Inhibition of N-linked glycosylation of the human type 1α metabotropic glutamate receptor by tunicamycin: effects on cell-surface receptor expression and function

@article{Mody1999InhibitionON,
  title={Inhibition of N-linked glycosylation of the human type 1α metabotropic glutamate receptor by tunicamycin: effects on cell-surface receptor expression and function},
  author={N. Mody and E. Hermans and S. Nahorski and R. Challiss},
  journal={Neuropharmacology},
  year={1999},
  volume={38},
  pages={1485-1492}
}
The potential role of N-linked glycosylation of the human type 1alpha metabotropic glutamate (mGlu1alpha) receptor was studied in a recombinant, inducible expression system, where receptor expression was induced in the absence and presence of tunicamycin. In the absence of tunicamycin the mGlu1alpha receptor appeared to be expressed, at least in part, as a dimer consisting of monomers of approx. 145 and 160 KDa relative molecular mass (Mr). In the presence of tunicamycin only a single monomeric… Expand
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