The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The role of EGF-related peptides in tumor growth
Open accessAbstract
The epidermal growth factor (EGF) family of peptides encodes several proteins that can function as growth factors. The EGF-like peptides, with the exception of proteins of the EGF-CFC subfamily, bind and activate tyrosine kinase receptors that belong to the erbB family. The EGF-like peptides are overexpressed in a majority of human carcinomas as compared with their nontransformed counterpart. By using different approaches, it has been shown that several different EGF-like peptides function as autocrine growth factors in carcinoma cell lines of different histological origin. Direct evidence that the EGF-like growth factors might function as transforming genes has been provided by in vitro and in vivo studies. In particular, the development of different transgenic mouse lines in which EGF-like growth factors have been overexpressed by means of tissue-specific or nonspecific promoters has provided invaluable information relating to their ability to function as dominantly transforming oncogenes. Cooperation of the EGF-like peptides with cellular protooncogenes in determining cell transformation has been demonstrated by using both in vitro and transgenic mice systems. Taken together, these data strongly suggest that the EGF-like peptides are involved in the pathogenesis of human carcinomas, and that they might represent suitable targets for novel therapeutic approaches.
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
Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia
Joutel, A., Corpechot, C., Ducros, A., Vahedi, K., Chabriat, H., Mouton, P., Alamowitch, S., Domenga, V., Cécillion, M., Maréchal, E., et al. (1996) · Nature · doi:10.1038/383707a0 · Cited by 2,068
Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity.
Guy, P. M., Platko, J. V., Cantley, L. C., Cerione, R. A., & Carraway, K. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8132 · Cited by 698 · cited 1×
“This homology is less pronounced for erbB-3 and in fact it has been shown that this receptor has an impaired tyrosine kinase domain (80).”
BackgroundPeles, E., Bacus, S. S., Koski, R. A., Lu, H. S., Wen, D., Ogden, S. G., Levy, R. B., & Yarden, Y. (1992) · Cell · doi:10.1016/0092-8674(92)90131-u · Cited by 524
Higashiyama, S., Lau, K., Besner, G. E., Abraham, J. A., & Klagsbrun, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42682-8 · Cited by 349
Isobe, T., Okuyama, T., Toyoda, H., Komurasaki, T., Uchida, D., Takayama, Y., & Hanada, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7495 · Cited by 269
Cited by
Targeting RAS signalling pathways in cancer therapy
Downward, J. (2003) · Nature Reviews Cancer · doi:10.1038/nrc969 · Cited by 3,256
Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
Li, S., Schmitz, K. R., Jeffrey, P. D., Wiltzius, J. J. W., Kussie, P., & Ferguson, K. M. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.03.003 · Cited by 1,118
Direct small-molecule inhibitors of KRAS: from structural insights to mechanism-based design
Ostrem, J. M. L., & Shokat, K. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.139 · Cited by 641
The function and clinical application of extracellular vesicles in innate immune regulation
Zhou, X., Xie, F., Wang, L., Zhang, L., Zhang, S., Fang, M., & Zhou, F. (2020) · Cellular & Molecular Immunology · doi:10.1038/s41423-020-0391-1 · Cited by 294
Metadata
- Authors
- Normanno, N.
- Venue
- Frontiers in Bioscience
- Publisher
- IMR Press
- Published
- 2001
- Volume
- 6
- Issue
- 3
- Pages
- d685-707
- ISSN
- 1093-4715 (ISSN-L)
- 1093-9946
- DOI
- 10.2741/a635
- OpenAlex
- W1966736953
- Cited by
- 216
- References
- 5
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- bronze
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
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.