Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor (Q28241723)

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R J Mann

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L Kravets

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F M Smith

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T A Bucci

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K F Maxwell

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G J Howlett

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J E Olsson

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T Vanden Bos

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D P Cerretti

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A W Boyd

Journal of Biological Chemistry

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language of work or name

English

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publication date

27 June 1997

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published in

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volume

272

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issue

26

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page(s)

16521-30

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cites work

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Cell signalling. Receptor orphans find a family

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Eph receptor tyrosine kinases, axon repulsion, and the development of topographic maps.

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A novel putative tyrosine kinase receptor encoded by the eph gene

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Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines

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Identification and cloning of ELF-1, a developmentally expressed ligand for the Mek4 and Sek receptor tyrosine kinases

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In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases

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Purification of a ligand for the EPH-like receptor HEK using a biosensor-based affinity detection approach

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Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation

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Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity

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The gene encoding LERK-7 (EPLG7, Epl7), a ligand for the Eph-related receptor tyrosine kinases, maps to human chromosome 5 at band q21 and to mouse chromosome 17.

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Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity

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Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases

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Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase

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B61 is a ligand for the ECK receptor protein-tyrosine kinase

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Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk

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Molecular cloning of two novel transmembrane ligands for Eph-related kinases (LERKS) that are related to LERK-2.

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Use of a biosensor with surface plasmon resonance detection for the determination of binding constants: measurement of interleukin-6 binding to the soluble interleukin-6 receptor.

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Characterization of two novel pre-B-cell lines (LK63 and LiLa-1): potential models of pre-B-cell differentiation

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cDNA cloning and characterization of a Cek7 receptor protein-tyrosine kinase ligand that is identical to the ligand (ELF-1) for the Mek-4 and Sek receptor protein-tyrosine kinases

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Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics.

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Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis

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Consequences of ligand bivalency in interactions involving particulate receptors: equilibrium and kinetic studies with Sephadex-concanavalin A, butylagarose-phosphorylase b, and Fc receptor-IgG dimer interactions as model systems

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Dissociation kinetics of bivalent ligand-immunoglobulin E aggregates in solution.

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Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus

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Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance

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Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods.

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Influence of interleukin-6 (IL-6) dimerization on formation of the high affinity hexameric IL-6.receptor complex.

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Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-alpha-induced angiogenesis

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Complementary gradients in expression and binding of ELF-1 and Mek4 in development of the topographic retinotectal projection map

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Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera

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Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis

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Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system

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