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Details on Person Binding of ligand to AGER results in the activation of multi...

Class:IdSummation:997396
_displayNameBinding of ligand to AGER results in the activation of multi...
_timestamp2010-11-09 12:40:18
created[InstanceEdit:997401] Jupe, S, 2010-11-09
literatureReference[LiteratureReference:997403] Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress
[LiteratureReference:997408] Receptor for advanced glycation end products (RAGE)-mediated neurite outgrowth and activation of NF-kappaB require the cytoplasmic domain of the receptor but different downstream signaling pathways
[LiteratureReference:997404] The receptor for advanced glycation end products is induced by the glycation products themselves and tumor necrosis factor-alpha through nuclear factor-kappa B, and by 17beta-estradiol through Sp-1 in human vascular endothelial cells
[LiteratureReference:879440] The receptor for advanced glycation end-products (RAGE) directly binds to ERK by a D-domain-like docking site
textBinding of ligand to AGER results in the activation of multiple signaling pathways, including the mitogen-activated protein kinase (MAPK) cascade (Lander et al. 1997), cdc42/Rac (Huttunen et al. 1999), and activation of NF-?B (Tanaka et al. 2000). A membrane-proximal cytoplasmic region of the advanced glycation end-products receptor (AGER) is responsible for binding to extracellular signal-regulated protein kinase-1 and -2 (ERK1/2 or MAPK3/1). This region is similar to the D-domain, an ERK docking site which is conserved in some ERK substrates (Ishihara et al. 2003).
(summation)[Reaction:879362] AGER binds ERK1/2 [Homo sapiens]
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