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
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
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
1993
Effects of mutations of Torpedo acetylcholine receptor alpha 1 subunit residues 184-200 on alpha-bungarotoxin binding in a recombinant fusion protein.
Chaturvedi V, Donnelly-Roberts D, Lentz T. Effects of mutations of Torpedo acetylcholine receptor alpha 1 subunit residues 184-200 on alpha-bungarotoxin binding in a recombinant fusion protein. Biochemistry 1993, 32: 9570-6. PMID: 8373764, DOI: 10.1021/bi00088a008.Peer-Reviewed Original ResearchConceptsAlpha 1 subunitFusion proteinAlpha-bungarotoxin bindingFusion protein containingOligonucleotide-directed mutagenesisEffects of mutationsPossible structure-function relationshipsStructure-function relationshipsTyr-189Dissimilar residuesPro-194Recombinant fusion proteinHigher apparent affinityAlpha subunitTyr-198Asp-195Cys-192Cys-193Protein containingFunctional interactionAmino acidsSubunitsResiduesMutationsPosition 184Sodium 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
1991
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.
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
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 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
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 ResearchConceptsAcetylcholine 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
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 determinant
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
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 ResearchConceptsAlpha subunitProtein blotsEndoglycosidase HHigh-mannose oligosaccharide chainsAcetylcholine receptorsAssociation of toxinAcetylcholine receptor subunitsReceptor-containing membranesOligosaccharide sideTorpedo electric organSingle labeled bandDirect bindingTorpedo acetylcholine receptorTorpedo californicaSubunits
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