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"

No evidence text available

No evidence text available

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."

No evidence text available

No evidence text available

No evidence text available