2013
Assembly of the SLIP1–SLBP Complex on Histone mRNA Requires Heterodimerization and Sequential Binding of SLBP Followed by SLIP1
Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R. Assembly of the SLIP1–SLBP Complex on Histone mRNA Requires Heterodimerization and Sequential Binding of SLBP Followed by SLIP1. Biochemistry 2013, 52: 520-536. PMID: 23286197, PMCID: PMC3580866, DOI: 10.1021/bi301074r.Peer-Reviewed Original ResearchCarrier ProteinsHistonesHumansKineticsMRNA Cleavage and Polyadenylation FactorsMutagenesis, Site-DirectedMutant ProteinsNuclear ProteinsPeptide FragmentsPhosphorylationPoint MutationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Processing, Post-TranslationalRecombinant ProteinsRNA FoldingRNA-Binding ProteinsRNA, MessengerSerineThreonineTyrosine
2005
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
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
2002
Mapping of protein:protein contact surfaces by hydrogen/deuterium exchange, followed by on-line high-performance liquid chromatography–electrospray ionization fourier-transform ion-cyclotron-resonance mass analysis
Lam TT, Lanman JK, Emmett MR, Hendrickson CL, Marshall AG, Prevelige PE. Mapping of protein:protein contact surfaces by hydrogen/deuterium exchange, followed by on-line high-performance liquid chromatography–electrospray ionization fourier-transform ion-cyclotron-resonance mass analysis. Journal Of Chromatography A 2002, 982: 85-95. PMID: 12489858, DOI: 10.1016/s0021-9673(02)01357-2.Peer-Reviewed Original ResearchConceptsHigh-Performance Liquid Chromatography-Electrospray IonizationMass analysisHydrogen/deuterium exchangeLiquid Chromatography-Electrospray IonizationNuclear magnetic resonance analysisX-ray diffractionFront-end separationMagnetic resonance analysisBackbone amide hydrogensProtein contact surfacesAmide hydrogensDeuterium exchangeConventional X-ray diffractionH/2H exchangeReaction periodResonance analysisLow concentrationsDiffractionProtein complexesComplexedHydrogenComplexesIonizationSeparationSurface