2004
NMR-Driven Discovery of Benzoylanthranilic Acid Inhibitors of Far Upstream Element Binding Protein Binding to the Human Oncogene c-myc Promoter
Huth JR, Yu L, Collins I, Mack J, Mendoza R, Isaac B, Braddock DT, Muchmore SW, Comess KM, Fesik SW, Clore GM, Levens D, Hajduk PJ. NMR-Driven Discovery of Benzoylanthranilic Acid Inhibitors of Far Upstream Element Binding Protein Binding to the Human Oncogene c-myc Promoter. Journal Of Medicinal Chemistry 2004, 47: 4851-4857. PMID: 15369388, DOI: 10.1021/jm0497803.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCombinatorial Chemistry TechniquesDNA HelicasesDNA, Single-StrandedDNA-Binding ProteinsDrug DesignGenes, mycHumansInhibitory Concentration 50LigandsMagnetic Resonance SpectroscopyModels, MolecularPromoter Regions, GeneticProtein ConformationProtein Structure, TertiaryProto-Oncogene MasRepetitive Sequences, Amino AcidRNA-Binding ProteinsStructure-Activity RelationshipConceptsUpstream element binding proteinC-myc expressionElement-binding proteinC-Myc pathwayTranscription factorsBinding proteinHost of proteinsRelated transcription factorsAberrant gene expressionC-myc promoterGel shift analysisSlow cell growthC-myc regulationProto-oncogene c-mycFBP bindsKH domainsFBP functionInhibits DNADevelopment of therapeuticsOwn expressionGene expressionHydrophobic pocketC-MycBinding pocketsCell growth
1998
Structure−Function Relationships in Side Chain Lactam Cross-Linked Peptide Models of a Conserved N-Terminal Domain of Apolipoprotein E †
Benzinger T, Braddock D, Dominguez S, Burkoth T, Miller-Auer H, Subramanian R, Fless G, Jones D, Lynn D, Meredith S. Structure−Function Relationships in Side Chain Lactam Cross-Linked Peptide Models of a Conserved N-Terminal Domain of Apolipoprotein E †. Biochemistry 1998, 37: 13222-13229. PMID: 9748329, DOI: 10.1021/bi980482f.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApolipoproteins ECell LineCircular DichroismConserved SequenceEmbryo, MammalianFibroblastsIodine RadioisotopesLactamsMiceModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryReceptors, LDLStructure-Activity RelationshipConceptsPeptide IVPeptide modelsConformational switchSide chain lactamLipid surfaceSide chainsBioactive peptidesStructural orderMultiple conformationsBiological activityStructure-function relationshipsLactamsAlpha-helixStrategic modificationsSecondary structureHelical segmentsPeptide IIIConformationAlpha-helical segmentsShort alpha helixCOOHHelixAntipodeStructureSolution