2019
Evidence for vesicle-mediated antigen export by the human pathogen Babesia microti
Thekkiniath J, Kilian N, Lawres L, Gewirtz MA, Graham MM, Liu X, Ledizet M, Mamoun C. Evidence for vesicle-mediated antigen export by the human pathogen Babesia microti. Life Science Alliance 2019, 2: e201900382. PMID: 31196872, PMCID: PMC6572159, DOI: 10.26508/lsa.201900382.Peer-Reviewed Original ResearchConceptsApicomplexan parasitesCell fractionation studiesImmunoelectron microscopy analysisMode of secretionInvasion of erythrocytesParasite effectorsTrafficking motifsPlasma membraneExport mechanismClose relativesParasitophorous vacuoleHost erythrocyteMorphogenic changesFractionation studiesNovel mechanismHuman malariaFatal tick-borne diseaseMalaria-like illnessMouse red blood cellsParasitesAntigen exportTick-borne diseaseRed blood cellsHuman babesiosisImmunodominant antigens
2001
The Sonic Hedgehog Receptor Patched Associates with Caveolin-1 in Cholesterol-rich Microdomains of the Plasma Membrane* 210
Karpen H, Bukowski J, Hughes T, Gratton J, Sessa W, Gailani M. The Sonic Hedgehog Receptor Patched Associates with Caveolin-1 in Cholesterol-rich Microdomains of the Plasma Membrane* 210. Journal Of Biological Chemistry 2001, 276: 19503-19511. PMID: 11278759, DOI: 10.1074/jbc.m010832200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBlotting, WesternCaveolin 1CaveolinsCell MembraneCholesterolCOS CellsDNA, ComplementaryDrosophila ProteinsElectrophoresis, Polyacrylamide GelGlutathione TransferaseHumansImmunohistochemistryMembrane MicrodomainsMembrane ProteinsMicroscopy, ConfocalModels, BiologicalMolecular Sequence DataMutationPatched ReceptorsPrecipitin TestsProtein BindingProtein Structure, TertiaryProtein TransportReceptors, Cell SurfaceReceptors, G-Protein-CoupledRecombinant Fusion ProteinsSignal TransductionSmoothened ReceptorSubcellular FractionsTime FactorsConceptsCholesterol-rich microdomainsRaft microdomainsCaveolin-1Receptor complexEarly embryonic patterningFractionation studiesHedgehog receptor complexCaveolin-enriched microdomainsBuoyant density fractionsEmbryonic patterningHh proteinsLipid raftsSubcellular localizationPlasma membranePatchedPlasmalemmal cholesterolProtein experimentsImmunoprecipitation studiesSmoothenedMicrodomainsConfocal microscopyImmunocytochemistry dataComplexesMembraneDrosophila
1997
Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase
Kwon Y, Lee S, Choi Y, Greengard P, Nairn A. Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 2168-2173. PMID: 9122166, PMCID: PMC20059, DOI: 10.1073/pnas.94.6.2168.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1PP-1Phosphatase 1Cdc2 kinaseMammalian protein phosphatase 1Cell cycle-dependent phosphorylationCyclin-dependent protein kinase inhibitorEukaryotic cell cycle progressionCell synchronization studiesIntact mammalian cellsNormal cell divisionPP-1 activityCell fractionation studiesState of phosphorylationProtein kinase inhibitorsCell cycle progressionMammalian cellsCell divisionThr-320Cycle progressionMitotic cellsT320NIH 3T3PhosphorylationFractionation studies
1993
Analysis of the structure and subcellular location of filamentous phage pIV
Russel M, Kaźmierczak B. Analysis of the structure and subcellular location of filamentous phage pIV. Journal Of Bacteriology 1993, 175: 3998-4007. PMID: 8320216, PMCID: PMC204828, DOI: 10.1128/jb.175.13.3998-4007.1993.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseBacterial ProteinsCell CompartmentationColiphagesDNA Mutational AnalysisGene Expression Regulation, BacterialGenes, ViralHeat-Shock ProteinsMembrane ProteinsMutationOperonRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidSpheroplastsSubcellular FractionsViral ProteinsVirus ReplicationConceptsMembrane localization domainIntegral membrane proteinsSubstrate-binding domainAmino-terminal halfCarboxy-terminal halfSeries of genesCell fractionation studiesCytoplasmic domainPhage assemblyDeletion mutantsMembrane proteinsSubcellular locationLocalization domainFusion proteinFractionation studiesFilamentous phagePhosphatase activityFilamentous bacteriophageAlkaline phosphatase activityMissense mutationsProteinAssemblyDomainMutantsGenes
1988
Mitochondrial Import and Processing of Mutant Human Ornithine Transcarbamylase Precursors in Cultured Cells
Isaya G, Fenton W, Hendrick J, Furtak K, Kalousek F, Rosenberg L. Mitochondrial Import and Processing of Mutant Human Ornithine Transcarbamylase Precursors in Cultured Cells. Molecular And Cellular Biology 1988, 8: 5150-5158. DOI: 10.1128/mcb.8.12.5150-5158.1988.Peer-Reviewed Original ResearchLeader peptideMitochondrial importMutant precursorHeLa cellsAssociated with mitochondriaHuman ornithine transcarbamylaseAmino acid substitutionsOrnithine transcarbamylase precursorIntact HeLa cellsIntramitochondrial locationLack of bindingMutant proteinsMitochondrial matrixAcid substitutionsActive enzymeActive trimerMitochondrial fractionTrypsin protectionAffinity columnFractionation studiesMitochondriaCultured cellsCytosolOrnithine transcarbamylaseMutations
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