Results 11 to 20 of about 37,965 (302)
Global, site-specific analysis of neuronal protein S-acylation [PDF]
Scientific Reports, 2017 Protein S-acylation (palmitoylation) is a reversible lipid modification that is an important regulator of dynamic membrane-protein interactions. Proteomic approaches have uncovered many putative palmitoylated proteins however, methods for comprehensive ...
Mark O. Collins +2 more
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The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A [PDF]
BiomoleculesThe broad-spectrum antiviral functions of interferon-inducible transmembrane 1 (IFITM1) rely on S-palmitoylation post-translational modification.
Xuemeng Shi +11 more
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Exploring the role of protein palmitoylation in cancer progression and therapy: a comprehensive bibliometric study (2004–2024) [PDF]
Discover OncologyObjective This study aims to qualitatively and quantitatively assess the research landscape of palmitoylation in oncology using bibliometric analysis, thereby providing insights into research hotspots and emerging trends.
Yu Chen, Yuxuan Dai, Xing Wang, Jian Liu
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Protein regulatory network mediated by palmitoylation modifications in the pathological progression of Parkinson’s disease: a narrative review [PDF]
Frontiers in ImmunologyPalmitoylation is a reversible lipid modification regulated by palmitoyl transferases and acyl-protein thioesterases, in which palmitic acid is attached to protein cysteine residues.
Jingjing Liu +7 more
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Palmitoylation-dependent regulation of GPX4 suppresses ferroptosis
Nature CommunicationsS-palmitoylation is a reversible and widespread post-translational modification, but its role in the regulation of ferroptosis has been poorly understood. Here, we elucidate that GPX4, an essential regulator of ferroptosis, is reversibly palmitoylated on
Bin Huang +10 more
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Learning by palmitoylation [PDF]
The Journal of Cell Biology, 2002 ![Graphic][1] Clusters of AMPA receptors (red spots) disperse when PSD-95 palmitoylation is blocked (right). Bredt/ElsevierLearning is probably driven by use-dependent changes in synaptic strength.
Nicole LeBrasseur
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Cell Death and Disease, 2022 The dynamics of synaptic vesicles (SVs) within presynaptic domains are tightly controlled by synapsin1 phosphorylation; however, the mechanism underlying the anchoring of synapsin1 with F-actin or SVs is not yet fully understood. Here, we found that Syn1
Peipei Yan +14 more
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Regulation of NCX1 by palmitoylation [PDF]
Cell Calcium, 2020 Palmitoylation (S-acylation) is the reversible conjugation of a fatty acid (usually C16 palmitate) to intracellular cysteine residues of proteins via a thioester linkage. Palmitoylation anchors intracellular regions of proteins to membranes because the palmitoylated cysteine is recruited to the lipid bilayer.
Fuller, William, Gök, Caglar
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Protein S -palmitoylation in immunity [PDF]
Open Biology, 2021 S -palmitoylation is a reversible posttranslational lipid modification of proteins. It controls protein activity, stability, trafficking and protein–protein interactions. Recent global profiling of immune cells and targeted analysis have identified many S -palmitoylated immunity-associated proteins. Here,
Howard C. Hang +3 more
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Frontiers in Physiology, 2022 S-palmitoylation is an essential lipid modification catalysed by zDHHC-palmitoyl acyltransferases that regulates the localisation and activity of substrates in every class of protein and tissue investigated to date.
Alice Main +11 more
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