Evidence map›Paper›PMID 10938100›Full record

ArticleMolecular and cellular biology2000

The molecular chaperone activity of simian virus 40 large T antigen is required to disrupt Rb-E2F family complexes by an ATP-dependent mechanism.

C S Sullivan, P Cantalupo, J M Pipas

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

65 citing papers in PubMed, 111 citations in OpenAlex.

  1. Review
  2. Article
  3. Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. The Biology and Clinical Features of Cutaneous Polyomaviruses.The Journal of investigative dermatology · 2019
    Review
  12. Breaking Bad: How Viruses Subvert the Cell Cycle.Frontiers in cellular and infection microbiology · 2018
    Review
  13. Viral Oncology: Molecular Biology and Pathogenesis.Journal of clinical medicine · 2017
    Review
  14. Article
  15. Review
  16. J domain independent functions of J proteins.Cell stress & chaperones · 2016
    Review
  17. Article
  18. Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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.

C S SullivanDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
P Cantalupo
J M Pipas
University of Pittsburgh · US

Funding

SV40 T ANTIGEN--ROLE IN VIRUS GROWTH AND TRANSFORMATIONR01CA040586 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PIPAS, JAMES M · 1985 to 2010
$2.7M
GENETIC ANALYSIS OF THE SV40 LARGE TUMOR ANTIGENR37CA040586 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PIPAS, JAMES M · 1988 to 1995
–
NCI NIH HHS CA40586NCI NIH HHS R01 CA040586
6 · The paper itself

Abstract

The simian virus 40 large T antigen (T antigen) inactivates tumor suppressor proteins and therefore has been used in numerous studies to probe the mechanisms that control cellular growth and to generate immortalized cell lines. Binding of T antigen to the Rb family of growth-regulatory proteins is necessary but not sufficient to cause transformation. The molecular mechanism underlying T-antigen inactivation of Rb function is poorly understood. In this study we show that T antigen associates with pRb and p130-E2F complexes in a stable manner. T antigen dissociates from a p130-E2F-4-DP-1 complex, coincident with the release of p130 from E2F-4-DP-1. The dissociation of this complex requires Hsc70, ATP, and a functional T-antigen J domain. We also report that the "released" E2F-DP-1 complex is competent to bind DNA containing an E2F consensus binding site. We propose that T antigen disrupts Rb-E2F family complexes through the action of its J domain and Hsc70. These findings indicate how Hsc70 supports T-antigen action and help to explain the cis requirement for a J domain and Rb binding motif in T-antigen-induced transformation. Furthermore, this is the first demonstration linking Hsc70 ATP hydrolysis to the release of E2F bound by Rb family members.

Indexed as

Cell Cycle ProteinsDNA-Binding ProteinsHSP70 Heat-Shock ProteinsProteinsAdenosine TriphosphateAnimalsAntigens, Viral, TumorBinding SitesCarrier ProteinsCell LineE2F Transcription FactorsElectrophoresis, Polyacrylamide GelHSC70 Heat-Shock ProteinsHydrolysisInsectaModels, BiologicalAdenosine TriphosphateAntigens, Viral, TumorCarrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsE2F Transcription FactorsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesPhosphoproteinsProteinsRetinoblastoma-Binding Protein 1Retinoblastoma-Like Protein p130Retinoblastoma ProteinTranscription Factor DP1Transcription Factors

Identifiers

PMID10938100
PMCPMC86098
OpenAlexW2150815282

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.