2013
Competitive displacement of cofilin can promote actin filament severing
Elam WA, Kang H, De La Cruz EM. Competitive displacement of cofilin can promote actin filament severing. Biochemical And Biophysical Research Communications 2013, 438: 728-731. PMID: 23911787, PMCID: PMC3785092, DOI: 10.1016/j.bbrc.2013.07.109.Peer-Reviewed Original Research
2010
Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11
Kucera K, Koblansky AA, Saunders LP, Frederick KB, De La Cruz EM, Ghosh S, Modis Y. Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11. Journal Of Molecular Biology 2010, 403: 616-629. PMID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCrystallography, X-RayDNA PrimersImmunity, InnateIn Vitro TechniquesMacrophages, PeritonealMiceMice, KnockoutModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPlasmodium falciparumProfilinsProtein Structure, SecondaryProtozoan ProteinsRabbitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionStatic ElectricityToll-Like ReceptorsToxoplasmaConceptsAcidic loopToll-like receptor 11Β-hairpinLong β-hairpinApicomplexan parasite Cryptosporidium parvumActin-binding surfaceFilament barbed endsStructure-based analysisYeast profilinGondii profilinProfilin mutantsGliding motilityParasite Cryptosporidium parvumT. gondii profilinNucleotide exchangeToxoplasma gondii profilinRabbit actinPlasmodium falciparum resultsActin polymerizationApicomplexan protozoaHomologous loopBarbed endsHost cellsIL-12 secretionInnate immune responsePathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA
Henn A, Cao W, Licciardello N, Heitkamp SE, Hackney DD, De La Cruz EM. Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 4046-4050. PMID: 20160110, PMCID: PMC2840157, DOI: 10.1073/pnas.0913081107.Peer-Reviewed Original Research
2002
Kinetic Characterization of the Weak Binding States of Myosin V †
Yengo CM, De La Cruz EM, Safer D, Ostap EM, Sweeney HL. Kinetic Characterization of the Weak Binding States of Myosin V †. Biochemistry 2002, 41: 8508-8517. PMID: 12081502, DOI: 10.1021/bi015969u.Peer-Reviewed Original ResearchActin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin*
Yengo CM, De La Cruz EM, Chrin LR, Gaffney DP, Berger CL. Actin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin*. Journal Of Biological Chemistry 2002, 277: 24114-24119. PMID: 11959853, DOI: 10.1074/jbc.m111253200.Peer-Reviewed Original Research
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