2021
Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome
Sztacho M, Šalovská B, Červenka J, Balaban C, Hoboth P, Hozák P. Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome. Cells 2021, 10: 68. PMID: 33406800, PMCID: PMC7824793, DOI: 10.3390/cells10010068.Peer-Reviewed Original ResearchConceptsGene expressionHuman nuclear proteomeLimited proteolysisLabel-free quantitative mass spectrometryNuclear pore complexGene ontology analysisCell cycle regulationQuantitative mass spectrometryNuclear proteomeProtein effectorsPore complexPol IIRNA splicingOntology analysisMRNA splicingCycle regulationPIP2 bindingProtein interactionsDNA repairBioinformatics analysisNuclear envelopeFunctional domainsMass spectrometry identifiesSpecific proteinsCell cycle
2011
Phosphoproteomics: Searching for a needle in a haystack
Tichy A, Salovska B, Rehulka P, Klimentova J, Vavrova J, Stulik J, Hernychova L. Phosphoproteomics: Searching for a needle in a haystack. Journal Of Proteomics 2011, 74: 2786-2797. PMID: 21839867, DOI: 10.1016/j.jprot.2011.07.018.Peer-Reviewed Original ResearchConceptsCharacterization of phosphoproteinsReversible phosphorylationCellular processesSignal transductionCell divisionNon-phosphorylated peptidesGene expressionInsufficient ionizationLow abundanceTryptic protein digestsMass spectrometryCritical roleProtein digestsEnrichment techniquePhosphoproteomePhosphoproteomicsPhosphoproteinPowerful toolTransductionPhosphorylationPhosphopeptidesProteinAbundanceApoptosisDifferentiation