Literature summary for 2.7.10.1 extracted from

Sheth, P.R.; Hays, J.L.; Elferink, L.A.; Watowich, S.J.
Biochemical basis for the functional switch that regulates hepatocyte growth factor receptor tyrosine kinase activation (2008), Biochemistry, 47, 4028-4038.

Search for more literature for 2.7.10.1

Activating Compound

Activating Compound	Comment	Organism	Structure
hepatocyte growth factor	activation of c-MET occurs in response to binding the physiological ligand hepatocyte growth factor	Chlorocebus aethiops
internalin B	activation of c-MET occurs in response to binding the internalin B protein of Listeria monocytogenes	Chlorocebus aethiops
additional information	ligand-dependent nonlinear increase in the level of c-MET phosphorylation in serum-starved Vero cells. c-MET activation response is sensitive to the dimer autophosphorylation rate. Stimulated monomeric c-MET, although clearly an active kinase molecule, is incapable of existing in an activated (i.e., phosphorylated, signaling competent) state due to synergistic effects of the biochemical properties associated with the c-MET monomeric state	Chlorocebus aethiops

Application

Application	Comment	Organism
additional information	model of c-MET activation. Relative importance of the main regulatory processes that work in concert to sharply switch between an inactive and active c-MET state. Importance of dimerization mediated changes in c-MET kinetic, biochemical, and dephosphorylation properties for enabling activation specificity. Ligand-stimulated c-MET is a highly competent signaling species and its activation is sensitive to changes in its biochemical parameters	Chlorocebus aethiops

Organism

Organism	UniProt	Comment	Textmining
Chlorocebus aethiops	Q2IBA6	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
Vero cell	-	Chlorocebus aethiops	-

Synonyms

Synonyms	Comment	Organism
c-met	-	Chlorocebus aethiops
hepatocyte growth factor receptor	-	Chlorocebus aethiops

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Release 2023.1 (January 2023)