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 enzymesMedicationsDiabetesMaldigestionDuodenumTherapyActivityMice
2022
Tuning protein half-life in mouse using sequence-defined biopolymers functionalized with lipids
Vanderschuren K, Arranz-Gibert P, Khang M, Hadar D, Gaudin A, Yang F, Folta-Stogniew E, Saltzman WM, Amiram M, Isaacs FJ. Tuning protein half-life in mouse using sequence-defined biopolymers functionalized with lipids. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2103099119. PMID: 35046019, PMCID: PMC8794819, DOI: 10.1073/pnas.2103099119.Peer-Reviewed Original ResearchConceptsSequence-defined biopolymersProtein-based drugsModel fusion proteinProof of conceptSynthetic biopolymersBroad applicationsMaterials scienceProgrammable approachLow toxicityHigh specificityPeptide therapeuticsBiopolymersLimited side effectsConjugation sitesBlood serumBiotechnologyTechnical foundationFusion proteinMouse serumBiophysical propertiesAzidophenylalanineApplicationsPast decadeTherapeutics
2016
Homodimerization enhances both sensitivity and dynamic range of the ligand‐binding domain of type 1 metabotropic glutamate receptor
Serebryany E, Folta‐Stogniew E, Liu J, Yan EC. Homodimerization enhances both sensitivity and dynamic range of the ligand‐binding domain of type 1 metabotropic glutamate receptor. FEBS Letters 2016, 590: 4308-4317. PMID: 27800613, PMCID: PMC5154874, DOI: 10.1002/1873-3468.12473.Peer-Reviewed Original Research
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 cyclase
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