The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.

The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

The covalent attachment of sialic acid to a substrate molecule.

The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.

The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.

A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.

An immune response mediated through a body fluid.

The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form a core O-glycan structure.

The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.

Any process that activates or increases the frequency, rate or extent of mononuclear cell proliferation.

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus.

Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient.

Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient.

The covalent attachment of sialic acid to a substrate molecule.

The covalent attachment of sialic acid to a substrate molecule.

Any process that modulates the frequency, rate or extent of substrate adhesion-dependent cell spreading.

Any process that modulates the frequency, rate or extent of substrate adhesion-dependent cell spreading.

A protein modification process that results in the addition of a sialic acid unit to the end of an oligosaccharide chain in a glycoprotein.

A protein modification process that results in the addition of a sialic acid unit to the end of an oligosaccharide chain in a glycoprotein.

Any process that stops, prevents, or reduces the frequency, rate or extent of macrophage apoptotic process.

Any process that stops, prevents, or reduces the frequency, rate or extent of macrophage apoptotic process.

The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

The Golgi cisterna farthest from the endoplasmic reticulum; the final processing compartment through which proteins pass before exiting the Golgi apparatus; the compartment in which N-linked protein glycosylation is completed.

The Golgi cisterna farthest from the endoplasmic reticulum; the final processing compartment through which proteins pass before exiting the Golgi apparatus; the compartment in which N-linked protein glycosylation is completed.

The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

The middle Golgi cisterna (or cisternae).

The middle Golgi cisterna (or cisternae).