ArticleJournal of virology2008
The interaction between human papillomavirus type 16 and FADD is mediated by a novel E6 binding domain.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
19 citing papers in PubMed, 34 citations in OpenAlex.
- 30-hydroxygambogic acid activates overlapping and independent apoptotic pathways in HPV positive and HPV negative oral cancer cells.Tumour virus research · 2026Article
- Protein-DNA Interactions Regulate Human Papillomavirus DNA Replication, Transcription, and Oncogenesis.International journal of molecular sciences · 2023Review
- PPI Modulators of E6 as Potential Targeted Therapeutics for Cervical Cancer: Progress and Challenges in Targeting E6.Molecules (Basel, Switzerland) · 2021Review
- A high-content AlphaScreen™ identifies E6-specific small molecule inhibitors as potential therapeutics for HPVOncotarget · 2021Article
- Effects of HPV16 E6 protein on Daxx-induced apoptosis in C33A cells.Cellular & molecular biology letters · 2020Article
- The Association and Significance of p53 in Gynecologic Cancers: The Potential of Targeted Therapy.International journal of molecular sciences · 2019Review
- Identification of potential binding pocket on viral oncoprotein HPV16 E6: a promising anti-cancer target for small molecule drug discovery.BMC molecular and cell biology · 2019Article
- [Analysis of the current status of research on human papillomavirus-associated head and neck cancers based on recent Chinese literature].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2017Review
- Expression of FADD and cFLIPMolecular and cellular biochemistry · 2016Article
- FADD regulates NF-κB activation and promotes ubiquitination of cFLIPL to induce apoptosis.Scientific reports · 2016Article
- Flavonol and imidazole derivatives block HPV16 E6 activities and reactivate apoptotic pathways in HPV⁺ cells.Cell death & disease · 2016Article
- Review
- hpvPDB: An Online Proteome Reserve for Human Papillomavirus.Genomics & informatics · 2013Article
- Modulation of apoptotic pathways by human papillomaviruses (HPV): mechanisms and implications for therapy.Viruses · 2012Review
- Small molecule inhibitors of the HPV16-E6 interaction with caspase 8.Bioorganic & medicinal chemistry letters · 2012Article
- The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.Molecular biology of the cell · 2010Article
- Review
- The full-length isoform of human papillomavirus 16 E6 and its splice variant E6* bind to different sites on the procaspase 8 death effector domain.Journal of virology · 2010Article
- Papillomavirus E6 proteins.Virology · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
High-risk strains of human papillomavirus, such as types 16 and 18, have been etiologically linked to cervical cancer. Most cervical cancer tissues are positive for both the E6 and E7 oncoproteins, since it is their cooperation that results in successful transformation and immortalization of infected cells. We have reported that E6 binds to tumor necrosis factor receptor 1 and to Fas-associated death domain (FADD) and, in doing so, prevents E6-expressing cells from responding to apoptotic stimuli. The binding site of E6 to FADD localizes to the first 23 amino acids of FADD and has now been further characterized by the use of deletion and site-directed mutants of FADD in pull-down and functional assays. The results from these experiments revealed that mutations of serine 16, serine 18, and leucine 20 obstruct FADD binding to E6, suggesting that these residues are part of the E6 binding domain on FADD. Because FADD does not contain the two previously identified E6 binding motifs, the LxxphiLsh motif, and the PDZ motif, a novel binding domain for E6 has been identified on FADD. Furthermore, peptides that correspond to this region can block E6/FADD binding in vitro and can resensitize E6-expressing cells to apoptotic stimuli in vivo. These results demonstrate the existence of a novel E6 binding domain.
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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.