2008
The putative oncoprotein DEK, part of a chimera protein associated with acute myeloid leukaemia, is an autoantigen in juvenile rheumatoid arthritis
SIERAKOWSKA H, WILLIAMS K, SZER I, SZER W. The putative oncoprotein DEK, part of a chimera protein associated with acute myeloid leukaemia, is an autoantigen in juvenile rheumatoid arthritis. Clinical & Experimental Immunology 2008, 94: 435-439. PMID: 8252804, PMCID: PMC1534440, DOI: 10.1111/j.1365-2249.1993.tb08214.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArthritis, JuvenileAutoantigensCells, CulturedChild, PreschoolChromatography, High Pressure LiquidChromatography, Ion ExchangeChromosomal Proteins, Non-HistoneElectrophoresis, Polyacrylamide GelHeLa CellsHumansLeukemia, MyeloidMolecular Sequence DataMolecular WeightOncogene ProteinsPeptide MappingPoly-ADP-Ribose Binding ProteinsRatsConceptsJuvenile rheumatoid arthritisAcute myeloid leukemiaRheumatoid arthritisMyeloid leukemiaRare subtypeLeukaemic cellsBone marrowImmunoblot assayRat tissuesDEK proteinArthritisFive-step chromatographic procedureAutoantigensLeukemiaOncogene DEKAntigenSerumPartial amino acid sequencingDEKAmino acid sequencingOncoprotein DEKPatientsSpleenProteinMarrow
1992
Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster
Shuai K, Gupta C, Hawley R, Chase J, Stone K, Williams K. Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster. Nucleic Acids Research 1992, 20: 1379-1385. PMID: 1313969, PMCID: PMC312186, DOI: 10.1093/nar/20.6.1379.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsChromatography, DEAE-CelluloseChromatography, High Pressure LiquidDNA, Single-StrandedDrosophila melanogasterElectrophoresis, Polyacrylamide GelEndonucleasesExonucleasesHot TemperatureHydrogen-Ion ConcentrationKineticsMolecular Sequence DataMolecular WeightSodium ChlorideSubstrate SpecificityUltracentrifugation
1990
Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.
Kumar A, Widen S, Williams K, Kedar P, Karpel R, Wilson S. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. Journal Of Biological Chemistry 1990, 265: 2124-2131. PMID: 2404980, DOI: 10.1016/s0021-9258(19)39949-1.Peer-Reviewed Original ResearchConceptsNH2-terminal domainDNA polymerase betaLarge-scale overproductionPolymerase betaMammalian DNA polymerase betaCOOH-terminal domainProtease-sensitive regionNucleic acidsProteolysis experimentsRat proteinRecombinant proteinsPolypeptide chainDNA polymerase activityIntact proteinEscherichia coliAmino acidsTryptic peptidesDNA polymeraseDomain structureProteinPolymerase activityDomainPolymeraseAcidDNA
1989
The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis
Rush J, Lin T, Quinones M, Spicer E, Douglas I, Williams K, Konigsberg W. The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis. Journal Of Biological Chemistry 1989, 264: 10943-10953. PMID: 2786875, DOI: 10.1016/s0021-9258(18)60410-7.Peer-Reviewed Original ResearchConceptsAccessory proteinsATP hydrolysisDNA-dependent ATP hydrolysisT4 DNA polymerase accessory proteinsDNA polymerase accessory proteinPolymerase accessory proteinsTotal cellular proteinAccessory protein complexProtein complexesCellular proteinsPlasmid resultsSubunitsProteinATPase activityOverexpression plasmidProductive interactionInduction of cellsPlasmidSpecific activityComplexesSubcomplexInductionGenesOverexpressionATPase
1987
Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA.
Spicer E, Horton R, Bloem L, Bach R, Williams K, Guha A, Kraus J, Lin T, Nemerson Y, Konigsberg W. Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 5148-5152. PMID: 3037536, PMCID: PMC298811, DOI: 10.1073/pnas.84.15.5148.Peer-Reviewed Original ResearchConceptsMature proteinPrimary structureHuman placental cDNA libraryAmino acid sequenceHigh molecular weight precursorTissue factor genePlacental cDNA librarySequence data banksCarbohydrate attachment sitesSingle polypeptide chainMolecular weight precursorDependent serine proteaseSignificant homologyCDNA clonesCDNA librarySequence dataLeader sequenceNucleotide sequenceFactor genesAcid sequenceTissue factorExtracellular domainLambda phageDistinct domainsPolypeptide chain
1986
Mammalian single‐stranded DNA binding protein UP I is derived from the hnRNP core protein A1.
