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Structural and functional diversity in 4-alpha-helical proteins.
Nature. 1980 Sep 4;287(5777):82-4
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Primary structure of alpha-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence.
Nature. 1982 Oct 28;299(5886):793-7
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Primary structures of beta- and delta-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences.
Nature. 1983 Jan 20;301(5897):251-5
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Structural homology of Torpedo californica acetylcholine receptor subunits.
Nature. 1983 Apr 7;302(5908):528-32
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Complete mRNA coding sequence of the acetylcholine binding alpha-subunit of Torpedo marmorata acetylcholine receptor: a model for the transmembrane organization of the polypeptide chain.
Proc Natl Acad Sci U S A. 1983 Apr;80(7):2067-71
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Nucleotide and deduced amino acid sequences of Torpedo californica acetylcholine receptor gamma subunit.
Proc Natl Acad Sci U S A. 1983 Feb;80(4):1111-5
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Acetylcholine receptor channel ionic selectivity: ions experience an aqueous environment.
Proc Natl Acad Sci U S A. 1983 Oct;80(19):6110-3
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Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor.
Proc Natl Acad Sci U S A. 1984 Jan;81(1):155-9
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A structural model of the acetylcholine receptor channel based on partition energy and helix packing calculations.
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Analysis of membrane and surface protein sequences with the hydrophobic moment plot.
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Isolation and characterization of a cDNA clone for the complete protein coding region of the delta subunit of the mouse acetylcholine receptor.
Proc Natl Acad Sci U S A. 1984 Dec;81(24):7970-4
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Structure linkage, and sequence of the two genes encoding the delta and gamma subunits of the nicotinic acetylcholine receptor.
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Kinetic analysis of channel gating. Application to the cholinergic receptor channel and the chloride channel from Torpedo californica.
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Primary structure of delta subunit precursor of calf muscle acetylcholine receptor deduced from cDNA sequence.
Eur J Biochem. 1985 May 15;149(1):5-13
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The structure of the voltage-sensitive sodium channel. Inferences derived from computer-aided analysis of the Electrophorus electricus channel primary structure.
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Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta subunit is labeled by [3H]chlorpromazine.
Proc Natl Acad Sci U S A. 1986 Apr;83(8):2719-23
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Transmembrane topography of nicotinic acetylcholine receptor: immunochemical tests contradict theoretical predictions based on hydrophobicity profiles.
Biochemistry. 1986 May 6;25(9):2633-43
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The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits.
FEBS Lett. 1986 Sep 1;205(1):137-42
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Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics.
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Location of a delta-subunit region determining ion transport through the acetylcholine receptor channel.
Nature. 1986 Dec 18-31;324(6098):670-4
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Monovalent and divalent cation permeation in acetylcholine receptor channels. Ion transport related to structure.
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Ionophore properties of a synthetic alpha-helical transmembrane fragment of the mitochondrial H+ ATP synthetase of Saccharomyces cerevisiae. Comparison with alamethicin.
Biophys J. 1988 Feb;53(2):193-203
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Channel protein engineering: synthetic 22-mer peptide from the primary structure of the voltage-sensitive sodium channel forms ionic channels in lipid bilayers.
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Synthetic amphiphilic peptide models for protein ion channels.
Science. 1988 May 27;240(4856):1177-81
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Photoaffinity labeling of functional states of the nicotinic acetylcholine receptor.
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Use of helical wheels to represent the structures of proteins and to identify segments with helical potential.
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