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EphA2 has a role in extracellular vesicle secretion from senescent cells that promote cancer cell proliferation
Combination of polymorphisms in the NOD2, IL17RA, EPHA2 and KALRN genes could play a significant role in the development of sarcoidosis by maintaining a chronic pro-inflammatory status in macrophages
Phosphorylation of RCP at Ser(435) by Lemur tyrosine kinase-3 (LMTK3) and of EphA2 at Ser(897) by Akt are both necessary to promote Rab14-dependent (and Rab11-independent) trafficking of EphA2 which generates cell:cell repulsion events that drive tumour cells apart.
EphA2 SAM (zeige TTN Proteine) domain inhibits kinase activity by reducing receptor oligomerization.
miR (zeige MLXIP Proteine)-141 inhibits glioma neovascularization by controlling EphA2 expression.
when overexpressed, EphA2 induces ERK (zeige EPHB2 Proteine) activation through its tyrosine kinase (zeige TXK Proteine) activity, leading to S897 phosphorylation and promotion of glioblastoma cell proliferation.
findings suggested inhibition of HDACs-EphA2 signaling axis with WW437 alone or in combination with other agents may be a promising therapeutic strategy for advanced breast cancer.
High EPHA2 expression is associated with epithelial-mesenchymal transition in gastric cancer.
Ligand-independent activation of EphA2 was triggered by VEGF (zeige VEGFA Proteine) released from CAF (zeige KAT2B Proteine)-CM.
EphA2-mediates glutaminolysis through YAP (zeige YAP1 Proteine)/TAZ (zeige TAZ Proteine) activation in HER2 (zeige ERBB2 Proteine)-positive breast cancer and may serve as potential therapeutic targets in patients.
The present study successfully assessed the expression pattern of miR26b in the pituitary tissue of Yanbian cattle, and also confirmed that EphA2 was a target gene of miR26b in Yanbian cattle in vitro.
that Epha2 and Efna5 (zeige EFNA5 Proteine) participate in the complex, global patterning of lens fiber cells that is necessary for maximal optical quality
EphA2 mAb treatment could partially inhibit LPSinduced inactivation of EphBEphrin B3 signalling, while Ephrin B3 (zeige EFNB3 Proteine) overexpression could abrogate LPSinduced activation of EphA2Ephrin A1 signalling. EphB1 (zeige EPHB1 Proteine)/Ephrin B3 (zeige EFNB3 Proteine) signalling may antagonise the EphA2/Ephrin A1dependent pathway following LPS (zeige TLR4 Proteine) treatment.
These results suggest that EphA2/Efna1/Egfr genes, linked to a possible control by miR-200a and miR-26b, could be proposed as novel CRC prognostic biomarkers. Moreover, EphA2 could be linked to a mechanism of resistance to cetuximab alternative to KRAS mutations.
Collectively, these data suggest that ATRA attenuates bleomycin-induced pulmonary fibrosis by regulating EphA2-EphrinA1 and PI3K-Akt (zeige AKT1 Proteine) signaling.
Lipopolysaccharide exposure significantly up-regulated EphA2 and EphrinA1 expression.
modulation of EphA2 signaling might contribute to effective transplantation of tissue-specific resident macrophages and/or monocytes
Our data suggest that EphA2 is closely related to the formation of osteoblasts and resorption of osteoclast and is likely to play an role in bone resorption induced in chronic periodontitis
We examined the roles of ephrin-A2 (zeige EFNA2 Proteine) and ephrin-A5 (zeige EFNA5 Proteine) signaling in contralateral targeting and topographic ordering in the ventral cochlear nucleus
EphA2 acts as a KRas cooperative tumor suppressor
Data shows that modulation of angiostatic factor Slit2 (zeige SLIT2 Proteine) by EphA2 receptor regulates endothelial responses to VEGF (zeige VEGFA Proteine)-mediated angiogenesis and tumor neovascularization.
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. Mutations in this gene are the cause of certain genetically-related cataract disorders.
ephrin type-A receptor 2
, epithelial cell receptor protein tyrosine kinase
, soluble EPHA2 variant 1
, tyrosine-protein kinase receptor ECK
, ephrin receptor EphA2
, epoxide hydrolase
, EPH receptor A2
, epithelial cell kinase
, tyrosine-protein kinase receptor MPK-5
, tyrosine-protein kinase receptor SEK-2
, protein tyrosine kinase EphA2
, eph-like receptor tyrosine kinase 6
, EPH receptor A2 L homeolog
, ephrin receptor EphA2 (tyrosine kinase family)