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Recapitulating the potential contribution of protein S-palmitoylation in cancer
Cancer and Metastasis ReviewsProtein S-palmitoylation is a reversible form of protein lipidation in which the formation of a thioester bond occurs between a cysteine (Cys) residue of a protein and a 16-carbon fatty acid chain. This modification is catalyzed by a family of palmitoyl acyl transferases, the DHHC enzymes, so called because of their Asp-His-His-Cys (DHHC) catalytic ...
Suchi, Chaturvedi, Avinash, Sonawane
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S-palmitoylation in ferroptosis: molecular mechanisms, modulators, and interplay with autophagy
ApoptosisS-palmitoylation, a reversible lipid post-translational modification, plays a dynamically regulatory role in cell death signaling pathways by modulating protein-membrane affinity, subcellular localization, and functional interactions. Emerging evidence has linked dysregulated S-palmitoylation to various pathologies including cancer and ...
Leilei, Wang, Chuan, Wang, Hong, He
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The shadow of cancer therapeutic resistance: Unveiling the role of S-palmitoylation
Drug Resistance UpdatesCancer therapeutic resistance remains a formidable challenge due to its diverse underlying mechanisms. S-palmitoylation (or called S-acylation), a reversible post-translational modification involving the attachment of long-chain fatty acids to cysteine residues, has emerged as a critical regulator of cancer progression and treatment response.
Xue, Yang +3 more
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S-palmitoylation in bone biology: emerging insights and therapeutic potential
Biochemical PharmacologyS-Palmitoylation, the reversible covalent attachment of palmitate to cysteine residues, is a dynamic post-translational lipid modification that regulates the localization, stability, and function of a wide array of proteins. Although traditionally linked to membrane trafficking and signaling, recent preliminary studies have begun to reveal its ...
Xing Ji +4 more
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Full-Length P2X7 Structures Reveal How Palmitoylation Prevents Channel Desensitization
Cell, 2019Craig Yoshioka, Steven E Mansoor
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Rapid and transient palmitoylation of the tyrosine kinase Lck mediates Fas signaling
Proceedings of the National Academy of Sciences of the United States of America, 2015Askar M Akimzhanov +2 more
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