ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface
Open Access
- 15 June 2004
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 569 (1-3), 332-336
- https://doi.org/10.1016/j.febslet.2004.06.014
Abstract
To understand signaling by the neuregulin (NRG) receptor ErbB3/HER3, it is important to know whether ErbB3 forms homodimers upon ligand binding. Previous biophysical studies suggest that the ErbB3 ex...Keywords
This publication has 32 references indexed in Scilit:
- The ErbB receptors and their role in cancer progressionExperimental Cell Research, 2003
- Structure of the extracellular region of HER2 alone and in complex with the Herceptin FabNature, 2003
- Structure of the Extracellular Region of HER3 Reveals an Interdomain TetherScience, 2002
- Extracellular domains drive homo- but not hetero-dimerization of erbB receptorsThe EMBO Journal, 2000
- NEW EMBO MEMBERS' REVIEW: The ErbB signaling network: receptor heterodimerization in development and cancerThe EMBO Journal, 2000
- The oncogenic ErbB-2/ErbB-3 heterodimer is a surrogate receptor of the epidermal growth factor and betacellulinOncogene, 1998
- ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signalingThe EMBO Journal, 1997
- Neu Differentiation Factor/Neuregulin Isoforms Activate Distinct Receptor CombinationsPublished by Elsevier ,1996
- The Epidermal Growth Factor Receptor Couples Transforming Growth Factor-α, Heparin-binding Epidermal Growth Factor-like Factor, and Amphiregulin to Neu, ErbB-3, and ErbB-4Published by Elsevier ,1996
- Binding of Neu Differentiation Factor with the Extracellular Domain of Her2 and Her3Published by Elsevier ,1995