2011
Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate
Wu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 18672-18677. PMID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportCrystallography, X-RayDeath Domain Receptor Signaling Adaptor ProteinsGuanineGuanine Nucleotide Exchange FactorsHumansKineticsNucleotidesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsConceptsGuanine nucleotide exchange factorsDENN domain proteinsMembrane traffic pathwaysNucleotide exchange factorsGDP-bound formGTP-bound formSwitch regions IHigher eukaryotesRab GTPasesGEF familyEukaryotic cellsTraffic pathwaysExchange factorSwitch INucleotide bindingKey regulatorConformational changesFirst structureNovel insightsRab35ProteinDENND1BEukaryotesRegion IGTPasesCofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries
Suarez C, Roland J, Boujemaa-Paterski R, Kang H, McCullough BR, Reymann AC, Guérin C, Martiel JL, De La Cruz EM, Blanchoin L. Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries. Current Biology 2011, 21: 862-868. PMID: 21530260, PMCID: PMC3100394, DOI: 10.1016/j.cub.2011.03.064.Peer-Reviewed Original Research
2005
Thymosin β4 Induces a Conformational Change in Actin Monomers
Dedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG. Thymosin β4 Induces a Conformational Change in Actin Monomers. Biophysical Journal 2005, 90: 985-992. PMID: 16272441, PMCID: PMC1367123, DOI: 10.1529/biophysj.105.063081.Peer-Reviewed Original ResearchAcrylamideActinsAdenosine TriphosphateAnimalsCalorimetry, Differential ScanningCysteineElectrophoresis, Polyacrylamide GelFluorescence Resonance Energy TransferHot TemperatureKineticsLysineModels, MolecularMolecular ConformationNucleotidesProtein BindingProtein ConformationProtein Structure, TertiaryPurinesRabbitsSolventsSpectrometry, FluorescenceTemperatureThymosin
2004
Mechanism of Nucleotide Binding to Actomyosin VI EVIDENCE FOR ALLOSTERIC HEAD-HEAD COMMUNICATION*
Robblee JP, Olivares AO, De La Cruz EM. Mechanism of Nucleotide Binding to Actomyosin VI EVIDENCE FOR ALLOSTERIC HEAD-HEAD COMMUNICATION*. Journal Of Biological Chemistry 2004, 279: 38608-38617. PMID: 15247304, DOI: 10.1074/jbc.m403504200.Peer-Reviewed Original ResearchActinsActomyosinAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAllosteric SiteAnimalsCell LineDose-Response Relationship, DrugHydrogen-Ion ConcentrationInsectaKineticsModels, BiologicalModels, ChemicalModels, StatisticalMuscle, SkeletalMyosin Heavy ChainsNucleotidesProtein BindingPyrenesRabbitsTime Factors