1990
Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities.
Sine S, Claudio T, Sigworth F. Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities. Journal Of General Physiology 1990, 96: 395-437. PMID: 1698917, PMCID: PMC2228994, DOI: 10.1085/jgp.96.2.395.Peer-Reviewed Original Research
1987
Genetic Reconstitution of Functional Acetylcholine Receptor Channels in Mouse Fibroblasts
Claudio T, Green W, Hartman D, Hayden D, Paulson H, Sigworth F, Sine S, Swedlund A. Genetic Reconstitution of Functional Acetylcholine Receptor Channels in Mouse Fibroblasts. Science 1987, 238: 1688-1694. PMID: 3686008, DOI: 10.1126/science.3686008.Peer-Reviewed Original ResearchConceptsExpression systemDNA-mediated gene transfer techniquesMouse fibroblast cellsDNA-mediated gene transferLigand-gated ion channelsCell surface AChRsNew expression systemFibroblast cellsTorpedo AChRClonal cell linesGene transfer techniquesForeign genesGene productsGenetic reconstitutionRecombinant DNACellular componentsTorpedo acetylcholine receptorComplementary DNASurface AChRsAcetylcholine receptor channelsFunctional consequencesGene transferIon channelsHomogenous cellsMouse fibroblasts
1986
Binding of rabies virus to purified Torpedo acetylcholine receptor
Lentz T, Benson R, Klimowicz D, Wilson P, Hawrot E. Binding of rabies virus to purified Torpedo acetylcholine receptor. Brain Research 1986, 1: 211-219. DOI: 10.1016/0169-328x(86)90027-6.Peer-Reviewed Original ResearchAcetylcholine receptorsRabies virusRabies virus receptorTorpedo acetylcholine receptorReceptor concentrationNeurotransmitter receptorsΑ-bungarotoxinVirus receptorTorpedo electric organReceptorsVirusIncubation mediumVirus interactionsVirus particlesVirus concentrationDirect bindingElectric organAtropineAcetylcholineAChRBinding of rabies virus to purified Torpedo acetylcholine receptor.
Lentz T, Benson R, Klimowicz D, Wilson P, Hawrot E. Binding of rabies virus to purified Torpedo acetylcholine receptor. Brain Research 1986, 387: 211-9. PMID: 3828757, DOI: 10.1016/0169-328x(86)90027-6.Peer-Reviewed Original ResearchConceptsAcetylcholine receptorsRabies virusRabies virus receptorTorpedo acetylcholine receptorReceptor concentrationNeurotransmitter receptorsVirus receptorTorpedo electric organReceptorsVirusIncubation mediumVirus interactionsVirus particlesVirus concentrationDirect bindingElectric organAtropineAcetylcholineAChRMapping of the Alpha‐Bungarotoxin Binding Site on the Primary Amino Acid Sequence of the Torpedo Acetylcholine Receptor
WILSON P, LENTZ T, HAWROT E. Mapping of the Alpha‐Bungarotoxin Binding Site on the Primary Amino Acid Sequence of the Torpedo Acetylcholine Receptor. Annals Of The New York Academy Of Sciences 1986, 463: 243-246. DOI: 10.1111/j.1749-6632.1986.tb21559.x.Peer-Reviewed Original Research
1983
Binding of alpha-bungarotoxin to isolated alpha subunit of the acetylcholine receptor of Torpedo californica: quantitative analysis with protein blots.
Gershoni J, Hawrot E, Lentz T. Binding of alpha-bungarotoxin to isolated alpha subunit of the acetylcholine receptor of Torpedo californica: quantitative analysis with protein blots. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 4973-4977. PMID: 6576369, PMCID: PMC384170, DOI: 10.1073/pnas.80.16.4973.Peer-Reviewed Original ResearchConceptsAlpha subunitProtein blotsEndoglycosidase HHigh-mannose oligosaccharide chainsAcetylcholine receptorsAssociation of toxinAcetylcholine receptor subunitsReceptor-containing membranesOligosaccharide sideTorpedo electric organSingle labeled bandDirect bindingTorpedo acetylcholine receptorTorpedo californicaSubunits
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