1996
Rabies virus binding to the nicotinic acetylcholine receptor α subunit demonstrated by virus overlay protein binding assay
Gastka M, Horvath J, Lentz T. Rabies virus binding to the nicotinic acetylcholine receptor α subunit demonstrated by virus overlay protein binding assay. Journal Of General Virology 1996, 77: 2437-2440. PMID: 8887475, DOI: 10.1099/0022-1317-77-10-2437.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBinding, CompetitiveBungarotoxinsElectric OrganRabies virusReceptors, NicotinicReceptors, VirusTorpedoConceptsAlpha subunitNicotinic acetylcholine receptor α subunitAcetylcholine receptor α subunitElectric organ membranesVirus overlay proteinVirus overlay protein binding assaysTransfer of proteinsReceptor α subunitProtein binding assaysAChR alpha subunitOverlay proteinRabies virusΑ-subunitSubunitsGel electrophoresisAcetylcholine receptorsBinding assaysCuraremimetic neurotoxinsProteinMembraneVirusBindingAChRBlot
1995
Differential binding of nicotine and alpha-bungarotoxin to residues 173-204 of the nicotinic acetylcholine receptor alpha 1 subunit.
Lentz T. Differential binding of nicotine and alpha-bungarotoxin to residues 173-204 of the nicotinic acetylcholine receptor alpha 1 subunit. Biochemistry 1995, 34: 1316-22. PMID: 7827079, DOI: 10.1021/bi00004a026.Peer-Reviewed Original Research
1992
Substitution of Torpedo acetylcholine receptor alpha 1-subunit residues with snake alpha 1- and rat nerve alpha 3-subunit residues in recombinant fusion proteins: effect on alpha-bungarotoxin binding.
Chaturvedi V, Donnelly-Roberts D, Lentz T. Substitution of Torpedo acetylcholine receptor alpha 1-subunit residues with snake alpha 1- and rat nerve alpha 3-subunit residues in recombinant fusion proteins: effect on alpha-bungarotoxin binding. Biochemistry 1992, 31: 1370-5. PMID: 1736994, DOI: 10.1021/bi00120a012.Peer-Reviewed Original Research
1991
Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor.
Lentz T. Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor. Biochemistry 1991, 30: 10949-57. PMID: 1932020, DOI: 10.1021/bi00109a020.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding, CompetitiveCell MembraneElapid VenomsElectric OrganGlycoproteinsKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataNeurotoxinsPeptidesProtein ConformationRabies virusReceptors, NicotinicSequence Homology, Nucleic AcidTorpedoTubocurarineViral ProteinsConceptsRabies virus glycoproteinAcetylcholine receptorsVirus glycoproteinNicotinic acetylcholine receptorsTorpedo electric organ membranesElectric organ membranesD-tubocurarineToxin BReceptorsLoop 2Synthetic peptidesGlycoproteinPeptidesHigh affinityStructure-function relationshipsPhe-33GroupAcetylcholineBinding sites for alpha-bungarotoxin and the noncompetitive inhibitor phencyclidine on a synthetic peptide comprising residues 172-227 of the alpha-subunit of the nicotinic acetylcholine receptor.
Donnelly-Roberts D, Lentz T. Binding sites for alpha-bungarotoxin and the noncompetitive inhibitor phencyclidine on a synthetic peptide comprising residues 172-227 of the alpha-subunit of the nicotinic acetylcholine receptor. Biochemistry 1991, 30: 7484-91. PMID: 1854749, DOI: 10.1021/bi00244a017.Peer-Reviewed Original Research
1990
Rabies virus binding to an acetylcholine receptor α‐subunit peptide
Lentz T. Rabies virus binding to an acetylcholine receptor α‐subunit peptide. Journal Of Molecular Recognition 1990, 3: 82-88. PMID: 2361061, DOI: 10.1002/jmr.300030205.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptorsAcetylcholine receptorsRabies virusNeuronal nicotinic acetylcholine receptorsUseful antiviral agentsReceptor peptideBinding of virusAcetylcholine receptor αSynthetic peptidesHost cell receptorsRabies virus glycoproteinAttachment of virusViral attachment proteinAntiviral agentsAlpha 1 peptideReceptor αNeurotoxin bindsSynthetic peptide comprisingAlpha-subunit peptidesCell receptorCuraremimetic neurotoxinsReceptorsVirusSnake venomVirus glycoprotein
1989
Antibodies against an α-bungarotoxin-binding peptide of the α-subunit of the acetylcholine receptor
Donnelly-Roberts D, Lentz T. Antibodies against an α-bungarotoxin-binding peptide of the α-subunit of the acetylcholine receptor. Biochemical And Biophysical Research Communications 1989, 160: 289-295. PMID: 2469418, DOI: 10.1016/0006-291x(89)91654-9.Peer-Reviewed Original Research
1988
Distribution of alpha-bungarotoxin binding sites over residues 173-204 of the alpha subunit of the acetylcholine receptor.
Wilson P, Hawrot E, Lentz T. Distribution of alpha-bungarotoxin binding sites over residues 173-204 of the alpha subunit of the acetylcholine receptor. Molecular Pharmacology 1988, 34: 643-50. PMID: 3193956.Peer-Reviewed Original Research
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
1985
Rabies virus binding to cellular membranes measured by enzyme immunoassay
Lentz T, Chester J, Benson R, Hawrot E, Tignor G, Smith A. Rabies virus binding to cellular membranes measured by enzyme immunoassay. Muscle & Nerve 1985, 8: 336-345. PMID: 16758601, DOI: 10.1002/mus.880080411.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholinesteraseAnimalsAntibodiesBinding Sites, AntibodyBinding, CompetitiveCationsCell MembraneChick EmbryoCricetinaeDogsEmbryo, MammalianEnzyme-Linked Immunosorbent AssayGuinea PigsHumansHydrogen-Ion ConcentrationMiceMuscle Fibers, SkeletalNeuroblastomaPropiolactoneRabies virusRatsReceptors, CholinergicTemperatureTrypsinConceptsEnzyme-linked immunosorbent assayRabies virusAcetylcholine receptor contentTreatment of virusRabies virus antibodiesMost parenchymal organsReceptor contentSalivary gland membranesVirus antibodiesAcetylcholine receptorsParenchymal organsEnzyme immunoassayImmunosorbent assaySimilar developmental changesEmbryonic chick myotubesGland membranesSurface moleculesVirusMyotube membranesAntibodiesSecond antibodyInactivation of virusesChick myotubesDevelopmental changesLow levels
1984
Binding of alpha-bungarotoxin to proteolytic fragments of the alpha subunit of Torpedo acetylcholine receptor analyzed by protein transfer on positively charged membrane filters.
Wilson P, Gershoni J, Hawrot E, Lentz T. Binding of alpha-bungarotoxin to proteolytic fragments of the alpha subunit of Torpedo acetylcholine receptor analyzed by protein transfer on positively charged membrane filters. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 2553-2557. PMID: 6371817, PMCID: PMC345101, DOI: 10.1073/pnas.81.8.2553.Peer-Reviewed Original Research
1982
Is the Acetylcholine Receptor a Rabies Virus Receptor?
Lentz T, Burrage T, Smith A, Crick J, Tignor G. Is the Acetylcholine Receptor a Rabies Virus Receptor? Science 1982, 215: 182-184. PMID: 7053569, DOI: 10.1126/science.7053569.Peer-Reviewed Original Research