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Mouse (Murine) Ephrin A3 Protein expressed in Human Cells - ABIN2008028
Zhou: The Eph family receptors and ligands. in Pharmacology & therapeutics 1998
Show all 4 references for ABIN2008028
Human Ephrin A3 Protein expressed in Human Cells - ABIN2002292
Stein, Savaskan, Ninnemann, Nitsch, Zhou, Skutella: A role for the Eph ligand ephrin-A3 in entorhino-hippocampal axon targeting. in The Journal of neuroscience : the official journal of the Society for Neuroscience 1999
Show all 4 references for ABIN2002292
Human Ephrin A3 Protein expressed in HEK-293 Cells - ABIN2181027
Kozlosky, Maraskovsky, McGrew, VandenBos, Teepe, Lyman, Srinivasan, Fletcher, Gayle, Cerretti: Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins. in Oncogene 1995
Show all 2 references for ABIN2181027
Findings suggest a putative novel mechanism for desipramine to modulate long-term potentiation through the regulation of the ephrinA3/EphA4 (show EPHA4 Proteins) signaling pathway
The ephrin-A2 (show EFNA2 Proteins)/-A3 DKO mice have utility as a novel ASD (show GUSB Proteins) model with an emphasis on sensory abnormalities and restricted, repetitive behavioral symptoms.
Ephrin-A2 (show EFNA2 Proteins) and -A3 are negative regulators of the proliferative and neurogenic potentials of Muller cells.
Ephrin-A3 suppresses Wnt (show WNT2 Proteins) signaling to control retinal stem cell potency.
Downregulation of the EphA4 (show EPHA4 Proteins) receptor via siRNA transfection reduced the repulsive effect of ephrin-A3, indicating that EphA4 (show EPHA4 Proteins) mediates at least in part the repulsive effect of ephrin-A3.
Data show that a number of Eph (show EPHA1 Proteins) receptors and ephrins were expressed in hematopoietic stem cells.
Ephrin-A3 is localized on astrocytic processes that envelop spines. Activation of EphA4 (show EPHA4 Proteins) by ephrin-A3 caused spine retraction; inhibiting ephrin/EphA4 (show EPHA4 Proteins) interactions distorted spine shape and organization in hippocampal slices.
Organ of Corti and spiral ganglion showed strong expression of ephrin-A3, ephrin-B2 (show EFNB2 Proteins) and ephrin-B3 (show EFNB3 Proteins). In lateral wall, ephrin-A3 and ephrin-B2 (show EFNB2 Proteins) were strongly expressed. Ephrin-A3 was strongly expressed in utricular and saccular sensory epithelia.
Results demonstrate that neurons expressing different odorant receptors express different levels of ephrin-A3 and -A5 protein (show NRP1 Proteins) on their axons.
In mice deficient for ephrin-A2, A3 and A5, eye-specific inputs segregated but shape and location of eye-specific layers were profoundly disrupted. Ephrin-As and neural activity act together to control patterning of eye-specific retinogeniculate layers.
Results show that EFNA3 serves as a tumor suppressor in malignant peripheral nerve sheath tumor cells and it may play a critical role in the FAK signaling and VEGF-associated tumor angiogenesis pathway.
The present study provides evidence that microglia upregulates endothelial ephrin-A3 and ephrin-A4 (show EFNA4 Proteins) to facilitate in vitro angiogenesis of brain endothelial cells, which is mediated by microglia-released TNF-alpha (show TNF Proteins).
The interaction between ephrin-As, Eph (show EPHA1 Proteins) receptors and integrin alpha3 is plausibly important for the crosstalk between Eph (show EPHA1 Proteins) and integrin signalling pathways at the membrane protrusions and in the migration of brain cancer cells.
EphA2 (show EPHA2 Proteins)/ephrin-A3 interactions may play a role in the localization and network of Langerhans cells in the epithelium and in the regulation of their trafficking.
analysis of molecular surfaces in ephrin-A5 (show EFNA5 Proteins) essential for a functional interaction with EphA3 (show EPHA3 Proteins)
Increasing ephrin-A expression enhances T-cell interactions not only with purified integrin ligands but also endothelial cells, while EphA activation down-regulates these interactions.
MicroRNA-210 modulates endothelial cell response to hypoxia and inhibits the receptor tyrosine kinase (show RET Proteins) ligand Ephrin-A3.
EphA3 (show EPHA3 Proteins) mutants with constitutively-released kinase domains efficiently support shedding, even when their kinase is disabled. Our data suggest that this phosphorylation-activated conformational switch of EphA3 (show EPHA3 Proteins) directly controls ADAM-mediated shedding.
This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin.
, EHK1 ligand
, EPH-related receptor tyrosine kinase ligand 3
, eph-related receptor tyrosine kinase ligand 3
, ligand of eph-related kinase 3