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
Bump-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