...Nicole Thompson; Warren Wakarchuk Protein glycosylation is ubiquitous throughout biology. From bacteria to humans, this post translational modification with sophisticated carbohydrate structures plays a profound role in the interaction of proteins with cells and changes the physiochemical...

... ectopically expressing N-terminally FLAG-tagged human GPR30 and three unique antibodies (Ab) specifically targetting the receptor N-terminal domain (N-domain) to investigate the role of N -glycosylation in receptor maturation and activity, the latter assayed by constitutive receptor-stimulated extracellular...

... , and they are frequently modified with N-glycans that contribute to protein function. TRPA1 possesses two putative N-linked glycosylation sites at Asn 747 and Asn 753 that have not yet been studied in detail. In the present study, we show that both of these sites can be modified with an N-glycan and that the glycan...

... characterized for cell surface expression and function. One mutant (I573A) showed disrupted glycosylation and reduced trafficking kinetics. In contrast with many ABC transporter folding mutations which appear to be ‘rescued’ by chemical chaperones or low temperature incubation, the I573A mutation...

..., distribution and reproduction in any medium, provided the original work is properly cited. epitope tag G protein-coupled receptor glucagon-like peptide-1 receptor glycosylation signal peptide synthesis GLP-1R (glucagon-like peptide-1 receptor) is a validated therapeutic target...

...Yoram Tekoah; Salit Tzaban; Tali Kizhner; Mariana Hainrichson; Anna Gantman; Myriam Golembo; David Aviezer; Yoseph Shaaltiel The glycosylation of recombinant β-glucocerebrosidase, and in particular the exposure of mannose residues, has been shown to be a key factor in the success of ERT (enzyme...

... of common features. All contain multiple glycosylation sites, and must be trimeric and undergo proteolytic cleavage to be fusogenically active. Subsequent to proteolytic cleavage, the subunit containing the transmembrane domain in each case has an extremely hydrophobic region, termed the fusion peptide...

... binding to CN and CR. © 1999 Plenum Publishing Corporation 1999 Apolipoprotein B Assembly Calnexin Calreticulin Chaperones Endoplasmic Reticulum Glycosylation Bioscience Reports, Vol. 19, No. 3, 1999 Interaction of Newly Synthesized Apolipoprotein B with Calnexin and Calreticulin Requires...

.... This enhanced incorporation is not due to a direct effect of monensin on glycosyltransferase activities themselves but is a consequence of a higher entry and accumulation of labelled sugar nucleotides in the dilated vesicles. Sugar nucleotide transport monensin glycosylation cell permeabilisation ©...