2001
Regulation of Ins(1,4,5)P3 receptor isoforms by endogenous modulators
Thrower E, Hagar R, Ehrlich B. Regulation of Ins(1,4,5)P3 receptor isoforms by endogenous modulators. Trends In Pharmacological Sciences 2001, 22: 580-586. PMID: 11698102, DOI: 10.1016/s0165-6147(00)01809-5.Peer-Reviewed Original Research
2000
Regulation of the Type III InsP3 Receptor by InsP3 and ATP
Hagar R, Ehrlich B. Regulation of the Type III InsP3 Receptor by InsP3 and ATP. Biophysical Journal 2000, 79: 271-278. PMID: 10866953, PMCID: PMC1300931, DOI: 10.1016/s0006-3495(00)76289-8.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAllosteric RegulationAnimalsBinding, CompetitiveCalcium ChannelsDose-Response Relationship, DrugEndoplasmic ReticulumInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsInsulinomaMicrosomesProtein IsoformsRatsReceptors, Cytoplasmic and NuclearSubstrate SpecificityTumor Cells, CulturedConceptsType IIIChannel activityIntracellular calciumMaximal channel activityATP concentrationProlonged stimulationDependent inhibitionAllosteric modulationInsP3 receptorEnhanced channel activityType IOpen probabilityOpen timeReceptorsHigh ATP concentrationsHigh levelsATPLow ATP concentrationsIsoformsActivity
1996
Ligand-gated calcium channels inside and out
Striggow F, Ehrlich B. Ligand-gated calcium channels inside and out. Current Opinion In Cell Biology 1996, 8: 490-495. PMID: 8791458, DOI: 10.1016/s0955-0674(96)80025-1.Peer-Reviewed Original ResearchConceptsLigand-gated calcium channelsStore-operated channelsCalcium-permeable channelsIntracellular membranesFunctional characterizationPlasma membraneAllosteric mechanismAssociated proteinsTrisphosphate receptorCalcium releaseRyanodine receptorIntracellular storesIntracellular calciumCalcium channelsMembraneReceptorsProteinTypes of channelsInositolRelease
1995
Functional properties of intracellular calcium-release channels
Ehrlich B. Functional properties of intracellular calcium-release channels. Current Opinion In Neurobiology 1995, 5: 304-309. PMID: 7580152, DOI: 10.1016/0959-4388(95)80042-5.Peer-Reviewed Original ResearchConceptsIntracellular calcium release channelsCalcium release channelLarge ion channelsCellular rolesCytoplasmic proteinsMolecular mechanismsRegulatory sitesTrisphosphate receptorFunctional interactionIon channelsRegulatory processesMajor classesRyanodine receptorProteinRecent studiesFunctional propertiesReceptorsCytoplasmInositol
1994
The pharmacology of intracellular Ca2+-release channels
Ehrlich B, Kaftan E, Bezprozvannaya S, Bezprozvanny I. The pharmacology of intracellular Ca2+-release channels. Trends In Pharmacological Sciences 1994, 15: 145-149. PMID: 7754532, DOI: 10.1016/0165-6147(94)90074-4.Peer-Reviewed Original ResearchStabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein
Brillantes A, Ondrias K, Scott A, Kobrinsky E, Ondriašová E, Moschella M, Jayaraman T, Landers M, Ehrlich B, Marks A. Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein. Cell 1994, 77: 513-523. PMID: 7514503, DOI: 10.1016/0092-8674(94)90214-3.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaffeineCalciumCalcium ChannelsCarrier ProteinsCell LineCloning, MolecularGene ExpressionHeat-Shock ProteinsIon Channel GatingIsometric ContractionLipid BilayersMuscle ProteinsPolyenesRabbitsRatsRecombinant ProteinsRNA, MessengerRuthenium RedRyanodineRyanodine Receptor Calcium Release ChannelSarcoplasmic ReticulumSirolimusTacrolimusTacrolimus Binding ProteinsConceptsCellular functionsFK506-binding proteinNatural cellular functionsRelease channel functionInsect cellsProline isomeraseIsomerase activityEndoplasmic reticulumChannel functionFKBP12Channel complexRyanodine receptorCytosolic receptorRelease channel complexRelease channelRapamycinProteinFunctional Ca2Open probabilityCaffeine activationIntracellular Ca2Mean open timeImmunosuppressant drugsCopurifiesReceptors
1993
ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites
Bezprozvanny I, Ehrlich B. ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites. Neuron 1993, 10: 1175-1184. PMID: 7686381, DOI: 10.1016/0896-6273(93)90065-y.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCalciumCalcium ChannelsCerebellumDogsEndoplasmic ReticulumInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsIon Channel GatingIon ChannelsKineticsLipid BilayersMathematicsMicrosomesModels, NeurologicalReceptors, Cell SurfaceReceptors, Cytoplasmic and NuclearSignal TransductionConceptsPresence of IP3Effect of ATPTrisphosphate-gated channelsIntracellular Ca2Average durationAllosteric modulationSingle-channel levelFunction of inositolIP3 receptorChannel activityCell viabilityReceptorsTrisphosphate receptorIP3Channel openingPermeable channelsCa2ATPInositolAddition of ATPNonhydrolyzable ATP analogChannel conductanceChannel incorporation