTMs), serves as a dynamic regulatory mechanism linking cellular metabolism, epigenetic regulation, and inflammatory responses.
Jiayi Ding   +4 more
doaj   +1 more source

Determination of Protein S-Acylation State by Enhanced Acyl-Switch Methods [PDF]

open access: yes, 2019
S-Acylation is increasingly being recognized as an important dynamic posttranslational modification of cysteine residues in proteins. Various approaches have been described for assaying protein S-acylation with acyl-switch approaches being the most common and accessible.
Hurst, Charlotte H.   +2 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy