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
1998
Identification of Protein-ArginineN-Methyltransferase as 10-Formyltetrahydrofolate Dehydrogenase*
Kim S, Park G, Joo W, Paik W, Cook R, Williams K. Identification of Protein-ArginineN-Methyltransferase as 10-Formyltetrahydrofolate Dehydrogenase*. Journal Of Biological Chemistry 1998, 273: 27374-27382. PMID: 9765265, DOI: 10.1074/jbc.273.42.27374.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBlotting, WesternChromatography, AffinityChromatography, High Pressure LiquidGas Chromatography-Mass SpectrometryLeucovorinLiverMolecular Sequence DataOxidoreductases Acting on CH-NH Group DonorsPeptide MappingProtein-Arginine N-MethyltransferasesRatsRecombinant ProteinsSepharoseSequence AnalysisUse of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis
Stone K, Deangelis R, LoPresti M, Jones J, Papov V, Williams K. Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. Electrophoresis 1998, 19: 1046-1052. PMID: 9638951, DOI: 10.1002/elps.1150190620.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate-polyacrylamide gel electrophoresisQuadrupole ion trap mass spectrometerIon trap mass spectrometerDodecyl sulfate-polyacrylamide gel electrophoresisLow pmol levelSulfate-polyacrylamide gel electrophoresisIonization tandem mass spectrometryTrap mass spectrometerLiquid chromatography-electrospray ionization-tandem mass spectrometryLiquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysisMS/MS approachProtein identificationIonization tandem mass spectrometry analysisFmol levelFacile approachMass spectrometry analysisMass spectrometerEng et alMass spectrometryPmol levelLC-MS/MS approachTryptic digestMS approachSpectrometry analysisGel electrophoresis
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-Ionization
1995
Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping
Williams K, Stone K. Identifying Sites of Posttranslational Modifications in Proteins Via HPLC Peptide Mapping. Methods In Molecular Biology 1995, 40: 157-175. PMID: 7633521, DOI: 10.1385/0-89603-301-5:157.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsChromatography, High Pressure LiquidPeptide FragmentsPeptide MappingProtein Processing, Post-TranslationalConceptsHPLC peptide mappingMass spectrometryPosttranslational modificationsIntact proteinPeptide mappingAtomic mass unitsAccurate massNet chargeDifferent posttranslational modificationsSulfoxide formationMass unitsCovalent changesOxidationSpectrometryProtein stabilityDeamidationProteinIsoelectric focusingPhosphorylationModification
1990
[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
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 Hormones