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
Novel Antibodies for the Simple and Efficient Enrichment of Native O-GlcNAc Modified Peptides
Burt RA, Dejanovic B, Peckham HJ, Lee KA, Li X, Ounadjela JR, Rao A, Malaker SA, Carr SA, Myers SA. Novel Antibodies for the Simple and Efficient Enrichment of Native O-GlcNAc Modified Peptides. Molecular & Cellular Proteomics 2021, 20: 100167. PMID: 34678516, PMCID: PMC8605273, DOI: 10.1016/j.mcpro.2021.100167.Peer-Reviewed Original ResearchConceptsO-GlcNAc-modified peptidesPosttranslational modificationsNumerous biological processesUbiquitin remnantsMouse brain tissue samplesGlcNAc signalingThreonine residuesLysine acetylationGlcNAc transferaseO-GlcNAcylationGlcNAc antibodiesBiological processesO-GalNAcExtended glycansN-acetylglucosamineEnrichment strategyFundamental roleDisease statesPeptidesInstrument timeModified peptidePhosphotyrosineNovel antibodyBrain tissue samplesImmunoprecipitation
2020
Generating orthogonal glycosyltransferase and nucleotide sugar pairs as next-generation glycobiology tools
Cioce A, Malaker SA, Schumann B. Generating orthogonal glycosyltransferase and nucleotide sugar pairs as next-generation glycobiology tools. Current Opinion In Chemical Biology 2020, 60: 66-78. PMID: 33125942, PMCID: PMC7955280, DOI: 10.1016/j.cbpa.2020.09.001.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsCell surface glycoproteomeProtein glycosylationBiological processesQuantitative biologyMutant glycosyltransferasesGlycoproteomicsDifferent glycansGlycansPrecision toolsGlycosyltransferasesBiosynthesisGlycoproteomeGlycomeGlycosyltransferaseBiologyGlycosylationGlycobiologyLabeling reagentLimited specificityPhysiologySpecificityParticular subtypeRoleCellsBump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living Cells
Schumann B, Malaker SA, Wisnovsky SP, Debets MF, Agbay AJ, Fernandez D, Wagner LJS, Lin L, Li Z, Choi J, Fox DM, Peh J, Gray MA, Pedram K, Kohler JJ, Mrksich M, Bertozzi CR. Bump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living Cells. Molecular Cell 2020, 78: 824-834.e15. PMID: 32325029, PMCID: PMC7276986, DOI: 10.1016/j.molcel.2020.03.030.Peer-Reviewed Original ResearchConceptsLiving cellsPolypeptide N-acetylgalactosaminyl transferasesCell surface glycomesEssential biological processesComplex biosynthetic machineryMajor physiological processesN-acetylgalactosaminyl transferaseBiosynthetic regulationBiosynthetic machineryGlycosyltransferase familyIndividual glycosyltransferasesProtein glycosylationPosttranslational modificationsGlycan fine structureBiosynthetic pathwayPhysiological contextBiological processesPhysiological processesGlycan structuresSpecific substratesGlycosyltransferasesChemical functionalityExperimental strategiesCellsBiosynthesis