2019
Mammalian TRP ion channels are insensitive to membrane stretch
Nikolaev YA, Cox CD, Ridone P, Rohde PR, Cordero-Morales JF, Vásquez V, Laver DR, Martinac B. Mammalian TRP ion channels are insensitive to membrane stretch. Journal Of Cell Science 2019, 132: jcs238360. PMID: 31722978, PMCID: PMC6918743, DOI: 10.1242/jcs.238360.Peer-Reviewed Original ResearchConceptsTRP channelsTouch-insensitive mutantsMembrane stretchIon channelsTRP ion channel familyIon channel familyTransient receptor potential (TRP) ion channelsTRP ion channelsMammalian subfamiliesMammalian membersPotential ion channelsArtificial bilayer systemInsensitive mutantsCytoplasmic tethersDownstream componentsMechanosensory processesSignaling cascadesChannel familyCellular componentsBlood pressure regulationCell membraneCerebrospinal fluid flowMechanical forcesStretch activationPressure regulation
2015
Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog*
Tavoulari S, Margheritis E, Nagarajan A, DeWitt DC, Zhang YW, Rosado E, Ravera S, Rhoades E, Forrest LR, Rudnick G. Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog*. Journal Of Biological Chemistry 2015, 291: 1456-1471. PMID: 26582198, PMCID: PMC4714228, DOI: 10.1074/jbc.m115.692012.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAmino Acid Transport SystemsAquatic OrganismsBacterial ProteinsBinding SitesCysteineGram-Negative BacteriaLigandsLiposomesModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedMutationPlasma Membrane Neurotransmitter Transport ProteinsProtein ConformationProtein FoldingProtein StabilityProteolipidsRecombinant ProteinsSodiumConceptsConformational changesTransmembrane helix 1Open conformational stateDependent conformational changesTransporter homologExtracellular gateProkaryotic homologCytoplasmic pathwayHelix 1Interaction networksIntermediary interactionsBiophysical assaysNeurotransmitter transportersSubstrate pathwayNa2 siteConformational statesHelix motionsLeuTDirect interactionDependent closureHomologMutantsDistinct stepsResiduesComputational analysis
2012
SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open
Shi L, Shen QT, Kiel A, Wang J, Wang HW, Melia TJ, Rothman JE, Pincet F. SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open. Science 2012, 335: 1355-1359. PMID: 22422984, PMCID: PMC3736847, DOI: 10.1126/science.1214984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumDiffusionLipid BilayersLiposomesMembrane FusionMembrane ProteinsMiceNeurotransmitter AgentsProtein Structure, TertiaryProteolipidsRatsRecombinant Fusion ProteinsSNARE ProteinsSynaptic TransmissionSynaptic VesiclesSynaptosomal-Associated Protein 25Syntaxin 1Vesicle-Associated Membrane Protein 2ConceptsVesicle-associated membrane protein 2Bilayer fusionNative transmembrane domainNascent fusion poresLipid bilayer nanodiscsMembrane protein 2Synchronous neurotransmitter releaseSNARE complexTransmembrane helicesTransmembrane domainBilayer nanodiscsFused bilayersFusion porePore opensFusion partnerBiochemical studiesProtein 2Neurotransmitter releaseNanodiscsSnareEfficient releaseSynaptic transmissionSNAREpinsFusionRelevant time scales
2011
Lysosomal Trafficking, Antigen Presentation, and Microbial Killing Are Controlled by the Arf-like GTPase Arl8b
Garg S, Sharma M, Ung C, Tuli A, Barral D, Hava D, Veerapen N, Besra G, Hacohen N, Brenner M. Lysosomal Trafficking, Antigen Presentation, and Microbial Killing Are Controlled by the Arf-like GTPase Arl8b. Immunity 2011, 35: 182-193. PMID: 21802320, PMCID: PMC3584282, DOI: 10.1016/j.immuni.2011.06.009.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAntigen PresentationAntigensAntigens, CD1dCytokinesCytotoxicity, ImmunologicHeLa CellsHumansLymphocyte ActivationLysosomesNatural Killer T-CellsProtein BindingProtein TransportProteolipidsrab GTP-Binding Proteinsrab7 GTP-Binding ProteinsRNA, Small InterferingVesicular Transport ProteinsConceptsHomotypic fusion and vacuole protein sortingGTPase Arl8bMicrobial killingVacuole protein sortingPhagosome-lysosome fusionCargo traffickingProtein sortingArl8bShRNA librarySilenced cellsLysosomal traffickingPlasma membraneMolecular regulationImmunological screeningHost defenseLysosomesTraffickingAntigen presentationT cell activationCargo deliveryRegulationKillingCell activationImmunological functionsEffector
