Evidence map›Paper›PMID 1850036›Full record

ArticleJournal of virology1991

Adenovirus E3 14.7K protein functions in the absence of other adenovirus proteins to protect transfected cells from tumor necrosis factor cytolysis.

T M Horton, T S Ranheim, L Aquino, D I Kusher, S K Saha, C F Ware, W S Wold, L R Gooding

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 78 citations in OpenAlex.

  1. Adenoviral E3/49K: CD45-targeted immune evasion and therapeutic potential.Frontiers in cellular and infection microbiology · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

T M HortonDepartment of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322.
T S Ranheim
L Aquino
D I Kusher
S K Saha
C F Ware
W S Wold
L R Gooding
Emory University · US

Funding

MECHANISM OF ADENOVIRUS-INDUCED TNF RESISTANCER01CA048219 · NCI · EMORY UNIVERSITY · PI GOODING, LINDA R · 1988 to 1991
–
MOLECULAR MECHANISMS OF TNF-ADENOVIRUS INTERACTIONSU01AI026035 · NIAID · EMORY UNIVERSITY · PI GOODING, LINDA R · 1988 to 1991
–
NCI NIH HHS CA48219NIAID NIH HHS AI26035
6 · The paper itself

Abstract

A 14,700-kDa protein (14.7K) encoded by the E3 region of adenovirus has been shown to protect adenovirus-infected mouse C3HA cells from lysis by tumor necrosis factor (TNF) (L. R. Gooding, L. W. Elmore, A. E. Tollefson, H. A. Brady, and W. S. M. Wold, Cell 53:341-346, 1988). These infected cells are sensitized to TNF by expression of the adenovirus E1A proteins (P. Duerksen-Hughes, W. S. M. Wold, and L. R. Gooding, J. Immunol. 143:4193-4200, 1989). In this study we show that 14.7K suppresses TNF cytolysis independently of adenovirus infection. Mouse C3HA and C127 cells were transfected with the 14.7K gene controlled by the mouse metallothionein promoter, and permanent 14.7K-expressing cell lines were tested for sensitivity to TNF cytolysis. Transfected cells which were sensitized to TNF either by inhibitors of protein synthesis, microfilament-destabilizing agents, or adenovirus infection were found to be resistant to TNF cytolysis. Two monoclonal antibodies were isolated and used to quantitate 14.7K in transfected and infected cells. Enzyme-linked immunosorbent assay (ELISA) analysis with these monoclonal antibodies and 14.7K immunoblots showed that 14.7K expression can be induced with cadmium in C3HA and C127 transfectants. The 14.7K induction correlated with a dose-dependent decrease in sensitivity to TNF cytotoxicity. The 14.7K protein does not substantially alter cell surface TNF receptor numbers or affinity on C3HA mouse fibroblasts, as determined by Scatchard analysis of 125I-TNF binding. The 14.7K protein also does not alter TNF signal transduction in general, because TNF induction of cell surface class I major histocompatibility complex molecules on 14.7K transfectants was unmodified. Our findings indicate that the adenovirus 14.7K protein functions as a specific inhibitor of TNF cytolysis in the absence of other adenovirus proteins and thus is a unique tool to study the mechanism of TNF cytotoxicity.

Indexed as

TransfectionAdenoviridaeAdenovirus Early ProteinsAnimalsCadmiumCell LineEnzyme-Linked Immunosorbent AssayGenes, ViralImmunoblottingMajor Histocompatibility ComplexMiceOncogene Proteins, ViralReceptors, Cell SurfaceReceptors, Tumor Necrosis FactorSignal TransductionTumor Cells, CulturedAdenovirus Early ProteinsCadmiumOncogene Proteins, ViralReceptors, Cell SurfaceReceptors, Tumor Necrosis FactorTumor Necrosis Factor-alpha

Identifiers

PMID1850036
PMCPMC240621
OpenAlexW1916905989

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.