Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket
Calmodulin (CaM) modulates the activity of several proteins that play a key role in excitation-contraction coupling (ECC). In cardiac muscle, the major binding partner of CaM is the type-2 ryanodine receptor (RyR2) and altered CaM binding contributes to defects in sarcoplasmic reticulum (SR) calcium...
محفوظ في:
| المؤلف الرئيسي: | Angelos, Thanassoulas (author) |
|---|---|
| مؤلفون آخرون: | Vassilakopoulou, Vyronia (author), Calver, Brian L. (author), Buntwal, Luke (author), Smith, Adrian (author), Lai, Christopher (author), Kontogianni, Iris (author), Livaniou, Evangelia (author), Nounesis, George (author), Lai, F. Anthony (author), Nomikos, Michail (author) |
| التنسيق: | article |
| منشور في: |
2023
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| الموضوعات: | |
| الوصول للمادة أونلاين: | http://dx.doi.org/10.1016/j.bbagen.2023.130313 https://www.sciencedirect.com/science/article/pii/S0304416523000119 http://hdl.handle.net/10576/39329 |
| الوسوم: |
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مواد مشابهة
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Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket
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