2010
MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney
Carmosino M, Rizzo F, Procino G, Basco D, Valenti G, Forbush B, Schaeren-Wiemers N, Caplan MJ, Svelto M. MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney. Molecular Biology Of The Cell 2010, 21: 3985-3997. PMID: 20861303, PMCID: PMC2982131, DOI: 10.1091/mbc.e10-05-0456.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineEndocytosisEpithelial CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMembrane Transport ProteinsMiceMice, TransgenicMyelin and Lymphocyte-Associated Proteolipid ProteinsMyelin ProteinsPhosphorylationProtein BindingProteolipidsRatsRats, Inbred WKYRNA InterferenceSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 1SwineConceptsRegulation of NKCC2Apical membraneMajor salt transport pathwayC-terminal tailCell surface retentionApical sortingPorcine kidney cellsCotransporter phosphorylationTransgenic mice resultsNephron structuresRegulated absorptionImportant roleNew playersKidney cellsSurface expressionMice resultsSurface retentionTransport pathwaysNKCC2MembraneRegulationLymphocyte-associated proteinCyst formationRat kidney medullaColocalizeProtein Determinants of SNARE-Mediated Lipid Mixing
Ji H, Coleman J, Yang R, Melia TJ, Rothman JE, Tareste D. Protein Determinants of SNARE-Mediated Lipid Mixing. Biophysical Journal 2010, 99: 553-560. PMID: 20643074, PMCID: PMC2905075, DOI: 10.1016/j.bpj.2010.04.060.Peer-Reviewed Original ResearchConceptsSNARE proteinsN-ethylmaleimide-sensitive factor attachment protein receptorsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSensitive factor attachment protein receptorsFactor attachment protein receptorsT-SNARE complexMembrane SNARE proteinsT-SNARE proteinsAttachment protein receptorsLipid mixingMembrane SNAREsProtein receptorsProtein determinantsReconstitution conditionsReconstitution protocolsSnareLiposome fusionProteinLiposome populationsSpecific activityLipidsOptimal lipidProteoliposomesPhysiologyRecent work
2009
Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
Wang L, Sigworth FJ. Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 2009, 461: 292-295. PMID: 19718020, PMCID: PMC2797367, DOI: 10.1038/nature08291.Peer-Reviewed Original ResearchConceptsVoltage sensor domainNative membrane environmentMembrane proteinsMembrane environmentChannel voltage-sensor domainElectron cryomicroscopyVoltage-activated potassium channelsSingle-particle electron cryomicroscopyIndividual protein particlesPotassium channelsBK potassium channelsLarge conductance calciumLipid membranesX-ray crystal structureBK channelsStructural studiesProtein particlesProteinCryomicroscopyCrystal structureFormation of crystalsDomainStructureCrystalsChannelsMammaglobin B is an independent prognostic marker in epithelial ovarian cancer and its expression is associated with reduced risk of disease recurrence
Tassi RA, Calza S, Ravaggi A, Bignotti E, Odicino FE, Tognon G, Donzelli C, Falchetti M, Rossi E, Todeschini P, Romani C, Bandiera E, Zanotti L, Pecorelli S, Santin AD. Mammaglobin B is an independent prognostic marker in epithelial ovarian cancer and its expression is associated with reduced risk of disease recurrence. BMC Cancer 2009, 9: 253. PMID: 19635143, PMCID: PMC2724548, DOI: 10.1186/1471-2407-9-253.Peer-Reviewed Original ResearchConceptsEpithelial ovarian cancerOvarian cancerEOC patientsMammaglobin BFresh-frozen tissue biopsiesMultiple histological subtypesDisease-free survivalLong-term prognosisAdditional prognostic informationRisk of recurrenceIndependent prognostic markerIndependent prognostic valueProtein levelsUnivariate survival analysisCancer-related deathAggressive tumor behaviorNormal ovarian controlsPrimary surgeryClinicopathologic characteristicsDisease recurrencePrognostic factorsClinical outcomesClinicopathologic featuresDecreased riskHistological subtypes
