The DOI matches its Crossref record.
Dimerization of the Human Papillomavirus E7 Oncoproteinin Vivo
Abstract
We have used a yeast two-hybrid system to show that human papillomavirus E7 proteins can form oligomeric complexes in vivo. The carboxyl-terminal cysteine-rich metal-binding domain is critical for this activity although amino-terminal sequences also contribute to oligomerization. Our experiments also reveal that E7 possesses an intrinsic transcription activation activity in yeast, which resides in the amino terminus of the protein.
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“E7 has also been shown to form dimers [62,67,68], tetramers [69] and higher order oligomers [70,71]”
From The Not-So-Good, the Bad and the Ugly: HPV E5, E6 and E7 Oncoproteins in the Orchestration of Carcinogenesis (2021) · cites this paper as [68]
Citations
Cited by
Basukala, O., & Banks, L. (2021) · Viruses · doi:10.3390/v13101892 · Cited by 137
Metadata
- Authors
- CLEMENS, K. E., BRENT, R., GYURIS, J., & MÜNGER, K.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 214
- Issue
- 1
- Pages
- 289-293
- ISSN
- 0042-6822
- Cited by
- 52
- References
- 0
- Language
- en
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