2024
Beyond glucose: The crucial role of redox signaling in β-cell metabolic adaptation
Holendová B, Šalovská B, Benáková Š, Plecitá-Hlavatá L. Beyond glucose: The crucial role of redox signaling in β-cell metabolic adaptation. Metabolism 2024, 161: 156027. PMID: 39260557, DOI: 10.1016/j.metabol.2024.156027.Peer-Reviewed Original ResearchPost-translational modificationsReactive oxygen speciesEndoplasmic reticulumTricarboxylic acidRedox signalingPancreatic B-cellsGlucose stimulationModification of proteinsB-cell metabolismRedox signaling pathwaysReversible cysteine oxidationIncreased ROS levelsProduction of reactive oxygen speciesB cell functionInsulin secretionB cellsProtein functionProtein processingCysteine thiol modificationsGlucose-induced increaseOxidative phosphorylationPyruvate metabolismProtein activityRegulatory mechanismsMetabolic pathways
2023
A basic phosphoproteomic-DIA workflow integrating precise quantification of phosphosites in systems biology
Di Y, Li W, Salovska B, Ba Q, Hu Z, Wang S, Liu Y. A basic phosphoproteomic-DIA workflow integrating precise quantification of phosphosites in systems biology. Biophysics Reports 2023, 9: 82-98. PMID: 37753060, PMCID: PMC10518521, DOI: 10.52601/bpr.2023.230007.Peer-Reviewed Original ResearchPost-translational modificationsData-independent acquisitionSystems biologySite-specific phosphorylation eventsImportant post-translational modificationMost human proteinsCritical protein functionsPhosphorylation eventsProtein functionPhosphoproteomic studiesPhosphoproteomic analysisBioinformatics AdvancesHuman proteinsMass spectrometry technologyBioinformatics analysisLarge-scale quantificationExperimental workflowHigh-resolution mass spectrometry technologySpectrometry technologyPhosphoproteomicsPhosphorylationBiologyProteinSystems medicineSingle experiment
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
2012
Enrichment strategies for phosphoproteomics: state-of-the-art
Salovska B, Tichy A, Rezacova M, Vavrova J, Novotna E. Enrichment strategies for phosphoproteomics: state-of-the-art. Reviews In Analytical Chemistry 2012, 31: 29-41. DOI: 10.1515/revac-2011-0025.Peer-Reviewed Original ResearchProtein phosphorylationReversible post-translational modificationPost-translational modificationsAffinity enrichment techniquesPhosphorylated peptides/proteinsSubsequent mass spectrometry analysisAnalysis of phosphorylationEnrichment strategyDifferent enrichment strategiesTranslational regulationPhosphorylation sitesCellular signalingPhosphorylated proteinsMass spectrometry analysisPeptides/proteinsKey regulatorBiological processesChemical derivatizationLow abundancePhosphorylationMass spectrometryProteinSpectrometry analysisNonphosphorylated proteinsEnrichment techniqueRadio-Sensitization of Human Leukaemic MOLT-4 Cells by DNA-Dependent Protein Kinase Inhibitor, NU7026
Tichý A, Novotná E, Ďurišová K, Šalovská B, Sedlaříková R, Pejchal J, Zárybnická L, Vávrová J, Šinkorová Z, Řezáčová M. Radio-Sensitization of Human Leukaemic MOLT-4 Cells by DNA-Dependent Protein Kinase Inhibitor, NU7026. Acta Medica 2012, 55: 66-73. PMID: 23101268, DOI: 10.14712/18059694.2015.57.Peer-Reviewed Original ResearchConceptsMOLT-4 cellsDNA repairDNA-dependent protein kinase inhibitorDNA-dependent protein kinaseDNA damage responsePost-translational modificationsCheckpoint kinase 2Protein kinase inhibitorsG2 phase arrestInduction of apoptosisATM kinaseDamage responseProtein kinaseKinase 2Cell cycle analysisNU7026Specific inhibitorCellular mechanismsPronounced apoptosisApoptosisKinase inhibitorsAmount of cellsCellsCycle analysisInhibitors