2008
Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding
Au JK, Olivares AO, Henn A, Cao W, Safer D, De La Cruz EM. Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding. Biochemistry 2008, 47: 4181-4188. PMID: 18327913, PMCID: PMC2587058, DOI: 10.1021/bi701769u.Peer-Reviewed Original ResearchConceptsActin Binding AffinityActin bindingProline residuesHydrophobic residuesAlanine residuesLysine residuesPro27Thymosin beta4Actin monomersPro29MutagenesisHydrophobic contactsLeu28Slow association rateResiduesLys19Thymosin β4Ile34Tbeta4Lys18Binding affinitiesTwo-step mechanismAssociation ratePro4Cis-trans isomerization
2007
Contributions from All Over
AU JK, DE LA CRUZ EM, SAFER D. Contributions from All Over. Annals Of The New York Academy Of Sciences 2007, 1112: 38-44. PMID: 17468230, DOI: 10.1196/annals.1415.015.Peer-Reviewed Original ResearchConceptsProline residuesActin bindingWild-type complexHydrophobic contactsSite-directed mutagenesisStrong actin bindingHydrophobic residuesAlanine residuesCysteine 374Slow association rateRate of associationResiduesMutantsComplex variesTbeta4Association rateSulfo-1BindingCis-trans isomerizationKinetic basisComplexesPro27Pro29Lys19Mutagenesis
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
2001
Structural biology. Actin' up.
De La Cruz E, Pollard T. Structural biology. Actin' up. Science 2001, 293: 616-8. PMID: 11474090, DOI: 10.1126/science.1063558.Peer-Reviewed Original ResearchActin Depolymerizing FactorsActinsAdenosine DiphosphateAdenosine TriphosphateBiopolymersContractile ProteinsCrystallography, X-RayHydrolysisMicrofilament ProteinsPhosphatesProfilinsProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsRhodaminesThymosin
2000
Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers
De La Cruz E, Ostap E, Brundage R, Reddy K, Sweeney H, Safer D. Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers. Biophysical Journal 2000, 78: 2516-2527. PMID: 10777749, PMCID: PMC1300842, DOI: 10.1016/s0006-3495(00)76797-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBiophysical PhenomenaBiophysicsCircular DichroismCross-Linking ReagentsFluorescent DyesHumansIn Vitro TechniquesKineticsMacromolecular SubstancesModels, MolecularMuscle, SkeletalMutagenesis, Site-DirectedNaphthalenesulfonatesOsmotic PressureProtein BindingProtein ConformationRabbitsRecombinant ProteinsThermodynamicsThymosinTritiumViscosityConceptsActin monomersActin monomer poolMgATP-actinMetazoan cellsNucleotide exchangeC-terminusSubdomain 2Conformational changesMonomer poolN-iodoacetyl-N'Cleavage siteActinThymosin β4Rate of dissociationAmide protonsSulfo-1Unique abilityBindingStructural dynamicsConformationTerminusNucleotidesProteolysisDifferent stabilitiesDegrees C