The Nicotinic Acetylcholine Receptor: Structure and Autoimmune Pathology
- 1 January 1994
- journal article
- research article
- Published by Taylor & Francis in Critical Reviews in Biochemistry and Molecular Biology
- Vol. 29 (2) , 69-123
- https://doi.org/10.3109/10409239409086798
Abstract
The nicotinic acetylcholine receptors (AChR) are presently the best-characterized neurotransmitter receptors. They are pentamers of homologous or identical subunits, symmetrically arranged to form a transmembrane cation channel. The AChR subunits form a family of homologous proteins, derived from a common ancestor. An autoimmune response to muscle AChR causes the disease myasthenia gravis. This review summarizes recent developments in the understanding of the AChR structure and its molecular recognition by the immune system in myasthenia.Keywords
This publication has 371 references indexed in Scilit:
- Myasthenia gravis: recognition of a human autoantigen at the molecular levelImmunology Today, 1993
- Molecular dissection of cholinergic binding sites: How do snakes escape the effect of their own toxins?Biochemical and Biophysical Research Communications, 1991
- Amino acid residues forming the interface of a neuronal nicotinic acetylcholine receptor with κ-bungarotoxin: A study using single residue substituted peptide analogsBiochemical and Biophysical Research Communications, 1991
- Molecular mimicry among human autoantigensImmunology Today, 1991
- The main immunogenic region of the nicotinic acetylcholine receptor: Interaction of monoclonal antibodies with synthetic peptidesBiochemical and Biophysical Research Communications, 1989
- Universally immunogenic T cell epitopes: promiscuous binding to human MHC class II and promiscuous recognition by T cellsEuropean Journal of Immunology, 1989
- Photoaffinity labeling of functional states of the nicotinic acetylcholine receptorProtein Journal, 1988
- Acetylcholine receptor dimers are stabilized by extracellular disulfide bondingBiochemical and Biophysical Research Communications, 1986
- Structural features of the nicotinic acetylcholine receptor revealed by antibodies to synthetic peptidesBiochemical and Biophysical Research Communications, 1984
- Affinity directed crosslinking of acetylcholine receptor polypeptide components in post-synaptic membranesBiochemical and Biophysical Research Communications, 1978