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 ResearchMeSH KeywordsClick ChemistryGlycopeptidesGlycosylationMucinsProtein Processing, Post-TranslationalProteomicsSugarsTandem Mass SpectrometryConceptsMass 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 modificationsGlycopeptidesSpectrometryVectorMOD: Method for Bottom-Up Proteomic Characterization of rAAV Capsid Post-Translational Modifications and Vector Impurities
Rumachik NG, Malaker SA, Paulk NK. VectorMOD: Method for Bottom-Up Proteomic Characterization of rAAV Capsid Post-Translational Modifications and Vector Impurities. Frontiers In Immunology 2021, 12: 657795. PMID: 33868302, PMCID: PMC8047074, DOI: 10.3389/fimmu.2021.657795.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsAkkermansiaAmino Acid SequenceElectronsGlycopeptidesPeptide HydrolasesProteolysisTandem Mass SpectrometryConceptsO-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 proteasesElectronsSpectrometryOptimal Dissociation Methods Differ for N- and O‑Glycopeptides
Riley NM, Malaker SA, Driessen MD, Bertozzi CR. Optimal Dissociation Methods Differ for N- and O‑Glycopeptides. Journal Of Proteome Research 2020, 19: 3286-3301. PMID: 32500713, PMCID: PMC7425838, DOI: 10.1021/acs.jproteome.0c00218.Peer-Reviewed Original Research