1993
Sodium dodecyl sulfate- and carbamylcholine-induced changes in circular dichroism spectra of acetylcholine receptor synthetic peptides
Donnelly-Roberts D, Lentz T. Sodium dodecyl sulfate- and carbamylcholine-induced changes in circular dichroism spectra of acetylcholine receptor synthetic peptides. Brain Research 1993, 19: 55-61. PMID: 8361345, DOI: 10.1016/0169-328x(93)90148-i.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfatePresence of SDSDodecyl sulfateCircular dichroism spectroscopyCritical micelle concentrationCircular dichroism spectraResidue peptideSecondary structureSynthetic peptidesDichroism spectroscopySignificant secondary structureAromatic chromophoresMicelle concentrationCircular dichroismDichroism spectraNanomolar rangeAsymmetric environmentConformational changesConformationPeptidesSulfateSpectraSpectroscopyChromophore
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
1990
Rabies susceptibility and acetylcholine receptor
Baer G, Shaddock J, Quirion R, Dam T, Lentz T. Rabies susceptibility and acetylcholine receptor. The Lancet 1990, 335: 664-665. PMID: 1969042, DOI: 10.1016/0140-6736(90)90454-d.Peer-Reviewed Original ResearchAnimalsDisease SusceptibilityFoxesIn Vitro TechniquesMusclesOpossumsRabies virusReceptors, Cholinergic
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 ResearchSynthetic 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
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 ResearchBinding of alpha-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the alpha subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high-affinity binding by sodium dodecyl sulfate.
Wilson P, Lentz T. Binding of alpha-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the alpha subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high-affinity binding by sodium dodecyl sulfate. Biochemistry 1988, 27: 6667-74. PMID: 3196679, DOI: 10.1021/bi00418a004.Peer-Reviewed Original ResearchNeurotoxin-Binding Site on The Acetylcholine Receptor
Lentz T, Wilson P. Neurotoxin-Binding Site on The Acetylcholine Receptor. International Review Of Neurobiology 1988, 29: 117-160. PMID: 3042662, DOI: 10.1016/s0074-7742(08)60085-9.Peer-Reviewed Original ResearchConceptsAcetylcholine-binding siteBinding of acetylcholineToxin-binding sitesPrimary amino acid sequenceAmino acid sequenceAcetylcholine receptorsCation-selective channelsAcid sequenceGenetic engineeringEssential functionsChemical signalsConformational changesNicotinic acetylcholine receptorsUse of toxinsMotor nerve terminalsMuscle cellsAChRCuraremimetic neurotoxinsBindingNeurotransmitter acetylcholineNeuromuscular junctionNicotinic AChRsReceptorsNerve terminalsHigh affinitySynthetic 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 ResearchMeSH KeywordsAnimalsCloning, MolecularGene Expression RegulationHumansMembrane GlycoproteinsNeurotoxinsRabies virusReceptors, CholinergicConceptsSnake 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
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, 387: 211-9. PMID: 3828757, DOI: 10.1016/0169-328x(86)90027-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBungarotoxinsChemical PhenomenaChemistryElectric OrganHydrogen-Ion ConcentrationKineticsRabies virusReceptors, CholinergicTubocurarineConceptsAcetylcholine receptorsRabies virusRabies virus receptorTorpedo acetylcholine receptorReceptor concentrationNeurotransmitter receptorsVirus receptorTorpedo electric organReceptorsVirusIncubation mediumVirus interactionsVirus particlesVirus concentrationDirect bindingElectric organAtropineAcetylcholineAChRα-Bungarotoxin binding to a high molecular weight component from lower vertebrate brain identified on dodecyl sulfate protein-blots
Hawrot E, Wilson P, Gershoni J, Reese J, Lentz T. α-Bungarotoxin binding to a high molecular weight component from lower vertebrate brain identified on dodecyl sulfate protein-blots. Brain Research 1986, 373: 227-234. PMID: 3719308, DOI: 10.1016/0006-8993(86)90335-5.Peer-Reviewed Original Research
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
