ArticleJournal of virology1994
Mutation of the bovine papillomavirus E5 oncoprotein at amino acid 17 generates both high- and low-transforming variants.
Article in Journal of virology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- De novo selection of oncogenes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The E5 proteins.Virology · 2013Review
- The human papillomavirus type 16 E5 oncoprotein translocates calpactin I to the perinuclear region.Journal of virology · 2011Article
- The human papillomavirus type 16 E5 oncoprotein inhibits epidermal growth factor trafficking independently of endosome acidification.Journal of virology · 2010Article
- The canine papillomavirus and gamma HPV E7 proteins use an alternative domain to bind and destabilize the retinoblastoma protein.PLoS pathogens · 2010Article
- Membrane orientation of the human papillomavirus type 16 E5 oncoprotein.Journal of virology · 2010Article
- The canine papillomavirus e5 protein signals from the endoplasmic reticulum.Journal of virology · 2009Article
- The bovine papillomavirus E5 protein and the PDGF beta receptor: it takes two to tango.Virology · 2009Review
- Karyopherin beta3: a new cellular target for the HPV-16 E5 oncoprotein.Biochemical and biophysical research communications · 2008Article
- Modulation of cell function by small transmembrane proteins modeled on the bovine papillomavirus E5 protein.Oncogene · 2005Review
- Endoplasmic reticulum-localized human papillomavirus type 16 E5 protein alters endosomal pH but not trans-Golgi pH.Journal of virology · 2005Article
- c-Src activation by the E5 oncoprotein enables transformation independently of PDGF receptor activation.Oncogene · 2002Article
- Role of glutamine 17 of the bovine papillomavirus E5 protein in platelet-derived growth factor beta receptor activation and cell transformation.Journal of virology · 1998Article
- Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein.Journal of virology · 1997Article
- Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Serum- and calcium-induced differentiation of human keratinocytes is inhibited by the E6 oncoprotein of human papillomavirus type 16.Journal of virology · 1996Article
- E5 oncoprotein transmembrane mutants dissociate fibroblast transforming activity from 16-kilodalton protein binding and platelet-derived growth factor receptor binding and phosphorylation.Journal of virology · 1996Article
- Mutational analysis of the beta-type platelet-derived growth factor receptor defines the site of interaction with the bovine papillomavirus type 1 E5 transforming protein.Journal of virology · 1995Article
- Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells.Journal of virology · 1995Article
- E5 oncoprotein retained in the endoplasmic reticulum/cis Golgi still induces PDGF receptor autophosphorylation but does not transform cells.The EMBO journal · 1995Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The E5 transforming protein of bovine papillomavirus type 1 is a 44-amino-acid, hydrophobic protein which localizes predominantly to Golgi membranes. The E5 transmembrane domain contains a highly conserved glutamine residue at position 17 which, from previous limited mutagenic analysis, appeared essential for transforming activity. In order to determine the specific amino acid requirements at this position, we constructed a series of substitution mutants, representing all classes of amino acids, employing a vector which expressed E5 independently of other bovine papillomavirus gene products. All of the expressed E5 mutant proteins were stable, dimerized normally, and localized to the Golgi. Our results obtained with C127 mouse cells demonstrated that acidic amino acids (and serine) increased E5 transforming activity, whereas basic amino acids greatly inhibited E5 activity. Nonpolar amino acid substitutions were also defective. Interestingly, the relative transforming activities of these E5 mutant proteins changed dramatically when assayed with NIH 3T3 cells, suggesting that an auxiliary cellular protein(s) may modulate E5 transformation or that there are additional or different mechanisms of E5 transformation which are utilized in these two cell lines.
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