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
Quantification of cellular protein and redox imbalance using SILAC-iodoTMT methodology
Vajrychova M, Salovska B, Pimkova K, Fabrik I, Tambor V, Kondelova A, Bartek J, Hodny Z. Quantification of cellular protein and redox imbalance using SILAC-iodoTMT methodology. Redox Biology 2019, 24: 101227. PMID: 31154163, PMCID: PMC6545335, DOI: 10.1016/j.redox.2019.101227.Peer-Reviewed Original ResearchConceptsCellular proteomeCysteine oxidationProtein thiol residuesRedox statusCellular protein expressionRedox changesCellular redox statusOrganismal physiologyVersatile experimental approachProtein functionCellular proteinsTranscription factorsRedox homeostasisReporter ion quantificationOxidation processMetabolic labelingFunctional analysisProtein turnoverNew analytical methodThiol residuesIon quantificationRedox alterationsRedox modulatingBiological relevanceRedox imbalance