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MYOT encodes a cystoskeletal protein which plays a significant role in the stability of thin filaments during muscle contraction. Additionally we are shipping Myotilin Proteins (5) and Myotilin Kits (2) and many more products for this protein.
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Genetic association studies show that different TTID genotypes were significantly associated with carcass traits, including skin percentage, loin eye area and average skin thickness.
Sequence analysis and polymorphism identification in the TTID gene associated with meat quyality traits in Sus scrofa.
Describe the first homozygous mutation in the myotilin gene leading to a novel, autosomal recessive subtype of myofibrillar myopathy (MFM).
Analysis of myotilin turnover provides mechanistic insight into the role of myotilinopathy-causing mutations
A second known pedigree with LGMD1A: this finding constitutes a gold standard of proof that mutations in the myotilin gene cause Limb-Girdle Muscular Dystrophy 1A
Myotilin a thin filament-associated Z-disc protein.It binds to alpha-actinin and filamin c and is mutated in limb girdle muscular dystrophy 1A (LGMD1A).myotilin binds F-actin and prevents filament disassembly induced by Latrunculin A
Mutations in myotilin cause MFM; exon 2 of MYOT is a hotspot for mutations; peripheral neuropathy, cardiomyopathy, and distal weakness greater than proximal weakness are part of the spectrum of myotilinopathy; not all cases have a limb-girdle phenotype
Our findings provide evidence for a novel connection between the Z-disc protein myotilin and the sarcolemma via filamins and beta1 integrins.
The function of the myotilin protein is studied with regards its actin-organizing properties.
A novel mutation in the myotilin gene results in the clinical and pathologic phenotype termed "spheroid body myopathy." Mutations in this gene also cause limb-girdle muscular dystrophy 1A and are associated with myofibrillar myopathy.
Mutations within the MYOT gene are not a cause for Vocal Cord and Pharyngeal Weakness with Distal Myopathy (VCPDM (show MATR3 Antibodies)).
multigenerational French family in which gene sequencing identified a S60F myotilin mutation in all patients with full penetrance despite very late onset
Myotilin does not have a significant influence on muscle mass, muscle fiber size, or regulation of muscle contraction. Alternatively, compensatory over-expressions of other elements may compensate for the lack of myotilin.
features suggest an important role for myotilin in sarcomere organization.
either myotilin does not participate in muscle development and basal function maintenance or other proteins serve as structural and functional compensatory molecules when myotilin is absent
In single-transgenic mutant mice, double-transgenic mice overexpressing myotilin showed more severe muscle degeneration, enhanced myofibrillar aggregation, and earlier onset of aggregation.
This gene encodes a cystoskeletal protein which plays a significant role in the stability of thin filaments during muscle contraction. This protein binds F-actin, crosslinks actin filaments, and prevents latrunculin A-induced filament disassembly. Mutations in this gene have been associated with limb-girdle muscular dystrophy and myofibrillar myopathies. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
titin immunoglobulin domain protein
, titin immunoglobulin domain protein (myotilin)
, 57 kDa cytoskeletal protein
, myofibrillar titin-like Ig domains protein
, titan-like protein