ArticleJournal of virology1995
The adenovirus E3 10.4K and 14.5K proteins, which function to prevent cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor, are localized in the plasma membrane.
Article in Journal of virology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
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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.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
- A bivalent live-attenuated vaccine candidate elicits protective immunity against human adenovirus types 4 and 7.Emerging microbes & infections · 2021Article
- How do viruses control mitochondria-mediated apoptosis?Virus research · 2015Review
- STAT1 interaction with E3-14.7K in monocytes affects the efficacy of oncolytic adenovirus.Journal of virology · 2014Article
- The cytomegaloviral protein pUL138 acts as potentiator of tumor necrosis factor (TNF) receptor 1 surface density to enhance ULb'-encoded modulation of TNF-α signaling.Journal of virology · 2011Article
- Open reading frame E3-10.9K of subspecies B1 human adenoviruses encodes a family of late orthologous proteins that vary in their predicted structural features and subcellular localization.Journal of virology · 2010Article
- Adenovirus RIDalpha regulates endosome maturation by mimicking GTP-Rab7.The Journal of cell biology · 2007Article
- A tyrosine-based signal plays a critical role in the targeting and function of adenovirus RIDalpha protein.Journal of virology · 2007Article
- Adenovirus RIDalphabeta complex inhibits lipopolysaccharide signaling without altering TLR4 cell surface expression.Journal of virology · 2006Article
- Mechanism for removal of tumor necrosis factor receptor 1 from the cell surface by the adenovirus RIDalpha/beta complex.Journal of virology · 2005Article
- Functional interactions of antiapoptotic proteins and tumor necrosis factor in the context of a replication-competent adenovirus.Gene therapy · 2005Article
- Inhibition of tumor necrosis factor (TNF) signal transduction by the adenovirus group C RID complex involves downregulation of surface levels of TNF receptor 1.Journal of virology · 2004Article
- Adenovirus E3-6.7K protein is required in conjunction with the E3-RID protein complex for the internalization and degradation of TRAIL receptor 2.Journal of virology · 2004Article
- Distinct domains in the adenovirus E3 RIDalpha protein are required for degradation of Fas and the epidermal growth factor receptor.Journal of virology · 2003Article
- To kill or be killed: viral evasion of apoptosis.Nature immunology · 2002Review
- Adenovirus RIDbeta subunit contains a tyrosine residue that is critical for RID-mediated receptor internalization and inhibition of Fas- and TRAIL-induced apoptosis.Journal of virology · 2002Article
- The adenovirus E3 RID complex protects some cultured human T and B lymphocytes from Fas-induced apoptosis.Journal of virology · 2002Article
- Inhibition of TRAIL-induced apoptosis and forced internalization of TRAIL receptor 1 by adenovirus proteins.Journal of virology · 2001Article
- Review
- The adenovirus E3-10.4K/14.5K complex mediates loss of cell surface Fas (CD95) and resistance to Fas-induced apoptosis.Journal of virology · 1997Article
- Tumor necrosis factor alpha plays a central role in immune-mediated clearance of adenoviral vectors.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The adenovirus type 2 and 5 E3 10,400- and 14,500-molecular-weight (10.4K and 14.5K) proteins are both required to protect some cell lines from lysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor. We have shown previously that both 10.4K and 14.5K are integral membrane proteins and that 14.5K is phosphorylated and O glycosylated. The 10.4K protein coimmunoprecipitates with 14.5K, indicating that the two proteins function as a complex. Here we show, using immunofluorescence and two different cell surface-labeling techniques, that both proteins are localized in the plasma membrane. In addition, we show that trafficking of each protein to the plasma membrane depends on concomitant expression of the other protein. Finally, neither protein could be immunoprecipitated from conditioned media, indicating that neither is secreted. Taken together, these results suggest that the plasma membrane is the site at which 10.4K and 14.5K function to inhibit cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor.
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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.