2005
Multicomponent Internal Recalibration of an LC−FTICR-MS Analysis Employing a Partially Characterized Complex Peptide Mixture: Systematic and Random Errors
Yanofsky CM, Bell AW, Lesimple S, Morales F, Lam TT, Blakney GT, Marshall AG, Carrillo B, Lekpor K, Boismenu D, Kearney RE. Multicomponent Internal Recalibration of an LC−FTICR-MS Analysis Employing a Partially Characterized Complex Peptide Mixture: Systematic and Random Errors. Analytical Chemistry 2005, 77: 7246-7254. PMID: 16285672, DOI: 10.1021/ac050640q.Peer-Reviewed Original ResearchConceptsIon cyclotron resonance mass spectrometryRandom errorsCyclotron resonance mass spectrometryComplex mixturesResonance mass spectrometryComplex peptide mixturesFourier Transform Ion Cyclotron Resonance Mass Spectrometry for the Analysis of Small Ubiquitin-like Modifier (SUMO) Modification: Identification of Lysines in RanBP2 and SUMO Targeted for Modification during the E3 AutoSUMOylation Reaction
Cooper HJ, Tatham MH, Jaffray E, Heath JK, Lam TT, Marshall AG, Hay RT. Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for the Analysis of Small Ubiquitin-like Modifier (SUMO) Modification: Identification of Lysines in RanBP2 and SUMO Targeted for Modification during the E3 AutoSUMOylation Reaction. Analytical Chemistry 2005, 77: 6310-6319. PMID: 16194093, DOI: 10.1021/ac058019d.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCyclotronsFourier AnalysisIonsLysineMass SpectrometryMethylationMolecular ChaperonesMolecular Sequence DataMolecular WeightNuclear Pore Complex ProteinsProtein BindingRecombinant ProteinsSequence AlignmentSmall Ubiquitin-Related Modifier ProteinsUbiquitinUbiquitin-Protein LigasesConceptsFourier transform ion cyclotron resonance mass spectrometryTransform ion cyclotron resonance mass spectrometryIon cyclotron resonance mass spectrometryFourier transform ion cyclotron resonanceCyclotron resonance mass spectrometryMass spectrometryTransform ion cyclotron resonanceElectron capture dissociationResonance mass spectrometryMass spectrometry techniquesSUMO modificationIon cyclotron resonanceIdentification of LysinesCapture dissociationFunctional analysisUbiquitin-like protein SUMOLysine residuesSmall ubiquitin-like modifier (SUMO) modificationFT-ICRAcceptor lysine residuesImportant cellular processesSpectrometry techniquesSite-directed mutagenesisSites of sumoylationSUMO polymers
2004
Identification of Sites of Ubiquitination in Proteins: A Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Approach
Cooper HJ, Heath JK, Jaffray E, Hay RT, Lam TT, Marshall AG. Identification of Sites of Ubiquitination in Proteins: A Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Approach. Analytical Chemistry 2004, 76: 6982-6988. PMID: 15571350, DOI: 10.1021/ac0401063.Peer-Reviewed Original ResearchConceptsSites of ubiquitinationPolyubiquitin chainsFourier transform ion cyclotron resonance mass spectrometryTransform ion cyclotron resonance mass spectrometryIon electron capture dissociationIon cyclotron resonance mass spectrometryCyclotron resonance mass spectrometryLysine residuesTandem mass spectrometric techniquesElectron capture dissociationResonance mass spectrometryExtensive sequence coverageMass spectrometric techniquesConsequences of ubiquitinationCapture dissociationMass spectrometry approachPolyubiquitinated speciesSingle ubiquitinFT-ICRStructural elucidationCellular functionsUbiquitinated proteinsModified peptideUbiquitination modificationSpectrometric techniques