ArticleThe EMBO journal1997
The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 80 citations in OpenAlex.
- The Role of Eph/Ephrin-Driven Actomyosin Contractility in Promoting Cell Segregation and Boundary Formation.International journal of molecular sciences · 2026Review
- Beyond cell-cell contact: therapeutic potential of Eph signaling in central nervous system tumors.Frontiers in molecular neuroscience · 2025Review
- Potential role of the Eph/ephrin system in colorectal cancer: emerging druggable molecular targets.Frontiers in oncology · 2024Review
- Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Review
- Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors.International journal of molecular sciences · 2021Review
- Roles of Eph/ephrin bidirectional signaling in central nervous system injury and recovery.Experimental and therapeutic medicine · 2018Article
- Tie2 and Eph receptor tyrosine kinase activation and signaling.Cold Spring Harbor perspectives in biology · 2014Review
- Biochemical and biophysical characterization of four EphB kinase domains reveals contrasting thermodynamic, kinetic and inhibition profiles.Bioscience reports · 2013Article
- Eph-dependent cell-cell adhesion and segregation in development and cancer.Cellular and molecular life sciences : CMLS · 2012Review
- Structure of the ligand-binding domain of the EphB2 receptor at 2 A resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Differential regulation of EphA2 in normal and malignant cells.The American journal of pathology · 2003Review
- The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner.Molecular and cellular biology · 2001Article
- Review
- Polydom: a secreted protein with pentraxin, complement control protein, epidermal growth factor and von Willebrand factor A domains.The Biochemical journal · 2000Article
- Roles of Eph receptors and ephrins in segmental patterning.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2000Review
- Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors.Molecular and cellular biology · 2000Article
- Fibroblast growth factor receptor-mediated rescue of x-ephrin B1-induced cell dissociation in Xenopus embryos.Molecular and cellular biology · 2000Article
- Growth factor signaling pathways in vascular development.Oncogene · 1999Review
- Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through alphavbeta3 and alpha5beta1 integrins.The EMBO journal · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Eph family of receptor protein-tyrosine kinases (RTKs) have recently been implicated in patterning and wiring events in the developing nervous system. Eph receptors are unique among other RTKs in that they fall into two large subclasses that show distinct ligand specificities and for the fact that they themselves might function as 'ligands', thereby activating bidirectional signaling. To gain insight into the mechanisms of ligand-receptor interaction, we have mapped the ligand binding domain in Eph receptors. By using a series of deletion and domain substitution mutants, we now report that an N-terminal globular domain of the Nuk/Cek5 receptor is the ligand binding domain of the transmembrane ligand Lerk2. Using focus formation assays, we show that the Cek5 globular domain is sufficient to confer Lerk2-dependent transforming activity on the Cek9 orphan receptor. Extending our binding studies to other members of both subclasses of receptors, it became apparent that the same domain is used for binding of both transmembrane and glycosylphosphatidyl-anchored ligands. Our 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.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.