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Our study demonstrates that high ActA level is an independent prognosis factor of survival in cancer patients. More than a basic marker of the severity of the neoplastic disease or of the inflammatory process, ActA seems to influence survival by contributing to the development of cachexia and loss of skeletal muscle mass.
The study confirmed ACTA1 mutations in four patients, including one with intranuclear rods, one with large intracytoplasmic aggregates, and two with nemaline intracytoplasmic rods.
Study shows that clinically severe ACTA1-related myopathy can present with muscle morphological findings suggestive of cytoplasmic body myopathy in the absence of definite nemaline rods.
Shorter than normal thin filament length contributes to the impaired force generation in patients with thin filament myopathy, but only in those who harbor specific mutations in NEB or ACTA1.
Over-expression of TNC (show TNC Proteins), SMA (show SMN1 Proteins), and vimentin (show VIM Proteins) were significantly correlated with the lower overall survival in prostate cancer patients.
ANA (show BTG3 Proteins) and ASMA evaluation in patients with liver transplantation and no history of autoimmune disease has no clinical relevance, since it varies in time and is not related to any risk factors or liver injury. Routine autoimmunity evaluation should be avoided.
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.
Titin-actin interaction: PEVK-actin-based viscosity in a large animal.
alpha smooth muscle actin (show ACTG2 Proteins) (alphaSMA (show ACTA2 Proteins)) was identified as a marker of osteoprogenitor cells in bone and periodontium.
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 (show UTRN Proteins) 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.
A genetic actc1b mutant exhibits mild muscle defects and is unaffected by injection of the actc1b targeting morpholino. The milder phenotype results from a compensatory transcriptional upregulation of an actin paralogue providing a novel approach to be explored for the treatment of actin myopathy. These findings provide further evidence that genetic compensation may influence the penetrance of disease-causing mutations.
Data show that local actin monomer depletion and network architecture can tune the rate of network growth to impose steering during motility.
Data suggest that mutations in troponin C (TnC (show TNNC2 Proteins)) found in patients with hypertrophic cardiomyopathy (A8V, C84Y, and D145E) stabilize the active state of regulated actin (the actin-tropomyosin (show TPM2 Proteins)-troponin complex) to various extents; at a saturating Ca2 (show CA2 Proteins)+ concentration, all TnC (show TNC Proteins) mutants investigated increase the level of active M state compared to the wild type.
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions
Structure of a Bud6/Actin complex reveals a novel wh2-like actin monomer recruitment motif.
Data suggest that toxofilin has two actin binding sites, and and the affinities of these actin binding sites are identical or very close to each other.
The activation of vinculin (show VCL Proteins) by stretched talin induces a positive feedback that reinforces the actin-talin-vinculin (show VCL Proteins) association.
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 skeletal muscle
, nemaline myopathy type 3
, alpha actin 1
, skeletal alpha actin
, alpha 1 skeletal muscle actin
, actin alpha 1
, actin, alpha 1, skeletal muscle
, actin, alpha, cardiac muscle 1
, Actin, alpha skeletal muscle
, LOW QUALITY PROTEIN: actin, alpha skeletal muscle
, cytoplasmic beta-actin
, actin, muscle
, skeletal alpha-actin
, skeletal muscle alpha-actin