IndraLab

Statements


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sparser
"We did not observe any interaction between eNOS and CAV1, despite showing a specific and calcium-dependent interaction of eNOS and CALM1 using the same cf expression system."

No evidence text available

"Electrons flow from the C-terminal reductase domain of one NOS monomer to the N-terminal oxygenase domain of the other NOS monomer (Siddhanta et al., 1998). The primary mode of enzyme activation is the binding of calcium-bound calmodulin to the N-terminal CaM-binding domain. This facilitates a structure change and the flow of electrons from NADPH through the flavins to the oxygenase domain of the other eNOS monomer"

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sparser
"Additionally, CR can act on the genes of the upstream pathway, such as IL1B and TNF, which are proinflammatory mediators [ xref , xref ], while ATR can act on downstream genes, such as CALM1 and NOS3, which are associated with learning and memory and anti-inflammatory processes."