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E-cadherin is overexpressed and paradoxically associated with especially aggressive type.
Tumors were considered positive for E-cadherin when cells showed membrane staining.
E-cadherin is also used by pathologists to diagnose different kinds of breast cancer.
E-cadherin (epithelial) is the most well-studied member of the cadherin family.
In the very early stages of development, E-cadherin (epithelial cadherin) is most greatly expressed.
In the adherens junctions of epithelial cells, E-cadherin is the most abundant.
Another cadherin, E-cadherin, is expressed by ectodermal cells in the process of neural plate development.
E-cadherin, which is expressed on epithelial cells, transmits antigrowth signals.
About half of the KC expressed high levels of E-cadherin.
F9 cells were genetically engineered to lack β-catenin, resulting in increased association of plakoglobin with E-cadherin.
Relative frequency of loss of E-cadherin and CD44 has also been observed.
Cell-cell interactions mediated by E-cadherin are crucial to blastula formation in many animals.
E-cadherin is a crucial type of cell-cell adhesion to hold the epithelial cells tight together.
A, located in the promoter region of E-cadherin, has been found to alter the transcriptional activity of this gene.
The methylation patterns of the E-cadherin 5' CpG island are not stable.
Loss of E-cadherin is common in lobular carcinoma but is also seen in other breast cancers.
Loss of E-cadherin is considered to be a fundmental event in EMT.
The cell-cell adhesion molecule E-cadherin has been shown to be required for the radial intercalation of the deep cells.
E-cadherin is an important switch in EMT.
The head domain of vinculin associates to E-cadherin via α-catenin, β-catenin, and γ-catenin.
E-cadherin is first expressed in the 2-cell stage of mammalian development, and becomes phosphorylated by the 8-cell stage, where it causes compaction.
E-cadherin is a tumor suppressor gene in which germline mutations cause a hereditary form of gastric carcinoma.
Interestingly, the level the adhesion molecule, E-cadherin, was unaltered and the biophysical properties of cells between the two compartments were the same.
These findings are all consistent with previous observations that embryonic stem cells resemble epithelial cells and express E-cadherin.
In F9 cells lacking both β-catenin and plakoglobin, very little E-cadherin and α-catenin accumulated at the cell surface.