2024
Analysis 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 Research
2022
Cell-specific bioorthogonal tagging of glycoproteins
Cioce A, Calle B, Rizou T, Lowery SC, Bridgeman VL, Mahoney KE, Marchesi A, Bineva-Todd G, Flynn H, Li Z, Tastan OY, Roustan C, Soro-Barrio P, Rafiee MR, Garza-Garcia A, Antonopoulos A, Wood TM, Keenan T, Both P, Huang K, Parmeggian F, Snijders AP, Skehel M, Kjær S, Fascione MA, Bertozzi CR, Haslam SM, Flitsch SL, Malaker SA, Malanchi I, Schumann B. Cell-specific bioorthogonal tagging of glycoproteins. Nature Communications 2022, 13: 6237. PMID: 36284108, PMCID: PMC9596482, DOI: 10.1038/s41467-022-33854-0.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsArtificial biosynthetic pathwayTumor-derived cell linesCellular model systemNon-transfected cellsCellular functionsProtein glycosylationBiosynthetic pathwayProteome analysisGlycosylation sitesBioorthogonal tagsCancer developmentCell linesModel systemImportant modulatorIntricate interactionsCo-culture modelGlycoproteinCellsGlycoprotein expressionMouse modelGlycoproteomeGlycosylationTaggingMonocultureCurrent strategies for characterization of mucin-domain glycoproteins
Ince D, Lucas TM, Malaker SA. Current strategies for characterization of mucin-domain glycoproteins. Current Opinion In Chemical Biology 2022, 69: 102174. PMID: 35752002, DOI: 10.1016/j.cbpa.2022.102174.Peer-Reviewed Original ResearchConceptsGlycopeptide mimeticsPost-translational modificationsCurrent characterization techniquesCellular glycosylation pathwaysSynthetic methodCharacterization techniquesGlycosylation pathwayMucin domainO-glycosylationBiological functionsGlycoproteomic workflowGlycosylationGlycoproteinExciting avenuesRecent breakthroughsMucin glycoproteinsRecent developmentsRevealing the human mucinome
Malaker SA, Riley NM, Shon DJ, Pedram K, Krishnan V, Dorigo O, Bertozzi CR. Revealing the human mucinome. Nature Communications 2022, 13: 3542. PMID: 35725833, PMCID: PMC9209528, DOI: 10.1038/s41467-022-31062-4.Peer-Reviewed Original ResearchConceptsModular protein domainsKey molecular signaturesProtein domainsTransmembrane proteinDetection of hundredsMucin domainGlycoprotein identificationHuman diseasesMolecular signaturesCell lysatesEnrichment strategyGlycoproteinVivo sourceOverlapping populationsImportant roleDomainStcEProteinLysatesOvarian cancer patientsComplex samples
2021
Interleukin-22 regulates B3GNT7 expression to induce fucosylation of glycoproteins in intestinal epithelial cells
Carroll DJ, Burns MWN, Mottram L, Propheter DC, Boucher A, Lessen GM, Kumar A, Malaker SA, Xing C, Hooper LV, Yrlid U, Kohler JJ. Interleukin-22 regulates B3GNT7 expression to induce fucosylation of glycoproteins in intestinal epithelial cells. Journal Of Biological Chemistry 2021, 298: 101463. PMID: 34864058, PMCID: PMC8808068, DOI: 10.1016/j.jbc.2021.101463.Peer-Reviewed Original ResearchOn-tissue spatially resolved glycoproteomics guided by N-glycan imaging reveal global dysregulation of canine glioma glycoproteomic landscape
Malaker SA, Quanico J, Raffo-Romero A, Kobeissy F, Aboulouard S, Tierny D, Bertozzi CR, Fournier I, Salzet M. On-tissue spatially resolved glycoproteomics guided by N-glycan imaging reveal global dysregulation of canine glioma glycoproteomic landscape. Cell Chemical Biology 2021, 29: 30-42.e4. PMID: 34102146, PMCID: PMC8617081, DOI: 10.1016/j.chembiol.2021.05.007.Peer-Reviewed Original Research
2020
Metabolic precision labeling enables selective probing of O-linked N-acetylgalactosamine glycosylation
Debets MF, Tastan OY, Wisnovsky SP, Malaker SA, Angelis N, Moeckl LKR, Choi J, Flynn H, Wagner LJS, Bineva-Todd G, Antonopoulos A, Cioce A, Browne WM, Li Z, Briggs DC, Douglas HL, Hess GT, Agbay AJ, Roustan C, Kjaer S, Haslam SM, Snijders AP, Bassik MC, Moerner WE, Li VSW, Bertozzi CR, Schumann B. Metabolic precision labeling enables selective probing of O-linked N-acetylgalactosamine glycosylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 25293-25301. PMID: 32989128, PMCID: PMC7568240, DOI: 10.1073/pnas.2007297117.Peer-Reviewed Original ResearchConceptsStructure-based design processN-acetylgalactosamine glycosylationProtein glycosylation eventsCell surface glycoproteomeCRISPR knockout screensMetabolic labeling experimentsGlycan subtypesGlycosylation eventsSecretory pathwayGalNAc glycosylationProtein glycosylationEctopic expressionSer/GalNAc-T2Superresolution microscopyGlycan typesLiving cellsBioorthogonal tagsGlycosylationIntestinal organoidsMetabolic interconversionSuch specificityUridine diphosphateLabeling experimentsCells