AbstractThe fatty acid acylation of polypeptides was studied in vivo and in vitro by incorporation of radiolabeled palmitic acid into Semliki Forest viral polypeptides. Utilizing a cell-free system for acylation protein fatty acyltransferase was characterized as an integral membrane protein. No acylation activity was detected in the cytosol. During subcellular fractionation of a variety of mammalian or avian cells the enzyme was localized to the rough endoplasmic reticulum. Therefore this posttranslational hydrophobic modification starts earlier in the biosynthesis of acylated polypeptides than previously believed
AbstractWe describe in this report the fatty acylation of some of the main polypeptides from the eye...
AbstractProtein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues ...
Acylation of proteins with fatty acids is important for the regulation of membrane association, traf...
AbstractFatty acid acylation of membrane proteins was studied on human erythrocytes by measuring inc...
Fatty acid acylation of proteins corresponds to the co- or post-translational covalent lin...
acyltransferase activ arle ive an onnec ylvani form A wide variety of cellular and viral proteins un...
AbstractMany glycoproteins of enveloped viruses as well as cellular proteins are covalently modified...
Red blood cells (RBCs) have long been known to contain acylated proteins and to display an active pa...
The enzyme acyl-CoA:cholesterol acyltransferase (ACAT) is normally localized in the endoplasmic reti...
Post-translational acylation of lysine side chains is a common mechanism of protein regulation. Modi...
In recent years several proteins have been found to be acylated with fatty acids as well as with iso...
Non-histone protein acylation is increasingly recognized as an important posttranslational modificat...
S-Fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16...
Post-translational modifications are covalent and generally enzyme-mediated modifications of protein...
Three related studies were performed to better characterize the intracellular process of protein S-a...
AbstractWe describe in this report the fatty acylation of some of the main polypeptides from the eye...
AbstractProtein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues ...
Acylation of proteins with fatty acids is important for the regulation of membrane association, traf...
AbstractFatty acid acylation of membrane proteins was studied on human erythrocytes by measuring inc...
Fatty acid acylation of proteins corresponds to the co- or post-translational covalent lin...
acyltransferase activ arle ive an onnec ylvani form A wide variety of cellular and viral proteins un...
AbstractMany glycoproteins of enveloped viruses as well as cellular proteins are covalently modified...
Red blood cells (RBCs) have long been known to contain acylated proteins and to display an active pa...
The enzyme acyl-CoA:cholesterol acyltransferase (ACAT) is normally localized in the endoplasmic reti...
Post-translational acylation of lysine side chains is a common mechanism of protein regulation. Modi...
In recent years several proteins have been found to be acylated with fatty acids as well as with iso...
Non-histone protein acylation is increasingly recognized as an important posttranslational modificat...
S-Fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16...
Post-translational modifications are covalent and generally enzyme-mediated modifications of protein...
Three related studies were performed to better characterize the intracellular process of protein S-a...
AbstractWe describe in this report the fatty acylation of some of the main polypeptides from the eye...
AbstractProtein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues ...
Acylation of proteins with fatty acids is important for the regulation of membrane association, traf...