2017
Structural Characterization of the Recognition of U6 snRNA by the Yeast U6 Biogenesis Protein Usb1
DeLaitsch A, Didychuk A, Montemayor E, Larson M, Lucarelli S, Butcher S. Structural Characterization of the Recognition of U6 snRNA by the Yeast U6 Biogenesis Protein Usb1. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.910.8.Peer-Reviewed Original ResearchU6 snRNAU6 RNAMutation of active site residuesTerminal phosphateDenaturing polyacrylamide gel electrophoresisBinding of RNACatalytically active spliceosomePrecursor messenger RNANon-coding intronsActive site residuesPolyacrylamide gel electrophoresisSnRNA biogenesisExoribonuclease activityS. cerevisiaeSequence identityActive spliceosomeEukaryotic cellsConserved UFluorescent RNADiffracted X-raysU6 snRNPActive siteProtein complexesSite residuesUSB1
2008
Mirror Image DNA Nanostructures for Chiral Supramolecular Assemblies
Lin C, Ke Y, Li Z, Wang JH, Liu Y, Yan H. Mirror Image DNA Nanostructures for Chiral Supramolecular Assemblies. Nano Letters 2008, 9: 433-436. PMID: 19063615, PMCID: PMC2669104, DOI: 10.1021/nl803328v.Peer-Reviewed Original ResearchConceptsChiral supramolecular assembliesStructural DNA nanotechnologyNatural d-DNACircular dichroism spectraSupramolecular assembliesDNA supramoleculesAtomic force microscopeDNA nanostructuresDNA nanotechnologyL-DNADichroism spectraVivo medical applicationsNuclease resistanceForce microscopePolyacrylamide gel electrophoresisOpposite chiralityNanostructuresD-DNAPeriodic nanostructuresMedical applicationsSupramoleculesGel electrophoresisSubstantial complementChiralityNanotechnology
2003
Temporal and Geographic Genetic Variation in Culex pipiens quinquefasciatus (Diptera: Culicidae) from Florida
Nayar J, Knight J, Munstermann L. Temporal and Geographic Genetic Variation in Culex pipiens quinquefasciatus (Diptera: Culicidae) from Florida. Journal Of Medical Entomology 2003, 40: 882-889. PMID: 14765666, DOI: 10.1603/0022-2585-40.6.882.Peer-Reviewed Original ResearchConceptsGeographic samplesGenetic variationGenetic distanceColony samplesGene flow estimatesGeographic genetic variationGenetic variability valuesRogers' genetic distanceGene flowObserved heterozygosityPutative lociField samplesPolymorphic lociAverage Nei'sFlorida populationsField populationsHardy-WeinbergEcological conditionsPolyacrylamide gel electrophoresisQuinquefasciatus populationsCulex pipiens quinquefasciatusLociMinimum populationFlorida samplesTemporal samplesMapping the proteome of Leishmania Viannia parasites using two-dimensional polyacrylamide gel electrophoresis and associated technologies.
Góngora R, Acestor N, Quadroni M, Fasel N, Saravia NG, Walker J. Mapping the proteome of Leishmania Viannia parasites using two-dimensional polyacrylamide gel electrophoresis and associated technologies. Biomédica 2003, 23: 153-60. PMID: 12872554, DOI: 10.7705/biomedica.v23i2.1207.Peer-Reviewed Original ResearchConceptsProteome mapProteome analysisHeat shock protein familyRibosomal protein S12Comparative proteome analysisPeptide mass spectrometryTwo-dimensional polyacrylamide gel electrophoresisParaflagellar rod proteins 1Shock protein familyProtein expression profilesSpecies/strainsTwo-dimensional electrophoresisProtein expression studiesProtein S12Protein familyBioinformatics approachDistinct proteinsProtein spotsProtein mapsProtein 11Expression studiesExpression profilesUnknown functionDistinct parasite clonesPolyacrylamide gel electrophoresis
2002
Temporal and Geographic Genetic Variation in Culex nigripalpus Theobald (Culicidae: Diptera), a Vector of St. Louis Encephalitis Virus, from Florida
Nayar J, Knight J, Munstermann L. Temporal and Geographic Genetic Variation in Culex nigripalpus Theobald (Culicidae: Diptera), a Vector of St. Louis Encephalitis Virus, from Florida. Journal Of Medical Entomology 2002, 39: 854-860. PMID: 12495183, DOI: 10.1603/0022-2585-39.6.854.Peer-Reviewed Original ResearchConceptsGeographic genetic variationGenetic variationGeographic samplesGene flowGenetic distanceObserved heterozygosityColony samplesGene flow estimatesHigh gene flowGenetic variability valuesRogers' genetic distanceField-collected samplesEnzyme lociCulex nigripalpus TheobaldNm valuesField samplesPolymorphic lociAverage Nei'sField populationsHardy-WeinbergBeach populationsPolyacrylamide gel electrophoresisDistinct temporal patternsLociHeterozygosity
2001
Genetic variability among populations of Lutzomyia (Psathyromyia) shannoni (Dyar 1929) (Diptera: Psychodidae: Phlebotominae) in Colombia
