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MYBPC1 encodes a member of the myosin-binding protein C family. Additionally we are shipping Myosin Binding Protein C, Slow Type Antibodies (108) and Myosin Binding Protein C, Slow Type Kits (4) and many more products for this protein.
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MYBPC1 mutations impair skeletal muscle function in zebrafish models of arthrogryposis.
Increase of the MYBPC1 expression level might lead to high growth performance in cattle.
The NC_007303.5:g.70014208A>G SNP is associated with marbling in Japanese Black beef cattle, with the G allele resulting in high levels of marbling. This SNP might have an impact on MYBPC1 expression and marbling by affecting MYBPC1 promoter activity.
A novel milder MYBPC1 homozygous phenotype causes arthrogryposis multiplex congenita in a consanguineous Israeli Druze pedigree.
Ca(2 (show CA2 Proteins)+) modulates the interaction of cMyBP-C with the thin filament in the sarcomere.
Two novel mutations in myosin binding protein C slow causing distal arthrogryposis type 2 were both found to occur in the C2 immunoglobulin domain, which constitutes part of the binding site for the S2 subfragment of myosin.
Mutations in the MYH7 (show MYH7 Proteins) gene, rather than in the MYBPC3 (show MYBPC3 Proteins) gene, were also related to a worse prognosis. This is the first work characterizing HC molecular epidemiology in the Brazilian population for the 3 most important genes.
Autosomal recessive lethal congenital contractural syndrome type 4 (LCCS4) caused by a mutation in MYBPC1
Significant molecule MYBPC1 phosphoprotein network from 12 frontal cortex of HIV encephalitis (HIVE) control patients and 16 HIVE, was identified and constructed.
MyBPC1 acts as an adaptor to connect the ATP consumer (myosin) and the regenerator (muscle type creatine kinase) for efficient energy metabolism and homoeostasis.
These findings reveal that the MYBPC1 is a novel gene responsible for DA1 (show TPM2 Proteins), though the mechanism of disease may differ from how some cardiac MYBPC3 (show MYBPC3 Proteins) mutations cause hypertrophic cardiomyopathy.
The present study demonstrates slow skeletal muscle type C-protein in moderate amount in right atrium and interatrial septum of adult human, rabbit, rat and bovine hearts using both immunocytochemical and immunoblotting procedures.
to determine whether HCM mutations in beta myosin heavy chain (show MYH7 Proteins) located within the light meromyosin portion alter the binding of cMyBP-C, and to define the precise region of this binding.
Data show that the NH2 and COOH termini of myosin binding protein C slow type (sMyBP-C) have distinct functions, which are regulated by differential splicing, and are compromized by the presence of missense point mutations linked to muscle disease.
This gene encodes a member of the myosin-binding protein C family. Myosin-binding protein C family members are myosin-associated proteins found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. The encoded protein is the slow skeletal muscle isoform of myosin-binding protein C and plays an important role in muscle contraction by recruiting muscle-type creatine kinase to myosin filaments. Mutations in this gene are associated with distal arthrogryposis type I. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
myosin binding protein C, slow type
, myosin-binding protein C, slow-type
, myosin-binding protein C, slow-type-like
, C-protein, skeletal muscle slow isoform
, skeletal muscle C-protein
, slow MyBP-C
, muscle C-protein
, MyBP-C slow
, Slow-type C-protein