Results 41 to 50 of about 3,365,420 (200)

PalmPred: an SVM based palmitoylation prediction method using sequence profile information.

open access: yesPLoS ONE, 2014
Protein palmitoylation is the covalent attachment of the 16-carbon fatty acid palmitate to a cysteine residue. It is the most common acylation of protein and occurs only in eukaryotes.
Bandana Kumari   +2 more
doaj   +1 more source

Selenoprotein K and Protein Palmitoylation [PDF]

open access: yesAntioxidants & Redox Signaling, 2015
Significance: Selenoprotein K (SelK) is an endoplasmic reticulum (ER) membrane protein, and its expression is sensitive to dietary selenium levels. A recently described role for SelK as a cofactor in catalyzing protein palmitoylation reactions provides an important ...
Gregory J, Fredericks, Peter R, Hoffmann
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

Mechanisms and functional implications of ZDHHC5 in cellular physiology and disease

open access: yesJournal of Lipid Research
Post-translational lipid modification by palmitoylation is a reversible process crucial for maintaining cellular functionality. The palmitoyl acyltransferase zinc finger Asp-His-His-Cys motif-containing 5 (ZDHHC5) has garnered significant attention due ...
Huicong Liu   +4 more
doaj   +1 more source

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

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

Protein palmitoylation in protozoan parasites

open access: yesFrontiers in Bioscience, 2011
Palmitoylation plays an important role in the regulation of the localization and function of the modified protein. Although many aspects of protein palmitoylation have been identified in mammalian and yeast cells, little information is available of this modification in protozoan parasites.
Maria Martha, Corvi   +2 more
openaire   +2 more sources

Global, site-specific analysis of neuronal protein S-acylation

open access: yesScientific 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
doaj   +1 more source

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

Radiation‐Induced Tumor‐Intrinsic LTβR N‐Glycosylation Suppresses Pyroptosis Through TRIM28‐Mediated PCBP2 SUMOylation to Promote Gastric Cancer Radioresistance

open access: yesAdvanced Science, EarlyView.
Radiotherapy triggers LTβR N‐glycosylation, enhancing its overall protein stability and nuclear retention. This accumulation drives TRIM28‐mediated PCBP2 SUMOylation, suppressing pyroptosis and conferring gastric cancer radioresistance. Therapeutically, a targeted nanoplatform (cRGD‐Lipo@EMD) effectively disrupts this regulatory axis, offering a highly
Weijie Zang   +8 more
wiley   +1 more source

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