tyrosine kinase receptor.
Dimerization and phosphorylation
dimerization and phosphorylation.
tyrosine kinase receptor!!
Receptor proteins are designed so special molecules can bind to them, and send messages to the cell that trigger some sort of reaction within the cell.They are embedded in either the plasma membrane or cytoplasm of a cell, to which a mobile signaling (or "signal") molecule may attach.Sources: http://en.wikipedia.org/wiki/Receptor_proteins
tyrosine kinase receptor.
Dimerization and phosphorylation
dimerization and phosphorylation.
Receptor tyrosine kinases do not require the use of second messengers while G protein-coupled receptors need.
tyrosine kinase receptor!!
receptor tyrosine kinases
called receptor tyrosine-kinases
J. Schlessinger has written: 'Cellular signaling by receptor tyrosine kinases'
receptor tyrosine kinase activity
Is the genetic abnormality which is a characteristic of a haematological malignancy, chronic myeloid leukemia.
1. Insulin binding to insulin receptor tyrosine kinase on hepatocyte: increased glucose uptake, increased glycogen and fatty acid production and decreased catabolism in general (decreased gluconeogenesis, lipolysis, and proteolysis). Insulin binding causes receptor dimerization and self-phosphorylation. Phosphorylated receptor recruits scaffold proteins and downstream target proteins and phosphorylate them. Phosphorylated target proteins serve as kinases and activate or deactivate other proteins by phosphorylation, effecting appropriate effects. 2. Erythropoietin binding to EPO cytokine receptor on Common Myeloid Progenitor cell: eventual differentiation into erythrocyte. Cytokine receptor induces the Jak/STAT pathway resulting in altered gene expression by transcription factors, drastically changing the function and morphology of the cell.
Joanne Chan has written: 'Characterizaton of receptor protein-tyrosine kinases, EEK and IRR'