2024
Proteomic Profile of Circulating Extracellular Vesicles in the Brain after Δ9-Tetrahydrocannabinol Inhalation
Lallai V, Lam T, Garcia-Milian R, Chen Y, Fowler J, Manca L, Piomelli D, Williams K, Nairn A, Fowler C. Proteomic Profile of Circulating Extracellular Vesicles in the Brain after Δ9-Tetrahydrocannabinol Inhalation. Biomolecules 2024, 14: 1143. PMID: 39334909, PMCID: PMC11430348, DOI: 10.3390/biom14091143.Peer-Reviewed Original ResearchConceptsImmediate early gene c-fosChronic THC exposureEarly gene c-fosCannabinoid 1 receptorGene c-fosSex-specific mannerTHC exposurePsychoactive componentExtracellular vesiclesCentral signaling mechanismDrug effectsTHCChoroid plexus epithelial cellsFemale ratsC-fosPlexus epithelial cellsBrainCannabisRelease of EVsRegulate intercellular communicationCerebrospinal fluidEpithelial cellsIntercellular signaling mediatorsEV signalingIntercellular communication
2015
Development of a highly automated and multiplexed targeted proteome pipeline and assay for 112 rat brain synaptic proteins
Colangelo CM, Ivosev G, Chung L, Abbott T, Shifman M, Sakaue F, Cox D, Kitchen RR, Burton L, Tate SA, Gulcicek E, Bonner R, Rinehart J, Nairn AC, Williams KR. Development of a highly automated and multiplexed targeted proteome pipeline and assay for 112 rat brain synaptic proteins. Proteomics 2015, 15: 1202-1214. PMID: 25476245, PMCID: PMC4698340, DOI: 10.1002/pmic.201400353.Peer-Reviewed Original Research
2012
A molecular characterization of the choroid plexus and stress-induced gene regulation
Sathyanesan M, Girgenti MJ, Banasr M, Stone K, Bruce C, Guilchicek E, Wilczak-Havill K, Nairn A, Williams K, Sass S, Duman JG, Newton SS. A molecular characterization of the choroid plexus and stress-induced gene regulation. Translational Psychiatry 2012, 2: e139-e139. PMID: 22781172, PMCID: PMC3410626, DOI: 10.1038/tp.2012.64.Peer-Reviewed Original ResearchConceptsStress-induced gene regulationGene expression changesGene expression analysisCP gene expressionGlial fibrillary acidic proteinChoroid plexusMolecular functionsGene regulationSitu hybridization analysisTranscriptomic characterizationHigh-resolution tandem mass spectrometryTarget genesExpression analysisGene expressionExpression changesTarget proteinsCP proteinsMolecular characterizationAdult choroid plexusHybridization analysisCP functionGene profilesProteinBlood-cerebrospinal fluid barrierResolution tandem mass spectrometry
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
2000
PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*
Tang J, Frankel A, Cook R, Kim S, Paik W, Williams K, Clarke S, Herschman H. PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*. Journal Of Biological Chemistry 2000, 275: 7723-7730. PMID: 10713084, DOI: 10.1074/jbc.275.11.7723.Peer-Reviewed Original ResearchConceptsProtein arginine methyltransferase activityArginine methyltransferase activityMurine tissue extractsMammalian cellsRat1 cellsMethyltransferase activityType I protein arginine methyltransferasesType I protein arginine methyltransferaseHeterogeneous nuclear ribonucleoprotein A1Protein arginine methyltransferasesProtein arginine methyltransferaseFDH activityHigh molecular weight complexesDomain fusion proteinMolecular weight complexesMethyl donor substrateDimethylarginine residuesArginine methyltransferasesArginine methyltransferaseEucaryotic proteinsPRMT1 activityDehydrogenase proteinFusion proteinEnzyme activity presentWeight complexes
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 Analysis
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
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 bindsDNAFragmentsDomainStudies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.
