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Details on Person When Ca+2 is high, calcium is bound to calmodulin through th...
| Class:Id | Summation:74027 |
|---|---|
| _displayName | When Ca+2 is high, calcium is bound to calmodulin through th... |
| _timestamp | 2003-10-06 10:40:22 |
| created | [InstanceEdit:74470] Carleton, KL, 2003-07-22 11:02:31 |
| modified | [InstanceEdit:74163] Joshi-Tope, G, 2003-07-15 16:33:00 [InstanceEdit:74429] Schmidt, EE, 2003-07-22 11:02:16 [InstanceEdit:74483] Schmidt, EE, 2003-07-24 04:44:36 [InstanceEdit:74823] Schmidt, EE, 2003-08-20 08:52:29 [InstanceEdit:74921] Carleton, KL, 2003-07-30 11:40:37 [InstanceEdit:74920] Schmidt, EE, 2003-07-30 11:40:34 [InstanceEdit:76256] Schmidt, EE, 2003-10-06 06:37:17 |
| text | When Ca+2 is high, calcium is bound to calmodulin through the EF hand binding domains . This changes the conformation of calmodulin such that it can bind to the channel through the beta subunit (Hsu and Molday 1993; Chen et al. 1994). This decreases affinity of channel for cGMP. There are two calcium binding sites per calmodulin (Bauer 1997). The channel can also be phosphorylated, but it is thought that this does not modify channel conductivity (Warren and Molday 2003). Feedback regulation: When the channels close, the Ca level drops. This causes calcium to dissociate from calmodulin and the calmodulin to dissociate from the channel. This increases the binding efficiency of the channel for cGMP. |
| (summation) | [Pathway:74451] Regulation of calcium influx channel activity [Bos taurus] |
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