1989
Synthetic peptides of neurotoxins and rabies virus glycoprotein behave as antagonists in a functional assay for the acetylcholine receptor.
Donnelly-Roberts D, Lentz T. Synthetic peptides of neurotoxins and rabies virus glycoprotein behave as antagonists in a functional assay for the acetylcholine receptor. Chemical Biology & Drug Design 1989, 2: 221-6. PMID: 2520759.Peer-Reviewed Original ResearchConceptsLoop 2Acetylcholine receptorsLarge macromolecular complexesVirus glycoproteinCompetitive antagonist d-tubocurarineRabies virus glycoproteinSegment interactsMacromolecular complexesSynthetic peptidesNicotinic acetylcholine receptorsBC3H-1 cellsLarge moleculesFunctional assaysShort synthetic peptidesMicromolar rangeIon transportAntagonist d-tubocurarineEffective peptideBiological effectsIC50 valuesPeptidesReceptorsGlycoproteinNeurotoxinGlycoprotein peptide
1987
Synthetic peptides corresponding to sequences of snake venom neurotoxins and rabies virus glycoprotein bind to the nicotinic acetylcholine receptor
Lentz T, Hawrot E, Wilson P. Synthetic peptides corresponding to sequences of snake venom neurotoxins and rabies virus glycoprotein bind to the nicotinic acetylcholine receptor. Proteins Structure Function And Bioinformatics 1987, 2: 298-307. PMID: 3448605, DOI: 10.1002/prot.340020406.Peer-Reviewed Original ResearchConceptsLoop 2Alpha-bungarotoxin bindingAcetylcholine receptorsProtein-protein interactionsElectric organ acetylcholine receptorAlpha-subunit peptidesApparent affinityVirus glycoproteinCompetitive antagonist d-tubocurarineRabies virus glycoproteinSynthetic peptidesSnake venom neurotoxinsViral homologsAlpha subunitNative proteinNicotinic acetylcholine receptorsGlycoprotein actsGlu residuesIntact subunitVenom neurotoxinsHydrophobic subsitePosition 173Recognition sitesAntagonist d-tubocurarineArg37