Cárdenas E, Munstermann L, Martínez O, Corredor D, Ferro C. Genetic variability among populations of Lutzomyia (Psathyromyia) shannoni (Dyar 1929) (Diptera: Psychodidae: Phlebotominae) in Colombia. Memórias Do Instituto Oswaldo Cruz 2001, 96: 189-196. PMID: 11285496, DOI: 10.1590/s0074-02762001000200010.Peer-Reviewed Original ResearchConceptsGenetic distanceNei's genetic distanceWright's F-statisticsF-statisticsGene flowF STIsozyme lociForest populationsMean heterozygosityGPI locusInfected insectsGenetic variationColony samplesGenetic variabilityLutzomyia shannoniPolyacrylamide gel electrophoresisConsequences of colonizationLaboratory coloniesLociInfected hostStomatitis virusGel electrophoresisCentral ColombiaMagdalena ValleyLow levels
1996
Purification and characterization of a recombinant hepatitis E protein vaccine candidate by liquid chromatography-mass spectrometry
McAtee C, Zhang Y, Yarbough P, Fuerst T, Stone K, Samander S, Williams K. Purification and characterization of a recombinant hepatitis E protein vaccine candidate by liquid chromatography-mass spectrometry. Journal Of Chromatography B 1996, 685: 91-104. PMID: 8930757, DOI: 10.1016/0378-4347(96)00143-0.Peer-Reviewed Original ResearchConceptsMass spectrometryCarboxyl terminusReversed phase liquid chromatographyAmino terminusLaser desorption mass spectrometryDesorption mass spectrometryMolecular massLiquid chromatography-mass spectrometryCarboxyl-terminal sequencingChromatography-mass spectrometryBaculovirus expression vectorSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisLC-MSLiquid chromatographyExpression vectorTerminal sequencingSequence analysisPolyacrylamide gel electrophoresisSpectrometryIntact proteinInternal sequencesDoublet proteinsTerminus
1994
Production of RNA by a polymerase protein encapsulated within phospholipid vesicles
Chakrabarti A, Breaker R, Joyce G, Deamer D. Production of RNA by a polymerase protein encapsulated within phospholipid vesicles. Journal Of Molecular Evolution 1994, 39: 555-559. PMID: 7528810, DOI: 10.1007/bf00160400.Peer-Reviewed Original ResearchConceptsRNA polymeraseTemplate-independent RNA polymeraseProduction of RNACatalyzed polymerization reactionsBoundary membraneMacromolecular catalystsRNA productsPolymerization reactionPolymerase proteinDimyristoyl phosphatidylcholine vesiclesPolyacrylamide gel electrophoresisEthidium bromide fluorescenceEarly cellsRNA polymersPhase transition temperatureSubstrate fluxPhospholipid vesiclesVesiclesFree enzymeSuch reactionsGel electrophoresisPhosphatidylcholine vesiclesComponent lipidsPolymeraseCatalyst
1993
Processing of proTRH to its intermediate products occurs before the packing into secretory granules of transfected AtT20 cells
Nillni E, Sevarino K, Jackson I. Processing of proTRH to its intermediate products occurs before the packing into secretory granules of transfected AtT20 cells. Endocrinology 1993, 132: 1271-1277. DOI: 10.1210/en.132.3.1271.Peer-Reviewed Original ResearchPulse-chase studiesProcessing of proTRHSecretory granulesAtT20 cellsAssay of marker enzymesPolyacrylamide gel electrophoresisPulse-chase experimentsCryptic peptidesC-terminal processing productsNitrogen cavitationSubcellular compartmentsSG fractionGel electrophoresisRER fractionPosttranslational processingSubcellular fractionsIntracellular compartmentsPurified antibodiesProTRH processingIntermediate processing productsGolgiIntact precursorMarker enzymesPeptideProcessing products
1992
Elution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins
Stone K, LoPresti M, Williams K, Mcnulty D, Crawford J, DeAngelis R. Elution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins. 1992, 23-34. DOI: 10.1016/b978-0-12-058756-8.50008-0.Peer-Reviewed Original ResearchPVDF membranePolyacrylamide gel electrophoresisPolyvinylidene difluoride membraneTryptic digestMolecular weightReversed-phase HPLCSDS-polyacrylamide gel electrophoresisHigh yieldsTotal purificationDifluoride membraneEnzymatic cleavageTryptic peptidesPhase HPLCCyanogen bromide peptidesCyanogen bromide cleavageCleavageInternal amino acid sequencingGel electrophoresisPeptidesAmino acid sequencingMembraneElutionPurification
1991
Population Genetic Analysis of Host Seeking and Resting Behaviors in the Malaria Vector, Anopheles balabacensis (Diptera: Culicidae)
Hii J, Chew M, Sang V, Munstermann L, Tan S, Panyim S, Yasothornsrikul S. Population Genetic Analysis of Host Seeking and Resting Behaviors in the Malaria Vector, Anopheles balabacensis (Diptera: Culicidae). Journal Of Medical Entomology 1991, 28: 675-684. PMID: 1682492, DOI: 10.1093/jmedent/28.5.675.Peer-Reviewed Original ResearchConceptsPopulation genetic analysesIsocitrate dehydrogenase 3Host preference experimentsHost choice experimentsIsozyme lociGenetic heterozygosityFemales of AnGenetic analysisEsterase-3Fragment length polymorphism analysisPopulation componentsHost identificationPolyacrylamide gel electrophoresisDehydrogenase 3Length polymorphism analysisSequence profilesMalaria vectorsBovid hostsGel electrophoresisPolymorphism analysisGenotypic frequenciesAnopheles balabacensisHost