2007
Mammaglobin B expression in human endometrial cancer
TASSI RA, BIGNOTTI E, FALCHETTI M, CALZA S, RAVAGGI A, ROSSI E, MARTINELLI F, BANDIERA E, PECORELLI S, SANTIN AD. Mammaglobin B expression in human endometrial cancer. International Journal Of Gynecological Cancer 2007, 18: 1090-1096. PMID: 18021217, DOI: 10.1111/j.1525-1438.2007.01137.x.Peer-Reviewed Original ResearchConceptsReal-time polymerase chain reactionPolymerase chain reactionG3 casesNormal endometrial cellsHuman endometrial cancerFresh frozen biopsiesSignificant higher levelsParaffin-embedded tissuesEndometrial cancerG1 casesMammaglobin BNormal endometriumEndometrial tumorsEndometrial cellsOvarian cancerFrozen biopsyNovel molecular markersB expressionNEC controlsGene expression profilingImmunohistochemistryProtein expressionProtein levelsG2 casesChain reactionMAL decreases the internalization of the aquaporin-2 water channel
Kamsteeg EJ, Duffield AS, Konings IB, Spencer J, Pagel P, Deen PM, Caplan MJ. MAL decreases the internalization of the aquaporin-2 water channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16696-16701. PMID: 17940053, PMCID: PMC2034241, DOI: 10.1073/pnas.0708023104.Peer-Reviewed Original ResearchConceptsAquaporin-2 water channelIntracellular vesiclesApical membrane proteinsMembrane-associated proteinsTrafficking of AQP2Apical surface expressionEpithelial cellsCell surface retentionApical plasma membraneInvolvement of MALBody water homeostasisS256 phosphorylationWater channel proteinsSurface expressionApical deliveryRegulated traffickingSorting eventsRenal epithelial cellsMembrane associationMembrane proteinsPosttranslational modificationsProtein interactionsPlasma membraneChannel proteinsWater channelsOverexpression of mammaglobin B in epithelial ovarian carcinomas
Tassi RA, Bignotti E, Rossi E, Falchetti M, Donzelli C, Calza S, Ravaggi A, Bandiera E, Pecorelli S, Santin AD. Overexpression of mammaglobin B in epithelial ovarian carcinomas. Gynecologic Oncology 2007, 105: 578-585. PMID: 17343903, DOI: 10.1016/j.ygyno.2007.01.043.Peer-Reviewed Original ResearchConceptsEpithelial ovarian carcinomaHuman ovarian surface epitheliumMammaglobin BOvarian cancerReal-time PCRBenign cystadenomasOvarian carcinomaNormal ovariesNovel ovarian cancer biomarkersB expressionNormal human ovarian surface epitheliumPrimary epithelial ovarian carcinomaSerous papillary ovarian cancerMammaglobin B mRNAMultiple histological typesOvarian cancer biopsiesSerous papillary tumorsClear cell tumorsOvarian surface epitheliumFresh frozen biopsiesOvarian cancer biomarkersParaffin-embedded tissuesMixed histologyBorderline tumorsHistologic type
2002
Marrow-Derived Cells as Vehicles for Delivery of Gene Therapy to Pulmonary Epithelium
Grove JE, Lutzko C, Priller J, Henegariu O, Theise ND, Kohn DB, Krause DS. Marrow-Derived Cells as Vehicles for Delivery of Gene Therapy to Pulmonary Epithelium. American Journal Of Respiratory Cell And Molecular Biology 2002, 27: 645-651. PMID: 12444022, DOI: 10.1165/rcmb.2002-0056rc.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBone Marrow TransplantationFemaleGene ExpressionGenetic TherapyGreen Fluorescent ProteinsHematopoietic Stem Cell TransplantationIndicators and ReagentsLuminescent ProteinsLung DiseasesMiceMice, Inbred C57BLProtein PrecursorsProteolipidsRespiratory MucosaRetroviridaeRNA, MessengerConceptsBone marrow-derived stem cellsLung epithelial cellsLung epitheliumEpithelial cellsMarrow-derived stem cellsGene therapyBMSC transplantationLung diseaseFemale miceAirway epitheliumAlveolar spaceLong-term transgene expressionMale marrowPulmonary epitheliumLong-term gene expressionGene therapy applicationsGene expressionPulmonary airwaysAdenoviral vectorEpitheliumMarrowTherapyTransient gene expressionNonviral vectorsStem cellsPulmonary type II cell hypertrophy and pulmonary lipoproteinosis are features of chronic IL-13 exposure
