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At the trailing edge of the cell the focal adhesion must be dissolved.
Many proteins are required for proper focal adhesion production and maintenance.
During cell migration, both the composition and the morphology of the focal adhesion change.
Focal adhesions at the leading edge provide the necessary traction allowing the cell to pull itself forward.
Focal adhesions can contain over 100 different proteins, which suggests a considerable functional diversity.
Focal adhesion kinase has four defined regions, or tertiary structure domains.
Functions include downregulation of stress fibres and focal adhesions.
The dynamic assembly and disassembly of focal adhesions plays a central role in cell migration.
These connection sites are called focal adhesions.
DLC1 is localized to focal adhesions located at the periphery of cells.
Cells can form intergrin mediated attachments sites called focal adhesions.
Filopodia form focal adhesions with the substratum, linking it to the cell surface.
Thus, vinculin appears to play a key role in shape control based on its ability to modulate focal adhesion structure and function.
Connection between focal adhesions and proteins of the extracellular matrix generally involves integrins.
Focal adhesions are macromolecular structures that function in the transmission of mechanical force and regulatory signals.
Mechanical forces can be transmitted by focal adhesion sites, integrins, and cell-cell junctions.
GAK is also known to be associated with focal adhesions though the exact relationship between the two is unknown.
NHE1 (a sodium hydrogen exchanger, involved in focal adhesions and actin organisation)
Syndecan-4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.
Maspin treatment of breast cancer cells leads to increased focal adhesions and stress fibers that in turn reduce cell motility.
It distrupt focal adhesion in fibroblasts.
The tyrosine phosphorylated form of caveolin-1 colocalizes with focal adhesions, suggesting a role for caveolin-1 in migration.
RhoA regulates the actin cytoskeleton and forms stress fibers and focal adhesions.
Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis.
Since these regions would several years later be named focal adhesions, α-actinin was the first protein found to be concentrated at these sites.
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