2000
Bile salt excretion in skate liver is mediated by a functional analog of Bsep/Spgp, the bile salt export pump
Ballatori N, Rebbeor J, Connolly G, Seward D, Lenth B, Henson J, Sundaram P, Boyer J. Bile salt excretion in skate liver is mediated by a functional analog of Bsep/Spgp, the bile salt export pump. AJP Gastrointestinal And Liver Physiology 2000, 278: g57-g63. PMID: 10644562, DOI: 10.1152/ajpgi.2000.278.1.g57.Peer-Reviewed Original ResearchConceptsTransport activityPlasma membrane vesiclesApparent molecular massVertebrate evolutionATP-dependent componentMultidrug resistance protein 1Similar transport activityFunctional characterizationPlasma membraneApical localizationCanalicular membraneResistance protein 1Liver plasma membrane vesiclesATP-dependent uptakeSkate liverMembrane vesiclesWestern blot analysisDominant protein bandsMammalian liverMolecular massLittle skateFunctional analogueProtein 1Raja erinaceaCanalicular multidrug resistance
1999
Molecular Cloning and Characterization of the Ehrlichia chaffeensis Variable-Length PCR Target: an Antigen-Expressing Gene That Exhibits Interstrain Variation
Sumner J, Childs J, Paddock C. Molecular Cloning and Characterization of the Ehrlichia chaffeensis Variable-Length PCR Target: an Antigen-Expressing Gene That Exhibits Interstrain Variation. Journal Of Clinical Microbiology 1999, 37: 1447-1453. PMID: 10203503, PMCID: PMC84798, DOI: 10.1128/jcm.37.5.1447-1453.1999.Peer-Reviewed Original ResearchConceptsOpen reading frameAmino acid sequenceApparent molecular massE. chaffeensisGenomic libraryMolecular cloningReading frameAcid sequenceDifferentiation of isolatesPCR targetsClose homologyMolecular massNucleotide sequencingImmunoreactive proteinDifferent isolatesDNA samplesInterstrain variationGenesRepeat unitsMolecular databasesCell culturesAmblyomma americanum ticksSequencePCR detectionChaffeensisMolecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells
Endo S, Suzuki M, Sumi M, Nairn A, Morita R, Yamakawa K, Greengard P, Ito M. Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 2467-2472. PMID: 10051666, PMCID: PMC26808, DOI: 10.1073/pnas.96.5.2467.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCerebellumCloning, MolecularCyclic GMP-Dependent Protein KinasesDatabases as TopicExpressed Sequence TagsHumansMolecular Sequence DataNerve Tissue ProteinsPurkinje CellsRabbitsRecombinant ProteinsRNA, MessengerSequence AlignmentSequence Homology, Amino AcidTranscription, GeneticConceptsAmino acid sequenceProtein phosphatase 1G-substrateAcid sequencePhosphatase 1Deduced amino acid sequenceRadiation hybrid panel analysisProtein phosphatase 2APutative phosphorylation sitesCGMP-dependent protein kinaseProtein kinase cascadeProtein phosphatase inhibitorSequence tag databaseSites of phosphorylationVitro translation productsHuman brain libraryCGMP-dependent proteinAcid-soluble proteinsApparent molecular massSDS/PAGEPhosphatase 2AThr-35Kinase cascadePhosphorylation sitesTag database
1997
Actin-binding membrane proteins identified by F-actin blot overlays.
