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Rat (Rattus) Ephrin B3 Protein expressed in Human Cells - ABIN2009180
Brückner, Pablo Labrador, Scheiffele, Herb, Seeburg, Klein: EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. in Neuron 1999
Show all 2 references for ABIN2009180
Mouse (Murine) Ephrin B3 Protein expressed in Human Cells - ABIN2008692
Bergemann, Zhang, Chiang, Brambilla, Klein, Flanagan: Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. in Oncogene 1998
Show all 2 references for ABIN2008692
The morphological and behavioural abnormalities in ephrin-B3 mutant mice are rescued by conditional knock-in of wild-type ephrin-B3 during the critical period when axon targeting and fear responses are initiated.
ephrin-B3 specifies the synaptic localization of PSD-95 (show DLG4 Proteins) and likely links the synaptic stability of PSD-95 (show DLG4 Proteins) to changes in neuronal activity
Ephrin-B3 knockout mice had significantly reduced pre-pulse inhibition compared with controls.
Conclude that EphB3 (show EPHB3 Proteins) mediates cell death in the adult cortex through a novel dependence receptor-mediated cell death mechanism in the injured adult cortex and is attenuated following ephrinB3 stimulation.
findings indicate that a single guidance system, ephrinB3/EphA4 (show EPHA4 Proteins), controls the formation of ascending and descending longitudinal axons in the spinal cord.
EphB2 and EphB3 are involved in the control of thymic epithelial cells (TEC) survival and that the absence of these molecules causes increased apoptotic TEC.
these data introduce EphB3 (show EPHB3 Proteins) as a new biomarker to identify beta-cells at a critical step during their step-wise differentiation and define the timeframe of endocrine differentiation.
Induction of experimental stroke results in enhanced cell proliferation and neuronal differentiation around the lesion site of ephrin-B3-deficient compared to ephrin-B3-expressing mice.
cell contact-mediated bidirectional ephrinB3/EphA4 (show EPHA4 Proteins) signaling mediates the sorting of medial ganglionic eminence- and preoptic area-derived interneurons in the deep and superficial migratory stream.
This study demonistrated tht ephrin-B reverse signaling into three distinct intracellular pathways and protein-protein interactions that mediate the maturation of postsynaptic neurons.
Data suggest that fusion of Nipah viruses with host cells is facilitated by two of viral membrane proteins, the G protein and the F protein (show HPD Proteins); G head domain binds to human ephrins B2 and B3 altering conformational density of entire G head domain.
Ephrin-B3 binds to B (show TDO2 Proteins) lymphocytes, most likely via a non-classical receptor, and induces migration of the memory B cell subpopulation.
Phosphoproteomic profiling of nonsmall cell lung cancer cells reveals that ephrin B3 regulates pro-survival signaling through Akt1 (show AKT1 Proteins)-mediated phosphorylation of the EphA2 (show EPHA2 Proteins) receptor.
evidence for an unknown ephrin-B3-binding cell-surface proteoglycan (show Vcan Proteins) involved in cellular signalling
EphrinB3 is a bona fide alternate receptor for NiV entry, and two residues in the G-H loop of the ephrin B-class ligands are critical determinants of NiV receptor activity.
Immunohistochemistry shows robust staining for phosphorylated ephrin-B and ephrin-B3 in invading glioblastoma cells.
Transgenic EphB1 (show EPHB1 Proteins) and ephrin-B3 cooperatively regulate the proliferation and migration of neural progenitors in the hippocampus
report the crystal structures of the NiV-G both in its receptor-unbound state and in complex with ephrin-B3, providing, to our knowledge, the first view of a paramyxovirus attachment complex in which a cellular protein is used as the virus receptor
EFNB3, a member of the ephrin gene family, is important in brain development as well as in its maintenance. Moreover, since levels of EFNB3 expression were particularly high in several forebrain subregions compared to other brain subregions, it may play a pivotal role in forebrain function. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH Receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). 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. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.
, ephrin B3
, ephrin ligand B3
, EPH-related receptor transmembrane ligand ELK-L3
, Ephrin B3
, eph-related receptor tyrosine kinase ligand 8