ArticleOncogene2002
c-Src activation by the E5 oncoprotein enables transformation independently of PDGF receptor activation.
Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Review
- The E5 proteins.Virology · 2013Review
- Molecular mechanisms underlying the apoptotic effect of KCNB1 K+ channel oxidation.The Journal of biological chemistry · 2013Article
- Papillomavirus E5: the smallest oncoprotein with many functions.Molecular cancer · 2011Review
- The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango.Virology · 2009Review
- Koilocytosis: a cooperative interaction between the human papillomavirus E5 and E6 oncoproteins.The American journal of pathology · 2008Article
- Karyopherin beta3: a new cellular target for the HPV-16 E5 oncoprotein.Biochemical and biophysical research communications · 2008Article
- Transcriptional changes induced by bovine papillomavirus type 1 in equine fibroblasts.Journal of virology · 2008Article
- Productive interaction between transmembrane mutants of the bovine papillomavirus E5 protein and the platelet-derived growth factor beta receptor.Journal of virology · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The E5 oncoprotein of bovine papillomavirus type 1 is a Golgi-resident, hydrophobic polypeptide that can transform immortalized fibroblasts by activating endogenous platelet-derived growth factor receptor beta (PDGF-R). However, the existence of E5 mutants that dissociate transformation from PDGF-R activation implies that there are additional mechanism(s) by which E5 can transform cells. We now show that both wt E5, and transforming E5 mutants that are defective for PDGF-R activation, constitutively activate endogenous c-Src in NIH3T3 cell lines to levels normally associated with acute growth factor stimulation. The ubiquitous Src family protein tyrosine kinase (PTK) Fyn is not activated by these E5 constructs, nor are focal adhesion kinase and endogenous receptor PTKs for insulin, epidermal growth factor, basic fibroblast growth factor and insulin-like growth factor. We further demonstrate that transforming activity of the L26A E5 mutant, which is highly defective for PDGF-R activation, depends on its ability to activate Src. L26A E5 does not transform SYF cells that are deficient for Src, Fyn and Yes, unless Src expression is reconstituted, and does not transform NIH3T3 cells in which Src PTK activity is maintained at a basal level by means of kinase-defective K295R Src overexpression.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.