IndraLab

Statements


AR is modified
| 36
AR is glycosylated. 10 / 36
| 36

sparser
"The role of glycosylation in α 2a -AR trafficking was previous examined in polarized MDCK cells, where a glycosylation deficient mutant α 2a -AR displayed normal binding and trafficking to the basolateral membrane ( xref )."

sparser
"β 1 AR glycosylation influences responses to agonistic autoantibodies."

sparser
"These data reveal that blocking β 1 AR N-linked glycosylation impairs β 1 AR dimerization."

sparser
"The observation that the untagged β 1 AR is processed (like the tagged β 1 AR) to a ~69-kDa protein that contains sialylated N- and O-linked glycans in ldlD cells grown with Gal/GalNAc establishes that the N- and C-terminal tags do not influence β 1 AR glycosylation."

sparser
"Taken together, the immunofluorescence, FACS analysis, and endoglycosidase experiments suggest that asparagine-linked glycosylation of α 2c -ARs is not the predominate mechanism responsible for the distinct trafficking behavior observed for the α 2c -ARs."

sparser
"N-Linked glycosylation of the alpha(1B)-AR occurs at four asparagines on the N-terminus of the receptor."

sparser
"MS/MS analysis of β 2 AR following PNGase F treatment lead to the identification of peptides originating from the N-terminus (residues 1-19), confirming that β 2 AR was heavily glycosylated."

sparser
"The average median fluorescent intensity of cell surface expressed receptors obtained for three α 2c -AR glycosylation mutants, α 2c - (N19Q)-AR, α 2c - (N33Q)-AR and α 2c - (N19Q/N33Q)-AR, were lower than wild type α 2c -AR (57+/− 11%, 54 +/− 12% and 46.5 +/− 5%, respectively)."

sparser
"Here we demonstrate that the polypeptide GalNAc-transferase 2 (GalNAc-T2) specifically O -glycosylates β 1 AR at five residues in the extracellular N terminus, including the Ser-49 residue at the location of the common S49G single-nucleotide polymorphism."

sparser
"β 1 AR Glycosylation Sites."
GALNT2 affects AR
| 1
GALNT2 glycosylates AR. 1 / 1
| 1

reach
"Here we demonstrate that the polypeptide GalNAc-transferase 2 (GalNAc-T2) specifically O -glycosylates beta 1 AR at five residues in the extracellular N terminus, including the Ser 49 residue at the location of the common S49G single-nucleotide polymorphism."