1990
Mammalian heterogeneous nuclear ribonucleoprotein A1. Nucleic acid binding properties of the COOH-terminal domain.
Kumar A, Casas-Finet J, Luneau C, Karpel R, Merrill B, Williams K, Wilson S. Mammalian heterogeneous nuclear ribonucleoprotein A1. Nucleic acid binding properties of the COOH-terminal domain. Journal Of Biological Chemistry 1990, 265: 17094-17100. PMID: 2145269, DOI: 10.1016/s0021-9258(17)44873-3.Peer-Reviewed Original ResearchConceptsCOOH-terminal domainNH2-terminal domainTerminal domainCOOH-terminal fragmentNucleic acid-binding proteinsCOOH-terminalHeterogeneous nuclear ribonucleoproteinsTwo-domain proteinVertebrate homologuesNucleic acidsAcid-binding proteinIntact A1Nuclear ribonucleoproteinAmino acids bindFluorescent reportersPrimary structureIntact proteinPolynucleotide latticeCore proteinProteinProteolytic fragmentsAcid bindsDNAFragmentsDomain[21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins
Stone K, Elliott J, Peterson G, McMurray W, Williams K. [21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins. Methods In Enzymology 1990, 193: 389-412. PMID: 2074828, DOI: 10.1016/0076-6879(90)93429-o.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyReversed-phase high-performance liquid chromatographyReversed phase high performance liquid chromatographyLiquid chromatographyEnzymatic digestsHigh peak capacityMass spectrometric approachProtein chemistsSpectrometric approachMass spectrometryPeak capacityComplex mixturesMolecular weightChemical cleavageGradient timeCleavage productsChromatographyTryptic peptidesPeptidesDigestsChemistsSpectrometryFractionationProductsPrimary structure
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 differencesProteinARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine- innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleus
Williams K, Hemmings H, LoPresti M, Greengard P. ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine- innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleus. Journal Of Neuroscience 1989, 9: 3631-3637. PMID: 2552036, PMCID: PMC6569913, DOI: 10.1523/jneurosci.09-10-03631.1989.Peer-Reviewed Original ResearchConceptsARPP-21CAMP-dependent protein kinaseMolecular massMajor cytosolic substrateDopamine-innervated brain regionsAmino acid sequenceAmino acid sequencingProtein phosphorylationCytosolic substratesProtein kinaseAcid sequenceSeryl residuesHistidinyl residuesMolecular mechanismsBovine caudate nucleusPrimary structureNH2-terminalEdman degradationDopamine-innervated regionsPolypeptide chainAmino acid analysisCysteinyl residuesGas-phase sequencingPosition 55SDS-PAGE
1988
Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein.
Merrill B, Stone K, Cobianchi F, Wilson S, Williams K. Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein. Journal Of Biological Chemistry 1988, 263: 3307-3313. PMID: 2830282, DOI: 10.1016/s0021-9258(18)69073-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCattleChromatography, AffinityChromatography, High Pressure LiquidDNA HelicasesDNA, Single-StrandedElectrophoresis, Polyacrylamide GelHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataNucleic AcidsPeptide FragmentsPhenylalaninePhenylthiohydantoinPhotochemistryPoly TRatsRibonucleoproteinsRNA-Binding ProteinsSerine EndopeptidasesThymus HormonesTrypsinConceptsRNA-binding proteinHeterogeneous nuclear ribonucleoproteinsA1 heterogeneous nuclear ribonucleoproteinNuclear ribonucleoproteinRepeat sequencesPhenylalanine residuesRNA-binding pocketDNA-cellulose chromatographyInternal repeat sequencesStaphylococcus aureus VSequence homologyCovalent adduct formationA1 proteinPrimary structurePartial proteolysisAnalogous positionsAmino acidsTryptic peptidesProteinPolypeptideProteolytic fragmentsRibonucleoproteinFirst experimental evidenceResiduesCellulose chromatographySynthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus.