Homer RJ, Zheng T, Chupp G, He S, Zhu Z, Chen Q, Ma B, Hite RD, Gobran LI, Rooney SA, Elias JA. Pulmonary type II cell hypertrophy and pulmonary lipoproteinosis are features of chronic IL-13 exposure. American Journal Of Physiology - Lung Cellular And Molecular Physiology 2002, 283: l52-l59. PMID: 12060560, DOI: 10.1152/ajplung.00438.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAsthmaBronchoalveolar Lavage FluidGene ExpressionHypertrophyImmunohistochemistryInterleukin-13MiceMice, Inbred C57BLMice, Inbred CBAMice, TransgenicProteolipidsPulmonary AlveoliPulmonary FibrosisPulmonary Surfactant-Associated Protein APulmonary Surfactant-Associated ProteinsPulmonary SurfactantsRNA, MessengerConceptsType II cell hypertrophyIL-13Cell hypertrophyChronic pulmonary conditionsPathogenesis of asthmaBronchoalveolar lavage fluidTh2-mediated immunityIL-13 exposureProminent interstitial fibrosisWild-type miceAirway hyperresponsivenessMucus metaplasiaEosinophilic inflammationPulmonary diseaseInterstitial fibrosisLavage fluidPulmonary conditionsTwo- to threefold increaseSurfactant accumulationLittermate controlsPotent stimulatorSurfactant phospholipidsFibrosisKey mediatorHypertrophy
2001
Biochemical and Biological Characterization of the Protective Leishmania pifanoi Amastigote Antigen P-8
Colmenares M, Tiemeyer M, Kima P, McMahon-Pratt D. Biochemical and Biological Characterization of the Protective Leishmania pifanoi Amastigote Antigen P-8. Infection And Immunity 2001, 69: 6776-6784. PMID: 11598050, PMCID: PMC100055, DOI: 10.1128/iai.69.11.6776-6784.2001.Peer-Reviewed Original ResearchConceptsAntigen PFurther vaccine studiesSignificant T cell activationT cell activationWestern blot analysisProtective immunityVaccine studiesApolipoprotein EMurine modelCutaneous leishmaniasisSignificant protectionComparable protectionImmunodominant componentAntigenic glycolipidsImmunity studiesAntigenCysteine proteinasesGlycolipid componentBiochemical analysisBiological characterizationSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisInfectionLeishmaniasisExpression of thyroid transcription factor-1 and other markers in sclerosing hemangioma of the lung.
Illei P, Rosai J, Klimstra D. Expression of thyroid transcription factor-1 and other markers in sclerosing hemangioma of the lung. Archives Of Pathology & Laboratory Medicine 2001, 125: 1335-9. PMID: 11570910, DOI: 10.5858/2001-125-1335-eottfa.Peer-Reviewed Original ResearchConceptsThyroid transcription factor-1Sclerosing hemangiomaTranscription factor 1Tumor cellsPulmonary epitheliumThyroid transcription factor-1 positivityFactor 1Expression of thyroid transcription factor-1Pale cellsLining cellsSolid areasPulmonary sclerosing hemangiomaCell typesPan-epithelialEpithelial tumorsFocal stainingEMA stainingVascular neoplasmPapillary structuresEpithelial markersAlveolar epitheliumHemangiomaNeoplastic cellsStaining intensityTumorSurfactant protein gene A, B, and D marker alleles in chronic obstructive pulmonary disease of a Mexican population
Guo X, Lin H, Lin Z, Montaño M, Sansores R, Wang G, DiAngelo S, Pardo A, Selman M, Floros J. Surfactant protein gene A, B, and D marker alleles in chronic obstructive pulmonary disease of a Mexican population. European Respiratory Journal 2001, 18: 482-490. PMID: 11589345, DOI: 10.1183/09031936.01.00043401.Peer-Reviewed Original ResearchAgedAllelesCarrier ProteinsCase-Control StudiesChi-Square DistributionConfounding Factors, EpidemiologicFemaleGenotypeGlycoproteinsHumansLogistic ModelsMaleMexicoMicrosatellite RepeatsMiddle AgedPolymerase Chain ReactionPolymorphism, Restriction Fragment LengthProtein PrecursorsProteolipidsPulmonary Disease, Chronic ObstructivePulmonary Surfactant-Associated Protein APulmonary Surfactant-Associated Protein DPulmonary Surfactant-Associated ProteinsPulmonary SurfactantsSeroepidemiologic StudiesSmokingWhite PeopleExpression of Thyroid Transcription Factor-1, Surfactant Proteins, Type I Cell–associated Antigen, and Clara Cell Secretory Protein in Pulmonary Hypoplasia
