Ligand-induced receptor oligomerization is an established mechanism for receptor-tyrosine
kinase activation. However, numerous receptor-tyrosine kinases are expressed in …

Nerve growth factor engages two structurally distinct transmembrane receptors, TrkA and
p75, which have been proposed to create a" high-affinity" NGF binding site through …

Nerve growth factor binds independently to two transmembrane receptors, the p75
neurotrophin receptor and the p140trk (trkA) tyrosine kinase receptor, which are both co …

Nerve growth factor (NGF) functions as a ligand for two receptors, the TrkA tyrosine kinase
receptor and the p75 neurotrophin receptor (p75NTR). The Ig-like domains of Trk receptors …

While the central role played by TrkA in nerve growth factor (NGF) signalling has been
established by dissecting its signal transduction pathways, insight into the mechanism of …

The low-affinity p75 neurotrophin receptor is believed to participate with the Trk receptor
tyrosine kinase in the formation of high-affinity binding sites for nerve growth factor (NGF). To …

It has been proposed that the high affinity nerve growth factor (NGF) receptor required for
NGF response is a complex of two receptor proteins, gp75 and the tyrosine kinase TrkA, but …

Nerve growth factor (NGF), like many other growth factors and hormones, binds to two
different receptor molecules on responsive cells. The product of the proto-oncogene trk …

We have investigated the molecular nature of the high affinity nerve growth factor (NGF)
receptors by using cell lines expressing gp75 LNGFR and gp140 trk Our results suggest that …

Limited proteolysis and site-directed mutagenesis of human nerve growth factor (hNGF) was
utilized to determine the role of the NH2 terminus in p140TrkA (TrkA) receptor function …