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Chemical Compound Review

GLYCOPROTEIN     (2S)-2-acetamido-N'- [(3R,4R,5S,6R)-3...

Synonyms: CPD-8582, AC1L96W8, 2859-EP2270015A1, 2859-EP2284159A1, 2859-EP2287167A1, ...
 
 
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Disease relevance of GLYCOPROTEIN

 

Psychiatry related information on GLYCOPROTEIN

 

High impact information on GLYCOPROTEIN

 

Chemical compound and disease context of GLYCOPROTEIN

 

Biological context of GLYCOPROTEIN

 

Anatomical context of GLYCOPROTEIN

 

Associations of GLYCOPROTEIN with other chemical compounds

  • Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation [31].
  • In some cases (Fc receptor, lysosomal glycoprotein Igp120), the determinant appears similar to that required for endocytosis via clathrin-coated pits; for Igp120, elimination of a single cytoplasmic domain tyrosine both blocks internalization and results in apical transport [32].
  • We establish that the position-specific antigen 2 (PS2), a Drosophila cell surface glycoprotein complex, is an invertebrate member of the vertebrate fibronectin receptor (integrin) family [33].
  • Here, we show that EXT1 is an ER-resident type II transmembrane glycoprotein whose expression in cells results in the alteration of the synthesis and display of cell surface heparan sulfate glycosaminoglycans (GAGs) [34].
  • The transport of sugar residues into the endoplasmic reticulum (ER) during glycoprotein synthesis was studied by examining the transmembrane orientations of the oligosaccharide-lipid precursors of asparagine-linked oligosaccharides [35].
 

Gene context of GLYCOPROTEIN

 

Analytical, diagnostic and therapeutic context of GLYCOPROTEIN

References

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  32. Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinant. Hunziker, W., Harter, C., Matter, K., Mellman, I. Cell (1991) [Pubmed]
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  34. The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate. McCormick, C., Leduc, Y., Martindale, D., Mattison, K., Esford, L.E., Dyer, A.P., Tufaro, F. Nat. Genet. (1998) [Pubmed]
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  45. The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae. Braell, W.A., Balch, W.E., Dobbertin, D.C., Rothman, J.E. Cell (1984) [Pubmed]
 
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