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
2021
Mucinomics as the Next Frontier of Mass Spectrometry
Rangel-Angarita V, Malaker SA. Mucinomics as the Next Frontier of Mass Spectrometry. ACS Chemical Biology 2021, 16: 1866-1883. PMID: 34319686, DOI: 10.1021/acschembio.1c00384.Peer-Reviewed Original ResearchSmall RNAs are modified with N-glycans and displayed on the surface of living cells
Flynn RA, Pedram K, Malaker SA, Batista PJ, Smith BAH, Johnson AG, George BM, Majzoub K, Villalta PW, Carette JE, Bertozzi CR. Small RNAs are modified with N-glycans and displayed on the surface of living cells. Cell 2021, 184: 3109-3124.e22. PMID: 34004145, PMCID: PMC9097497, DOI: 10.1016/j.cell.2021.04.023.Peer-Reviewed Original ResearchConceptsLiving cellsGlycan biosynthetic machineryDomains of lifeMultiple cell typesRNA biologySmall RNAsExtracellular biologyBiosynthetic machineryBiochemical approachesMammalian speciesBattery of chemicalAnti-dsRNA antibodiesN-glycansCell typesReceptor familyCultured cellsCell surfaceRNAThird scaffoldGlycoRNABiologyMajor targetGlycosylationGlycansSialic acid
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.ChaptersMeSH KeywordsAnimalsCD4-Positive T-LymphocytesHumansMajor Histocompatibility ComplexMass SpectrometryPeptidesConceptsMass spectrometryAntibody conjugationImmunoaffinity purificationSurface of cellsMajor histocompatibility complexAutoimmune diseasesT cellsImmune componentsDisease processMoleculesHistocompatibility complexAntigenic peptidesMHCAssociated peptidePurificationPeptidesSurfaceSpectrometryElutionCellsComplexesConjugationCD8CD4CancerMass Spectrometric Identification and Molecular Modeling of Glycopeptides Presented by MHC Class I and II Processing Pathways
Malaker SA, Ferracane MJ. Mass Spectrometric Identification and Molecular Modeling of Glycopeptides Presented by MHC Class I and II Processing Pathways. Methods In Molecular Biology 2019, 2024: 269-285. PMID: 31364056, DOI: 10.1007/978-1-4939-9597-4_17.ChaptersThe mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins
Malaker SA, Pedram K, Ferracane MJ, Bensing BA, Krishnan V, Pett C, Yu J, Woods EC, Kramer JR, Westerlind U, Dorigo O, Bertozzi CR. The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 7278-7287. PMID: 30910957, PMCID: PMC6462054, DOI: 10.1073/pnas.1813020116.Peer-Reviewed Original ResearchConceptsModular protein domainsProtein domainsSecreted proteinsMucin domainFunctional analysisHuman diseasesMucin biologyGlycosylation patternsCultured cellsMolecular levelCell surfaceSequence coverageKey playersBacterial proteasesCancer-associated mucinsDiscrete peptidesBiological ligandsProteaseHuman mucinsGlycoform analysisStcESiglec-9Domain structureMass spectrometryDomain