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 ResearchMeSH KeywordsAnimalsArginineMethylationMiceMice, Mutant StrainsOxidoreductases Acting on CH-NH Group DonorsProtein MethyltransferasesProtein Processing, Post-TranslationalProtein-Arginine N-MethyltransferasesRatsS-AdenosylmethionineConceptsProtein 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