Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+ binding and cause misfolding
Abstract
Key points Mutations in the calmodulin protein (CaM) are associated with arrhythmia syndromes. This study focuses on understanding the structural characteristics of CaM disease mutants and their interactions with the voltage‐gated calcium channel Ca V 1.2. Arrhythmia mutations in CaM can lead to loss of Ca 2+ binding, uncoupling of Ca 2+ binding cooperativity, misfolding of the EF‐hands and altered affinity for the calcium channel. These results...
Paper Details
Title
Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca2+ binding and cause misfolding
Published Date
Feb 18, 2020
Journal
Volume
598
Issue
6
Pages
1169 - 1186
Citation AnalysisPro
You’ll need to upgrade your plan to Pro
Looking to understand the true influence of a researcher’s work across journals & affiliations?
- Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
- Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.
Notes
History