2017
Protein O-GlcNAcylation: emerging mechanisms and functions
Yang X, Qian K. Protein O-GlcNAcylation: emerging mechanisms and functions. Nature Reviews Molecular Cell Biology 2017, 18: 452-465. PMID: 28488703, PMCID: PMC5667541, DOI: 10.1038/nrm.2017.22.Peer-Reviewed Original ResearchConceptsPost-translational modificationsO-GlcNAcylationAdaptor proteinGlcNAcylation levelsO-GlcNAc homeostasisTetratricopeptide repeat domainDiverse cellular processesProtein-protein interactionsOptimal cellular functionContext-dependent recruitmentPost-translational levelCell signaling dynamicsUnwanted protein aggregationCellular O-GlcNAcylationSubstrate-specific interactionsSpecific cell typesN-acetylglucosamine moietiesLevels of OGTGlcNAc signalingMitochondrial proteinsSpatiotemporal regulationCellular functionsCellular processesEpigenetic modificationsProtein substrates
2016
Solution Structures and Molecular Associations of a Peptide-Based Catalyst for the Stereoselective Baeyer–Villiger Oxidation
Abascal NC, Miller SJ. Solution Structures and Molecular Associations of a Peptide-Based Catalyst for the Stereoselective Baeyer–Villiger Oxidation. Organic Letters 2016, 18: 4646-4649. PMID: 27588823, PMCID: PMC5130343, DOI: 10.1021/acs.orglett.6b02282.Peer-Reviewed Original ResearchConceptsBaeyer-Villiger oxidationPeptide-based catalystsStereoselective Baeyer–Villiger oxidationsCatalytic reactionStereoselective catalystsEffect of additivesSolution conformationCatalystMolecular associationSubstrate-specific interactionsUnique structureSolution structureOxidationStructural analysisAdvantageous featuresSelectivityExperimental observationsPeptidesConformationStructureAdditivesReaction
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