Evidence map›Paper›PMID 7542742›Full record

ArticleMolecular and cellular biology1995

Association of insulin receptor substrate 1 with simian virus 40 large T antigen.

Z L Fei, C D'Ambrosio, S Li, E Surmacz, R Baserga

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

30 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Review
  3. Inhibition of Cullin-RING E3 ubiquitin ligase 7 by simian virus 40 large T antigen.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  4. Article
  5. Nuclear IRS-1 and cancer.Journal of cellular physiology · 2012
    Review
  6. Article
  7. Article
  8. Article
  9. Deactivation of Akt by a small molecule inhibitor targeting pleckstrin homology domain and facilitating Akt ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Review
  11. Article
  12. Article
  13. Article
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  15. Article
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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

5 authors at 1 institution in 1 country.

Z L FeiJefferson Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
C D'Ambrosio
S Li
E Surmacz
R Baserga
Thomas Jefferson University · US

Funding

BIOLOGY OF THE PROLIFERATING CELL NUCLEAR ANTIGENR01CA053484 · NCI · THOMAS JEFFERSON UNIVERSITY · PI BASERGA, RENATO LUIGI · 1991 to 2000
$179k
BIOLOGY OF THE P53 PROTEINR01GM033694 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI BASERGA, RENATO LUIGI · 1985 to 1999
–
NCI NIH HHS CA 53484NIGMS NIH HHS GM 33694
6 · The paper itself

Abstract

Mouse embryo cells expressing a wild-type number of insulin-like growth factor I receptors (IGF-IR) (W cells) can be transformed either by simian virus 40 large T antigen (SV40 T) or by overexpressed insulin receptor substrate 1 (IRS-1), singly transfected. Neither SV40 T antigen nor IRS-1, individually, can transform mouse embryo cells with a targeted disruption of the IGF-IR genes (R- cells). However, cotransfection of SV40 T antigen and IRS-1 does transform R- cells. In this study, using different antibodies and different cell lines, we found that SV40 T antigen and IRS-1 are coprecipitated from cell lysates in a specific fashion, regardless of whether the lysates are immunoprecipitated with an antibody to SV40 T antigen or an antibody to IRS-1. The same antibody to SV40 T antigen, however, fails to coprecipitate another substrate of IGF-IR, the transforming protein Shc, and two other signal-transducing molecules, Grb2 and Sos. Finally, an SV40 T antigen lacking the amino-terminal 250 amino acids fails to coprecipitate IRS-1 and also fails to transform R- cells overexpressing mouse IRS-1. These experiments indicate that IRS-1 associates with SV40 T antigen and that this association plays a critical role in the combined ability of these proteins to transform R- cells. This finding is discussed in light of the crucial role of the IGF-IR in the establishment and maintenance of the transformed phenotype.

Indexed as

Cell Transformation, Neoplastic3T3 CellsAnimalsAntigens, Viral, TumorInsulin Receptor Substrate ProteinsMiceMice, Inbred BALB CPeptide FragmentsPhosphoproteinsPrecipitin TestsProtein BindingProto-Oncogene Proteins pp60(c-src)Receptor, IGF Type 1Sequence HomologySignal TransductionSimian virus 40Antigens, Viral, TumorInsulin Receptor Substrate ProteinsIrs1 protein, mousePeptide FragmentsPhosphoproteinsProto-Oncogene Proteins pp60(c-src)Receptor, IGF Type 1

Identifiers

PMID7542742
PMCPMC230662
OpenAlexW2122312605

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.