Luna E, Pestonjamasp K, Cheney R, Strassel C, Lu T, Chia C, Hitt A, Fechheimer M, Furthmayr H, Mooseker M. Actin-binding membrane proteins identified by F-actin blot overlays. Society Of General Physiologists Series 1997, 52: 3-18. PMID: 9210216.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAmino Acid SequenceAnimalsBlotting, WesternBrainBreast NeoplasmsCattleChick EmbryoDictyosteliumElectrophoresis, Polyacrylamide GelHeLa CellsHumansIodine RadioisotopesMammalsMembrane ProteinsMiceMicrofilament ProteinsNeuroblastomaNeuropeptidesNeutrophilsSodium Dodecyl SulfateTumor Cells, CulturedConceptsBlot overlayApparent molecular massMembrane proteinsF-actinF-actin binding proteinMolecular massControl cell shapePeripheral membrane proteinsSpecialized membrane domainsCell-cell adhesionPlasma membrane-enriched fractionActin-binding proteinsMammalian cell linesCell surface extensionsMembrane-enriched fractionMembrane rufflesProtein 4.1Membrane domainsMammalian cellsDictyostelium discoideumSoil amoebaPseudopod dynamicsCell shapeEfficient chemotaxisMembrane bilayer
1994
Identification of membrane proteins that comprise the plasmalemmal junction between migrating neurons and radial glial cells
Cameron R, Rakic P. Identification of membrane proteins that comprise the plasmalemmal junction between migrating neurons and radial glial cells. Journal Of Neuroscience 1994, 14: 3139-3155. PMID: 8182462, PMCID: PMC6577439, DOI: 10.1523/jneurosci.14-05-03139.1994.Peer-Reviewed Original ResearchConceptsRadial glial cellsGlial cellsMembrane proteinsCell-cell recognitionFocal adhesion plaquesApparent molecular massRadial glial cell processesNeuronal cell migrationCerebellar glial cellsActin cytoskeletonGlial cell processesMicrotubule cytoskeletonNon-neural tissuesSurface microdomainsMembrane polypeptidesIndividual proteinsAdhesion plaquesProcess-bearing astrocytesIntact microtubulesAdult stageMolecular massCell migrationMigration eventsIntegrin subunitsJunctional complexes
1993
Human SR proteins and isolation of a cDNA encoding SRp75.
Zahler A, Neugebauer K, Stolk J, Roth M. Human SR proteins and isolation of a cDNA encoding SRp75. Molecular And Cellular Biology 1993, 13: 4023-4028. PMID: 8321209, PMCID: PMC359951, DOI: 10.1128/mcb.13.7.4023.Peer-Reviewed Original ResearchConceptsRNA recognition motifSR proteinsN-terminal RNA recognition motifLong C-terminal domainPolymerase II transcriptionHuman SR proteinsSR family membersC-terminal domainFamily of proteinsGlycine-rich regionApparent molecular massCDNA clonesRecognition motifSRp75Mobility shiftArginine residuesMolecular massSR domainProteinInternal regionSerineCommon epitopesActive siteFamily membersSRp55Human SR Proteins and Isolation of a cDNA Encoding SRp75
Zahler A, Neugebauer K, Stolk J, Roth M. Human SR Proteins and Isolation of a cDNA Encoding SRp75. Molecular And Cellular Biology 1993, 13: 4023-4028. DOI: 10.1128/mcb.13.7.4023-4028.1993.Peer-Reviewed Original ResearchRNA recognition motifSR proteinsN-terminal RNA recognition motifLong C-terminal domainPolymerase II transcriptionHuman SR proteinsSR family membersC-terminal domainFamily of proteinsGlycine-rich regionApparent molecular massCDNA clonesRecognition motifSRp75Mobility shiftArginine residuesMolecular massSR domainProteinInternal regionSerineCommon epitopesActive siteFamily membersSRp55
1992
Expression of a cloned gamma-aminobutyric acid transporter in mammalian cells.
Keynan S, Suh Y, Kanner B, Rudnick G. Expression of a cloned gamma-aminobutyric acid transporter in mammalian cells. Biochemistry 1992, 31: 1974-9. PMID: 1536839, DOI: 10.1021/bi00122a011.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCarrier ProteinsChloridesCloning, MolecularDNAGABA Plasma Membrane Transport Proteinsgamma-Aminobutyric AcidGene ExpressionGenetic VectorsHeLa CellsHumansKineticsL CellsMembrane ProteinsMembrane Transport ProteinsMiceNerve Tissue ProteinsOrganic Anion TransportersPlasmidsPrecipitin TestsRatsSodiumTransfectionTunicamycinXenopusConceptsMammalian cellsGABA transportMouse Ltk- cellsT7 RNA polymerasePlasma membrane vesiclesL cellsApparent molecular massGABA transporterSynaptic plasma membrane vesiclesGamma-aminobutyric acid transporterPresence of tunicamycinEukaryotic expression vectorRNA polymeraseTransient expressionExpression vectorAcid transportersMembrane vesiclesStable expressionLtk- cellsFunctional expressionGAT-1Molecular massHeLa cellsTransportersTransfection
1991
Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum.
