2019
A Positioning Device for the Placement of Mice During Intranasal siRNA Delivery to the Central Nervous System.
Ullah I, Chung K, Beloor J, Lee SK, Kumar P. A Positioning Device for the Placement of Mice During Intranasal siRNA Delivery to the Central Nervous System. Journal Of Visualized Experiments 2019 PMID: 31475960, DOI: 10.3791/59201.Peer-Reviewed Original ResearchConceptsCentral nervous systemBlood-brain barrierNervous systemIntranasal drug deliveryBody temperatureMin rest periodMouse body temperatureCNS uptakeReceptor-binding domainRabies virus glycoproteinCNS deliveryAnesthetized miceDominant handNondominant handMiceInhalationDelivery of siRNASiRNA approachDelivery of drugsRest periodHeating padMouse headAdministrationVirus glycoproteinForward position
2007
Transvascular delivery of small interfering RNA to the central nervous system
Kumar P, Wu H, McBride JL, Jung KE, Hee Kim M, Davidson BL, Kyung Lee S, Shankar P, Manjunath N. Transvascular delivery of small interfering RNA to the central nervous system. Nature 2007, 448: 39-43. PMID: 17572664, DOI: 10.1038/nature05901.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBlood-Brain BarrierBrainCell LineDrug Delivery SystemsEncephalitis Virus, JapaneseEncephalitis, JapaneseGene SilencingGenetic VectorsGlycoproteinsGreen Fluorescent ProteinsHeLa CellsHumansLentivirusLiposomesMiceMice, Inbred BALB CMice, Inbred C57BLMice, Inbred NODMice, SCIDMolecular Sequence DataNeuronsOligopeptidesRabies virusReceptors, NicotinicRecombinant ProteinsRNA, Small InterferingSuperoxide DismutaseSuperoxide Dismutase-1Viral ProteinsConceptsRVG-9RBlood-brain barrierRabies virus glycoproteinNeuronal cellsTransvascular deliveryFatal viral encephalitisCentral nervous systemTherapeutic moleculesIntravenous treatmentViral encephalitisInflammatory cytokinesAntiviral siRNAIntravenous injectionNervous systemAcetylcholine receptorsNeurological diseasesAnti-peptide antibodiesChimaeric peptidesNoninvasive approachDelivery of siRNABrainSiRNAMiceVirus glycoproteinRobust protection
1991
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
Whitt M, Buonocor L, Prehaud C, Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 1991, 185: 681-688. PMID: 1660200, DOI: 10.1016/0042-6822(91)90539-n.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralBase SequenceCell LineCentrifugation, Density GradientCricetinaeFlow CytometryGenetic Complementation TestGlycoproteinsHumansHydrogen-Ion ConcentrationKineticsMacromolecular SubstancesMembrane FusionMembrane GlycoproteinsMiceMolecular Sequence DataPlasmidsRabies virusRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsVSV G proteinG protein trimersMembrane fusion activityVirus G proteinG proteinsRabies G proteinFusion activityHybrid proteinProtein trimerVesicular stomatitis virus G proteinVirus glycoproteinRabies virus glycoproteinCytoplasmic domainMembrane fusionExtracellular domainHeLa cellsRabies virus G proteinCell surfaceProteinVSV particlesSucrose gradientsVSV infectivityGlycoproteinSpike glycoproteinChemical crosslinkingStructure-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
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
1988
Synthetic 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
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
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