2023
Uncovering biology by single-cell proteomics
Mansuri M, Williams K, Nairn A. Uncovering biology by single-cell proteomics. Communications Biology 2023, 6: 381. PMID: 37031277, PMCID: PMC10082756, DOI: 10.1038/s42003-023-04635-2.Peer-Reviewed Original Research
2007
X!!Tandem, an Improved Method for Running X!Tandem in Parallel on Collections of Commodity Computers
Bjornson RD, Carriero NJ, Colangelo C, Shifman M, Cheung KH, Miller PL, Williams K. X!!Tandem, an Improved Method for Running X!Tandem in Parallel on Collections of Commodity Computers. Journal Of Proteome Research 2007, 7: 293-299. PMID: 17902638, PMCID: PMC3863625, DOI: 10.1021/pr0701198.Peer-Reviewed Original ResearchMeSH KeywordsDatabases, ProteinMethodsProtein Processing, Post-TranslationalProteinsSoftwareTandem Mass SpectrometryTime Factors
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
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