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MYBPC3 encodes the cardiac isoform of myosin-binding protein C. Additionally we are shipping MYBPC3 Kits (13) and MYBPC3 Proteins (3) and many more products for this protein.
Showing 10 out of 59 products:
Human Polyclonal MYBPC3 Primary Antibody for EIA, IHC (p) - ABIN953556
Bailey, Xie, Do, Montpetit, Diaz, Mohan, Keavney, Yusuf, Gerstein, Engert, Anand: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study. in Diabetes Care 2010
Show all 5 references for ABIN953556
N terminus of cMyBP-C interacts with F-actin through multiple distinct binding sites and that binding at one or more sites is reduced by phosphorylation
MYBPC3 mutations is elevated oxidative stress that corresponded to severe cardiac dysfunction, myocyte damage, and myocardial remodeling.
MBPC and troponin-I phosphorylation modulate myofilament length-dependent activation
MYBPC has unexpected inhibitory functions during postnatal myocyte cytokinesis and cell cycle progression.
Haploinsufficiency occurs in heterozygote MYBPC3 mutant carriers.
cMyBP-C is a principal mediator of increased contractility observed with beta-adrenergic stimulation or increased pacing because of protein kinase A and CaMKIIdelta phosphorylations of cMyB (show MYB Antibodies)-C.
Data suggest that cardiac myosin binding protein C (cMyBP-C) is an allosteric activator of myosin to increase cross-bridge force, and its phosphorylation status modulates the force.
Mybpc3 S282A mice displayed normal basal in vivo cardiac function but impaired rates of pressure development in response to beta-adrenergic stimulation.
Amptomatic heterozygous MYBPC3 carriers do suffer impairments that may presage the onset of hypertrophic cardiomyopathy.
Mammalian target of rapamycin (mTOR (show FRAP1 Antibodies)) inhibition with rapamycin improves cardiac function in type 2 diabetic mice: potential role of attenuated oxidative stress and altered contractile protein (show TNNT2 Antibodies) expression.
Data indicate that slow and fast skeletal muscles in myosin binding (show PPP1R12A Antibodies) protein-C (show PROC Antibodies) cMyBP-C((t/t)) mice showed no histological or ultrastructural changes in comparison to the wild-type control.
5 out of 102 (4.9%) athletes carried mutations: a heterozygous MYH7 (show MYH7 Antibodies) Glu935Lys mutation, a heterozygous MYBPC3 Arg160Trp mutation and another heterozygous MYBPC3 Thr1046Met mutation, all of which had been reported as HCM-associated mutations
a significant role of MYBPC3 gene mutations in Hypertrophic cardiomyopathy(HCM) disease and can be used for pre-symptomatic diagnosis of at risk family members of affected individuals.
Atrial fibrillation occurred in 74 patients with hypertrophic cardiomyopathy (31%), but with no difference among genotype groups (31% in MYBPC3, 37% in MYH7 (show MYH7 Antibodies) and 18% in other genotypes, p = 0.15).
The detection of MYBPC3 mutation, especially the PTC (show F9 Antibodies) mutation and double-mutation, may serve as a molecular marker for clinical risk stratification of HCM.
Demonstrate that MYBPC3 gene mutations, revealed by next-generation sequencing, were associated with familial and sporadic restrictive cardiomyopathy phenotype in patients.
Data indicate that homozygous or compound heterozygous truncating pathogenic myosin binding (show PPP1R12A Antibodies) protein C (show PROC Antibodies) (MYBPC3) mutations cause severe neonatal cardiomyopathy with features of left ventricular noncompaction and septal defects.
Mutations in the MYBPC3 and CASQ2 (show CASQ2 Antibodies) genes and six combinations between loci in the MYBPC3, MYH7 (show MYH7 Antibodies) and CASQ2 (show CASQ2 Antibodies) genes were responsible for cardiomyopathy risk in a studied cohort.
Although females with MYBPC3 mutations showed later onset of hypertrophic cardiomyopathy, female patients were more symptomatic at diagnosis and had more frequent heart failure events once they had developed hypertrophy.
A founder MYBPC3 mutation results in HCM with a high risk of sudden death after the fourth decade of life
Mutations in MYBPC3 are associated with cardiomyopathy. [Review]
small es, CyrillicMyBP-C modulates interaction of myosin with actin
MYBPC3 encodes the cardiac isoform of myosin-binding protein C. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. MYBPC3, the cardiac isoform, is expressed exclussively in heart muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase (PKA) upon adrenergic stimulation may be linked to modulation of cardiac contraction. Mutations in MYBPC3 are one cause of familial hypertrophic cardiomyopathy.
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