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
1991
Structural 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
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
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
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
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
1974
MICROFILAMENTS IN EPIDERMAL CANCER CELLS
Malech H, Lentz T. MICROFILAMENTS IN EPIDERMAL CANCER CELLS. Journal Of Cell Biology 1974, 60: 473-482. PMID: 4813215, PMCID: PMC2109157, DOI: 10.1083/jcb.60.2.473.Peer-Reviewed Original Research