Evidence map›Paper›PMID 17608567›Full record

ArticlePLoS biology2007

Structural basis of PP2A inhibition by small t antigen.

Uhn Soo Cho, Seamus Morrone, Anna A Sablina, Jason D Arroyo, William C Hahn, Wenqing Xu

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Review
  3. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. PP2A Phosphatase as an Emerging Viral Host Factor.Frontiers in cellular and infection microbiology · 2021
    Review
  19. Article
  20. Article

15 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

6 authors at 3 institutions in 1 country.

Uhn Soo ChoDepartment of Biological Structure, University of Washington, Seattle, Washington, United States of America.
Seamus Morrone
Anna A Sablina
Jason D Arroyo
William C Hahn
Wenqing Xu
University of Washington · USBroad Institute · USDana-Farber Cancer Institute · US

Funding

VIRAL ONCOPROTEIN PERTURBATION OF RB/E2F PATHWAYP01CA050661 · NCI · DANA-FARBER CANCER INSTITUTE · PI HOWLEY, PETER M · 1989 to 2013
$35.8M
NCI NIH HHS P01 CA050661NCI NIH HHS P01 CA50661
6 · The paper itself

Abstract

The SV40 small t antigen (ST) is a potent oncoprotein that perturbs the function of protein phosphatase 2A (PP2A). ST directly interacts with the PP2A scaffolding A subunit and alters PP2A activity by displacing regulatory B subunits from the A subunit. We have determined the crystal structure of full-length ST in complex with PP2A A subunit at 3.1 A resolution. ST consists of an N-terminal J domain and a C-terminal unique domain that contains two zinc-binding motifs. Both the J domain and second zinc-binding motif interact with the intra-HEAT-repeat loops of HEAT repeats 3-7 of the A subunit, which overlaps with the binding site of the PP2A B56 subunit. Intriguingly, the first zinc-binding motif is in a position that may allow it to directly interact with and inhibit the phosphatase activity of the PP2A catalytic C subunit. These observations provide a structural basis for understanding the oncogenic functions of ST.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsAntigens, Viral, TumorBinding SitesCrystallography, X-RayDNA Mutational AnalysisHumansMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingProtein Phosphatase 2Protein SubunitsSequence AlignmentAntigens, Viral, TumorProtein Phosphatase 2Protein Subunits

Identifiers

PMID17608567
PMCPMC1945078
OpenAlexW2101038605

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.