Unified Nomenclature for Eph Family Receptors and Their Ligands, the Ephrins

  title={Unified Nomenclature for Eph Family Receptors and Their Ligands, the Ephrins},
  author={D. Joe Anderson and Mariano Barbacid and L J Berg and Andrew D Bergemann and Friedrich Bonhoeffer and B B{\"o} and A W Boyd and A W Br{\"a} and Marianne Bronner‐Fraser and Ingrid W Caras and Douglas Pat Cerretti and P. Chambon and Patrick Charnay and H J Cheng and Thomas Ciossek and Ira O. Daar and Samuel Davis and Vishva M. Dixit and Uwe Drescher and Andreas Faissner and John G. Flanagan and Frederick A. Fletcher and Gary M. Fox and Jonas Fris{\'e}n and Nick Gale and Pascale Gilardi-Hebenstreit and Corey S. Goodman and Ali Hemmati‐Brivanlou and Mark Henkemeyer and Hisamura Hirai and Nakisha Holder and Sacha J. Holland and Tony Hunter and Naohiko Ikegaki and R{\"u}diger Klein and Simon Andrea Koblar and Catherine Ellen Krull and R D Lansford and Greg Lemke and Richard A. Lindberg and Stewart D. Lyman and Peter C. Maisonpierre and C Marcelle and Giorgio Miescher and Bruno Monschau and Nicos A. Nicola and M. Angela Nieto and K Ohta and D D O 'leary and Donata Orioli and Elena B. Pasquale and Tony Pawson and Alastair D. Reith and John H. Rogers and Baerbel Rohrer and J R Sanes and T. D. Sargent and Jon B. Scales and B Figure and Homology Sequence and Trees and Eph Receptors and Ephrins Schindelholz and Doyle A. Siever and Klaus Strebhardt and Haruhiko Sugimura and H. Tanaka and X X Tang and Marc Tessier-Lavigne and Axel Ullrich and David M. Valenzuela and Anthony Verderame and V M Wanaka and Andrew A. R. Watt and David Welcher and Ronald Sterne Wilkinson and George Winning and R Yancopoulos and Arthur Zhou and S L Ziemiecki},

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Differential regulation of EphA2 in normal and malignant cells.
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Using structure-based mutagenesis, an extended loop is identified that packs against the concave β-sandwich surface near positions at which missense mutations cause signalling defects, localizing the ligand-binding region on the surface of the receptor.
Ephrins and their Eph receptors: multitalented directors of embryonic development
Although there is a high degree of promiscuity between ephrins and Eph receptors of the same class, they may not be functionally interchangeable and there are considerable differences in binding affinities between different ligand–receptor pairs within the sameclass, suggesting that there may be preferred ligands for certain receptors.
Eph receptors: the bridge linking host and virus
This review focuses on the relationship between Eph receptor family and virus infection that summarize the processes of viruses infecting target cells through Eph receptors and activating its downstream signaling pathways resulting in malignancies.
Expression and Function of the Eph A Receptors and Their Ligands Ephrins A in the Rat Thymus1
Different experimental approaches for analyzing the expression of four members of the Eph A family and their ligands, ephrins A, in the embryonic and adult rat thymus suggest an important role for this family of proteins in the cell mechanisms that drive intrathymic T cell development.
Crystal structure of an Eph receptor–ephrin complex
The crystal structure of the complex formed between EphB2 and ephrin-B2, determined at 2.7 Å resolution, is reported, promoting higher-order clustering and the initiation of bidirectional signalling.
The Value of EphB2 Receptor and Cognate Ephrin Ligands in Prognostic and Predictive Assessments of Human Breast Cancer
The clinical validity of a model whereby EphB2, along with its cognate ephrin ligands, have dual anti- and pro-tumor progression effects is shown, which reinforces the necessity of further biological investigations into Ephs and ephrins, prior to using them in targeted therapies.
Eph receptors are negatively controlled by protein tyrosine phosphatase receptor type O
Using the chick retinotectal projection system, it is shown that Ptpro controls the sensitivity of retinal axons to ephrins and thereby has a crucial role in the establishment of topographic projections.


2 The appropriate text citation for this letter in future publications is as follows: (Eph Nomenclature Committee
  • 2 The appropriate text citation for this letter in future publications is as follows: (Eph Nomenclature Committee
  • 1997
10591-6707. ‡ The Salk Institute
  • † Regeneron Pharmaceuticals