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-Binding ProteinsRNA, Heterogeneous NuclearSpectrometry, 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-Binding ProteinsRNA, Small NuclearSoftware
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-Binding ProteinsRNA, MessengerStructure-Activity Relationship
1995
Structural specificity of substrate for S-adenosylmethionine protein arginine N-methyltransferases
Rawal N, Rajpurohit R, Lischwe M, Williams K, Paik W, Kim S. Structural specificity of substrate for S-adenosylmethionine protein arginine N-methyltransferases. Biochimica Et Biophysica Acta 1995, 1248: 11-18. PMID: 7536038, DOI: 10.1016/0167-4838(94)00213-z.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMethylationMolecular Sequence DataMyelin Basic ProteinOligopeptidesPeptide FragmentsProtein-Arginine N-MethyltransferasesRatsRibonucleoproteinsS-AdenosylmethionineSubstrate SpecificityTrypsinConceptsProtein methylase IArginine residuesProtein A1Protein arginine N-methyltransferasesEnzymatic methylationPreferred amino acid sequencesArginine-methylated proteinsProtein arginine N-methyltransferaseHnRNP protein A1Arginine-rich motifAmino acid sequenceArginine N-methyltransferaseN-methyltransferasesRich motifN-terminal fragmentHPLC amino acid analysisC-terminusMethyl acceptorAmino acid analysisDisulfide bridgesS-adenosylmethionineProtein moleculesTrypsin digestionNG-monomethylarginineGood substrate
1994
Both RNA-binding domains in heterogenous nuclear ribonucleoprotein A1 contribute toward single-stranded-RNA binding.
Shamoo Y, Abdul-Manan N, Patten A, Crawford J, Pellegrini M, Williams K. Both RNA-binding domains in heterogenous nuclear ribonucleoprotein A1 contribute toward single-stranded-RNA binding. Biochemistry 1994, 33: 8272-81. PMID: 7518244, DOI: 10.1021/bi00193a014.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesCircular DichroismCloning, MolecularDNAElectrochemistryHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHydrogen-Ion ConcentrationMolecular Sequence DataOligonucleotidesPeptide FragmentsPoly UProtein Structure, SecondaryRibonucleoproteinsRNASodium ChlorideThermodynamicsPurification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts.
Amrute S, Abdul-Manan Z, Pandey V, Williams K, Modak M. Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts. Biochemistry 1994, 33: 8282-91. PMID: 7518245, DOI: 10.1021/bi00193a015.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCattleCell NucleusChromatographyChromatography, High Pressure LiquidCross-Linking ReagentsCyanogen BromideDNA, Single-StrandedHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataOligodeoxyribonucleotidesPeptide FragmentsRibonucleoproteinsRNASpectrometry, FluorescenceThymus GlandUltraviolet RaysConceptsHnRNP proteinsOccluded site sizeHeterogeneous nuclear ribonucleoproteinsNucleic acidsSingle-strand nucleic acidNH2-terminal sequencingEukaryotic RNATight tetramerSDS-polyacrylamide gel electrophoresisApparent molecular weightNuclear ribonucleoproteinNuclear extractsLimited proteolysisMass spectrometric analysisRNAProteinPhenylalanine 19Calf thymusGel electrophoresisAdditional ionic interactionsTerminal deoxynucleotidyl transferaseSite sizeAB formMajor siteCell disruptionDetermination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy.
Garrett D, Lodi P, Shamoo Y, Williams K, Clore G, Gronenborn A. Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 1994, 33: 2852-8. PMID: 8130198, DOI: 10.1021/bi00176a015.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesConserved SequenceEscherichia coliHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMagnetic Resonance SpectroscopyMammalsMolecular Sequence DataProtein FoldingProtein Structure, SecondaryRecombinant ProteinsRibonucleoproteinsRNA, Heterogeneous NuclearSequence Homology, Amino AcidConceptsHnRNP A1 proteinA1 proteinMultidimensional heteronuclear NMR spectroscopySecondary structureHeteronuclear magnetic resonance spectroscopyHeteronuclear NMR spectroscopySecondary structure elementsFirst RNARNAFolding patternProteinStructure elementsDomainLong domainNMR spectroscopyMarked variationFamilyMagnetic resonance spectroscopyMembersAntiparallelResonance spectroscopy
1991
Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions.
Nadler S, Merrill B, Roberts W, Keating K, Lisbin M, Barnett S, Wilson S, Williams K. Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions. Biochemistry 1991, 30: 2968-76. PMID: 1848781, DOI: 10.1021/bi00225a034.Peer-Reviewed Original ResearchAmino Acid SequenceCircular DichroismDNA HelicasesDNA-Binding ProteinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsKineticsMolecular Sequence DataNucleic Acid DenaturationPoly A-UPoly dA-dTPolydeoxyribonucleotidesPolyribonucleotidesRibonucleoproteinsSpectrometry, FluorescenceThermodynamicsThymus Hormones
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
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 chromatographyMammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids.
Cobianchi F, Karpel R, Williams K, Notario V, Wilson S. Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids. Journal Of Biological Chemistry 1988, 263: 1063-1071. PMID: 2447078, DOI: 10.1016/s0021-9258(19)35461-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBase SequenceCelluloseDNADNA, Single-StrandedEscherichia coliFluorescent DyesHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataPoly ARecombinant ProteinsRibonucleoproteinsRNAConceptsLarge-scale overproductionNH2-terminal domainTerminal domainDomain peptideCooperative protein-protein interactionsEscherichia coliProtein-induced fluorescence enhancementAmino acidsProtein-protein interactionsNucleic acidsAlpha-helix structureProtein A1Cooperative bindingAssociation constantsSynthetic polypeptide analogueProteinDirect interactionNatural proteinsRecombinant A1Low association constantsBindingIntact A1ColiFluorescence enhancementOverproduction
1987
Amino acid sequence of UP1, an hnRNP‐derived single‐stranded nucleic acid binding protein from calf thymus
MERRILL B, LOPRESTI M, STONE K, WILLIAMS K. Amino acid sequence of UP1, an hnRNP‐derived single‐stranded nucleic acid binding protein from calf thymus. Chemical Biology & Drug Design 1987, 29: 21-39. PMID: 3032834, DOI: 10.1111/j.1399-3011.1987.tb02226.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCattleChromatography, High Pressure LiquidCyanogen BromideDNA HelicasesHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsPeptide FragmentsPeptide HydrolasesRibonucleoproteinsThymus GlandThymus HormonesConceptsHeterogeneous nuclear ribonucleoproteinsAmino acid sequenceHnRNP proteinsAcid sequenceSolid-phase sequencingComplete amino acid sequenceNucleic acidsSingle-strand nucleic acidA1 hnRNP proteinCalf thymusInternal sequence homologyGlutamic acid residuesStaphylococcus aureus proteaseA1 heterogeneous nuclear ribonucleoproteinNuclear ribonucleoproteinSequence homologySequencing of peptides
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 acidsProtein