Evidence map›Paper›PMID 8709260›Full record

ArticleJournal of virology1996

Adenovirus early region 4 34-kilodalton protein directs the nuclear localization of the early region 1B 55-kilodalton protein in primate cells.

F D Goodrum, T Shenk, D A Ornelles

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Unveiling the Skin Anti-Aging Potential of the NovelInternational journal of molecular sciences · 2025
    Article
  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. Article
  16. Article
  17. Review
  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

3 authors at 1 institution in 1 country.

F D GoodrumMolecular Genetics Program, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem, North Carolina 27157-1064, USA.
T Shenk
D A Ornelles
Wake Forest University · US

Funding

Tumor Tissue CoreP30CA012197 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Ruben A. Mesa · 1985 to 2026
$55.4M
VIRAL AND CELLULAR ONCOGENES--MECHANISM OF ACTIONP01CA041086 · NCI · PRINCETON UNIVERSITY · PI WIESCHAUS, ERIC F · 1986 to 2005
$9.4M
ADENOVIRUS CONTROL OF MRNA TRANSPORTR29AI035589 · NIAID · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI ORNELLES, DAVID ARNOLD · 1995 to 1999
–
NCI NIH HHS CA-12197NCI NIH HHS CA 41086NIAID NIH HHS AI 35589
6 · The paper itself

Abstract

The localization of the adenovirus type 5 34-kDa E4 and 55-kDa E1B proteins was determined in the absence of other adenovirus proteins. When expressed by transfection in human, monkey, hamster, rat, and mouse cell lines, the E1B protein was predominantly cytoplasmic and typically was excluded from the nucleus. When expressed by transfection, the E4 protein accumulated in the nucleus. Strikingly, when coexpressed by transfection in human, monkey, or baby hamster kidney cells, the E1B protein colocalized in the nucleus with the E4 protein. A complex of the E4 and E1B proteins was identified by coimmunoprecipitation in transfected HeLa cells. By contrast to the interaction observed in primate and baby hamster kidney cells, the E4 protein failed to direct the E1B protein to the nucleus in rat and mouse cell lines as well as CHO and V79 hamster cell lines. This failure of the E4 protein to direct the nuclear localization of the E1B protein in REF-52 rat cells was overcome by fusion with HeLa cells. Within 4 h of heterokaryon formation and with protein synthesis inhibited, a portion of the E4 protein present in the REF-52 nuclei migrated to the HeLa nuclei. Simultaneously, the previously cytoplasmic E1B protein colocalized with the E4 protein in both human and rat cell nuclei. These results suggest that a primate cell-specific factor mediates the functional interaction of the E1B and E4 proteins of adenovirus.

Indexed as

3T3 CellsAdenovirus E1B ProteinsAdenovirus E4 ProteinsAdenoviruses, HumanAnimalsBase SequenceCell LineCell NucleusChlorocebus aethiopsCHO CellsCloning, MolecularCricetinaeFluorescent Antibody Technique, IndirectHeLa CellsHumansMiceAdenovirus E1B ProteinsAdenovirus E4 ProteinsOligodeoxyribonucleotidesRecombinant Proteins

Identifiers

PMID8709260
PMCPMC190658
OpenAlexW2149256718

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.