The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms.
Open accessAbstract
Neu differentiation factor (NDF or heregulin) elevates tyrosine phosphorylation of the ErbB-2 receptor tyrosine kinase, and it was, therefore, thought to function as a ligand of this receptor. However, several lines of evidence raised the possibility that the interaction between NDF and ErbB-2 involves another molecule, which belongs to the family of epidermal growth factor receptors. To address this question we constructed soluble chimeric proteins between alkaline phosphatase and the extracellular domains of ErbB-2 and either ErbB-3 or ErbB-4, two newly recognized members of the epidermal growth factor receptor family. Using the soluble proteins we found that beta isoforms of NDF specifically bind to the ErbB-3 and ErbB-4 receptors but not to the soluble ErbB-2 protein. When ectopically expressed in monkey fibroblasts, the full-length ErbB-3 and ErbB-4 receptors conferred specific binding to NDF. In these cells ErbB-3 displayed lower ligand binding affinity than ErbB-4, but like the latter receptor it preferred to bind the beta isoform over the alpha class of NDFs. These results indicate that both ErbB-3 and ErbB-4 function as physiological receptors of all NDF isoforms and suggest that a still unknown ligand of ErbB-2 exists.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Slamon, D. J., Clark, G. M., Wong, S. G., Levin, W. J., Ullrich, A., & McGuire, W. L. (1987) · Science · doi:10.1126/science.3798106 · Cited by 11,760
Studies of the HER-2/ neu Proto-Oncogene in Human Breast and Ovarian Cancer
Slamon, D. J., Godolphin, W., Jones, L. A., Holt, J. A., Wong, S. G., Keith, D. E., Levin, W. J., Stuart, S. G., Udove, J., Ullrich, A., et al. (1989) · Science · doi:10.1126/science.2470152 · Cited by 6,816
Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435
Aaronson, S. A. (1991) · Science · doi:10.1126/science.1659742 · Cited by 2,028
Identification of Heregulin, a Specific Activator of p185 erbB2
Holmes, W. E., Sliwkowski, M. X., Akita, R. W., Henzel, W. J., Lee, J., Park, J. W., Yansura, D., Abadi, N., Raab, H., Lewis, G. D., et al. (1992) · Science · doi:10.1126/science.256.5060.1205 · Cited by 962
The kit ligand: A cell surface molecule altered in steel mutant fibroblasts
Flanagan, J. G., & Leder, P. (1990) · Cell · doi:10.1016/0092-8674(90)90299-t · Cited by 748
Glial growth factors are alternatively spliced erbB2 ligands expressed in the nervous system
Marchionni, M. A., Goodearl, A. D. J., Su Chen, M., Bermingham-McDonogh, O., Kirk, C., Hendricks, M., Danehy, F., Misumi, D., Sudhalter, J., Kobayashi, K., et al. (1993) · Nature · doi:10.1038/362312a0 · Cited by 738
Kraus, M. H., Issing, W., Miki, T., Popescu, N. C., & Aaronson, S. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.23.9193 · Cited by 737
Plowman, G. D., Culouscou, J. M., Whitney, G. S., Green, J. M., Carlton, G. W., Foy, L., Neubauer, M. G., & Shoyab, M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1746 · Cited by 713
Falls, D. (1993) · Cell · doi:10.1016/0092-8674(93)90407-h · Cited by 607
Cited by
Klapper, L. N., Glathe, S., Vaisman, N., Hynes, N. E., Andrews, G. C., Sela, M., & Yarden, Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4995 · Cited by 455
Metadata
- Authors
- Tzahar, E., Levkowitz, G., Karunagaran, D., Yi, L., Peles, E., Lavi, S., Chang, D., Liu, N., Yayon, A., & Wen, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-10
- Volume
- 269
- Issue
- 40
- Pages
- 25226-25233
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1562926557
- Cited by
- 272
- References
- 25
- FWCI
- 10.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms. https://app.cochat.ai/papers/10.1016/s0021-9258(17)31521-1
- The paper
- Tzahar, E., Levkowitz, G., Karunagaran, D., Yi, L., Peles, E., Lavi, S., Chang, D., Liu, N., Yayon, A., & Wen, D. (1994). ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)31521-1
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