Riva S, Morandi C, Tsoulfas P, Pandolfo M, Biamonti G, Merrill B, Williams K, Multhaup G, Beyreuther K, Werr H. Mammalian single‐stranded DNA binding protein UP I is derived from the hnRNP core protein A1. The EMBO Journal 1986, 5: 2267-2273. PMID: 3023065, PMCID: PMC1167110, DOI: 10.1002/j.1460-2075.1986.tb04494.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesBase SequenceCattleCell NucleusCross ReactionsDNA HelicasesGenetic VectorsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular WeightPeptide MappingPlasmidsRibonucleoproteinsStructure-Activity RelationshipThymus GlandThymus HormonesPurification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins.
Kumar A, Williams K, Szer W. Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins. Journal Of Biological Chemistry 1986, 261: 11266-11273. PMID: 3733753, DOI: 10.1016/s0021-9258(18)67378-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceChromatography, High Pressure LiquidCircular DichroismDNA-Binding ProteinsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular WeightRibonucleoproteinsSpectrophotometry, UltravioletTrypsinConceptsHeterogeneous nuclear ribonucleoproteinsNucleic acid-binding domainProtein A1Glycine-rich proteinSsDNA-binding proteinDNA-binding proteinsHnRNP protein A1Helix-destabilizing activityHnRNP proteinsNuclear ribonucleoproteinTerminal domainHDP-1A1 bindsGlycine residueNative proteinPrimary structureLimited proteolysisHeLa cellsProtein A2Amino acidsProteinHigh pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus.
Merrill B, LoPresti M, Stone K, Williams K. High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus. Journal Of Biological Chemistry 1986, 261: 878-883. PMID: 3941105, DOI: 10.1016/s0021-9258(17)36178-1.Peer-Reviewed Original Research
1984
Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation.
Williams K, Murphy J, Chase J. Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation. Journal Of Biological Chemistry 1984, 259: 11804-11811. PMID: 6384214, DOI: 10.1016/s0021-9258(20)71283-4.Peer-Reviewed Original ResearchConceptsWild-type SSBMutant proteinsSSB-1Solid-phase protein sequencingSsb-1 mutationSSB-1 proteinHelix-destabilizing proteinNormal cellular concentrationTryptic peptide analysisSubstitution of tyrosineSingle-strand DNAProtein sequencingDNA sequencesMutant geneResidues 55Thermal melting transitionCellular concentrationTemperature inductionTetrameric structureEscherichia coliProteinGenesProtein concentrationPeptide analysisT transition
1983
Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.
Williams K, Spicer E, LoPresti M, Guggenheimer R, Chase J. Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. Journal Of Biological Chemistry 1983, 258: 3346-3355. PMID: 6298232, DOI: 10.1016/s0021-9258(18)32867-9.Peer-Reviewed Original ResearchConceptsCOOH terminusBacteriophage T4 gene 32 proteinDNA-induced conformational changesT4 gene 32 proteinConformational changesEscherichia coliHelix-destabilizing proteinGene 32 proteinE. coli DNA replicationSimilar functional domainsCOOH-terminal domainLimited proteolysis studiesEukaryotic DNADNA replicationDouble-helical DNAHomologous domainsTerminal domainFunctional domainsT4 DNAProteolysis studiesLimited proteolysisTerminal regionAmino acidsProteinHelical DNA
1979
Structural characteristics of interferons from mouse Ehrlich ascites tumor cells.
Cabrer B, Taira H, Broeze R, Kempe T, Williams K, Slattery E, Konigsberg W, Lengyel P. Structural characteristics of interferons from mouse Ehrlich ascites tumor cells. Journal Of Biological Chemistry 1979, 254: 3681-3684. PMID: 438151, DOI: 10.1016/s0021-9258(18)50635-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsAnimalsCarcinoma, Ehrlich TumorInterferonsMiceMolecular WeightPeptide FragmentsTrypsinConceptsAmino acidsMouse EhrlichNH2-terminal amino acidsTryptic peptide mapsSmaller speciesLarger speciesPeptide mapsSpeciesTumor cellsSize classesNewcastle disease virusDisease virusSpecific activityCellsGlycosylationProteinUnits/AcidEhrlichCarboxypeptidaseInterferonIsolationStructural characteristics
1977
Purification and some properties of Escherichia coli tRNA nucleotidyltransferase.
Schofield P, Williams K. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. Journal Of Biological Chemistry 1977, 252: 5584-5588. PMID: 328503, DOI: 10.1016/s0021-9258(19)63390-9.Peer-Reviewed Original ResearchConceptsTransition metal chelating agentsMetal chelating agentsSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisSulfate gel electrophoresisTurnover numberChelating agentOverall yieldMolecular weightPure enzymeIsoelectric pointKey stepIdentical isoelectric pointsSephadex chromatographyCrude extractPurificationAffinity columnGel electrophoresisEscherichia coli tRNA nucleotidyltransferaseSpecific activityAssay conditionsChromatographyEnzymeTRNA nucleotidyltransferaseOptimal assay conditions