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Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the vinculin tail helical bundle to mediate actin bundling.
This study reported the new information on the frequency and phenotypes of congenital myopathy caused by ACTA1 mutations in subjects >/=5 years of age.
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.
Mutations in ACTA1 can cause pathologic features consistent with myofibrillar myopathy.
TIMP-1 (show TIMP1 Proteins) significantly increased levels of alpha-SMA (show SMN1 Proteins).
Myopathy associated with zebra bodies is part of the spectrum of myopathies associated with the ACTA1 gene.
New scapuloperoneal phenotype associated with an ACTA1 mutation.
Antisynthetase syndrome-associated myositis is characterized by distinctive myonuclear actin filament inclusions.
The predominant pathway mediated by Australian bat (show BAAT Proteins) lyssavirus G envelope for internalization into HEK293T cells is clathrin-and actin-dependent also requiring Rab5 (show RAB5A Proteins).
Data show that the width and speed of the waves depend counter-intuitively on parameters, negative feedback, and the F-actin time scale.
Titin-actin interaction: PEVK-actin-based viscosity in a large animal.
WIP is a link between membrane lipid composition and actin cytoskeleton at dendritic spines.
ACTA1(Asp286Gly) mouse model of nemaline myopathy provide evidence of impaired in vivo muscle function, altered muscle structure and disturbed energy metabolism.
Combined MRI (show C7ORF49 Proteins) and (3)(1)P-MRS investigations of the ACTA1(H40Y) mouse model of nemaline myopathy show impaired muscle function and altered energy metabolism.
Data indicate roles for linkers of nucleus to cytoskeleton (LINC) molecules nesprin2giant and nesprin3, which anchor actin cap fibers to the nucleus.
Asp286Gly acts as a "poison-protein" and according to the computational analysis it modifies the actin-actin interface. This phenomenon is likely to prevent proper myosin cross-bridge binding.
Data show that upon actin binding, the two domains of utrophin become dramatically separated and ordered, indicating a transition to a single open and extended conformation.
Data indicated that CacyBP/SIP (show CACYBP Proteins) could simultaneously interact with tubulin (show TUBB Proteins) and actin, suggesting that CacyBP/SIP (show CACYBP Proteins) might link actin and tubulin (show TUBB Proteins) cytoskeletons.
Results provide the genetic proof that platelet production from megakaryocytes strictly requires dynamic changes in the actin cytoskeleton.
Data show that while increases in cardiac and vascular smooth-muscle actin can partially compensate for the lack of skeletal actin in null mice, this is not sufficient to support adequate skeletal muscle growth and/or function.
alpha-skeletal-muscle actin mutations have roles in development of myopathies
The product encoded by this gene belongs to the actin family of proteins, which are highly conserved proteins that play a role in cell motility, structure and integrity. Alpha, beta and gamma actin isoforms have been identified, with alpha actins being a major constituent of the contractile apparatus, while beta and gamma actins are involved in the regulation of cell motility. This actin is an alpha actin that is found in skeletal muscle. Mutations in this gene cause nemaline myopathy type 3, congenital myopathy with excess of thin myofilaments, congenital myopathy with cores, and congenital myopathy with fiber-type disproportion, diseases that lead to muscle fiber defects.
actin, alpha 1, skeletal muscle
, actin, alpha skeletal muscle
, nemaline myopathy type 3
, alpha actin 1
, skeletal alpha actin
, actin alpha 1