1997
Identification of N G-Methylarginine Residues in Human Heterogeneous RNP Protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe Is a Preferred Recognition Motif †
Kim S, Merrill B, Rajpurohit R, Kumar A, Stone K, Papov V, Schneiders J, Szer W, Wilson S, Paik W, Williams K. Identification of N G-Methylarginine Residues in Human Heterogeneous RNP Protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe Is a Preferred Recognition Motif †. Biochemistry 1997, 36: 5185-5192. PMID: 9136880, DOI: 10.1021/bi9625509.Peer-Reviewed Original ResearchAmino Acid SequenceArginineChromatography, High Pressure LiquidEnzyme InhibitorsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansMethylationMolecular Sequence DataPeptide MappingRibonucleoproteinsRNA, Heterogeneous NuclearRNA-Binding ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationCrystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution
Shamoo Y, Krueger U, Rice L, Williams K, Steitz T. Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution. Nature Structural & Molecular Biology 1997, 4: 215-222. PMID: 9164463, DOI: 10.1038/nsb0397-215.Peer-Reviewed Original ResearchBinding SitesComputer SimulationCrystallography, X-RayHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansModels, MolecularModels, StructuralProtein FoldingProtein Structure, SecondaryRibonucleoproteinsRNA SplicingRNA, Small NuclearRNA-Binding ProteinsSoftware
1996
hnRNP A1 Binds Promiscuously to Oligoribonucleotides: Utilization of Random and Homo-Oligonucleotides to Discriminate Sequence from Base-Specific Binding
Abdul-Manan N, Williams K. hnRNP A1 Binds Promiscuously to Oligoribonucleotides: Utilization of Random and Homo-Oligonucleotides to Discriminate Sequence from Base-Specific Binding. Nucleic Acids Research 1996, 24: 4063-4070. PMID: 8918813, PMCID: PMC146211, DOI: 10.1093/nar/24.20.4063.Peer-Reviewed Original ResearchBinding, CompetitiveHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsOligoribonucleotidesPoint MutationRibonucleoproteinsRNA PrecursorsRNA-Binding ProteinsSequence Homology, Nucleic AcidSpectrometry, FluorescenceTelomereOrigins of Binding Specificity of the A1 Heterogeneous Nuclear Ribonucleoprotein †
Abdul-Manan N, O'Malley S, Williams K. Origins of Binding Specificity of the A1 Heterogeneous Nuclear Ribonucleoprotein †. Biochemistry 1996, 35: 3545-3554. PMID: 8639505, DOI: 10.1021/bi952298p.Peer-Reviewed Original ResearchAmino Acid SequenceBase SequenceDNAGlobinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsIonsMolecular Sequence DataNucleic Acid ConformationOligoribonucleotidesProtein BindingRecombinant ProteinsRepetitive Sequences, Nucleic AcidRibonucleoproteinsRNA, MessengerRNA-Binding ProteinsStructure-Activity Relationship
1995
Multiple RNA binding domains (RBDs) just don't add up
Shamoo Y, Abdul-Manan N, Williams K. Multiple RNA binding domains (RBDs) just don't add up. Nucleic Acids Research 1995, 23: 725-728. PMID: 7535921, PMCID: PMC306750, DOI: 10.1093/nar/23.5.725.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesMolecular Sequence DataRNARNA-Binding ProteinsSequence Alignment
1992
Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif.
Nadler S, Kapouch J, Elliott J, Williams K. Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif. Journal Of Biological Chemistry 1992, 267: 3750-3757. PMID: 1740426, DOI: 10.1016/s0021-9258(19)50589-0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCarrier ProteinsCircular DichroismFungal ProteinsGenes, FungalHot TemperatureMolecular Sequence DataNucleic Acid DenaturationNucleic AcidsPeptide FragmentsPoly APoly A-UPoly(A)-Binding ProteinsRNA, FungalRNA-Binding ProteinsSaccharomyces cerevisiaeSpectrometry, FluorescenceSubstrate SpecificityConceptsNucleic acidsPeptide studiesResidue peptideSynthetic peptide studiesSynthetic peptidesSynthetic peptide analoguesFree energyProperties of fragmentsPeptide analoguesNucleic acid-binding domainParent proteinLatter peptideNucleic acid bindingAmino acidsStructure/function studiesAmino acid sequenceSignificant affinityAcidEukaryotic RNAPeptidesRNA specificityAmino acid compositionSimilar RNACarboxyl halfMolecular basis
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 chromatography
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