2000
Rabies virus entry at the neuromuscular junction in nerve–muscle cocultures
Lewis P, Fu Y, Lentz T. Rabies virus entry at the neuromuscular junction in nerve–muscle cocultures. Muscle & Nerve 2000, 23: 720-730. PMID: 10797395, DOI: 10.1002/(sici)1097-4598(200005)23:5<720::aid-mus9>3.0.co;2-5.Peer-Reviewed Original ResearchConceptsNerve cell bodiesRabies virus entryNerve-muscle coculturesNerve terminalsNerve fibersNeuromuscular junctionRabies virusCell bodiesVirus entryMotor nerve terminalsNerve-muscle contactsNicotinic acetylcholine receptorsVirus adsorption periodAcetylcholine receptorsLucifer YellowSynapsin ISynaptic vesiclesRetrograde transportVirusProgressive increaseEarly eventsCocultureSurface of cellsMyotube surfaceNeurons
1999
Waglerin-1 selectively blocks the epsilon form of the muscle nicotinic acetylcholine receptor.
McArdle J, Lentz T, Witzemann V, Schwarz H, Weinstein S, Schmidt J. Waglerin-1 selectively blocks the epsilon form of the muscle nicotinic acetylcholine receptor. Journal Of Pharmacology And Experimental Therapeutics 1999, 289: 543-50. PMID: 10087048.Peer-Reviewed Original ResearchConceptsWild-type miceEnd-plate potentialsAdult wild-type miceNicotinic acetylcholine receptorsWaglerin-1Miniature end-plate potentialsKO miceMuscle nicotinic acetylcholine receptorACh responseAcetylcholine receptorsEnd-plate responsesHeterozygous KO miceHomozygous KO miceNeonatal wild-type miceSpontaneous miniature end-plate potentialsMouse muscle nicotinic acetylcholine receptorHeterozygous litter matesAdult knockout miceLethal effectsNeonatal miceSuppressant effectKnockout miceLitter matesMiceAcetylcholine
1998
Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding
Lentz T, Chaturvedi V, Conti-Fine B. Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding. Biochemical Pharmacology 1998, 55: 341-347. PMID: 9484801, DOI: 10.1016/s0006-2952(97)00474-7.Peer-Reviewed Original ResearchConceptsNicotine bindingCys-192Cys-193Alpha1 subunitReceptor alpha1 subunitReceptor α1 subunitTyr-190Tyr-198Acetylcholine receptorsΑ1 subunitGreater reductionAsp-195Significant reductionFusion proteinPro-194Single concentrationThr-196Apparent KdAmino acidsSynthetic peptidesAsp-200Position 181Individual amino acidsResidues 181Previous studies
1997
Rabies virus infection of IMR-32 human neuroblastoma cells and effect of neurochemical and other agents
Lentz T, Fu Y, Lewis P. Rabies virus infection of IMR-32 human neuroblastoma cells and effect of neurochemical and other agents. Antiviral Research 1997, 35: 29-39. PMID: 9224959, DOI: 10.1016/s0166-3542(97)01036-x.Peer-Reviewed Original ResearchConceptsIMR-32 human neuroblastoma cellsIMR-32 cellsHuman neuroblastoma cellsNeuroblastoma cellsNeuronal nicotinic acetylcholine receptorsCentral nervous system receptorsRabies virusRabies virus infectionLysosomotropic agentsReceptor alpha1 subunitNicotinic acetylcholine receptorsNerve cell lineAttachment of virusNeurotropic virusesCholinergic agonistsViral antigensVirus infectionHuman neuronsAcetylcholine receptorsSynthetic peptidesCell bodiesInfectionAlpha1 subunitCholinergic ligandsBinding receptors
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 ResearchConceptsAlpha 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
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-33GroupAcetylcholineStructural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein
Donnelly-Roberts D, Lentz T. Structural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein. Brain Research 1991, 11: 107-113. PMID: 1661807, DOI: 10.1016/0169-328x(91)90112-b.Peer-Reviewed Original ResearchConceptsLoop 2Virus glycoproteinAcetylcholine receptorsRabies virus glycoproteinBeta-sheet structureCircular dichroism spectroscopyCuraremimetic neurotoxinsAcetylcholine-binding siteSynthetic peptidesNicotinic acetylcholine receptorsDichroism spectroscopyStructural similarityConformational similarityCorresponding peptidesPolyclonal antibodiesGlycoproteinPeptides
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 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
Neurotoxin-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 affinityChapter 9 Synthetic Peptides in the Study of the Nicotinic Acetylcholine Receptor
Hawrot E, Colson K, Lentz T, Wilson P. Chapter 9 Synthetic Peptides in the Study of the Nicotinic Acetylcholine Receptor. Current Topics In Membranes 1988, 33: 165-195. DOI: 10.1016/s0070-2161(08)60899-0.Peer-Reviewed Original ResearchSynthetic 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
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
1985
Determination of the primary amino acid sequence specifying the alpha-bungarotoxin binding site on the alpha subunit of the acetylcholine receptor from Torpedo californica.
Wilson P, Lentz T, Hawrot E. Determination of the primary amino acid sequence specifying the alpha-bungarotoxin binding site on the alpha subunit of the acetylcholine receptor from Torpedo californica. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 8790-8794. PMID: 3866252, PMCID: PMC391523, DOI: 10.1073/pnas.82.24.8790.Peer-Reviewed Original ResearchConceptsBungarotoxin-binding sitesPrimary amino acid sequenceAmino acid sequenceAlpha subunitAmino acidsAcid sequenceAcetylcholine receptorsNicotinic acetylcholine receptorsAlpha-bungarotoxin binding sitesEndoglycosidase H.Residues 173Torpedo californicaV8 proteaseSubunitsOligosaccharide chainsProteolytic fragmentsBinding sitesPresumed siteSize of fragmentsFragmentsSynthetic peptidesSequenceBind 125IDigestionMajor determinantRabies 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 ResearchConceptsAmino acid sequence similarityAcetylcholine receptorsNeurotropic rabies virusVirus glycoproteinRabies virus glycoproteinCuraremimetic neurotoxinsHost cell receptorsSequence similarityGreater identityDirect bindingLong neurotoxinsRabies virusReceptor-binding regionRecognition sitesViral glycoproteinsGlycoproteinEntire sequenceNeurotoxinReceptors