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Ephrin-A1, B61, ephrin-A
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 which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Eph, EphA2, CAN, SEK, V1a
Papers on Ephrin-A1
Biochemical characterization of EphA2 antagonists with improved physico-chemical properties by cell-based assays and surface plasmon resonance analysis.
Tognolini et al., Parma, Italy. In Biochem Pharmacol, Feb 2016
Amino acid conjugates of lithocholic acid (LCA) have been recently described as effective disruptors of the EphA2-ephrin-A1 interaction able to inhibit EphA2 phosphorylation in intact cells and thus able to block prometastatic responses such as cellular retraction and angiogenesis.
The Prediction of the Expected Current Selection Coefficient of Single Nucleotide Polymorphism Associated with Holstein Milk Yield, Fat and Protein Contents.
Kim et al., Seoul, South Korea. In Asian-australas J Anim Sci, Jan 2016
They are phosphodiesterase 4B (PDE4B), serine/threonine kinase 40 (STK40), collagen, type XI, alpha 1 (COL11A1), ephrin-A1 (EFNA1), netrin 4 (NTN4), neuron specific gene family member 1 (NSG1), estrogen receptor 1 (ESR1), neurexin 3 (NRXN3), spectrin, beta, non-erythrocytic 1 (SPTBN1), ADP-ribosylation factor interacting protein 1 (ARFIP1), mutL homolog 1 (MLH1), transmembrane channel-like 7 (TMC7), carboxypeptidase X, member 2 (CPXM2) and ADAM metallopeptidase domain 12 (ADAM12).
A Boolean Function for Neural Induction Reveals a Critical Role of Direct Intercellular Interactions in Patterning the Ectoderm of the Ascidian Embryo.
Satou et al., Kyoto, Japan. In Plos Comput Biol, Dec 2015
In the ascidian embryo, four signaling ligands, Ephrin-A.d
EphA2 promotes cell adhesion and spreading of monocyte and monocyte/macrophage cell lines on integrin ligand-coated surfaces.
Ogawa et al., Ōsaka, Japan. In Cell Adh Migr, Dec 2015
Using a cell attachment stripe assay, we have shown that, following stimulation with ephrin-A1, kinase-independent EphA2 promoted cell spreading/elongation as well as adhesion to integrin ligand-coated surfaces in cultured U937 (monocyte) and J774.1 (monocyte/macrophage) cells as well as sublines of these cells expressing dominant negative EphA2 that lacks most of the intracellular region.
Eph as a target in inflammation.
Ieguchi, Tokyo, Japan. In Endocr Metab Immune Disord Drug Targets, 2014
Moreover, the soluble form of artificially oligomerized or dimerized Fc-fused ephrin-A1 has been widely used in in vitro and/or in vivo studies to activate the EphA receptors, whereas its physiological functions as a membrane-anchored protein remain largely unknown.
Ephrin-A2 and ephrin-A5 guide contralateral targeting but not topographic mapping of ventral cochlear nucleus axons.
Cramer et al., Orange, United States. In Neural Dev, 2014
Here we examined the roles of ephrin-A signaling in both types of targeting.
Cy5.5-Anti-ephrin receptor B4 (EphB4) humanized monoclonal antibody hAb47
Leung, Bethesda, United States. In Unknown Journal, 2013
On the basis of their structures and sequence relationships, ephrins are divided into two classes: the ephrin-A class, Ephs that are anchored to the cell membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B class, Ephs that are transmembrane proteins.
Ephs and ephrins resurface in inflammation, immunity, and atherosclerosis.
Orr et al., Shreveport, United States. In Pharmacol Res, 2013
Herein we discuss the current evidence for how Eph/ephrin interactions, particularly EphA2/ephrinA1 and EphB/ephrinB2, affect inflammation and cardiovascular disease.
The EphA2 receptor drives self-renewal and tumorigenicity in stem-like tumor-propagating cells from human glioblastomas.
