2023
Metformin inhibits digestive proteases and impairs protein digestion in mice
Kelly C, Verdegaal A, Anderson B, Shaw W, Bencivenga-Barry N, Folta-Stogniew E, Goodman A. Metformin inhibits digestive proteases and impairs protein digestion in mice. Journal Of Biological Chemistry 2023, 299: 105363. PMID: 37863262, PMCID: PMC10663847, DOI: 10.1016/j.jbc.2023.105363.Peer-Reviewed Original ResearchConceptsGastrointestinal side effectsSide effectsDrug concentrationsDaily metformin doseFirst-line therapyType 2 diabetesEnteropeptidase activityPrescribed medicationsMetformin doseIntestinal lumenGastrointestinal tissuesMice exhibitMetforminProtein maldigestionHuman duodenumProtein digestionTrypsin activityDigestive enzymesMedicationsDiabetesMaldigestionDuodenumTherapyActivityMiceIron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection
Spiga L, Fansler R, Perera Y, Shealy N, Munneke M, David H, Torres T, Lemoff A, Ran X, Richardson K, Pudlo N, Martens E, Folta-Stogniew E, Yang Z, Skaar E, Byndloss M, Chazin W, Zhu W. Iron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection. Cell Host & Microbe 2023, 31: 1639-1654.e10. PMID: 37776864, PMCID: PMC10599249, DOI: 10.1016/j.chom.2023.08.018.Peer-Reviewed Original ResearchConceptsLipocalin-2Nutritional immunityProtein lipocalin 2Role of commensalIntestinal inflammationInflamed gutSalmonella infectionHost nutritional immunityImmunityGut bacteriaIron metabolismHost-pathogen interactionsGut commensal Bacteroides thetaiotaomicronPathogensBacteroides thetaiotaomicronSalmonellaInflammationInfectionHost sequestration
2022
Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins
Putnam EE, Abellon-Ruiz J, Killinger BJ, Rosnow JJ, Wexler AG, Folta-Stogniew E, Wright AT, van den Berg B, Goodman AL. Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins. MBio 2022, 13: e02845-21. PMID: 35227073, PMCID: PMC8941943, DOI: 10.1128/mbio.02845-21.Peer-Reviewed Original ResearchConceptsComplex microbial communitiesHuman gut commensalTerminal globular domainModel organismsGut microbiomeMicrobial communitiesCompetitive fitnessTransport systemStructural homologsAccessory proteinsNew proteinsAdditional proteinsTransport proteinsGlobular domainUnknown functionMultiple transport systemsSystem lociKey roleGut commensalsProteinDiverse repertoireRelated moleculesMajor groupsFitnessOrganisms
2010
Nucleobindin 1 Is a Calcium-regulated Guanine Nucleotide Dissociation Inhibitor of Gαi1 *
Kapoor N, Gupta R, Menon ST, Folta-Stogniew E, Raleigh DP, Sakmar TP. Nucleobindin 1 Is a Calcium-regulated Guanine Nucleotide Dissociation Inhibitor of Gαi1 *. Journal Of Biological Chemistry 2010, 285: 31647-31660. PMID: 20679342, PMCID: PMC2951237, DOI: 10.1074/jbc.m110.148429.Peer-Reviewed Original ResearchConceptsNucleobindin-1Dissociation inhibitorHeterotrimeric G protein α subunitsGuanine Nucleotide Dissociation InhibitorG protein α subunitsNucleotide Dissociation InhibitorHeterotrimeric G proteinsProtein α subunitsReceptor-mediated signal transduction pathwaysSignal transduction pathwaysGoLoco motifGDI activityProtein traffickingRGS proteinsBiochemical functionsTransduction pathwaysGDP releaseΑ-subunitCalcium-binding proteinsG proteinsConformational changesBiochemical propertiesTissue culture experimentsFluorescence spectroscopy experimentsAdenylyl cyclaseQuantitative 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 AcidSolutionsSucroseAnalysis of the cytoplasmic interaction between polycystin-1 and polycystin-2
Casuscelli J, Schmidt S, DeGray B, Petri ET, Ćelić A, Folta-Stogniew E, Ehrlich BE, Boggon TJ. Analysis of the cytoplasmic interaction between polycystin-1 and polycystin-2. American Journal Of Physiology. Renal Physiology 2009, 297: f1310-f1315. PMID: 19726544, PMCID: PMC2781345, DOI: 10.1152/ajprenal.00412.2009.Peer-Reviewed Original Research
