2011
Molecular Structure and Biological Activity of NPP-4, An Endothelial Cell Surface Pyrophosphatase/ Phosphodiesterase That Stimulates Platelet Aggregation and Secretion Via Liberation of ADP Upon Hydrolysis of Diadenosine Triphosphate
Ornstein D, Albright R, Chang W, Robert D, Cao W, De La Cruz E, Braddock D. Molecular Structure and Biological Activity of NPP-4, An Endothelial Cell Surface Pyrophosphatase/ Phosphodiesterase That Stimulates Platelet Aggregation and Secretion Via Liberation of ADP Upon Hydrolysis of Diadenosine Triphosphate. Blood 2011, 118: 701. DOI: 10.1182/blood.v118.21.701.701.Peer-Reviewed Original ResearchHigh-resolution structuresActive site threonineDense granule releaseDiadenosine triphosphateExtracellular spaceNanomolar concentrationsEnzyme familyPlatelet dense granulesMolecular foundationMolecular basisExtracellular enzymesStructural basisPhosphodiesterase enzyme familyGranule releaseEnzymatic mechanismCell surfaceRapid disaggregationEndothelial cell surfaceDense granulesPlatelet aggregationAp3AEnzymatic productBiological activityConcentration-dependent fashionADP
2008
The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes
Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell 2008, 133: 1202-1213. PMID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.Peer-Reviewed Original Research