2012
NPP4 is a procoagulant enzyme on the surface of vascular endothelium
Albright RA, Chang WC, Robert D, Ornstein DL, Cao W, Liu L, Redick ME, Young JI, De La Cruz EM, Braddock DT. NPP4 is a procoagulant enzyme on the surface of vascular endothelium. Blood 2012, 120: 4432-4440. PMID: 22995898, PMCID: PMC4017314, DOI: 10.1182/blood-2012-04-425215.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine DiphosphateAdultAnimalsBlood CoagulationCoagulantsCyclic Nucleotide Phosphodiesterases, Type 4Dinucleoside PhosphatesEndothelium, VascularFluorescent Antibody TechniqueHumansHydrolysisIn Vitro TechniquesInsectaPhosphoric Diester HydrolasesPlatelet AggregationPyrophosphatasesTissue DistributionConceptsPlatelet dense granule componentsNucleotide pyrophosphatase/phosphodiesteraseRelease of ADPUncharacterized enzymesPyrophosphatase/phosphodiesteraseGranule componentsEnzymatic basisRapid disaggregationDense granule releasePlatelet aggregationExtracellular spaceAp3AConcentration-dependent mannerEnzymeGranule releaseVascular endotheliumADPProcoagulant enzymeADP receptorActivationAggregationMutants
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