2012
Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness
Kang H, Bradley MJ, McCullough BR, Pierre A, Grintsevich EE, Reisler E, De La Cruz EM. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16923-16927. PMID: 23027950, PMCID: PMC3479481, DOI: 10.1073/pnas.1211078109.Peer-Reviewed Original ResearchConceptsCation-binding sitesActin assemblyEukaryotic biologyLong-pitch helixActin functionSalt-dependent effectsCell divisionCell motilityActin polymerizationFilament assemblyAdjacent subunitsIntracellular transportActin filamentsPhysiological salt concentrationsActin monomersCellular shapeNonspecific ionic strength effectsDiscrete sites
2007
Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates
Zhang H, Cao W, Zakharova E, Konigsberg W, De La Cruz EM. Fluorescence of 2-aminopurine reveals rapid conformational changes in the RB69 DNA polymerase-primer/template complexes upon binding and incorporation of matched deoxynucleoside triphosphates. Nucleic Acids Research 2007, 35: 6052-6062. PMID: 17766250, PMCID: PMC2094073, DOI: 10.1093/nar/gkm587.Peer-Reviewed Original ResearchConceptsHydroxyl groupsNucleotidyl transfer reactionMinimal kinetic schemeConformational changesDetectable fluorescence changeChemical quenchTransfer reactionsDependent fluorescence enhancementFluorescence enhancementFluorescence quenchingFluorescent probeRapid conformational changesTemplate complexN-positionRate constantsFluorescence changesRapid fluorescenceTernary complexKinetic schemeComplexesTemplating baseDependent conformational changesDp/TTemplateFluorescence
1999
The kinetic mechanism of myosin V
De La Cruz E, Wells A, Rosenfeld S, Ostap E, Sweeney H. The kinetic mechanism of myosin V. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 13726-13731. PMID: 10570140, PMCID: PMC24132, DOI: 10.1073/pnas.96.24.13726.Peer-Reviewed Original Research
1998
Regulation of G protein-coupled Receptor Kinase 5 (GRK5) by Actin*
Freeman J, De La Cruz E, Pollard T, Lefkowitz R, Pitcher J. Regulation of G protein-coupled Receptor Kinase 5 (GRK5) by Actin*. Journal Of Biological Chemistry 1998, 273: 20653-20657. PMID: 9685424, DOI: 10.1074/jbc.273.32.20653.Peer-Reviewed Original ResearchConceptsG protein-coupled receptor kinase 5G protein-coupled receptorsG protein-coupled receptor kinasesAgonist-occupied G protein-coupled receptorsAmino terminusPhosphorylation of GPCRsSoluble substratesMembrane-bound substratesProtein-coupled receptor kinasesMembrane-bound G protein-coupled receptorReceptor kinase 5Receptor kinasePresence of actinSubstrate specificityKinase activityActin filamentsActin bindsKinase 5Actin monomersAmino acidsPhosphorylationActinCalmodulinTerminusKinase