1989
Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles
Merrill B, Barnett S, LeStourgeon W, Williams K. Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Research 1989, 17: 8441-8449. PMID: 2587210, PMCID: PMC335017, DOI: 10.1093/nar/17.21.8441.Peer-Reviewed Original ResearchConceptsInsert sequenceHeterogeneous nuclear ribonucleoprotein particleSingle transcription unitAlternative splicing mechanismNuclear ribonucleoprotein particleAmino acid sequencingResidue insertHnRNP proteinsTranscription unitTryptic peptide mappingSplicing mechanismPrimary structure differencesC2 proteinSDS-polyacrylamide gel electrophoresisNuclear ribonucleoproteinProtein C1Ribonucleoprotein particleUntranslated regionPrimary structurePolyacrylamide gel electrophoresisAmino acidsPeptide mappingGel electrophoresisMolecular weight differencesProtein
1988
Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species
O'Neill G, Peterson D, Schön A, Chen M, Söll D. Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species. Journal Of Bacteriology 1988, 170: 3810-3816. PMID: 2900830, PMCID: PMC211375, DOI: 10.1128/jb.170.9.3810-3816.1988.Peer-Reviewed Original ResearchConceptsPrecursor delta-aminolevulinic acidHigher plantsUnicellular cyanobacterium Synechocystis spGlutamate-1-semialdehyde aminotransferaseCell extractsCyanobacterium Synechocystis spDelta-aminolevulinic acidSouthern blot analysisIdentical primary sequencesSynechocystis spNucleotide modificationsConversion of glutamateGene copiesALA synthesisPrimary sequenceSequence specificityTerminal enzymePolyacrylamide gel electrophoresisChloroplastsEuglena gracilisEscherichia coliSpeciesBlot analysisTRNAGel electrophoresis
1986
Enzyme Variation in Some Mosquito Species Related to Aedes (Ochlerotatus) Stimulans (Diptera: Culicidae)1
Eldridge B, Munstermann L, Craig G. Enzyme Variation in Some Mosquito Species Related to Aedes (Ochlerotatus) Stimulans (Diptera: Culicidae)1. Journal Of Medical Entomology 1986, 23: 423-428. PMID: 3735350, DOI: 10.1093/jmedent/23.4.423.Peer-Reviewed Original ResearchConceptsConventional morphological charactersEnzyme lociEnzyme variationRelated speciesMorphological charactersSingle locusAedes stimulansPolyacrylamide gel electrophoresisEnzyme phenotypesMosquito speciesIsozyme patternsSpeciesLociGene frequenciesMosquito populationsGel electrophoresisAllelic frequenciesBasis of differencesSubgenus OchlerotatusDipteraCluster analysisCorrect identificationAePhenotypeOchlerotatus
1985
Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis
Dumont M, Trewhella J, Engelman D, Richards F. Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis. The Journal Of Membrane Biology 1985, 88: 233-247. PMID: 3913776, DOI: 10.1007/bf01871088.Peer-Reviewed Original ResearchConceptsMolecular weight distributionFragments of bacteriorhodopsinVisible absorption spectraX-ray diffractionX-ray diffraction patternsDiffraction patternsAqueous mediaNative purple membraneUrea-polyacrylamide gel electrophoresisWeight distributionSmall soluble peptidesAbsorption spectraHydrophobic segmentsBacteriorhodopsin sequenceAmino acid analysisHigh-pressure liquid chromotographyPolyacrylamide gel electrophoresisDigestion conditionsPurple membraneOptical absorptionSoluble peptidesBacteriorhodopsinMembrane-embedded regionsLiquid chromotographyProducts of digestion
1983
[23] Erythrocyte membrane proteins: Detection of spectrin oligomers by gel electrophoresis
Morrow J, Haigh W. [23] Erythrocyte membrane proteins: Detection of spectrin oligomers by gel electrophoresis. Methods In Enzymology 1983, 96: 298-304. PMID: 6656632, DOI: 10.1016/s0076-6879(83)96027-5.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfateDodecyl sulfateGel electrophoresisPolyacrylamide gel electrophoresisGelMembrane proteinsProtein-protein associationSlab gelsOligomersSecond dimensionSpectrin oligomersElectrophoretic analysisPrincipal structural proteinPreparationErythrocyte membrane skeletonPolyacrylamide gel electrophoretic analysisErythrocyte membrane proteinsElectrophoresisGel electrophoretic analysisNondenaturing gelMembrane skeletonDistinct polypeptidesStructural proteinsSpectrin moleculesMolecules
1981
The carboxyl-terminal domain of human erythrocyte band 3. Description, isolation, and location in the bilayer.
