Epidermal growth factor receptor (EGFR) is widely spread in various types of cells and plays critical roles in cellular activities. Here we studied the EGFR distribution before and after activation by high-resolution mapping technique-topography and recognition imaging (TREC). The unbinding force between EGFR and its ligand, epidermal growth factor (EGF), was also measured by single-molecule force spectroscopy. Our results suggest that the majority of EGFRs are in the cluster state both in the resting and stimulated cells. This study provides qualitative information of the location, cluster state and binding kinetics of EGFRs in cell membranes at the molecular level
Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyr...
Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyr...
We have revealed a reorientation of ectodomain I of the epidermal growth factor receptor (EGFR; ErbB...
AbstractThe spatial arrangement of the epidermal growth factor receptor (EGFR) on the cellular plasm...
generally considered to be activated by either ligand-induced dimerisation or a ligand-induced confo...
The clustering of membrane receptors such as EGFR is critical for various biological processes, for ...
Detecting receptor dimerisation and other forms of clustering on the cell surface depends on methods...
To determine the distribution of the epidermal growth factor (EGF) receptor (EGFR) on the surface of...
AbstractThe spatial arrangement of the epidermal growth factor receptor (EGFR) on the cellular plasm...
Adaptor protein Grb2 binds phosphotyrosines in the epidermal growth factor (EGF) receptor (EGFR) and...
AbstractThe epidermal growth factor receptor (EGFR) is a well-studied receptor tyrosine kinase and a...
Adaptor protein Grb2 binds phosphotyrosines in the epidermal growth factor (EGF) receptor (EGFR) and...
AbstractWe investigated the association of signaling proteins with epidermal growth factor (EGF) rec...
AbstractRecent evidence suggests that the EGF receptor oligomerizes or clusters in cells even in the...
The epidermal growth factor receptor (EGFR) is a member of the erbB tyrosine kinase family of recept...
Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyr...
Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyr...
We have revealed a reorientation of ectodomain I of the epidermal growth factor receptor (EGFR; ErbB...
AbstractThe spatial arrangement of the epidermal growth factor receptor (EGFR) on the cellular plasm...
generally considered to be activated by either ligand-induced dimerisation or a ligand-induced confo...
The clustering of membrane receptors such as EGFR is critical for various biological processes, for ...
Detecting receptor dimerisation and other forms of clustering on the cell surface depends on methods...
To determine the distribution of the epidermal growth factor (EGF) receptor (EGFR) on the surface of...
AbstractThe spatial arrangement of the epidermal growth factor receptor (EGFR) on the cellular plasm...
Adaptor protein Grb2 binds phosphotyrosines in the epidermal growth factor (EGF) receptor (EGFR) and...
AbstractThe epidermal growth factor receptor (EGFR) is a well-studied receptor tyrosine kinase and a...
Adaptor protein Grb2 binds phosphotyrosines in the epidermal growth factor (EGF) receptor (EGFR) and...
AbstractWe investigated the association of signaling proteins with epidermal growth factor (EGF) rec...
AbstractRecent evidence suggests that the EGF receptor oligomerizes or clusters in cells even in the...
The epidermal growth factor receptor (EGFR) is a member of the erbB tyrosine kinase family of recept...
Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyr...
Signaling from the epidermal growth factor receptor (EGFR) via phosphorylation on its C-terminal tyr...
We have revealed a reorientation of ectodomain I of the epidermal growth factor receptor (EGFR; ErbB...