Roberts W, Elliott J, McMurray W, Williams K. Synthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus. Chemical Biology & Drug Design 1988, 1: 74-80. PMID: 2856555.Peer-Reviewed Original ResearchConceptsBeta strandsAlpha-helixDirect amino acid sequencingSynthetic peptide bindsMurine leukemia virus proteinsAmino acid sequencingLys-C peptidesRetroviral Gag polyproteinFasman analysisGene 32Nucleic acidsP10 proteinCircular dichroism experimentsCys-X2Cysteine positionsBacteriophage T4Endoproteinase Lys-C peptidesPrimary sequenceMurine leukemia virusNative proteinPrimary structureCys-X4Amino acid analysisProteinSimilar sequences
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
Purification 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 acidsProtein
1984
Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase
Horwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase. Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.Peer-Reviewed Original ResearchConceptsComplementary DNALeader peptideOrnithine transcarbamylaseAmino-terminal leader peptideMost mitochondrial proteinsComplete primary structureHuman ornithine transcarbamylaseFree cytoplasmic ribosomesMitochondrial matrix enzymeCultured HeLa cellsMitochondrial proteinsCytoplasmic ribosomesRegulatory elementsNucleotide sequenceStable transformantsMatrix enzymeAsparagine residuesAcidic residuesLarger precursorMature formPrimary structureProtein occursHeLa cellsEscherichia coliAmino acids
1982
Bacteriophage T4 gene 45. Sequences of the structural gene and its protein product.
Spicer E, Noble J, Nossal N, Konigsberg W, Williams K. Bacteriophage T4 gene 45. Sequences of the structural gene and its protein product. Journal Of Biological Chemistry 1982, 257: 8972-8979. PMID: 6284751, DOI: 10.1016/s0021-9258(18)34228-5.Peer-Reviewed Original ResearchConceptsGene 45T4 late gene transcriptionT4 DNA replication complexRNA polymerase recognitionT4 DNA replicationLate gene transcriptionDNA replication complexTranslation initiation regionNucleotide sequence analysisGenes 46Protein chemistry studiesRegA proteinStructural geneSequence similarityDNA replicationPutative promoterRNA polymeraseReplication complexGene transcriptionProtein productsSequence analysisPrimary structureInitiation regionRIIB genePolymerase recognitionComparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants
Williams K, L’Italien J, Guggenheimer R, Sillerud L, Spicer E, Chase J, Konigsberg W. Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants. Experimental Biology And Medicine 1982, 499-507. DOI: 10.1007/978-1-4612-5832-2_44.Peer-Reviewed Original ResearchPeptide mappingChemical modificationCovalent proteinComparative peptide mappingAmino acid analysisProtein structureParticular amino acid replacementsPrimary structureLac repressor moleculesHuman hemoglobinHPLCAcid analysisSubstitutionStructurePowerful approachSingle amino acid substitutionCrosslinkingMoleculesAmino acid substitutionsSubtitutionAcid substitutionsMutant proteins
1981
Primary structure of the bacteriophage T4 DNA helix-destabilizing protein.
Williams K, LoPresti M, Setoguchi M. Primary structure of the bacteriophage T4 DNA helix-destabilizing protein. Journal Of Biological Chemistry 1981, 256: 1754-1762. PMID: 6257686, DOI: 10.1016/s0021-9258(19)69872-8.Peer-Reviewed Original ResearchConceptsGene 32 proteinT4 DNA replication proteinsPrimary structureDNA replication proteinsDNA-binding proteinsHelix-destabilizing proteinLimited trypsin digestionGene 32Replication proteinsUnusual stretchesSerine residuesCyanogen bromide cleavageBacteriophage T4DNA bindingSequencing of peptidesAlpha-helixTyrosine residuesBeta sheetNative proteinStaphylococcal proteaseCooperative bindingAmino acidsTryptic peptidesPosition 72Protein
1980
Amino acid sequence of the T4 DNA helix-destabilizing protein.
Williams K, LoPresti M, Setoguchi M, Konigsberg W. Amino acid sequence of the T4 DNA helix-destabilizing protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 4614-4617. PMID: 6254033, PMCID: PMC349895, DOI: 10.1073/pnas.77.8.4614.Peer-Reviewed Original ResearchConceptsT4 DNA replication proteinsDNA replication proteinsDNA-binding proteinsHelix-destabilizing proteinGene 32 proteinProtein-protein interactionsAmino acid sequenceLimited trypsin digestionProtein self-associationGene 32Replication proteinsUnusual stretchesSerine residuesCyanogen bromide cleavageDNA bindingAcid sequenceTyrosine residuesPrimary structureStaphylococcal proteasePartial proteolysisIntact proteinPosition 73Amino acidsTryptic peptidesProtein