eNOS Monoclonal Antibody (9D10) - Citations

eNOS Monoclonal Antibody (9D10) - Citations

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Abstract
Compensatory phosphorylation and protein-protein interactions revealed by loss of function and gain of function mutants of multiple serine phosphorylation sites in endothelial nitric-oxide synthase.
AuthorsBauer PM, Fulton D, Boo YC, Sorescu GP, Kemp BE, Jo H, Sessa WC,
JournalJ Biol Chem
PubMed ID12591925
'We examined the influence of individual serine phosphorylation sites in endothelial nitric-oxide synthase (eNOS) on basal and stimulated NO release, cooperative phosphorylation, and co-association with hsp90 and Akt. Mutation of the serine phosphorylation sites 116, 617, and 1179 to alanines affected the phospho-state of at least one other site, demonstrating ... More
Hypoxia-induced acute lung injury in murine models of sickle cell disease.
AuthorsPritchard KA, Ou J, Ou Z, Shi Y, Franciosi JP, Signorino P, Kaul S, Ackland-Berglund C, Witte K, Holzhauer S, Mohandas N, Guice KS, Oldham KT, Hillery CA,
JournalAm J Physiol Lung Cell Mol Physiol
PubMed ID12972407
Vaso-occlusive events are the major source of morbidity and mortality in sickle cell disease (SCD); however, the pathogenic mechanisms driving these events remain unclear. Using hypoxia to induce pulmonary injury, we investigated mechanisms by which sickle hemoglobin increases susceptibility to lung injury in a murine model of SCD, where mice ... More
Localization of endothelial nitric-oxide synthase phosphorylated on serine 1179 and nitric oxide in Golgi and plasma membrane defines the existence of two pools of active enzyme.
Authors Fulton David; Fontana Jason; Sowa Grzegorz; Gratton Jean-Philippe; Lin Michelle; Li Kai-Xun; Michell Belinda; Kemp Bruce E; Rodman David; Sessa William C;
JournalJ Biol Chem
PubMed ID11729179
The subcellular localization of endothelial nitric-oxide synthase (eNOS) is critical for optimal coupling of extracellular stimulation to nitric oxide production. Because eNOS is activated by Akt-dependent phosphorylation to produce nitric oxide (NO), we determined the subcellular distribution of eNOS phosphorylated on serine 1179 using a variety of methodologies. Based on ... More