Stacy Malaker
Assistant ProfessorCards
About
Research
Publications
2025
In-depth analysis of the tear fluid glycoproteome reveals diverse lacritin glycosylation and spliceoforms
Chang V, Mahoney K, Lian I, Chen R, Chung N, Utheim T, Karlsson N, Malaker S. In-depth analysis of the tear fluid glycoproteome reveals diverse lacritin glycosylation and spliceoforms. Journal Of Biological Chemistry 2025, 301: 110580. PMID: 40784456, PMCID: PMC12450620, DOI: 10.1016/j.jbc.2025.110580.Peer-Reviewed Original ResearchO-glycoproteomics studiesMass spectrometryGlycan structuresDownstream biological processesProtein-level evidenceBackbone rigidityDiverse groupProtein foldingO-glycosylationExtracellular glycoproteinBiological processesGlycosylation profileO-glycositesBiochemical investigationsGlycansGlycosylationMolecular weightSpectrometrySpliceoformsAntimicrobial activityGlycoproteomicsGlycoproteinProteinComprehensive characterizationLacritinSmall RNAs are modified with N-glycans and displayed on the surface of living cells
Flynn R, Pedram K, Malaker S, Batista P, Smith B, Johnson A, George B, Majzoub K, Villalta P, Carette J, Bertozzi C. Small RNAs are modified with N-glycans and displayed on the surface of living cells. Cell 2025, 188: 4470. PMID: 40695275, PMCID: PMC12369702, DOI: 10.1016/j.cell.2025.07.019.Peer-Reviewed Original ResearchIdentification of Post-translationally Modified MHC Class I–Associated Peptides as Potential Cancer Immunotherapeutic Targets
Mahoney K, Reser L, Cuevas M, Abelin J, Shabanowitz J, Hunt D, Malaker S. Identification of Post-translationally Modified MHC Class I–Associated Peptides as Potential Cancer Immunotherapeutic Targets. Molecular & Cellular Proteomics 2025, 24: 100971. PMID: 40239839, PMCID: PMC12362676, DOI: 10.1016/j.mcpro.2025.100971.Peer-Reviewed Original ResearchCirculating cytotoxic T-cellsMHC class I processing pathwayClass I processing pathwayCancer immunotherapy targetCytotoxic T cellsCancer immunotherapeutic targetsVaccine development effortsModern immunotherapyImmunotherapy targetMHC-associated peptidesImmunotherapeutic targetT cellsMalignant cellsAntigen presentationAberrant signalingMHC-peptideMass spectrometry-based technologiesCancerMHCPost-translational modificationsDysregulationIdentification of post-translationallyPeptideImmunotherapyPathwayRecent Advances in Mass Spectrometry-Based Bottom-Up Proteomics
Movassaghi C, Sun J, Jiang Y, Turner N, Chang V, Chung N, Chen R, Browne E, Lin C, Schweppe D, Malaker S, Meyer J. Recent Advances in Mass Spectrometry-Based Bottom-Up Proteomics. Analytical Chemistry 2025, 97: 4728-4749. PMID: 40000226, PMCID: PMC12117541, DOI: 10.1021/acs.analchem.4c06750.Peer-Reviewed Original ResearchPNGaseF-Generated N‑Glycans Adduct onto Peptides in the Gas Phase
Rangel-Angarita V, Chongsaritsinsuk J, Mahoney K, Kim L, Chen R, Appah-Sampong A, Tran I, Steigmeyer A, Hollenhorst M, Malaker S. PNGaseF-Generated N‑Glycans Adduct onto Peptides in the Gas Phase. Journal Of The American Society For Mass Spectrometry 2025, 36: 542-552. PMID: 39938005, DOI: 10.1021/jasms.4c00431.Peer-Reviewed Original ResearchGlycoproteoforms of Osteoarthritis-associated Lubricin in Plasma and Synovial Fluid
Afshari A, Chang V, Thomsson K, Höglund J, Browne E, Karadzhov G, Mahoney K, Lucas T, Rangel-Angarita V, Ryberg H, Gidwani K, Pettersson K, Rolfson O, Björkman L, Eisler T, Schmidt T, Jay G, Malaker S, Karlsson N. Glycoproteoforms of Osteoarthritis-associated Lubricin in Plasma and Synovial Fluid. Molecular & Cellular Proteomics 2025, 24: 100923. PMID: 39922311, PMCID: PMC11925169, DOI: 10.1016/j.mcpro.2025.100923.Peer-Reviewed Original ResearchDecoding Extracellular Protein Glycosylation in Human Health and Disease