Amino Acid Sequence Similarity Between Rabies Virus Glycoprotein and Snake Venom Curaremimetic Neurotoxins
Lentz T, Wilson P, Hawrot E, Speicher D. Amino Acid Sequence Similarity Between Rabies Virus Glycoprotein and Snake Venom Curaremimetic Neurotoxins. Science 1984, 226: 847-848. PMID: 6494916, DOI: 10.1126/science.6494916.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsGlycoproteinsNeurotoxinsRabies virusReceptors, CholinergicSnake VenomsSnakesViral ProteinsConceptsAmino acid sequence similarityAcetylcholine receptorsNeurotropic rabies virusVirus glycoproteinRabies virus glycoproteinCuraremimetic neurotoxinsHost cell receptorsSequence similarityGreater identityDirect bindingLong neurotoxinsRabies virusReceptor-binding regionRecognition sitesViral glycoproteinsGlycoproteinEntire sequenceNeurotoxinReceptorsBinding 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
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 ResearchMeSH KeywordsAnimalsBungarotoxinsCell MembraneElectric OrganKineticsMacromolecular SubstancesReceptors, CholinergicTorpedoTubocurarineConceptsAlpha subunitProtein blotsEndoglycosidase HHigh-mannose oligosaccharide chainsAcetylcholine receptorsAssociation of toxinAcetylcholine receptor subunitsReceptor-containing membranesOligosaccharide sideTorpedo electric organSingle labeled bandDirect bindingTorpedo acetylcholine receptorTorpedo californicaSubunitsThe acetylcholine receptor as a cellular receptor for rabies virus.
Lentz T, Burrage T, Smith A, Tignor G. The acetylcholine receptor as a cellular receptor for rabies virus. The Yale Journal Of Biology And Medicine 1983, 56: 315-22. PMID: 6367238, PMCID: PMC2589619.Peer-Reviewed Original ResearchMeSH KeywordsAdhesivenessAnimalsHumansNervous SystemNeuromuscular JunctionRabiesRabies virusReceptors, CholinergicReceptors, VirusConceptsAcetylcholine receptorsHost cell receptorsRabies virusSpecific host cell receptorsCell receptorTissue tropismMotor nerve endingsRabies virus pathogenesisMyasthenia gravisAutoimmune diseasesCultured muscle cellsNerve endingsTranssynaptic transferViral antigensViral immunizationVirus pathogenesisDisease processNeurotransmitter receptorsViral infectionIntact hostCellular tropismNeuromuscular junctionInfected animalsMuscle cellsVirus attachment
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 ResearchDistribution of Cell Surface Saccharides and Fibronectin on Cultured Chick Myotubes: Relationship to Acetylcholine Receptor Clusters
Burrage T, Lentz T. Distribution of Cell Surface Saccharides and Fibronectin on Cultured Chick Myotubes: Relationship to Acetylcholine Receptor Clusters. Developmental Neuroscience 1982, 5: 533-545. PMID: 7160317, DOI: 10.1159/000112715.Peer-Reviewed Original Research
1981
Ultrastructural characterization of surface specializations containing high-density acetylcholine receptors on embryonic chick myotubes in vivo and in vitro
Burrage T, Lentz T. Ultrastructural characterization of surface specializations containing high-density acetylcholine receptors on embryonic chick myotubes in vivo and in vitro. Developmental Biology 1981, 85: 267-286. PMID: 7262458, DOI: 10.1016/0012-1606(81)90259-1.Peer-Reviewed Original Research
1977
Cytochemical localization of acetylcholine receptors at the neuromuscular junction by means of horseradish peroxidase-labelled α-bungarotoxin
Lentz T, Mazurkiewicz J, Rosenthal J. Cytochemical localization of acetylcholine receptors at the neuromuscular junction by means of horseradish peroxidase-labelled α-bungarotoxin. Brain Research 1977, 132: 423-442. PMID: 912399, DOI: 10.1016/0006-8993(77)90192-5.Peer-Reviewed Original ResearchConceptsMotor endplatesNerve terminalsACh receptorsJunctional foldsAcetylcholine receptorsNeuromuscular junctionPreincubation of tissuesIncubation of tissuePresynaptic activityAlpha-BTXHorseradish peroxidaseSynaptic cleftΑ-bungarotoxinNon-junctional regionsExtrajunctional regionsReceptorsMuscle fibersMuscle surfaceEndplateApical portionObvious accumulationTissueAxolemmaSlight activityCytochemical localization