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Investigated is the role that electrostatic field differences caused by the charge reversal mutation Rap1A K31E play in determining the binding specificity of RalGDS to Rap1A versus Ras.
Studies provide models for Ras in association with Raf (Montrer RAF1 Kits ELISA) kinase, RalGDS and PI3Kalpha (Montrer PIK3CA Kits ELISA) and PI3Kgamma (Montrer PIK3CG Kits ELISA).
involved in regulation of choline kinase activity by Ras proteins
identified Ral-GDS as a beta-arrestin-binding protein by yeast two-hybrid screening and co-immunoprecipitation from human polymorphonuclear neutrophilic leukocytes
RALGDS has a role in attenuating p53 (Montrer TP53 Kits ELISA)-independent DNA damage G2 checkpoint
Merlin (Montrer NF2 Kits ELISA) can function as a tumor suppressor by inhibiting the RalGDS-mediated oncogenic signals.
These data extend understanding of the functional roles of the Ral (Montrer rala Kits ELISA) pathway and begin to identify signaling pathways relevant for organ-specific metastasis.
results of screening suggest that RALGDS is not mutationally altered in cutaneous melanoma
overexpression of RalGDS promotes exocytosis of Weibel-Palade bodies from endothelial cells
RalGDS and RalA (Montrer rala Kits ELISA) act downstream of Rheb (Montrer RHEB Kits ELISA) and that RalA (Montrer rala Kits ELISA) activation is a crucial step in nutrient-induced mTORC1 activation
In this paper, we demonstrate a potential biochemical mechanism for such phenomena by showing that c-Met receptors promote the tyrosine phosphorylation of RalGDS at Y752 in its RBD (Montrer CACNA1D Kits ELISA), which blocks the binding of Ras to RalGDS.
Data implicate RalGDS-mediated induction of autophagy and exocyst function as a critical feature of load-induced cardiac hypertrophy.
constitutive RalGEF activation had a major impact on several malignant phenotypes, particularly anchorage-independent growth, indicating that this often overlooked pathway should be more carefully evaluated as a possible therapeutic target.
we investigated the activation of RalGDS, one of the Ras effector proteins with guanine-nucleotide exchange factor (Montrer ARHGEF12 Kits ELISA) activity for Ral (Montrer rala Kits ELISA).
Results identify RalGDS as a key component in Ras-dependent carcinogenesis in vivo.
Guanine nucleotide dissociation stimulators (GDSs, or exchange factors), such as RALGDS, are effectors of Ras-related GTPases (see MIM 190020) that participate in signaling for a variety of cellular processes.
ral guanine nucleotide exchange factor
, ral guanine nucleotide dissociation stimulator