2000
Nicotine Binding to Native and Substituted Peptides Comprising Residues 188–207 of Nicotinic Acetylcholine Receptor α1, α2, α3, α4, α5, and α7 Subunits
Lentz T. Nicotine Binding to Native and Substituted Peptides Comprising Residues 188–207 of Nicotinic Acetylcholine Receptor α1, α2, α3, α4, α5, and α7 Subunits. Biochemical And Biophysical Research Communications 2000, 268: 480-484. PMID: 10679230, DOI: 10.1006/bbrc.2000.2155.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptor α1Acetylcholine receptor alpha subunitNicotinic acetylcholine receptor alpha-subunitHigh affinity binding componentDifferent alpha subunitsReceptor alpha subunitNeuronal peptidesReceptor α1Alpha subunitΑ7 subunitAlpha4 subunitSignificant decreaseNicotineBinding componentSynthetic peptidesLow affinityPeptidesHigh affinity
1998
Rabies virus entry into cultured rat hippo campalneurons
Lewis P, Lentz T. Rabies virus entry into cultured rat hippo campalneurons. Brain Cell Biology 1998, 27: 559-573. PMID: 10405023, DOI: 10.1023/a:1006912610044.Peer-Reviewed Original ResearchConceptsRabies virus entryCultured hippocampal neuronsViral antigensHippocampal neuronsRabies virusVirus entryRabies virus infectionSynaptic vesicle markersAxon terminalsNerve terminalsVirus infectionLysosomotropic agent chloroquineSomatodendritic domainCell bodiesVirus-containing endosomesLucifer YellowNeuronsSynapsin IInfectionAntigenTransferrin receptorVirusWheat germ agglutininAgent chloroquineVesicle markers
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
1986
α-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
1980
Binding of horseradish peroxidase‐α‐bungarotoxin to axonal membranes at the node of ranvier
Freedman S, Lentz T. Binding of horseradish peroxidase‐α‐bungarotoxin to axonal membranes at the node of ranvier. The Journal Of Comparative Neurology 1980, 193: 179-185. PMID: 7430427, DOI: 10.1002/cne.901930112.Peer-Reviewed Original Research
1974
NEUROTROPHIC REGULATION AT THE NEUROMUSCULAR JUNCTION*
Lentz T. NEUROTROPHIC REGULATION AT THE NEUROMUSCULAR JUNCTION*. Annals Of The New York Academy Of Sciences 1974, 228: 323-337. PMID: 4366904, DOI: 10.1111/j.1749-6632.1974.tb20521.x.Peer-Reviewed Original Research