Eph Receptors and Ligands Comprise Two Major Specificity Subclasses and Are Reciprocally Compartmentalized during Embryogenesis

  title={Eph Receptors and Ligands Comprise Two Major Specificity Subclasses and Are Reciprocally Compartmentalized during Embryogenesis},
  author={Nicholas W. Gale and Sacha J. Holland and David M. Valenzuela and Ann M. Flenniken and Li Pan and Terrence E Ryan and Mark Henkemeyer and Klaus Strebhardt and Hisamaru Hirai and David G. Wilkinson and Tony Pawson and Samuel Davis and George D. Yancopoulos},

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Ephrins and their Eph receptors: multitalented directors of embryonic development
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Ephrins and their Receptors: Binding versus Biology
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Multiple roles of Eph-like kinases and their ligands during development
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Differential regulation of EphA2 in normal and malignant cells.
The N‐terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling
The studies have determined the first structural elements involved in ligand–receptor interaction and will allow more fine‐tuned genetic experiments to elucidate the mechanism of action of these important guidance molecules.
Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2
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Eph receptors and ephrins: regulators of guidance and assembly.


Elk-L3, a novel transmembrane ligand for the Eph family of receptor tyrosine kinases, expressed in embryonic floor plate, roof plate and hindbrain segments.
The identification and characterization of the third, and most divergent, member of the transmembrane group of Eph ligands, which is term Elk-L3 (Elk-related receptor ligand number 3), which is notable for its remarkably restricted and prominent expression in the floor plate and roof plate of the developing neural tube and its rhombomere-specificexpression in the developing hindbrain.
Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity.
A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified, suggesting that they require direct cell-to-cell contact to activate their receptors.
eph, the largest known family of putative growth factor receptors.
The recently discovered family of RTKs termed Eph, which currently consists of seven distinct members, eph, eck, elk, cek5, mek4/cek 4/hek, sek and hek2, all of whose cDNAs have been fully sequenced, appears to be the largest known family ofRTKs.
ELF-2, a new member of the Eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites
A new member of the Eph ligand family is described, designated ELF-2, which shows closest homology to the other known transmembrane ligand in the family, ELK-L/LERK-2/Cek5-L, with 57% identity in the extracellular domain and striking homology in the cytoplasmic domain.
Membrane‐bound LERK2 ligand can signal through three different Eph‐related receptor tyrosine kinases.
Preliminary mutagenesis of the LERK2 protein suggests a negative regulatory role for its cytoplasmic domain in LerK2 signaling, which is shown to signal through three different Eph‐related receptors, namely Cek5, Cek10 and Elk.
Identification of full-length and truncated forms of Ehk-3, a novel member of the Eph receptor tyrosine kinase family.
The identification and characterization of a novel member of the Eph receptor family is described, which is termed Ehk-3 for Eph Homologous Kinase 3, which displays all the major structural features shared by other members of theEph family, including a cysteine-rich region and tandem fibronectin type-III domains in its extracellular portion.
A novel putative tyrosine kinase receptor encoded by the eph gene.
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Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins.
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