1994
Purification 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 disruption
1989
ARPP-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 chromatography
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 HormonesSingle-Stranded DNA Binding Proteins Required for DNA Replication
Chase J, Williams K. Single-Stranded DNA Binding Proteins Required for DNA Replication. Annual Review Of Biochemistry 1986, 55: 103-136. PMID: 3527040, DOI: 10.1146/annurev.bi.55.070186.000535.Peer-Reviewed Original ResearchAcidic lipids enhance cathepsin D cleavage of the myelin basic protein
Williams K, Williams N, Konigsberg W, Yu R. Acidic lipids enhance cathepsin D cleavage of the myelin basic protein. Journal Of Neuroscience Research 1986, 15: 137-145. PMID: 2421004, DOI: 10.1002/jnr.490150203.Peer-Reviewed Original ResearchHigh 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
1985
Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma.
Williams K, Stone K, LoPresti M, Merrill B, Planck S. Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5666-5670. PMID: 2994041, PMCID: PMC390612, DOI: 10.1073/pnas.82.17.5666.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAmino acidsAnalogous proteinsAcid sequenceHelix-destabilizing proteinsComplete amino acid sequenceHelix-destabilizing proteinStaphylococcus aureus V8 proteaseSimilar amino acidsAureus V8 proteaseMouse proteinCyanogen bromide cleavageMouse sequencesProtein sequencesSequence homologyCOOH terminusNH2 terminusSolid-phase sequencingGas-phase sequencingV8 proteaseEndoproteinase LysTryptic peptidesProteinUP1Calf thymus