Lombroso P, Murdoch G, Lerner M. Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 7242-7246. PMID: 1714595, PMCID: PMC52270, DOI: 10.1073/pnas.88.16.7242.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid consensus sequenceAmino acid sequenceApparent molecular massRat striatal cDNA librarySingle geneVitro translationCDNA clonesStrong homologyCDNA libraryCytoplasmic membraneAcid sequenceRNA transcriptsN-terminusMolecular characterizationRNA analysisMolecular massAmino acidsProteinPhosphataseMRNASequenceHomologyGenesTerminusTwo glutamyl-tRNA reductase activities in Escherichia coli
Jahn D, Michelsen U, Söll D. Two glutamyl-tRNA reductase activities in Escherichia coli. Journal Of Biological Chemistry 1991, 266: 2542-2548. PMID: 1990004, DOI: 10.1016/s0021-9258(18)52279-1.Peer-Reviewed Original ResearchConceptsReductase activityGlu-tRNA reductaseMolecular massEscherichia coliApparent molecular massDifferent chromatographic separationsSequence-specific recognitionGlycerol gradient centrifugationThree-step conversionTetrapyrrole biosynthesisChlamydomonas reinhardtiiE. coli K12ALA formationChromatographic separationKey enzymeMonomeric structureActive enzymeBacillus subtilisColi K12Nondenaturing conditionsHomogeneous proteinMolecular weightDelta-aminolevulinic acidEnzyme activityAddition of GTPPurification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii.
Jahn D, Chen M, Söll D. Purification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1991, 266: 161-167. PMID: 1985889, DOI: 10.1016/s0021-9258(18)52416-9.Peer-Reviewed Original ResearchMeSH KeywordsAminooxyacetic AcidCell MembraneChlamydomonasChromatography, DEAE-CelluloseChromatography, GelChromatography, High Pressure LiquidChromatography, Ion ExchangeCyclohexanecarboxylic AcidsElectrophoresis, Polyacrylamide GelIntramolecular TransferasesIsomerasesKineticsMolecular WeightPyridoxal PhosphateConceptsGlutamate-1-semialdehyde aminotransferaseGlutamyl-tRNA synthetaseC5 pathwayChlamydomonas reinhardtiiGreen alga Chlamydomonas reinhardtiiGlu-tRNA reductaseTRNA-dependent transformationChloroplasts of plantsGlutamyl-tRNA reductaseAlga Chlamydomonas reinhardtiiDelta-aminolevulinic acidApparent molecular massWhole cell extractsChlorophyll biosynthesisSodium dodecyl sulfate-polyacrylamide gel electrophoresisC. reinhardtiiDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationFunctional characterizationThird enzymeGlycerol gradientsCell extractsReinhardtiiMembrane fraction
1990
Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme.
Chen M, Jahn D, Schön A, O'Neill G, Söll D. Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme. Journal Of Biological Chemistry 1990, 265: 4054-4057. PMID: 2303494, DOI: 10.1016/s0021-9258(19)39701-7.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseChloroplast enzymeApparent molecular massSequential column chromatographyChlamydomonas reinhardtiiActive enzymeMolecular massNondenaturing conditionsEscherichia coliDenaturing conditionsAcceptor RNASynthetaseMono S.Mono QEnzymeTRNAReinhardtiiYeastColumn chromatographyRNACytoplasmicProteinBarleyColiReversed phase chromatographyPurification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis.
Chen M, Jahn D, O'Neill G, Söll D. Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis. Journal Of Biological Chemistry 1990, 265: 4058-4063. PMID: 2303495, DOI: 10.1016/s0021-9258(19)39702-9.Peer-Reviewed Original ResearchConceptsGlu-tRNA reductaseGlutamyl-tRNA reductaseGlu-tRNAChlamydomonas reinhardtiiTRNA-dependent transformationChloroplasts of plantsDelta-aminolevulinic acid formationApparent molecular massChlorophyll biosynthesisGlutamyl-tRNAHomologous tRNAsSecond enzymeActive enzymeMolecular massNondenaturing conditionsDifferent chromatographic separationsCertain bacteriaReductaseDelta-aminolevulinic acidReinhardtiiPorphyrin biosynthesisBiosynthesisStable complexesChromatographic separationCarboxyl groups
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