Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non-identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex-Reference-Cited by-同舟云学术

Homomeric and native α7 acetylcholine receptors exhibit remarkably similar but non-identical pharmacological properties, suggesting that the native receptor is a heteromeric protein complex

Published:1993-07-26 Issue:2 Volume:327 Page:241-246
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Anand René,Peng Xiao,Lindstrom Jon

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(93)80177-V/fullpdf

Reference36 articles.

1. Brain α-bungarotoxin binding protein cDNAs and MAbs reveal subtypes of this branch of the ligand-gated ion channel gene superfamily

2. A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTX

3. Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor

4. Functional significance of aromatic amino acids from three peptide loops of the α7 neuronal nicotinic receptor site investigated by site-directed mutagenesis

5. Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain.

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