2016
d-3-Deoxy-dioctanoylphosphatidylinositol induces cytotoxicity in human MCF-7 breast cancer cells via a mechanism that involves downregulation of the D-type cyclin-retinoblastoma pathway
Gradziel CS, Jordan PA, Jewel D, Dufort FJ, Miller SJ, Chiles TC, Roberts MF. d-3-Deoxy-dioctanoylphosphatidylinositol induces cytotoxicity in human MCF-7 breast cancer cells via a mechanism that involves downregulation of the D-type cyclin-retinoblastoma pathway. Biochimica Et Biophysica Acta 2016, 1861: 1808-1815. PMID: 27600289, PMCID: PMC5115159, DOI: 10.1016/j.bbalip.2016.09.001.Peer-Reviewed Original ResearchMeSH KeywordsBreast NeoplasmsCell DeathCyclin D1Down-RegulationFemaleHumansMagnetic Resonance SpectroscopyMCF-7 CellsP38 Mitogen-Activated Protein KinasesPhosphatidic AcidsPhosphatidylinositolsPhosphorylationPleckstrin Homology DomainsProto-Oncogene Proteins c-aktRetinoblastoma ProteinRNA, Small InterferingSignal TransductionConceptsMCF-7 breast cancer cellsBreast cancer cellsAkt PH domainPhosphatidylinositol analoguesD-type cyclinsCancer cellsCyclin D1Cleavage of PARPPH domainProtein phosphorylationMembrane translocationActive AktHuman MCF-7 breast cancer cellsGrowth arrestCaspase-9Endogenous levelsCyclin D3Cell proliferationAlkylphospholipid perifosineMCF-7 cell proliferationAnti-proliferative activityAktPathwayDownregulation
2015
Site-Selective Reactions with Peptide-Based Catalysts
Giuliano MW, Miller SJ. Site-Selective Reactions with Peptide-Based Catalysts. 2015, 372: 157-201. PMID: 26307403, DOI: 10.1007/128_2015_653.Peer-Reviewed Original ResearchMeSH KeywordsCatalysisErythromycinGlycopeptidesMacrolidesOxidation-ReductionPeptidesPhosphorylationPyrones
2014
X‑ray Crystal Structure of Teicoplanin A2‑2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy
Han S, Le BV, Hajare HS, Baxter RH, Miller SJ. X‑ray Crystal Structure of Teicoplanin A2‑2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy. The Journal Of Organic Chemistry 2014, 79: 8550-8556. PMID: 25147913, PMCID: PMC4168787, DOI: 10.1021/jo501625f.Peer-Reviewed Original ResearchConceptsX-ray crystal structureTeicoplanin A2-2Crystal structurePeptide-based catalystsProtein ligation (IPL) techniqueCatalyst moietyPeptide catalystsComplex crystal structureMolecular arrangementN-methylimidazoleNucleophilic nitrogenObserved selectivitySugar ringCatalystPeptide sequencesT4 lysozymeDerivativesN-acetylglucosaminePhosphorylation reactionMoietyStructureSelectivityProtein strategyA2-2Complexes
2013
Asymmetric Catalysis at a Distance: Catalytic, Site-Selective Phosphorylation of Teicoplanin
Han S, Miller SJ. Asymmetric Catalysis at a Distance: Catalytic, Site-Selective Phosphorylation of Teicoplanin. Journal Of The American Chemical Society 2013, 135: 12414-12421. PMID: 23924210, PMCID: PMC3790668, DOI: 10.1021/ja406067v.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosamineBinding SitesBiocatalysisMannoseModels, MolecularPeptidomimeticsPhosphorylationProtein ConformationTeicoplaninConceptsTeicoplanin A2-2Site-selective phosphorylationPeptide-based catalystsSmall-molecule catalystsX-ray crystal structureCatalyst-substrate interactionsSet of catalystsDistinct hydroxyl groupsAsymmetric catalysisCatalytic controlStructural assignmentCatalystTeicoplanin derivativesNatural productsGlycopeptide structuresHydroxyl groupsCrystal structureMass spectrometryMechanistic studiesBiological activityCatalytic moietyAdditional functionalityCatalysisMoietySpectroscopy