2010
Quantitative Characterization of the Interactions among c-myc Transcriptional Regulators FUSE, FBP, and FIR
Hsiao HH, Nath A, Lin CY, Folta-Stogniew EJ, Rhoades E, Braddock DT. Quantitative Characterization of the Interactions among c-myc Transcriptional Regulators FUSE, FBP, and FIR. Biochemistry 2010, 49: 4620-4634. PMID: 20420426, DOI: 10.1021/bi9021445.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCarrier ProteinsDimerizationDNA HelicasesDNA-Binding ProteinsGuanine Nucleotide Exchange FactorsHumansModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProto-Oncogene Proteins c-mycRepressor ProteinsRho Guanine Nucleotide Exchange FactorsRNA Splicing FactorsRNA-Binding ProteinsSolutionsTrans-ActivatorsConceptsDNA strand preferencesProtein-DNA interactionsC-myc transcriptionPotent oncogenic factorHuman c-mycFBP bindsTranscriptional regulationActive transcriptionNear-physiological conditionsTripartite interactionCell homeostasisInhibitory complexStrand preferenceC-MycOncogenic factorRegulatory systemUnique modeTranscriptionStrand DNABiological experimentsComplex formationLow micromolar rangeDNADifferent conformationsMicromolar range
2009
Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding Site*
Hoopes JT, Liu X, Xu X, Demeler B, Folta-Stogniew E, Li C, Ha Y. Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding Site*. Journal Of Biological Chemistry 2009, 285: 2165-2173. PMID: 19906646, PMCID: PMC2804372, DOI: 10.1074/jbc.m109.018432.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsCrystallography, X-RayHeparinHumansHydrogen-Ion ConcentrationMembrane ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein StabilityProtein Structure, TertiarySequence Homology, Amino AcidSolutionsSucrose
1996
Base-Catalysis of Imino Proton Exchange in DNA: Effects of Catalyst upon DNA Structure and Dynamics
Folta-Stogniew E, Russu I. Base-Catalysis of Imino Proton Exchange in DNA: Effects of Catalyst upon DNA Structure and Dynamics. Biochemistry 1996, 35: 8439-8449. PMID: 8679602, DOI: 10.1021/bi952932z.Peer-Reviewed Original ResearchConceptsDNA dodecamerProton exchangeExchange catalystImino proton exchangeDQF-COSY experimentsImino protonsEffect of catalystNon-exchangeable protonsSelf-complementary DNA dodecamerNucleic acid moleculesNMR spectroscopyDNA structureOverall correlation timeAcid moleculesSolution conformationBase catalysisCatalystProton resonancesWater protonsProton relaxationRate of exchangeNucleic acidsProtonsDodecamerCorrelation time
1994
Sequence dependence of base-pair opening in a DNA dodecamer containing the CACA/GTGT sequence motif.
Folta-Stogniew E, Russu I. Sequence dependence of base-pair opening in a DNA dodecamer containing the CACA/GTGT sequence motif. Biochemistry 1994, 33: 11016-24. PMID: 8086418, DOI: 10.1021/bi00202a022.Peer-Reviewed Original Research