Cardiac myosin-binding protein C (MYBPC3) in cardiac pathophysiology
More than 350 individual MYPBC3 mutations have been identified in patients with inherited
hypertrophic cardiomyopathy (HCM), thus representing 40–50% of all HCM mutations …
hypertrophic cardiomyopathy (HCM), thus representing 40–50% of all HCM mutations …
Phosphorylation and function of cardiac myosin binding protein-C in health and disease
During the past 5 years there has been an increasing body of literature describing the roles
cardiac myosin binding protein C (cMyBP-C) phosphorylation play in regulating cardiac …
cardiac myosin binding protein C (cMyBP-C) phosphorylation play in regulating cardiac …
Myosin sequestration regulates sarcomere function, cardiomyocyte energetics, and metabolism, informing the pathogenesis of hypertrophic cardiomyopathy
Background: Hypertrophic cardiomyopathy (HCM) is caused by pathogenic variants in
sarcomere protein genes that evoke hypercontractility, poor relaxation, and increased …
sarcomere protein genes that evoke hypercontractility, poor relaxation, and increased …
Cardiac myosin-binding protein C mutations and hypertrophic cardiomyopathy: haploinsufficiency, deranged phosphorylation, and cardiomyocyte dysfunction
SJ Van Dijk, D Dooijes, C dos Remedios, M Michels… - Circulation, 2009 - Am Heart Assoc
Background—Mutations in the MYBPC3 gene, encoding cardiac myosin-binding protein C
(cMyBP-C), are a frequent cause of familial hypertrophic cardiomyopathy. In the present …
(cMyBP-C), are a frequent cause of familial hypertrophic cardiomyopathy. In the present …
β-Adrenergic receptor signaling in the heart: role of CaMKII
M Grimm, JH Brown - Journal of molecular and cellular cardiology, 2010 - Elsevier
The multifunctional Ca2+/calmodulin-dependent protein kinase II (CaMKII) targets a number
of Ca2+ homeostatic proteins and regulates gene transcription. Many of the substrates …
of Ca2+ homeostatic proteins and regulates gene transcription. Many of the substrates …
A new state of cardiac myosin with very slow ATP turnover: a potential cardioprotective mechanism in the heart
P Hooijman, MA Stewart, R Cooke - Biophysical journal, 2011 - cell.com
The mechanisms that control cardiac contractility are complex. Recent work we conducted in
vertebrate skeletal muscle identified a new state of myosin, the super-relaxed state (SRX) …
vertebrate skeletal muscle identified a new state of myosin, the super-relaxed state (SRX) …
Cardiac disorders and pathophysiology of sarcomeric proteins
J van der Velden, GJM Stienen - Physiological reviews, 2019 - journals.physiology.org
The sarcomeric proteins represent the structural building blocks of heart muscle, which are
essential for contraction and relaxation. During recent years, it has become evident that …
essential for contraction and relaxation. During recent years, it has become evident that …
Calcium-handling abnormalities underlying atrial arrhythmogenesis and contractile dysfunction in dogs with congestive heart failure
YH Yeh, R Wakili, XY Qi, D Chartier… - Circulation …, 2008 - Am Heart Assoc
Background—Congestive heart failure (CHF) is a common cause of atrial fibrillation. Focal
sources of unknown mechanism have been described in CHF-related atrial fibrillation. The …
sources of unknown mechanism have been described in CHF-related atrial fibrillation. The …
In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament
SP Harris, RG Lyons, KL Bezold - Circulation research, 2011 - Am Heart Assoc
In the 20 years since the discovery of the first mutation linked to familial hypertrophic
cardiomyopathy (HCM), an astonishing number of mutations affecting numerous sarcomeric …
cardiomyopathy (HCM), an astonishing number of mutations affecting numerous sarcomeric …
Cardiac myosin binding protein-C phosphorylation regulates the super-relaxed state of myosin
Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) accelerates cardiac
contractility. However, the mechanisms by which cMyBP-C phosphorylation increases …
contractility. However, the mechanisms by which cMyBP-C phosphorylation increases …