2024
Quantification and Site-Specific Analysis of Co-occupied N- and O‑Glycopeptides
Chongsaritsinsuk J, Rangel-Angarita V, Lucas T, Mahoney K, Enny O, Katemauswa M, Malaker S. Quantification and Site-Specific Analysis of Co-occupied N- and O‑Glycopeptides. Journal Of Proteome Research 2024 PMID: 39498894, DOI: 10.1021/acs.jproteome.4c00574.Peer-Reviewed Original ResearchElectron-based methodsO-glycopeptidesElectron-based fragmentation methodsFragmentation methodCo-occupancyO-glycosylated peptidesAnalysis of glycopeptidesPost-translational modificationsN-glycoproteomic analysisCore 1 structureComplex samplesO-glycansPurified proteinProtein glycosylationO-glycositesN-glycoproteomeNonmucin glycoproteinsTryptic peptidesDissociation methodO-linkedAnalysis of mucinsSite-specific analysisGlycoproteinGlycosylationProteinMass Spectrometry-Compatible Elution Technique Enables an Improved Mucin-Selective Enrichment Strategy to Probe the Mucinome
Mahoney K, Chang V, Lucas T, Maruszko K, Malaker S. Mass Spectrometry-Compatible Elution Technique Enables an Improved Mucin-Selective Enrichment Strategy to Probe the Mucinome. Analytical Chemistry 2024, 96: 5242-5250. PMID: 38512228, DOI: 10.1021/acs.analchem.3c05762.Peer-Reviewed Original ResearchMucin-domain glycoproteinsO-glycopeptidesGlycopeptide signalsIn-gel digestionMass spectrometryElution conditionsSolid supportBinding moietyElution stepDownstream analysisO-glycosylationIn-gelBiological functionsElutionHuman serumEnrichment strategyCell linesMoietyEffective isolationSpectrometryCatalyticallyGlycoproteinSampling requirementsGlycopeptidesStcE
2021
Benefits of Chemical Sugar Modifications Introduced by Click Chemistry for Glycoproteomic Analyses
Calle B, Bineva-Todd G, Marchesi A, Flynn H, Ghirardello M, Tastan OY, Roustan C, Choi J, Galan MC, Schumann B, Malaker SA. Benefits of Chemical Sugar Modifications Introduced by Click Chemistry for Glycoproteomic Analyses. Journal Of The American Society For Mass Spectrometry 2021, 32: 2366-2375. PMID: 33871988, PMCID: PMC7611619, DOI: 10.1021/jasms.1c00084.Peer-Reviewed Original ResearchConceptsMass spectrometryCharge densityMass spectrometric signatureLow charge densityIntact O-glycopeptidesHigh charge densityTandem mass spectrometryClick chemistryChemical methodsChemical modificationO-glycopeptidesETD fragmentationFragmentation behaviorMonosaccharide analoguesSpectrometric signaturesMucin-type O-glycansGlycoproteomic analysisCharge stateComplex post-translational modificationsRight analytical toolsGlycan structuresO-glycosylationSugar modificationsGlycopeptidesSpectrometry
2020
Electron-Based Dissociation Is Needed for O‑Glycopeptides Derived from OpeRATOR Proteolysis
Riley NM, Malaker SA, Bertozzi CR. Electron-Based Dissociation Is Needed for O‑Glycopeptides Derived from OpeRATOR Proteolysis. Analytical Chemistry 2020, 92: 14878-14884. PMID: 33125225, PMCID: PMC8329938, DOI: 10.1021/acs.analchem.0c02950.Peer-Reviewed Original ResearchConceptsO-glycopeptidesElectron-based fragmentationElectron-driven dissociationMS/MS spectraO-glycositesTandem mass spectrometryMS spectraMass spectrometryGlycoproteomic methodsOrthogonal cleavageDissociation methodO-glycoproteomicsPeptide fragmentsCombined digestionN-terminal residuesThreonine residuesBacterial enzymesO-glycoproteinsDissociationN-terminusExciting opportunitiesO-glycansCanonical proteasesElectronsSpectrometry