BIOMAT Database Logo BIOMAT Database Logo

Growth hormone receptor structure, dimerization and function. 1994

P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
INSERM Unité 344, Endocrinologie Moléculaire, Faculté de Médecine Necker, Paris, France.

UI MeSH Term Description Entries
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D011505 Protein-Tyrosine Kinases Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors. Tyrosine Protein Kinase,Tyrosine-Specific Protein Kinase,Protein-Tyrosine Kinase,Tyrosine Kinase,Tyrosine Protein Kinases,Tyrosine-Specific Protein Kinases,Tyrosylprotein Kinase,Kinase, Protein-Tyrosine,Kinase, Tyrosine,Kinase, Tyrosine Protein,Kinase, Tyrosine-Specific Protein,Kinase, Tyrosylprotein,Kinases, Protein-Tyrosine,Kinases, Tyrosine Protein,Kinases, Tyrosine-Specific Protein,Protein Kinase, Tyrosine-Specific,Protein Kinases, Tyrosine,Protein Kinases, Tyrosine-Specific,Protein Tyrosine Kinase,Protein Tyrosine Kinases,Tyrosine Specific Protein Kinase,Tyrosine Specific Protein Kinases
D011986 Receptors, Somatotropin Cell surface proteins that bind GROWTH HORMONE with high affinity and trigger intracellular changes influencing the behavior of cells. Activation of growth hormone receptors regulates amino acid transport through cell membranes, RNA translation to protein, DNA transcription, and protein and amino acid catabolism in many cell types. Many of these effects are mediated indirectly through stimulation of the release of somatomedins. Growth Hormone Receptors,Receptors, Growth Hormone,Somatomammotropin Receptors,Somatotropin Receptors,Growth Hormone Receptor,Receptor, Growth Hormone,Receptors, Somatomammotropin,Somatomammotropin Receptor,Somatotropin Receptor,Hormone Receptor, Growth,Hormone Receptors, Growth
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal

Related Publications

P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function.
October 2002, FEBS letters,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Growth hormone receptor: structure function relationships.
January 2011, Hormone research in paediatrics,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Structure and function of the growth-hormone-releasing hormone receptor.
January 2000, Vitamins and hormones,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Structure-function studies of ligand-induced epidermal growth factor receptor dimerization.
April 1998, Biochemistry,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Growth hormone and its receptor: from structure to function.
December 1993, The Journal of endocrinology,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Dimerization and signal transduction of the growth hormone receptor.
May 2003, Molecular endocrinology (Baltimore, Md.),
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
The prolactin/growth hormone receptor family: structure/function relationships.
January 1997, Journal of mammary gland biology and neoplasia,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics.
January 2010, Cell adhesion & migration,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
Growth hormone receptor: structure and signal transduction.
December 1995, European journal of endocrinology,
P A Kelly, and M C Postel-Vinay, and J Finidori, and M Edery, and A Sotiropoulos, and L Goujon, and N Esposito
The role of receptor dimerization domain residues in growth hormone signaling.
February 1997, The Journal of biological chemistry,
Copied contents to your clipboard!