2007
Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition
Crichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De La Cruz EM, Levens D, Lolis E, Braddock D. Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition. The EMBO Journal 2007, 27: 277-289. PMID: 18059478, PMCID: PMC2206118, DOI: 10.1038/sj.emboj.7601936.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCrystallography, X-RayDimerizationDNADNA HelicasesDNA-Binding ProteinsDrosophila ProteinsGene Expression RegulationHumansMagnetic Resonance SpectroscopyMolecular Sequence DataPromoter Regions, GeneticProtein BindingProto-Oncogene Proteins c-mycRepressor ProteinsRNA Splicing FactorsRNA-Binding ProteinsTranscription Factor TFIIHConceptsRRM domainDNA bindingFirst RRM domainSecond RRM domainC-myc transcriptional controlSite-directed mutationsDNA upstreamTranscriptional controlInfluences transcriptionC-Myc inhibitionNucleic acid recognitionPromoter sitesP1 promoterAnalogous mutationCell homeostasisC-MycTFIIHProteinLight scattering revealBinding sitesDNATranscriptionSingle strandsMutationsSize exclusion chromatographyThe structural basis of cyclic diguanylate signal transduction by PilZ domains
Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta‐Stogniew E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt JF. The structural basis of cyclic diguanylate signal transduction by PilZ domains. The EMBO Journal 2007, 26: 5153-5166. PMID: 18034161, PMCID: PMC2140105, DOI: 10.1038/sj.emboj.7601918.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBinding SitesCrystallography, X-RayCyclic GMPHumansMiceModels, MolecularMolecular ConformationMolecular Sequence DataPhylogenyProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentSequence Homology, Amino AcidSignal TransductionVibrio choleraeConceptsPilZ domain-containing proteinsPilZ domainDomain-containing proteinsN-terminal domainConformational switchSecond messenger cyclic diguanylateBeta-barrel foldN-terminal loopEvolutionary diversificationCyclic diguanylateSignal transductionBioinformatics analysisStructural basisInteraction surfaceSessile growthEffector pathwaysVibrio choleraeProteinV. choleraeGMPCholeraeDomainClose appositionDiguanylateEubacteria
1999
Rapid Exchange of A:T Base Pairs Is Essential for Recognition of DNA Homology by Human Rad51 Recombination Protein
Gupta R, Folta-Stogniew E, O'Malley S, Takahashi M, Radding C. Rapid Exchange of A:T Base Pairs Is Essential for Recognition of DNA Homology by Human Rad51 Recombination Protein. Molecular Cell 1999, 4: 705-714. PMID: 10619018, DOI: 10.1016/s1097-2765(00)80381-0.Peer-Reviewed Original ResearchConceptsRecognition of homologyBase pairsRad51 recombination proteinT base pairsRecombination proteinsHuman Rad51Genetic exchangeFluorescence resonance energy transferUbiquitous familyMechanism of recognitionDNA repairStrand exchangeDNA homologyBase substitutionsHomologyResonance energy transferDuplex DNAHelix destabilizationCritical roleBase mismatchesProteinSingle strandsRAD51Rapid exchangeKinetic analysisHuman Rad51 Protein Can Form Homologous Joints in the Absence of Net Strand Exchange*
Gupta R, Folta-Stogniew E, Radding C. Human Rad51 Protein Can Form Homologous Joints in the Absence of Net Strand Exchange*. Journal Of Biological Chemistry 1999, 274: 1248-1256. PMID: 9880493, DOI: 10.1074/jbc.274.3.1248.Peer-Reviewed Original ResearchConceptsStrand exchangeRecA proteinEscherichia coli RecA proteinColi RecA proteinHuman Rad51 proteinDNA strand exchange reactionStrand exchange reactionEukaryotic homologsHsRad51 proteinRad51 proteinHomologous pairingGC contentCentral enzymeHeteroduplex DNABiological roleHsRad51Oligonucleotide substratesRich DNAGC compositionHuman DNAProteinLinear duplexHomologous jointsDNAGC pairs