1988
Synthetic peptides in the study of the interaction of rabies virus and the acetylcholine receptor.
Lentz T, Hawrot E, Donnelly-Roberts D, Wilson P. Synthetic peptides in the study of the interaction of rabies virus and the acetylcholine receptor. Advances In Biochemical Psychopharmacology 1988, 44: 57-71. PMID: 3041753.Peer-Reviewed Original ResearchConceptsSnake venom neurotoxinsAmino acid sequence similarityCentral nervous systemAcetylcholine receptorsVirus glycoproteinVenom neurotoxinsPeriod of replicationRabies virus glycoproteinRegions of virusesNervous systemGenetic driftSequence similarityVirus-receptor interactionsMolecular basisRabies virusCertain neuronal populationsDirect bindingRNA virusesNicotinic acetylcholine receptorsCell surface constituentsBlood-brain barrierCell receptorGlycoproteinBindingD-tubocurarine
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