Bacterial lipopolysaccharides, phorbol myristate acetate, and zymosan induce the myristoylation of specific macrophage proteins.
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Zanvil Alexander Cohn 1926-1993Cloning and molecular characterization of the murine macrophage "68-kDa" protein kinase C substrate and its regulation by bacterial lipopolysaccharideInterferon gamma induces the myristoylation of a 48-kDa protein in macrophagesTumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate.Myristoylation: An Important Protein Modification in the Immune ResponseBacterial lipopolysaccharides prime human neutrophils for enhanced production of leukotriene B4.Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase.Inhibition of endotoxin-induced priming of human neutrophils by lipid X and 3-Aza-lipid X.Acylation of monocyte and glomerular mesangial cell proteins. Myristyl acylation of the interleukin 1 precursors.Calcium ionophore synergizes with bacterial lipopolysaccharides in activating macrophage arachidonic acid metabolism.Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae.Lipopolysaccharide/lipid A receptors on lymphocytes and macrophages.Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts.Regulation of membrane and subunit interactions by N-myristoylation of a G protein alpha subunit in yeast.Acylation of viral and eukaryotic proteins.MacMARCKS mutation blocks macrophage phagocytosis of zymosan.Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.Lipid A stimulates phospholipase D activity in rat mesangial cells via a G-protein.Human lung tissue macrophages, but not alveolar macrophages, express matrix metalloproteinases after direct contact with activated T lymphocytes.Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions.Possible role of Marcks in the cellular modulation of monocytic tissue factor-initiated hypercoagulation.Myristoylation does not modulate the properties of MARCKS-related protein (MRP) in solution.
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Bacterial lipopolysaccharides, phorbol myristate acetate, and zymosan induce the myristoylation of specific macrophage proteins.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on August 1986
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@en
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@nl
type
label
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@en
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@nl
prefLabel
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@en
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@nl
P2093
P2860
P356
P1476
Bacterial lipopolysaccharides, ...... specific macrophage proteins.
@en
P2093
P2860
P304
P356
10.1073/PNAS.83.16.5817
P407
P577
1986-08-01T00:00:00Z