2022
Toward a hypothesis‐free understanding of how phosphorylation dynamically impacts protein turnover
Li W, Salovska B, Fornasiero E, Liu Y. Toward a hypothesis‐free understanding of how phosphorylation dynamically impacts protein turnover. Proteomics 2022, 23: e2100387. PMID: 36422574, PMCID: PMC10964180, DOI: 10.1002/pmic.202100387.Peer-Reviewed Original ResearchConceptsPost-translational modificationsProtein turnoverDynamic stable isotope labelingCell starvationStable isotope labelingData-independent acquisition mass spectrometryAcquisition mass spectrometryProteome levelTurnover diversityPhosphoproteomic datasetsPhosphorylation stoichiometryMetabolic labelingIsotope labelingMass spectrometryPhosphorylationAmino acidsCell culturesBiological perspectiveStarvationTurnoverTurnover measurementsRecent studiesSILACProteoformsPeptidoforms
2019
Capillary zone electrophoresis-tandem mass spectrometry with ultraviolet photodissociation (213 nm) for large-scale top–down proteomics
McCool EN, Chen D, Li W, Liu Y, Sun L. Capillary zone electrophoresis-tandem mass spectrometry with ultraviolet photodissociation (213 nm) for large-scale top–down proteomics. Analytical Methods 2019, 11: 2855-2861. PMID: 31608127, PMCID: PMC6788745, DOI: 10.1039/c9ay00585d.Peer-Reviewed Original ResearchN-terminal acetylationPost-translational modificationsCapillary zone electrophoresis-tandem mass spectrometryN-terminal glycineSize-exclusion chromatography (SEC) fractionationProteomic datasetsZebrafish brainDifferent proteoformsBrain samplesProteoformsCZE-MS/MSProteomicsMass spectrometryTrimethylationAcetylationCalmodulinProteinUltraviolet photodissociationMyristoylationBackbone cleavageSEC fractionsMolecular weightGlobal scaleHigh throughputExperimental evidence