|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|408699||679041||2006||4 صفحه PDF||سفارش دهید||دانلود رایگان|
We have developed a computational model of the regulation of αα- and ββ-CaMKII activity, in order to examine (i) the importance of neighbour subunit interactions and (ii) the effect the higher CaMCa4 affinity of ββ-CaMKII has on the holoenzyme activity in different configurations with the same α:βα:β ratio. The model consists of a deterministic biochemical network coupled to stochastic activation of CaMKII. The results suggest that CaMKII holoenzyme activity is non-linear and dependent on the holoenzyme configuration of isoforms. This is especially pronounced in situations with a high-dephosphorylation rate of CaMKII.
Journal: Neurocomputing - Volume 69, Issues 10–12, June 2006, Pages 1010–1013