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
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
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
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 antibodiesGlycoproteinPeptidesBinding 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
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 glycoproteinThe recognition event between virus and host cell receptor: a target for antiviral agents
Lentz T. The recognition event between virus and host cell receptor: a target for antiviral agents. Journal Of General Virology 1990, 71: 751-766. PMID: 2109039, DOI: 10.1099/0022-1317-71-4-751.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntiviral AgentsHumansMolecular Sequence DataReceptors, VirusViral ProteinsViruses
1989
Synthetic 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
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