The well described fall in EGF receptor numbers after partial hepatectomy was confirmed.

This protein is a ligand for the EGF receptor.

The EGF receptor is a product of the erb-B oncogene.

Ligand binding to the EGF receptor therefore seems to be integrally associated with liver cell proliferation.

Src is activated by the EGF receptor family ligand Neuregulin.

Heterodimerization and functional interaction between EGF receptor family members: a new signaling paradigm with implications for breast cancer research.

In Drosophila this provides a mechanism for regulating EGF receptor activity in the brain.

This in turn dephosphorylates the EGF receptor, which is a member of the tyrosine kinase receptor family.

In cell culture, it has been used to study EGF receptor signaling and ErbB1 receptor trafficking.

Rhomboids were first discovered as proteases that regulate EGF receptor signalling in Drosophila.

A substantial body of evidence implicates events at the EGF receptor as the start of hepatocyte proliferation after partial hepatectomy.

SOS1 binds GBR2 at the plasma membrane after EGF receptor activation.

It is closely related to EGF, and can also bind to the EGF receptor with similar effects.

Helicobacter pylori-stimulated EGF receptor transactivation requires metalloprotease cleavage of HB-EGF.

These cell lines can also produce the alternate agonist of the EGF receptor, transforming growth factor α (TGF α).

Membrane phosphorylation studies, however, showed that TAGH induced phosphorylation of tyrosine residues in the EGF receptor.

These findings suggest TAGH infusion leads to a similar process of EGF receptor phosphorylation and internalisation as occurs after partial hepatectomy.

When cleaved from laminin this protein is powerfully mitogenic and may explain the growth promoting properties that laminin has been shown to have cells expressing EGF receptors.

On the other hand, EGF and the EGF receptor have a pH-resistant bond that persists until it is delivered to lysosomes for their degradation.

Based on this work imatinib was developed against chronic myelogenous leukemia (CML) and later gefitinib and erlotinib aiming at the EGF receptor.

Mature HB-EGF released from the cell surface is mitogenic and is able to bind to the EGF receptor [ 3 ] .

Moreover we, and others, have also shown that the density of EGF receptors is maximal in the basal layer of the squamous oesophagus, which is the proliferative zone.

The in vivo action of TAGH seems to entail recruitment of similar changes in the EGF receptor to those that occur after partial hepatectomy.

HB-EGF binding and activation of EGF receptors plays a critical role during cardiac valve tissue development and the maintenance of normal heart function in adults.

Such efforts have been successful at reducing EGF receptor expression, its downstream signaling, and consequently malignant behavior of the cancer cell such as migration, invasion, and cell detachment.

That's short for "human epidermal growth factor receptor 2."

Epidermal growth factor receptor has been shown to interact with:

The epidermal growth factor receptor system, as such, has been used as an intermediate example.

Both drugs aim to block a cancer-spurring protein called epidermal growth factor receptor.

The lack of understanding is shown in the case of drugs that block the epidermal growth factor receptor.

Cetuximab (marketed as Erbitux) targets the epidermal growth factor receptor.

Furthermore, epidermal growth factor receptor plays a crucial role in tumorigenesis, which is the production of a new tumor.

This endosomal protein regulates the cell-surface expression of epidermal growth factor receptor.

Erlotinib inhibits epidermal growth factor receptor, and works through a similar mechanism as gefitinib.

In the trial, epidermal growth factor receptor showed a rapid response to the inhibitor, as demonstrated by the improvement of the cancer symptoms.

GAPVD1 is also involved in the degradation of the epidermal growth factor receptor.

One of them was a gene called HER-2, human epidermal growth factor receptor No. 2.

The drug works by blocking activation of a molecule called epidermal growth factor receptor, which causes tumor cells to grow.

It suppresses the phosphorylation of the epidermal growth factor receptor in human colon carcinoma cells.

Paracrine activates epidermal growth factor receptor in endothelial cells of the tumor to do this.

For example, the insulin or epidermal growth factor receptors retain surface expression of oligosaccharides are present but incompletely processed.

Tykerb blocks not only Her-2 but also the epidermal growth factor receptor, another protein that spurs tumor growth.

A variety of cancers, such as breast and pancreatic caners over-express epidermal growth factor receptors.

He discovered this in studies of the epidermal growth factor receptor (EGFR).

Paracrine signalling mediates the response to epidermal growth factor receptor kinase inhibitors.

Mutations in the epidermal growth factor receptor activate signalling pathways that promote cell survival.

In each group, improvements were noted after a single week of epidermal growth factor receptor tyrosine kinase inhibitor treatment.

The expression of psoriasin is induced in skin wounds through activation of the epidermal growth factor receptor.

Also, a death occurred possibly due to epidermal growth factor receptor tyrosine kinase inhibitor treatment; however, the correlation is not exactly clear.

HER2 is named because it has a similar structure to human epidermal growth factor receptor, or HER1.