2021
Classification, structural biology, and applications of mucin domain-targeting proteases
Shon DJ, Kuo A, Ferracane MJ, Malaker SA. Classification, structural biology, and applications of mucin domain-targeting proteases. Biochemical Journal 2021, 478: 1585-1603. PMID: 33909028, DOI: 10.1042/bcj20200607.Peer-Reviewed Original ResearchConceptsClass of proteinsHost-microbe interfaceImmunoglobulin A (IgA) proteaseThreonine residuesGlycan repertoireStructural biologyDistinct bacteriaGlycan structuresSource of nutrientsHinge regionProteaseIgA proteaseIntricate interplayMucosal environmentColonizationStructural featuresMutualistsMucosal colonizationEpithelial surfaceBacterial colonizationMicrobesTranslocation of microbes
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 proteasesElectronsSpectrometry
2019
Engineering Orthogonal Polypeptide GalNAc-Transferase and UDP-Sugar Pairs
Choi J, Wagner LJS, Timmermans SBPE, Malaker SA, Schumann B, Gray MA, Debets MF, Takashima M, Gehring J, Bertozzi CR. Engineering Orthogonal Polypeptide GalNAc-Transferase and UDP-Sugar Pairs. Journal Of The American Chemical Society 2019, 141: 13442-13453. PMID: 31373799, PMCID: PMC6813768, DOI: 10.1021/jacs.9b04695.Peer-Reviewed Original Research
2016
Identification and Characterization of Complex Glycosylated Peptides Presented by the MHC Class II Processing Pathway in Melanoma
Malaker SA, Ferracane MJ, Depontieu FR, Zarling AL, Shabanowitz J, Bai DL, Topalian SL, Engelhard VH, Hunt DF. Identification and Characterization of Complex Glycosylated Peptides Presented by the MHC Class II Processing Pathway in Melanoma. Journal Of Proteome Research 2016, 16: 228-237. PMID: 27550523, PMCID: PMC5218890, DOI: 10.1021/acs.jproteome.6b00496.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesCarbohydrate SequenceCell Line, TumorComplementarity Determining RegionsCrystallography, X-RayDisulfidesGlycopeptidesGlycosylationHLA-DR AntigensHumansMelanocytesModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsThermodynamics