IndraLab

Statements


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sparser
"Previous research demonstrated that Ca 2+ and calmodulin regulate the interaction between Cav3.2 and calcineurin."

sparser
"The binding of Cav3.2 to calcineurin results in a reduction of the enzyme’s phosphatase activity and subsequently decrease the current density of Cav3.2, which has been identified as a key regulator of sperm acrosome reaction ( xref ; xref ; xref )."

sparser
"It was found that Calmodulin and 0.1 mM Ca 2+ enhanced the physical interaction between Cav3.2 and calcineurin, but 2 mM EGTA entirely eliminated it, suggesting that the interaction between Cav3.2 and calcineurin is Ca 2+ /calmodulin dependent."

reach
"The interaction between CaN and Cav3.2 was discovered via anti-tag immunoprecipitation."

reach
"It was found that Calmodulin and 0.1 mM Ca enhanced the physical interaction between Cav3.2 and calcineurin, but 2 mM EGTA entirely eliminated it, suggesting that the interaction between Cav3.2 and calcineurin is Ca /calmodulin dependent."

reach
"Calcineurin binds to Cav3.2 [17] and also dephosphorylates Cav3.2."

reach
"In earlier investigations, we observed a peak binding of calcineurin with Cav3.2 at a calcium concentration of 30 μM, along with 20% binding at a calcium concentration of 1 μM [17]."

reach
"This interaction between Cav3.2 and calcineurin is dependent on calmodulin and calcium concentration."

reach
"While it is established that calcineurin interacts with and modulates Cav3.2, the specific dephosphorylation of Cav3.2 by calcineurin has remained unclear."