ArticleStructure (London, England : 1993)2012
Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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Who cites it
72 citing papers in PubMed, 126 citations in OpenAlex.
- Article
- Targeted degradation of the HPV oncoprotein E6 reduces tumor burden in cervical cancer.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Computational analysis of lupenone derivatives as potential inhibitor of human papillomavirus oncoprotein E6 associated cervical cancer.Scientific reports · 2025Article
- DARPin-induced reactivation of p53 in HPV-positive cells.Nature structural & molecular biology · 2025Article
- HPV11E6/E7 induces nasal epithelial hyperplasia through JAK2/STAT3 signaling pathway.European journal of medical research · 2025Article
- [Advances in Multi-omics Analysis of Cervical Cancer].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2025Review
- Structural engineering of stabilized, expanded epitope nanoparticle vaccines for HPV.Frontiers in immunology · 2025Article
- A Self-Amplifying Human Papillomavirus 16 Vaccine Candidate Delivered by Tobacco Mosaic Virus-Like Particles.ACS applied bio materials · 2024Article
- Structure of the p53 degradation complex from HPV16.Nature communications · 2024Article
- Comparative structural studies on Bovine papillomavirus E6 oncoproteins: Novel insights into viral infection and cell transformation from homology modeling and molecular dynamics simulations.Genetics and molecular biology · 2024Article
- SNORD6 promotes cervical cancer progression by accelerating E6-mediated p53 degradation.Cell death discovery · 2023Article
- Viral subversion of the cell polarity regulator Scribble.Biochemical Society transactions · 2023Review
- Deciphering the mechanisms of HPV E6 mutations in the destabilization of E6/E6AP/p53 complex.Biophysical journal · 2022Article
- An enhanced triple fluorescence flow-cytometry-based assay shows differential activation of the Notch signaling pathway by human papillomavirus E6 proteins.Scientific reports · 2022Article
- Human Papillomaviruses as Infectious Agents in Gynecological Cancers. Oncogenic Properties of Viral Proteins.International journal of molecular sciences · 2022Review
- The polymorphism analysis and epitope predicted of Alphapapillomavirus 9 E6 in Sichuan, China.Virology journal · 2022Article
- Maternal HPV Infection: Effects on Pregnancy Outcome.Viruses · 2021Review
- The Not-So-Good, the Bad and the Ugly: HPV E5, E6 and E7 Oncoproteins in the Orchestration of Carcinogenesis.Viruses · 2021Review
- The Dimeric Form of HPV16 E6 Is Crucial to Drive YAP/TAZ Upregulation through the Targeting of hScrib.Cancers · 2021Article
- In Silico Approaches: A Way to Unveil Novel Therapeutic Drugs for Cervical Cancer Management.Pharmaceuticals (Basel, Switzerland) · 2021Review
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The viral oncoprotein E6 is an essential factor for cervical cancers induced by "high-risk" mucosal HPV. Among other oncogenic activities, E6 recruits the ubiquitin ligase E6AP to promote the ubiquitination and subsequent proteasomal degradation of p53. E6 is prone to self-association, which long precluded its structural analysis. Here we found that E6 specifically dimerizes through its N-terminal domain and that disruption of the dimer interface strongly increases E6 solubility. This allowed us to raise structural data covering the entire HPV16 E6 protein, including the high-resolution NMR structures of the two zinc-binding domains of E6 and a robust data-driven model structure of the N-terminal domain homodimer. Interestingly, homodimer interface mutations that disrupt E6 self-association also inactivate E6-mediated p53 degradation. These data suggest that E6 needs to self-associate via its N-terminal domain to promote the polyubiquitination of p53 by E6AP.
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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.