2013
Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦
Albright RA, Ornstein DL, Cao W, Chang WC, Robert D, Tehan M, Hoyer D, Liu L, Stabach P, Yang G, De La Cruz EM, Braddock DT. Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦. Journal Of Biological Chemistry 2013, 289: 3294-3306. PMID: 24338010, PMCID: PMC3916532, DOI: 10.1074/jbc.m113.505867.Peer-Reviewed Original ResearchConceptsExtracellular membrane proteinsMembrane proteinsSubstrate specificityMolecular basisHigh-resolution crystal structuresResolution crystal structureComparative structural analysisATP hydrolysisNPP1Brain vascular endotheliumCorresponding regionTerminal phosphateLow nanomolar concentrationsPurinergic signalsPlatelet aggregationProteinATPEnzymeNanomolar concentrationsVascular endotheliumPhosphodiesterases 4Ap3AMetabolismSurface of chondrocytesTissue mineralizationQuantitative full time course analysis of nonlinear enzyme cycling kinetics
Cao W, De La Cruz EM. Quantitative full time course analysis of nonlinear enzyme cycling kinetics. Scientific Reports 2013, 3: 2658. PMID: 24029878, PMCID: PMC3772379, DOI: 10.1038/srep02658.Peer-Reviewed Original ResearchConceptsKinetic time coursesProduct inhibitionSteady-state enzyme kinetic parametersReaction schemeEnzymology approachReaction productsReversible bindingEnzyme kinetic parametersProduct releasePractical general methodKinetic parametersEnzyme inhibitionGeneral methodProductsEnzyme systemEnzymatic parameters
2011
Kinetic Analysis of Autotaxin Reveals Substrate-specific Catalytic Pathways and a Mechanism for Lysophosphatidic Acid Distribution*
Saunders LP, Cao W, Chang WC, Albright RA, Braddock DT, De La Cruz EM. Kinetic Analysis of Autotaxin Reveals Substrate-specific Catalytic Pathways and a Mechanism for Lysophosphatidic Acid Distribution*. Journal Of Biological Chemistry 2011, 286: 30130-30141. PMID: 21719699, PMCID: PMC3191052, DOI: 10.1074/jbc.m111.246884.Peer-Reviewed Original ResearchConceptsLysophosphatidic acidSecreted lysophospholipase DThr-210Synthase cycleVivo substrateSubstrate bindingQuantitative physiological modelsSignaling cascadesPosition 210LPA signalingCatalytic threonineFluorescent lipidLysophospholipase DCancer metastasisSlow catalysisCatalytic pathwayDiazol-4PathwayAutotaxinProduct releaseBindsLPA synthesisFS-3Acid distributionBioactive form
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