2024
O-Glycoproteomics: Methods, Challenges, and New Opportunities
Riley N, Malaker S. O-Glycoproteomics: Methods, Challenges, and New Opportunities. 2024, 118-162. DOI: 10.1039/9781839166433-00118.Peer-Reviewed Original ResearchElectron transfer dissociationMass spectrometryBeam-type collision-induced dissociationSupplemental collisional activationCollision-induced dissociationSolid-phase extractionCollisional activationTransfer dissociationGlycopeptide analysisTandem MSO-glycoproteomeDissociationO-glycoproteinsSite-specific localizationGlycopeptidesEThcDO-glycansSpectrometryGlycoproteomicsSpectraElectronAnalysis of Mucin‐Domain Glycoproteins Using Mass Spectrometry
Mahoney K, Malaker S. Analysis of Mucin‐Domain Glycoproteins Using Mass Spectrometry. Current Protocols 2024, 4: e1100. PMID: 38984456, PMCID: PMC11239139, DOI: 10.1002/cpz1.1100.Peer-Reviewed Original ResearchGlycoproteomics: Charting new territory in mass spectrometry and glycobiology
Malaker S. Glycoproteomics: Charting new territory in mass spectrometry and glycobiology. Journal Of Mass Spectrometry 2024, 59: e5034. PMID: 38726698, DOI: 10.1002/jms.5034.Peer-Reviewed Original ResearchMass 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
2022
Glycoproteomics
Bagdonaite I, Malaker S, Polasky D, Riley N, Schjoldager K, Vakhrushev S, Halim A, Aoki-Kinoshita K, Nesvizhskii A, Bertozzi C, Wandall H, Parker B, Thaysen-Andersen M, Scott N. Glycoproteomics. Nature Reviews Methods Primers 2022, 2: 48. DOI: 10.1038/s43586-022-00128-4.Peer-Reviewed Original ResearchGlycan structuresMass spectrometryPost-translational additionIntact glycopeptide analysisSite of modificationProtein glycosylationProtein modificationBioinformatics platformBiological processesGlycopeptide analysisMS fragmentationGlycoproteomic methodsGlycoproteomicsGlycosylationProtein isolationProteolytic digestionPeptide sequencesSystem-wide contextStudy of glycopeptidesPrimersRecent advancesExciting fieldProteinGlycansSpectrometry
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
2019
Isolation of Major Histocompatibility Complex (MHC)-Associated Peptides by Immunoaffinity Purification
Penny SA, Malaker SA. Isolation of Major Histocompatibility Complex (MHC)-Associated Peptides by Immunoaffinity Purification. Methods In Molecular Biology 2019, 2024: 235-243. PMID: 31364053, DOI: 10.1007/978-1-4939-9597-4_14.ChaptersConceptsMass spectrometryAntibody conjugationImmunoaffinity purificationSurface of cellsMajor histocompatibility complexAutoimmune diseasesT cellsImmune componentsDisease processMoleculesHistocompatibility complexAntigenic peptidesMHCAssociated peptidePurificationPeptidesSurfaceSpectrometryElutionCellsComplexesConjugationCD8CD4Cancer