Gene interactions and pathways from curated databases and text-mining

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HSP90AB1 — NOS3

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Brouet et al., J Biol Chem 2001 : Association with heat shock protein 90 (hsp90) and phosphorylation by Akt were recently shown to separately activate eNOS upon VEGF stimulation in endothelial cells ... Further experiments in transfected COS cells expressing either wild-type or S1177A mutant eNOS led us to identify the serine 1177 as the critical residue for the hsp90 dependent Akt mediated activation of eNOS
Billecke et al., J Biol Chem 2002 : hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase : geldanamycin mediated oxidant generation is unrelated to any action of hsp90
Bucci et al., Br J Pharmacol 2002 : 3. Geldanamycin ( 10 microM ), a specific inhibitor of heat shock protein 90 (hsp90) and N ( omega ) -nitro-L-arginine-methyl ester ( L-NAME, 100 microM ), a nitric oxide synthase inhibitor , significantly inhibited E2-induced vasorelaxation ... 6. In conclusion, we demonstrate that E2 interaction with its receptor is followed by a vasorelaxant effect in rat aortic rings mediated by eNOS activation through both hsp90 and akt/pkb dependent mechanisms
Lin et al., J Biol Chem 2003 : T497A and T497A/S1179D eNOS generated 2-3 times more superoxide anion than WT eNOS, and both basal and stimulated interactions of T497A/S1179D eNOS with hsp90 were reduced in co-immunoprecipitation experiments
Huang et al., Curr Hypertens Rep 2003 : Regulation of endothelial NO synthase (eNOS) activity by fatty acid modifica-tions, intracellular localization, interactions with heat shock protein 90 (hsp90) and caveolin, substrate and cofactor dependence, and phosphorylation might all affect the level of bioavailable NO. A hypothesis is proposed that the final common pathway of diverse causes of endothelial dysfunction involves abnormalities in eNOS phosphorylation at Ser 1179 and other key phosphorylation sites
Billecke et al., J Biol Chem 2004 : The role of hsp90 in heme dependent activation of apo-neuronal nitric-oxide synthase