Markowitz S, Marchesi V. The carboxyl-terminal domain of human erythrocyte band 3. Description, isolation, and location in the bilayer. Journal Of Biological Chemistry 1981, 256: 6463-6468. PMID: 7240219, DOI: 10.1016/s0021-9258(19)69187-8.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate bindingBand 3 moleculesCarboxyl-terminal fragmentBand 3NH2-terminal cytoplasmic domainMembrane-spanning domainsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisBand 3 fragmentSulfate-polyacrylamide gel electrophoresisCarboxyl-terminal domainAnion channel proteinCarboxyl-terminal regionPolyacrylamide gel electrophoresisGel electrophoresisSulfate bindingHomogeneous polypeptideCytoplasmic domainIdentical peptide mapsMoleculesMajor transmembraneHuman erythrocyte band 3Channel proteinsBroad bandErythrocyte band 3
1980
Intracellular forms of simian virus 40 nucleoprotein complexes. III. Study of histone modifications
Coca-Prados M, Vidali G, Hsu M. Intracellular forms of simian virus 40 nucleoprotein complexes. III. Study of histone modifications. Journal Of Virology 1980, 36: 353-360. PMID: 6253661, PMCID: PMC353651, DOI: 10.1128/jvi.36.2.353-360.1980.Peer-Reviewed Original ResearchConceptsSimian virus 40 chromatinSimian virus 40 nucleoprotein complexesNucleoprotein complexesHistone modificationsAssembly intermediatesModification patternsMature virionsVirion assembly intermediatesCapsid proteinModification of histonesHistone modification patternsVirion assembly pathwayViral nucleoprotein complexesPulse-chase experimentsHost chromatinHistone patternsAssembly pathwayChromatinHistonesVirion assemblyPolyacrylamide gel electrophoresisAcetylation activityIntracellular formGel electrophoresisViral RNA
1979
Isolation and tissue localization of type AB2 collagen from normal lung parenchyma.
Madri J, Furthmayr H. Isolation and tissue localization of type AB2 collagen from normal lung parenchyma. American Journal Of Pathology 1979, 94: 323-31. PMID: 371411, PMCID: PMC2042247.Peer-Reviewed Original ResearchConceptsNormal lung parenchymaLung parenchymaAffinity-purified rabbit antibodiesLung tissuePassive hemagglutinationPlacental membranesChorionic membraneAB2 collagenTissue localizationIndirect immunofluorescence microscopyRabbit antibodiesBasement membraneChain ratioParenchymaImmunofluorescence microscopyCollagenPolyacrylamide gel electrophoresisGel electrophoresisAlpha ADifferential salt extractionCell surface
1977
δ-Crystallin gene expression in embryonic chick lens epithelia cultured in the presence of insulin
Milstone L, Piatigorsky J. δ-Crystallin gene expression in embryonic chick lens epithelia cultured in the presence of insulin. Experimental Cell Research 1977, 105: 9-14. PMID: 837998, DOI: 10.1016/0014-4827(77)90147-1.Peer-Reviewed Original ResearchConceptsEmbryonic lens epitheliumΔ-crystallin synthesisMessenger RNAΔ-crystallinGene expressionLens epitheliumPresence of insulinCultured lens epitheliumFetal calf serumChick lens epitheliumLens epithelial cellsCell elongationTranslational efficiencyCalf serumPolyacrylamide gel electrophoresisTotal protein synthesisProtein synthesisMolecular hybridizationGel electrophoresisSodium dodecyl sulfate-gradient polyacrylamide gel electrophoresisEpithelial cellsSynthesis increasesCellsExpressionHours of culture
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