Zhou H, Morotti R, Profitt S, Langston C, Wert S, Whitsett J, Greco M. Expression of Thyroid Transcription Factor-1, Surfactant Proteins, Type I Cell–associated Antigen, and Clara Cell Secretory Protein in Pulmonary Hypoplasia. Pediatric And Developmental Pathology 2001, 4: 364-371. PMID: 11441338, DOI: 10.1007/s10024001-0002-9.Peer-Reviewed Original ResearchConceptsClara cell secretory proteinPulmonary hypoplasiaWeeks gestational ageTranscription factor 1Thyroid transcription factor-1Cell-associated antigensSecretory proteinsTTF-1Surfactant proteinsHomeodomain transcription factorGestational ageFactor 1Distal lung developmentProximal-distal axisEpithelial gene expressionDistal lung parenchymaNormal fetal lungTranscription factorsFinal common pathwayLung organogenesisExpression patternsGene expressionImmunolocalization patternsProteinLung parenchyma
2000
Surfactant Protein Genetic Marker Alleles Identify a Subgroup of Tuberculosis in a Mexican Population
Floros J, Lin H, García A, Salazar M, Guo X, DiAngelo S, Montaño M, Luo J, Pardo A, Selman M. Surfactant Protein Genetic Marker Alleles Identify a Subgroup of Tuberculosis in a Mexican Population. The Journal Of Infectious Diseases 2000, 182: 1473-1478. PMID: 11023470, DOI: 10.1086/315866.Peer-Reviewed Original ResearchActivation of surfactant protein‐B transcription: Signaling through the SP‐A receptor utilizing the PI3 kinase pathway
Strayer D, Korutla L. Activation of surfactant protein‐B transcription: Signaling through the SP‐A receptor utilizing the PI3 kinase pathway. Journal Of Cellular Physiology 2000, 184: 229-238. PMID: 10867648, DOI: 10.1002/1097-4652(200008)184:2<229::aid-jcp11>3.0.co;2-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedDNA-Binding ProteinsFemaleGlycoproteinsHepatocyte Nuclear Factor 3-alphaLungNuclear ProteinsPhosphatidylinositol 3-KinasesPromoter Regions, GeneticProtein IsoformsProteolipidsPulmonary Surfactant-Associated Protein APulmonary Surfactant-Associated ProteinsPulmonary SurfactantsRatsReceptors, Cell SurfaceThyroid Nuclear Factor 1Transcription FactorsTranscription, GeneticConceptsSP-B promoterSP-B transcriptionPI3-kinaseHNF-3Consensus recognition elementSurfactant proteinsPI3-kinase pathwaySP-A receptorGel shift analysisCell transcriptional activityKinase localizationCellular functionsInteraction of SPTranscription factorsCell biologyNuclear localizationPlasma membraneKinase pathwayTranscriptional activityTranscriptionProteinSpCognate receptorsPromoterType II cells
1999
Congenital cystic adenomatoid malformation of the lung (CCAM): Evaluation of the cellular components
Morotti R, Cangiarella J, Gutierrez M, Jagirdar J, Askin F, Singh G, Profitt S, Wert S, Whitsett J, Greco M. Congenital cystic adenomatoid malformation of the lung (CCAM): Evaluation of the cellular components. Human Pathology 1999, 30: 618-625. PMID: 10374767, DOI: 10.1016/s0046-8177(99)90084-9.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, NeoplasmCD5 AntigensCystic Adenomatoid Malformation of Lung, CongenitalFetal DiseasesFetusGastrin-Releasing PeptideGlycoproteinsHumansHyaluronan ReceptorsNeoplasm ProteinsPeptidesProtein PrecursorsProteolipidsPulmonary Surfactant-Associated Protein CPulmonary SurfactantsSurface-Active AgentsConceptsCongenital cystic adenomatoid malformationCell-cell interactionsCystic adenomatoid malformationLung developmentCellular compositionAdenomatoid malformationProtein precursorCellular componentsNormal lung developmentPseudoglandular stageCCAM type 1Rare congenital lesionsSaccular stageNeuroendocrine cellsCell-associated antigensSurfactant proteinsEpithelial-lined cystsAdhesion moleculesCongenital lesionsCytodifferentiationImmunohistochemical stainsClara cellsFetal lungTracheobronchial treeMajor subtypes
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