Results 51 to 60 of about 30,111 (219)

Role of Palmitoylation of Postsynaptic Proteins in Promoting Synaptic Plasticity

open access: yesFrontiers in Molecular Neuroscience, 2019
Many postsynaptic proteins undergo palmitoylation, the reversible attachment of the fatty acid palmitate to cysteine residues, which influences trafficking, localization, and protein interaction dynamics.
Lucas Matt   +3 more
doaj   +1 more source

Protein palmitoylation and subcellular trafficking

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2011
Protein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues with the 16-carbon fatty acid palmitate, is the most common acylation of proteins in eukaryotic cells. This post-translational modification provides an important mechanism for regulating protein subcellular localization, stability, trafficking, translocation to ...
Aicart-Ramos, Clara   +2 more
openaire   +2 more sources

Assaying protein palmitoylation in plants [PDF]

open access: yesPlant Methods, 2008
Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes. Whilst prediction methods for S-acylation exist, prediction is imperfect.
Hemsley, PA, Taylor, LA, Grierson, CS
openaire   +4 more sources

A Simple, Semi-Quantitative Acyl Biotin Exchange-Based Method to Detect Protein S-Palmitoylation Levels

open access: yesMembranes, 2023
Protein S-palmitoylation is a reversible post-translational lipidation in which palmitic acid (16:0) is added to protein cysteine residue by a covalent thioester bond.
Valentina Buffa   +4 more
doaj   +1 more source

Primary fibroblasts from CSPα mutation carriers recapitulate hallmarks of the adult onset neuronal ceroid lipofuscinosis [PDF]

open access: yes, 2017
Mutations in the co- chaperone protein, CSPα, cause an autosomal dominant, adult-neuronal ceroid lipofuscinosis (AD-ANCL). The current understanding of CSPα function exclusively at the synapse fails to explain the autophagy-lysosome pathway (ALP ...
Benitez, Bruno A, Sands, Mark S
core   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Characterisation and expression of β1-, β2- and β3-adrenergic receptors in the fathead minnow (Pimephales promelas) [PDF]

open access: yes, 2011
This is the author’s version of a work that was accepted for publication in General and Comparative Endocrinology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control ...
Eccles, PD   +4 more
core   +1 more source

Palmitoylation of Platelet Proteins

open access: yesPlatelets, 1994
Palmitoylation as incorporation of [(3)H] palmitic acid into proteins occurred in platelets as in other cell systems. The linkage of palmitic acid to platelet proteins was stable to SDS and organic solvents but was sensitive to hydroxylamine, consistent with oxyester or thioester bond(s). Non-reduced SDS PAGE analysis revealed that the most prominantly
openaire   +2 more sources

The Drosophila protein palmitoylome: Characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases [PDF]

open access: yesFly, 2008
Palmitoylation is the post-translational addition of a palmitate moiety to a cysteine residue through a covalent thioester bond. The addition and removal of this modification is controlled by both palmitoyl acyl-transferases and thioesterases. Using bioinformatic analysis, we identified 22 DHHC family palmitoyl acyl-transferase homologs in the ...
Barbra A, Bannan   +11 more
openaire   +2 more sources

Hippo pathway at the crossroads of stemness and therapeutic resistance in breast cancer

open access: yesMolecular Oncology, EarlyView.
Dysregulation of the Hippo pathway drives nuclear accumulation of YAP/TAZ, activating stemness‐related transcriptional programs that sustain breast cancer stemness and fuel therapeutic resistance across subtypes, underscoring Hippo signaling as a targetable vulnerability. Figure created and edited with BioRender.com.
Giulia Schiavoni   +11 more
wiley   +1 more source

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