Vescovi et al., Milano, Italy. In Cancer Cell, 2013
Both ephrinA1-Fc, which caused EphA2 downregulation in TPCs, and siRNA-mediated knockdown of EPHA2 expression suppressed TPCs self-renewal ex vivo and intracranial tumorigenicity, pointing to EphA2 downregulation as a causal event in the loss of TPCs tumorigenicity.
Eph/Ephrin signaling in injury and inflammation.
Boyd et al., Australia. In Am J Pathol, 2012
There are 10 EphA receptors, and six EphB receptors, distinguished on sequence difference and binding preferences, that interact with the six glycosylphosphatidylinositol-linked ephrin-A ligands and the three transmembrane ephrin-B ligands, respectively.
Higher expression of EphA2 and ephrin-A1 is related to favorable clinicopathological features in pathological stage I non-small cell lung carcinoma.
Date et al., Kyoto, Japan. In Lung Cancer, 2012
in p-stage I NSCLC patients, those in the higher EphA2 expression and higher ephrin-A1 expression groups shared almost the same clinicopathological backgrounds which are generally considered to be better prognostic factors.
Ret is a multifunctional coreceptor that integrates diffusible- and contact-axon guidance signals.
Pfaff et al., Los Angeles, United States. In Cell, 2012
Ephrin-A receptors are thought to depend on transmembrane coreceptors for transmitting signals intracellularly.
Ephs and ephrins in cancer: ephrin-A1 signalling.
Debinski et al., Winston-Salem, United States. In Semin Cell Dev Biol, 2012
Multiple oncogenic signalling pathways are affected by ephrin-A1, from the promotion of a specific pathway in one cell or cancer type to the inhibition of the same pathway in another type of cell or cancer. [Review]
EphrinA1-EphA2 interaction-mediated apoptosis and FMS-like tyrosine kinase 3 receptor ligand-induced immunotherapy inhibit tumor growth in a breast cancer mouse model.
Mittal et al., West Lafayette, United States. In J Gene Med, 2012
The EphA2 ligand EphrinA1 induces EphA2 phosphorylation and intracellular internalization and degradation, thus inhibiting breast tumor progression.
EphA2/Ephrin-A1 signaling complexes restrict corneal epithelial cell migration.
Getsios et al., Chicago, United States. In Invest Ophthalmol Vis Sci, 2012
Elevated levels of ephrin-A1 may contribute to diabetic keratopathies by persistently engaging EphA2 and prohibiting Akt-dependent corneal epithelial repair processes.
Expression profile and role of EphrinA1 ligand after spinal cord injury.
Miranda et al., San Juan, United States. In Cell Mol Neurobiol, 2011
Data suggest that ephrinA1 ligands play a role in the pathophysiology of spinal cord injury.
(111)In-Labeled-TNYLFSPNGPIARAW (TNYL-RAW)-polyethylene glycol–coated core-cross-linked polymeric micelle-Cy7
Leung, Bethesda, United States. In Unknown Journal, 2011
Based on their structures and sequence relationships, ephrins are divided into the ephrin-A class, which are anchored to the cell membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B class, which are transmembrane proteins.
Restriction of receptor movement alters cellular response: physical force sensing by EphA2.
Groves et al., Berkeley, United States. In Science, 2010
Activation of the EphA2 receptor tyrosine kinase by ephrin-A1 ligands presented on apposed cell surfaces plays important roles in development and exhibits poorly understood functional alterations in cancer.
Integration of neuronal clones in the radial cortical columns by EphA and ephrin-A signalling.
Rakic et al., New Haven, United States. In Nature, 2009
Here we show that an Eph receptor A (EphA) and ephrin A (Efna) signalling-dependent shift in the allocation of clonally related neurons is essential for the proper assembly of cortical columns.
EphA2 mediates ligand-dependent inhibition and ligand-independent promotion of cell migration and invasion via a reciprocal regulatory loop with Akt.
Wang et al., Cleveland, United States. In Cancer Cell, 2009
While activation of EphA2 with its ligand ephrin-A1 inhibited chemotactic migration of glioma and prostate cancer cells, EphA2 overexpression promoted migration in a ligand-independent manner.
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