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Ephrin B3

Ephrin-B3, EFNB3
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Eph, Ephrin-B2, CAN, SEK, Ephrin-B1
Papers on Ephrin-B3
Antibody-mediated neutralization of myelin-associated EphrinB3 accelerates CNS remyelination.
Kotter et al., Göttingen, Germany. In Acta Neuropathol, Feb 2016
Here, we identify the transmembrane signalling protein EphrinB3 as important mediator of this inhibition, using a protein analytical approach in combination with a primary rodent OPC assay.
Functionalized collagen scaffold implantation and cAMP administration collectively facilitate spinal cord regeneration.
Dai et al., Beijing, China. In Acta Biomater, Feb 2016
The scaffold was specifically functionalized using neutralizing proteins (CBD-EphA4LBD, CBD-PlexinB1LBD and NEP1-40) and collagen-binding neurotrophic factors (CBD-BDNF and CBD-NT3) to simultaneously antagonize myelin inhibitory molecules (ephrinB3, Sema4D and Nogo) and exert neurotrophic protection and stimulation.
Anchoring and synaptic stability of PSD-95 is driven by ephrin-B3.
Dalva et al., Philadelphia, United States. In Nat Neurosci, Nov 2015
Here we show using super-resolution imaging, biochemical approaches and in vivo models that the trans-synaptic organizing protein ephrin-B3 controls the synaptic localization and stability of PSD-95 and links these events to changes in neuronal activity via negative regulation of a newly identified mitogen-associated protein kinase (MAPK)-dependent phosphorylation site on ephrin-B3, Ser332.
Functionalized Collagen Scaffold Neutralizing the Myelin-Inhibitory Molecules Promoted Neurites Outgrowth in Vitro and Facilitated Spinal Cord Regeneration in Vivo.
Dai et al., Beijing, China. In Acs Appl Mater Interfaces, Aug 2015
Here, two collagen-binding proteins, CBD-EphA4LBD and CBD-PlexinB1LBD, were constructed, respectively, to neutralize the axon guidance molecules ephrinB3 and sema4D that inhibit the regeneration of nerve fibers.
Novel Functions of Hendra Virus G N-Glycans and Comparisons to Nipah Virus.
Aguilar et al., Pullman, United States. In J Virol, Jul 2015
These two viruses bind the cellular entry receptors ephrin B2 and/or ephrin B3 via the viral attachment glycoprotein G, and the concerted efforts of G and the viral fusion glycoprotein F result in membrane fusion.
EphB3 receptors function as dependence receptors to mediate oligodendrocyte cell death following contusive spinal cord injury.
Liebl et al., Miami, United States. In Cell Death Dis, 2014
Spinal cord injury (SCI) is associated with tissue damage, cellular loss and disturbances in EphB3-ephrinB3 protein balance acutely (days) after the initial impact creating an environment for a dependence receptor-mediated cell death to occur.
EphB3 marks delaminating endocrine progenitor cells in the developing pancreas.
Cleaver et al., Dallas, United States. In Dev Dyn, 2012
these data introduce EphB3 as a new biomarker to identify beta-cells at a critical step during their step-wise differentiation and define the timeframe of endocrine differentiation.
Myelin-derived ephrinB3 restricts axonal regeneration and recovery after adult CNS injury.
Strittmatter et al., New Haven, United States. In Proc Natl Acad Sci U S A, 2012
EphrinB3 contributes to myelin-derived axonal growth inhibition and limits recovery from adult central nervous system trauma.
Ephrin-B2 and ephrin-B3 as functional henipavirus receptors.
Nikolov et al., New York City, United States. In Semin Cell Dev Biol, 2012
Members of the ephrin cell-surface protein family interact with the Eph receptors, the largest family of receptor tyrosine kinases, mediating bi-directional signaling during tumorogenesis and various developmental events.
Bidirectional ephrinB3/EphA4 signaling mediates the segregation of medial ganglionic eminence- and preoptic area-derived interneurons in the deep and superficial migratory stream.
Bolz et al., Jena, Germany. In J Neurosci, 2012
cell contact-mediated bidirectional ephrinB3/EphA4 signaling mediates the sorting of medial ganglionic eminence- and preoptic area-derived interneurons in the deep and superficial migratory stream.
Henipavirus membrane fusion and viral entry.
Iorio et al., Pullman, United States. In Curr Top Microbiol Immunol, 2011
The identification of ephrinB2 and ephrinB3 as henipavirus receptors has paved the way for recent advances in our understanding of henipavirus membrane fusion.
Henipavirus receptor usage and tropism.
Lee et al., Los Angeles, United States. In Curr Top Microbiol Immunol, 2011
HNV use ephrin-B2 and ephrin-B3, highly conserved proteins, as viral entry receptors.
A dual shaping mechanism for postsynaptic ephrin-B3 as a receptor that sculpts dendrites and synapses.
Henkemeyer et al., Dallas, United States. In Nat Neurosci, 2011
This study demonistrated tht ephrin-B reverse signaling into three distinct intracellular pathways and protein-protein interactions that mediate the maturation of postsynaptic neurons.
Enhancement of endogenous neurogenesis in ephrin-B3 deficient mice after transient focal cerebral ischemia.
Bähr et al., Essen, Germany. In Acta Neuropathol, 2011
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.
Modes of paramyxovirus fusion: a Henipavirus perspective.
Ataman et al., Los Angeles, United States. In Trends Microbiol, 2011
Henipavirus is a new genus of Paramyxoviridae that uses protein-based receptors (ephrinB2 and ephrinB3) for virus entry.
Ephrin Bs are essential components of the Reelin pathway to regulate neuronal migration.
Acker-Palmer et al., Frankfurt am Main, Germany. In Nature, 2011
Notably, compound mouse mutants (Reln(+/-); Efnb3(-/-) or Reln(+/-); Efnb2(-/-)) and triple ephrin B1, B2, B3 knockouts show neuronal migration defects that recapitulate the ones observed in the neocortex, hippocampus and cerebellum of the reeler mouse.
Neoadjuvant chemotherapy in Barrett's carcinoma - prognosis and response prediction.
Knoefel et al., Düsseldorf, Germany. In Anticancer Res, 2010
The strongest difference can be seen for tumour necrosis factor, polyribonucleotide nucleotidyltransferase and the ephrin-B3-receptor.
Epitope mapping of antibodies using bacterial surface display.
Ståhl et al., Stockholm, Sweden. In Nat Methods, 2008
We analyzed the binding sites of both monoclonal and polyclonal antibodies directed to three human protein targets: (i) the human epidermal growth factor receptor 2 (HER2), (ii) ephrin-B3 and (iii) the transcription factor SATB2.
Rac-GAP alpha-chimerin regulates motor-circuit formation as a key mediator of EphrinB3/EphA4 forward signaling.
Itohara et al., Wako, Japan. In Cell, 2007
Rac-GAP alpha-chimerin regulates motor-circuit formation as a key mediator of Efnb3 forward signaling.
Role of EphA4 and EphrinB3 in local neuronal circuits that control walking.
Kiehn et al., Göteborg, Sweden. In Science, 2003
conclude that ephrinB3-induced EphA4 signaling repels some components of the mammalian spinal central pattern generators (CPG) and restricts their axonal projections to one side of the spinal cord
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