Title : Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase.

Pub. Date : 2003 Jan

PMID : 12482742






3 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Two amino acids seem to be particularly important in regulating eNOS activity and these are a serine residue in the reductase domain (Ser(1177)) and a threonine residue (Thr(495)) located within the CaM-binding domain. Threonine nitric oxide synthase 3 Homo sapiens
2 Two amino acids seem to be particularly important in regulating eNOS activity and these are a serine residue in the reductase domain (Ser(1177)) and a threonine residue (Thr(495)) located within the CaM-binding domain. Threonine nitric oxide synthase 3 Homo sapiens
3 Simultaneous alterations in the phosphorylation of Ser(1177) and Thr(495) in response to a variety of stimuli are regulated by a number of kinases and phosphatases that continuously associate with and dissociate from the eNOS signaling complex. Threonine nitric oxide synthase 3 Homo sapiens