2008
β1 integrin expression by podocytes is required to maintain glomerular structural integrity
Pozzi A, Jarad G, Moeckel GW, Coffa S, Zhang X, Gewin L, Eremina V, Hudson BG, Borza DB, Harris RC, Holzman LB, Phillips CL, Fassler R, Quaggin SE, Miner JH, Zent R. β1 integrin expression by podocytes is required to maintain glomerular structural integrity. Developmental Biology 2008, 316: 288-301. PMID: 18328474, PMCID: PMC2396524, DOI: 10.1016/j.ydbio.2008.01.022.Peer-Reviewed Original ResearchConceptsEnd-stage renal failureStage renal failureGlomerular structural integrityWeeks of agePodocin-cre miceGlomerular basement membraneGlomerular filtration barrier integrityNormal glomerular basement membraneExpression of beta1Renal failureGlomerular pathologyFiltration barrier integrityProgressive podocyte lossPodocyte lossGlomerular filtrationΒ1 integrin expressionBarrier integrityPodocyte abnormalitiesHeteromeric receptorsCapillary loopsGlomerular capillary formationMiceIntegrin expressionExtracellular matrixPodocytes
2000
Evidence for coassembly of mutant GABACρ1 with GABAAγ2S, glycine α1 and glycine α2 receptor subunits in vitro
Pan Z, Zhang D, Zhang X, Lipton S. Evidence for coassembly of mutant GABACρ1 with GABAAγ2S, glycine α1 and glycine α2 receptor subunits in vitro. European Journal Of Neuroscience 2000, 12: 3137-3145. PMID: 10998097, DOI: 10.1046/j.1460-9568.2000.00198.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDose-Response Relationship, DrugElectrophysiologyGABA Antagonistsgamma-Aminobutyric AcidGene ExpressionIn Vitro TechniquesMutagenesisNeural InhibitionOocytesPicrotoxinProtein Structure, TertiaryRatsReceptors, GABAReceptors, GABA-AReceptors, GABA-BReceptors, GlycineRetinaXenopus laevisConceptsGlycine alpha1Rho1 subunitAlpha2 subunitHeteromeric receptorsGABA dose-response curveBlockade of GABAVoltage-clamp recordingsGamma-aminobutyric acidXenopus laevis oocyte expression systemTwo-electrode voltage-clamp recordingsDose-response curveResponse propertiesPicrotoxinin sensitivityOocyte expression systemGamma2 subunitGABAReceptor subunitsPharmacological propertiesReceptorsUnique gatingFunctional evidenceGABAAAlpha1Gamma2Homomeric
1998
Cloning and characterization of mouse GABAC receptor subunits
Greka A, Koolen J, Lipton S, Zhang D. Cloning and characterization of mouse GABAC receptor subunits. Neuroreport 1998, 9: 229-232. PMID: 9507960, DOI: 10.1097/00001756-199801260-00010.Peer-Reviewed Original Research
1995
Cloning of a gamma-aminobutyric acid type C receptor subunit in rat retina with a methionine residue critical for picrotoxinin channel block.
Zhang D, Pan Z, Zhang X, Brideau A, Lipton S. Cloning of a gamma-aminobutyric acid type C receptor subunit in rat retina with a methionine residue critical for picrotoxinin channel block. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 11756-11760. PMID: 8524843, PMCID: PMC40481, DOI: 10.1073/pnas.92.25.11756.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChloride ChannelsCloning, MolecularDose-Response Relationship, DrugDrug ResistanceElectric ConductivityGABA AntagonistsIon ChannelsMethionineMolecular Sequence DataMutagenesis, Site-DirectedPicrotoxinProtein ConformationRatsReceptors, GABARetinaSequence Homology, Amino AcidSesterterpenesStructure-Activity RelationshipConceptsGABAC responsesRat retinaRho 2 subunitsGamma-aminobutyric acidPTX resistanceHeteromeric receptorsReceptor subunitsFunctional homomeric receptorsRho 1 receptorsGABA receptor subunitsInhibitory neurotransmissionMechanism of blockGABA receptorsMammalian retinaConvulsant picrotoxininHomomeric receptorsRat receptorRetinaIonotropic receptorsReceptorsChannel blockPicrotoxininSecond membrane-spanning regionNative receptorPredominant determinant
1994
Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor
Sullivan J, Traynelis S, Chen H, Escobar W, Heinemann S, Lipton S. Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron 1994, 13: 929-936. PMID: 7524561, DOI: 10.1016/0896-6273(94)90258-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCysteineDithiothreitolElectrophysiologyFemaleIon Channel GatingIon ChannelsMolecular Sequence DataMutagenesis, Site-DirectedN-MethylaspartateOocytesOxidation-ReductionPatch-Clamp TechniquesRatsReceptors, N-Methyl-D-AspartateRecombinant ProteinsSpermineStructure-Activity RelationshipXenopus
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