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Cited by 381

The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.

Binding specificities and affinities of egf domains for ErbB receptors

Jones, Jennifer T, Akita, Robert W, Sliwkowski, Mark X·1999·FEBS Letters

Abstract

ErbB receptor activation is a complex process and is dependent upon the type and number of receptors expressed on a given cell. Previous studies with defined combinations of ErbB receptors expressed in mammalian cells have helped elucidate specific biological responses for many of the recognized gene products that serve as ligands for these receptors. However, no study has examined the binding of these ligands in a defined experimental system. To address this issue, the relative binding affinities of the egf domains of eleven ErbB ligands were measured on six ErbB receptor combinations using a soluble receptor‐ligand binding format. The ErbB2/4 heterodimer was shown to bind all ligands tested with moderate to very high affinity. In contrast, ErbB3 showed much more restrictive ligand binding specificity and measurable binding was observed only with heregulin, neuregulin2β, epiregulin and the synthetic heregulin/egf chimera, biregulin. These studies also revealed that ErbB2 preferentially enhances ligand binding to ErbB3 or ErbB4 and to a lesser degree to ErbB1.

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Metadata

Authors
Jones, J. T., Akita, R. W., & Sliwkowski, M. X.
Venue
FEBS Letters
Publisher
Wiley
Published
1999-03-26
Volume
447
Issue
2-3
Pages
227-231
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2083831897
Cited by
381
References
37
FWCI
5.53
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Binding specificities and affinities of egf domains for ErbB receptors. https://app.cochat.ai/papers/10.1016/s0014-5793(99)00283-5
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Jones, J. T., Akita, R. W., & Sliwkowski, M. X. (1999). Binding specificities and affinities of egf domains for ErbB receptors. FEBS Letters. https://doi.org/10.1016/s0014-5793(99)00283-5

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