A non-equilibrium isoelectric focusing method to determine states of phosphorylation of cardiac troponin I: Identification of Ser-23 and Ser-24 as significant sites of phosphorylation by protein kinase C
Author:
Publisher
Elsevier BV
Subject
Cardiology and Cardiovascular Medicine,Molecular Biology
Cited by 61 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Phosphorylation-dependent interactions of myosin-binding protein C and troponin coordinate the myofilament response to protein kinase A;Journal of Biological Chemistry;2023-01
2. HDAC Inhibition Regulates Cardiac Function by Increasing Myofilament Calcium Sensitivity and Decreasing Diastolic Tension;Pharmaceutics;2022-07-21
3. Contractile responses to endothelin-1 are regulated by PKC phosphorylation of cardiac myosin binding protein-C in rat ventricular myocytes;Journal of Molecular and Cellular Cardiology;2018-04
4. The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform;Expert Review of Proteomics;2017-10-16
5. Myofilament Calcium Sensitivity: Mechanistic Insight into TnI Ser-23/24 and Ser-150 Phosphorylation Integration;Frontiers in Physiology;2016-12-15
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