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MYO10 encodes a member of the myosin superfamily. Additionally we are shipping Myosin X Antibodies (12) and many more products for this protein.
MYO10 (myosin X), a direct miR340 target gene, mediated the migration and invasion of breast cancer cells
Results suggest that NF-kappaB (show NFKB1 ELISA Kits)-regulated miR (show MLXIP ELISA Kits)-124 targets MYO10, inhibits cell invasion and metastasis, and is down-regulated in node-positive NSCLC.
Myo10 plays a key role in integrating the actin and microtubule cytoskeletons to position centrosomes and mitotic spindles.
New research implicates Myo10 in a number of disease states including cancer metastasis and pathogen infection.
PCTK1 (show CDK16 ELISA Kits) regulates spindle orientation through phosphorylation of Ser83 on KAP0, a regulatory subunit of protein kinase A.
Elevated MYO10 expression and involvement in invadopodia formation increases the aggressiveness of breast cancer .
Study demonstrates a novel biological function for Hdl (show HSD11B1 ELISA Kits)-Myo10 and an important new role for both Myo10 isoforms in the development of dendritic spines and synapses.
Myo10 upregulation in mutant p53 (show TP53 ELISA Kits)-driven cancers is necessary for invasion and that plasma-membrane protrusions.
Phosphorylation of ADD1 (show ADD1 ELISA Kits) at Ser12 and Ser355 by cyclin-dependent kinase 1 (show CDK1 ELISA Kits) enables ADD1 (show ADD1 ELISA Kits) to bind to myosin-X (Myo10).
Authors conclude thatMyo10 generates the force to enhance bacterial-induced cell membrane protrusions by binding its head region to actin filaments and its PH tail domain to the peripheral membrane.
Myo10 is required for neurogenic cell migration through N-cadherin (show CDH2 ELISA Kits) mediated cell adhesion.
Myo10 is involved in neuronal development both in vitro and in vivo by regulating microtubule stability
Results indicate that, in neuronal cells, TNTs (show TNNI1 ELISA Kits) can arise from a subset of Myo10-driven dorsal filopodia, independent of its binding to integrins and N-cadherins.
The study analyzed and cloned 2-kb of the 5'-upstream sequences of mouse full-length Myo10 (fMyo10) and headless Myo10 (hMyo10) to understand the transcriptional regulation of the Myo10 gene.
headless Myo10 can function as a negative regulator of full-length Myo10 and that the two isoforms of Myo10 have opposing roles in axon outgrowth.
Myo10 was required for neuronal morphological transition during radial neuronal migration in the developmental neocortex
DCC (show DCC ELISA Kits) promotes movement of Myo (show SYNPO2 ELISA Kits) X along basal actin filaments and enhances Myo (show SYNPO2 ELISA Kits)-X-mediated basal filopodium elongation.
Myo10 plays a role in osteoclast attachment and podosome positioning by direct linkage of actin to the microtubule network
Myo10 provides a molecular link between PI(3 (show PI3 ELISA Kits))K and pseudopod extension during phagocytosis
Myosin-X is involved in cell-cell adhesion-associated signaling-linked membrane and/or cytoskeleton reorganization.
Single alpha-helices domain of MYO10 unfolds progressively as the length is increased and refolds progressively as the length is reduced.
At low optical trap loads, we observed staircase-like processive movements of myosin-10 interacting with the actin filament, consisting of up to six approximately 35-nm steps per binding interaction.
Myosin X is monomeric and the band 4.1 (show EPB41 ELISA Kits)-ezrin-radixin-moesin (show MSN ELISA Kits) (FERM) and pleckstrin (show PLEK ELISA Kits) homology (PH) domains bind to the head intramolecularly, forming an inhibited conformation.
the structural features of the motor and the track that allow myosin X to recognize actin filament bundles
myosin X is a membrane-associated molecular motor (show MYO1E ELISA Kits)
kinetic analysis of function of Myosin X as a high duty ratio motor
the predicted coiled coil of myosin 10 (show MYH10 ELISA Kits) forms a novel elongated structure in which the proximal region is a SAH (show ACSM3 ELISA Kits) domain and the distal region is a SAH (show ACSM3 ELISA Kits) domain (or has an unknown extended structure) that dimerizes only at its end
myosin X recognizes the local structural arrangement of filaments in long bundles, providing a mechanism for sorting cargo to distant target sites.
This gene encodes a member of the myosin superfamily. The protein represents an unconventional myosin\; it should not be confused with the conventional non-muscle myosin-10 (MYH10). Unconventional myosins contain the basic domains of conventional myosins and are further distinguished from class members by their tail domains. This gene functions as an actin-based molecular motor and plays a role in integration of F-actin and microtubule cytoskeletons during meiosis.
, myosin x
, unconventional myosin-10
, unconventional myosin-X
, unconventionnal myosin-X