4 edition of Activation of hormone and growth factor receptors found in the catalog.
|Statement||edited by Michael N. Alexis and Constantin E. Sekeris.|
|Series||NATO ASI series. Series C, Mathematical and physical sciences ;, vol. 295, NATO ASI Series., no. 295.|
|Contributions||Alexis, Michael N., 1951-, Sekeris, Constantin E., 1933-, North Atlantic Treaty Organization. Scientific Affairs Division.|
|LC Classifications||QP571.7 .N38 1988|
|The Physical Object|
|Pagination||xxi, 320 p. :|
|Number of Pages||320|
|LC Control Number||89026749|
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: Activation of Hormone and Growth Factor Receptors: Molecular Mechanisms and Consequences (Nato Science Series C:) ():.
This volume contains the papers presented in the NATO Advanced Research Workshop "Activation of Hormone and Growth Factor Receptors: Molecular Mechanisms and Consequences" held in Nafplion, Greece on September While growth factor receptors certainly play a role in the activation of integrins the reverse is also true (Miranti and Brugge, ; Wang et al., ).A good example is the interaction between the integrin αVβ3 and the epidermal growth factor receptor (EGFR/ERBB2) dimer.
Adherence to extracellular matrix causes phosphorylation of four tyrosine residues on the ERBB2 in a manner dependent. Activation of Hormone and Growth Factor Receptors: Molecular Mechanisms and Consequences: A record of the Meeting.- Signal Transduction and Control of Cell Proliferation and Differentiation.- Insulin Receptor and Insulin Action.- Signal Transduction by Growth Factor Receptors.- Cholera Toxin: Transport and Structural Basis of Action This volume contains the papers presented in the NATO Advanced Research Workshop "Activation of Hormone and Growth Factor Receptors: Molecular Mechanisms and Consequences" held in Nafplion, Greece on SeptemberThe objective of NATO ARW is to assess the state of-the-art in a given scientific area and to formulate recommendations for future research in emerging areas.
The kDa growth hormone receptor contains a single transmembrane domain with a glycosylated extracellular domain (Figure ).While the cytoplasmic domain becomes phosphorylated on tryrosine residues, this domain is different from other growth factor receptors, like those for EGF and PDGF, and has a different tyrosine kinase domain.
Activation of receptors that encode intrinsic tyrosine kinase activity, such as the insulin receptor, the epidermal growth factor receptor, and other tyrosine kinase growth factor receptors, is believed to involve the ligand-induced trans-autophosphorylation of closely apposed kinase domains within a dimeric receptor assemblage (31–34).
Among Cited by: Its actions are mediated via the growth hormone receptor, both directly by tyrosine kinase activation and indirectly by induction of insulin-like growth factor 1 (IGF-1).
Insensitivity to growth hormone (Laron syndrome) can result from mutations in the growth hormone receptor and can be treated with IGFCited by: Introduction. The growth hormone receptor (GHR) is a member of the class I cytokine receptor family, which includes more than 30 receptors such as the prolactin receptor (PRLR), erythropoietin receptor (EPOR), thrombopoietin receptor (TPOR), granulocyte-macrophage colony-stimulating factor receptor, interleukin-3 receptor, interleukin-6 receptor, and interleukin-7 receptor (1, 2).Cited by: A growth factor receptor is a receptor that binds to a growth factor.
Growth factor receptors are the first stop in cells where the signaling cascade for cell differentiation and proliferation begins. Growth factors, which are ligands that bind to the receptor are the initial step to activating the growth factor receptors and tells the cell to grow and/or superfamily: Platelet-derived growth factor, A.