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Univariate Cox regression analysis showed high expression of TWF1 to be independent prognostic indicator involved in overall survival and recurrence-free survival in lung adenocarcinoma, but not in lung squamous cell carcinoma
TWF1 and VIM are required for miR-30c to regulate breast cancer cell invasion.
An interleukin-6 family member, interleukin-11 is identified as a secondary target of twinfilin 1 in the microRNA-30c signalling pathway.
protein overexpression promotes cardiomyocyte hypertrophy
These data suggest that the association with an actin monomer induces a first-order conformational change within the twinfilin molecule.
mammals have two twinfilin isoforms, which are differentially expressed and regulated through distinct cellular signaling pathways
Here, the authors discover that the C-terminal tail of Twinfilin harbors a capping protein-interacting (CPI) motif, identifying it as a novel CPI-motif protein. Twinfilin binds competitively with CARMIL to capping protein, protecting capping protein from barbed-end displacement by CARMIL.
FGF signaling promotes the expansion of A6-expressing liver cells partly via AKT-dependent activation of beta-Catenin expansion of A6(+ive) periportal cells and possibly by reprogramming of centrolobular hepatocytes.
structural conservation between its actin monomer-binding sites and the binding site of actin-depolymerizing factor (ADF)/cofilin
a novel model for how sequential interactions between actin monomers, twinfilin, capping protein, and actin filaments promote cytoskeletal dynamics
The crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer, is presented.
like Twf1, mouse Twf2 is a filament barbed-end capping protein, and that two tissue-specific and biochemically distinct isoforms are generated from the Twf2 gene through alternative promoter usage
The results reveal that TWF1 is highly induced by the stimulation of amino acids and hormones and involved in regulation of milk bio-synthesis and cell proliferation via the mTOR pathway in bovine mammary epithelial cells.
Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity).
A6 protein tyrosine kinase
, PTK9 protein tyrosine kinase 9
, protein A6
, protein tyrosine kinase 9
, twinfilin, actin-binding protein, homolog 1
, actin monomer-binding protein
, twinfilin 1
, LOW QUALITY PROTEIN: twinfilin-1
, twinfilin, actin-binding protein, homolog 1b