N-Glycosylation at the conserved sites ensures the expression of properly folded functional ACh receptors
- 1 May 1997
- journal article
- Published by Elsevier in Molecular Brain Research
- Vol. 45 (2) , 219-229
- https://doi.org/10.1016/s0169-328x(96)00256-2
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Role of the Endoplasmic Reticulum Chaperone Calnexin in Subunit Folding and Assembly of Nicotinic Acetylcholine ReceptorsPublished by Elsevier ,1995
- Role of Two Acetylcholine Receptor Subunit Domains in Homomer Formation and Intersubunit Recognition, as Revealed by .alpha.3 and .alpha.7 Subunit ChimerasBiochemistry, 1994
- Analysis of subunit assembly of the Na-K-ATPaseAmerican Journal of Physiology-Cell Physiology, 1994
- The Nicotinic Acetylcholine Receptor: Structure and Autoimmune PathologyCritical Reviews in Biochemistry and Molecular Biology, 1994
- Acetylcholine receptor assembly: Subunit folding and oligomerization occur sequentiallyCell, 1993
- Site-directed mutagenesis of the conserved N-glycosylation site on the nicotinic acetylcholine receptor subunitsMolecular Brain Research, 1991
- Assembly intermediates of the mouse muscle nicotinic acetylcholine receptor in stably transfected fibroblasts.The Journal of cell biology, 1990
- Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptorNeuron, 1989
- Monoclonal antibodies specific for each of the two toxin binding sites of Torpedo acetylcholine receptorBiochemistry, 1987
- In vitro synthesis, glycosylation, and membrane insertion of the four subunits of Torpedo acetylcholine receptor.Proceedings of the National Academy of Sciences, 1981