Receptor tyrosine kinases (RTKs) are single-span transmembrane receptors in which
relatively conserved intracellular kinase domains are coupled to divergent extracellular …

The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase that plays a
critical role in the pathogenesis of many cancers. The structure of intact forms of this receptor …

Clustering of proteins into micrometer-sized structures at membranes is observed in many
signaling pathways. Most models of clustering are specific to particular systems, and …

How the epidermal growth factor receptor (EGFR) activates is incompletely understood. The
intracellular portion of the receptor is intrinsically active in solution, and to study its …

Signaling by the epidermal growth factor receptor requires an allosteric interaction between
the kinase domains of two receptors, whereby one activates the other. We show that the …

The epidermal growth factor receptor (EGFR) plays vital roles in cellular processes including
cell proliferation, survival, motility, and differentiation. The dysregulated activation of the …

The epidermal growth factor receptor (EGFR) is activated by dimerization, but activation also
generates higher-order multimers, whose nature and function are poorly understood. We …

Epidermal growth factor receptor (EGFR) and vascular endothelial growth factor receptor
(VEGFR) are two extensively studied membrane-bound receptor tyrosine kinase proteins …

Since the cloning of the critical adapter, LAT (linker for activation of T cells), more than 15
years ago, a combination of multiple scientific approaches and techniques continues to …

Ligand-driven dimerizations of ErbB receptor subunits fulfill a fundamental role in their
activation. We have used the number and brightness analysis technique to investigate the …