Kumar A, Widen S, Williams K, Kedar P, Karpel R, Wilson S. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. Journal Of Biological Chemistry 1990, 265: 2124-2131. PMID: 2404980, DOI: 10.1016/s0021-9258(19)39949-1.Peer-Reviewed Original ResearchConceptsNH2-terminal domainDNA polymerase betaLarge-scale overproductionPolymerase betaMammalian DNA polymerase betaCOOH-terminal domainProtease-sensitive regionNucleic acidsProteolysis experimentsRat proteinRecombinant proteinsPolypeptide chainDNA polymerase activityIntact proteinEscherichia coliAmino acidsTryptic peptidesDNA polymeraseDomain structureProteinPolymerase activityDomainPolymeraseAcidDNA
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
1986
Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.
Kraus J, Firgaira F, Novotný J, Kalousek F, Williams K, Williamson C, Ohura T, Rosenberg L. Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8049-8053. PMID: 3464942, PMCID: PMC386864, DOI: 10.1073/pnas.83.21.8049.Peer-Reviewed Original ResearchConceptsPropionyl-CoA carboxylaseNH2-terminal leader peptideAmino acid sequenceBeta subunitBeta-subunit precursorMature subunitAcid sequenceLeader peptideMitochondrial enzyme propionyl-CoA carboxylaseAmino acidsSubunit precursorOpen reading frameAlpha-helical segmentsEnzyme propionyl-CoA carboxylaseCarboxylaseNH2-terminal residuesFirst helixReading frameDNA sequencesPrecursorsCytoplasmic precursorMRNA sequencesArginine residuesHydrophobic momentMRNA transcripts
1985
Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5.
Williams K, Reddigari S, Patel G. Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5260-5264. PMID: 2991914, PMCID: PMC390547, DOI: 10.1073/pnas.82.16.5260.Peer-Reviewed Original ResearchConceptsHelix-destabilizing proteinSs-DNAAmino acid compositionHPLC tryptic peptide mapsNucleic acid helix-destabilizing proteinSolid-phase protein sequencingChemical modification studiesCoenzyme binding siteTyrosine-238Molecular weightSimilar amino acid compositionsTryptic peptide mapsAcid compositionLactate dehydrogenase 5Molecular homogeneitySimilar specific activitiesProtein sequencingLDH proteinDNA bindingAmino terminusBiological roleSingle proteinM chainTryptic peptidesVivo roleA cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites
Kraus J, Hodges P, Williamson C, Horwich A, Kalousek F, Williams K, Rosenberg L. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Research 1985, 13: 943-952. PMID: 3839075, PMCID: PMC341044, DOI: 10.1093/nar/13.3.943.Peer-Reviewed Original ResearchConceptsAmino acid sequenceLeader sequenceAcid sequenceBasic residuesAmino-terminal leader sequenceE. coliComplete sequence homologyAmino acid residuesProtein sequence dataOrnithine transcarbamylaseCDNA clonesSequence dataDNA complementaryOrnithine transcarbamylasesSequence homologyEntire proteinHuman enzymeAcid residuesTranscarbamylasesComplementary DNAAmino acidsMessenger RNARat enzymeNucleotidesCatalytic site
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
1983
Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase.
Horwich A, Kraus J, Williams K, Kalousek F, Konigsberg W, Rosenberg L. Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 4258-4262. PMID: 6576335, PMCID: PMC384016, DOI: 10.1073/pnas.80.14.4258.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseSequential Edman analysesCDNA probeMitochondrial matrix enzymeInsertion of cDNAAmino acid residuesConsecutive amino acid residuesCarboxyl-terminal portionCytoplasmic polysomesMolecular cloningCDNA clonesEdman analysisDifferential colony hybridizationTranslation assaysX chromosomeCDNA codingMatrix enzymeEnzyme subunitMessenger speciesAcid residuesSequence presentPolysome immunoadsorptionIdentical subunitsColony hybridizationEscherichia coli