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
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
2008
Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State
Das S, Stivison E, Folta-Stogniew E, Oliver D. Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State. Journal Of Bacteriology 2008, 190: 7302-7307. PMID: 18723626, PMCID: PMC2580686, DOI: 10.1128/jb.00593-08.Peer-Reviewed Original ResearchConceptsWild-type SecAProtein-conducting channelCell growthAmino-terminal regionSecA dimerSecA functionsProtein translocationSecA expressionMembrane associationMutant proteinsCell fractionationATPase specific activityCorresponding proteinProtein cargoCarboxyl terminusAmino terminusVivo functionSecADimerization defectFunctional stateMutantsBiochemical studiesResidue resultsProteinChemical cross
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 analysis