The major palmitoylated human erythrocyte membrane protein has an Mr of 55000. It is distinct from the glucose transporter and is not derived from band 3 or ankyrin. It resists salt extraction suggesting a high affinity for the membrane. Pulse chase experiments demonstrate that palmitoylation is a dynamic process, and it may therefore have regulatory significance in membrane protein-protein or protein-lipid interaction. Slower dynamics of palmitoylation in erythrocytes from patients suffering from chronic myelogenous leukemia, which are less stable than normal erythrocytes, strenghten this view
The reversible thioester linkage of palmitic acid on cysteines is known as protein S-palmitoylation,...
Palmitoylation is lipid post-translational modification of proteins. It is one of the most common pr...
S-palmitoylation is a posttranslational modification that regulates membrane–protein interactions. H...
AbstractFatty acid acylation of membrane proteins was studied on human erythrocytes by measuring inc...
S-Acylation of proteins is a ubiquitous post-translational modification and a common signal for memb...
Red blood cells (RBCs) have long been known to contain acylated proteins and to display an active pa...
AbstractIncubation of intact human erythrocytes with [3H]palmitate labeled a protein with electropho...
Protein palmitoylation is a post-translation modification, which typically regulates the protein int...
Erythrocyte lipid rafts are anchored to the underlying spectrin membrane skeleton [A. Ciana, C. Achi...
Protein palmitoylation involves the post-translational attachment of palmitate in thioester linkage ...
In this paper we report that palmitoyl-L-carnitine can be a metabolic intermediate of the fatty acid...
AbstractCovalent attachment of myristate and/or palmitate occurs on a wide variety of viral and cell...
acyltransferase activ arle ive an onnec ylvani form A wide variety of cellular and viral proteins un...
S-palmitoylation involves the attachment of a 16-carbon long fatty acid chain to the cysteine residu...
Protein 4.2 is a major protein of the human erythrocyte membrane. It has previously been shown to be...
The reversible thioester linkage of palmitic acid on cysteines is known as protein S-palmitoylation,...
Palmitoylation is lipid post-translational modification of proteins. It is one of the most common pr...
S-palmitoylation is a posttranslational modification that regulates membrane–protein interactions. H...
AbstractFatty acid acylation of membrane proteins was studied on human erythrocytes by measuring inc...
S-Acylation of proteins is a ubiquitous post-translational modification and a common signal for memb...
Red blood cells (RBCs) have long been known to contain acylated proteins and to display an active pa...
AbstractIncubation of intact human erythrocytes with [3H]palmitate labeled a protein with electropho...
Protein palmitoylation is a post-translation modification, which typically regulates the protein int...
Erythrocyte lipid rafts are anchored to the underlying spectrin membrane skeleton [A. Ciana, C. Achi...
Protein palmitoylation involves the post-translational attachment of palmitate in thioester linkage ...
In this paper we report that palmitoyl-L-carnitine can be a metabolic intermediate of the fatty acid...
AbstractCovalent attachment of myristate and/or palmitate occurs on a wide variety of viral and cell...
acyltransferase activ arle ive an onnec ylvani form A wide variety of cellular and viral proteins un...
S-palmitoylation involves the attachment of a 16-carbon long fatty acid chain to the cysteine residu...
Protein 4.2 is a major protein of the human erythrocyte membrane. It has previously been shown to be...
The reversible thioester linkage of palmitic acid on cysteines is known as protein S-palmitoylation,...
Palmitoylation is lipid post-translational modification of proteins. It is one of the most common pr...
S-palmitoylation is a posttranslational modification that regulates membrane–protein interactions. H...