Steigmeyer A, Lowery S, Rangel-Angarita V, Malaker S. Decoding Extracellular Protein Glycosylation in Human Health and Disease. Annual Review Of Analytical Chemistry 2025, 18: 241-264. PMID: 39813736, DOI: 10.1146/annurev-anchem-071024-124203.Peer-Reviewed Original ResearchPost-translational modificationsProtein glycosylationStudy protein glycosylationHeterogeneous post-translational modificationsBiologically relevant contextProtein foldingGlycan complexityNontemplated natureCell adhesionAberrant glycosylationProtein backboneGlycosylationBiochemical processesProteinGlycoprotein characterizationCovalent attachmentHealth and DiseaseGlycansStructural heterogeneityHuman healthRelevant contextGlycoproteinFoldingBiologyN-
2024
Unraveling O‑Glycan Diversity of Mucins: Insights from SmE Mucinase and Ultraviolet Photodissociation Mass Spectrometry
Helms A, Chang V, Malaker S, Brodbelt J. Unraveling O‑Glycan Diversity of Mucins: Insights from SmE Mucinase and Ultraviolet Photodissociation Mass Spectrometry. Analytical Chemistry 2024, 96: 19230-19237. PMID: 39576755, PMCID: PMC11653425, DOI: 10.1021/acs.analchem.4c02011.Peer-Reviewed Original ResearchUltraviolet photodissociationUltraviolet photodissociation mass spectrometryPhotodissociation Mass SpectrometryDomain proteinsMicroheterogeneity of glycosylationStructural characterizationMass spectrometryGlycan mappingTandem repeatsMUC-16Target proteasesPhotodissociationDiverse classSpectrometryTIM-1ProteinGlycoproteinQuantification and Site-Specific Analysis of Co-occupied N- and O‑Glycopeptides
Chongsaritsinsuk J, Rangel-Angarita V, Lucas T, Mahoney K, Enny O, Katemauswa M, Malaker S. Quantification and Site-Specific Analysis of Co-occupied N- and O‑Glycopeptides. Journal Of Proteome Research 2024, 23: 5449-5461. PMID: 39498894, PMCID: PMC12057997, DOI: 10.1021/acs.jproteome.4c00574.Peer-Reviewed Original ResearchElectron-based methodsO-glycopeptidesElectron-based fragmentation methodsFragmentation methodCo-occupancyO-glycosylated peptidesAnalysis of glycopeptidesPost-translational modificationsN-glycoproteomic analysisCore 1 structureComplex samplesO-glycansPurified proteinProtein glycosylationO-glycositesN-glycoproteomeNonmucin glycoproteinsTryptic peptidesDissociation methodO-linkedAnalysis of mucinsSite-specific analysisGlycoproteinGlycosylationProteinO-Glycoproteomics: Methods, Challenges, and New Opportunities
Riley N, Malaker S. O-Glycoproteomics: Methods, Challenges, and New Opportunities. 2024, 118-162. DOI: 10.1039/9781839166433-00118.Peer-Reviewed Original ResearchElectron transfer dissociationMass spectrometryBeam-type collision-induced dissociationSupplemental collisional activationCollision-induced dissociationSolid-phase extractionCollisional activationTransfer dissociationGlycopeptide analysisTandem MSO-glycoproteomeDissociationO-glycoproteinsSite-specific localizationGlycopeptidesEThcDO-glycansSpectrometryGlycoproteomicsSpectraElectron
Academic Achievements & Community Involvement
News
News
- October 17, 2025
Results Realized: Better Understanding the Structure of CA125
- September 08, 2023
WHRY Launches New Pilot Project Studies
- May 25, 2023Source: NBC CT
Yale Researcher Studying How to Detect Ovarian Cancer Earlier
- May 16, 2023
Women’s Health Research at Yale Funds Studies to Improve Early Detection of Ovarian Cancer, Treatment of Prenatal Infections, and Aortic Aneurysm Outcomes in Women