Evidence map›Paper›PMID 16924230›Full record

ArticleOncogene2007

Apoptin is modified by SUMO conjugation and targeted to promyelocytic leukemia protein nuclear bodies.

K Janssen, T G Hofmann, D A Jans, R T Hay, K Schulze-Osthoff, U Fischer

Abstract read
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In one paragraph

Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. The Role of Apoptin in Chicken Anemia Virus Replication.Pathogens (Basel, Switzerland) · 2020
    Review
  4. Apoptosis Triggered by ORF3 Proteins of theFrontiers in cellular and infection microbiology · 2020
    Review
  5. Review
  6. Article
  7. Article
  8. Viral genes as oncolytic agents for cancer therapy.Cellular and molecular life sciences : CMLS · 2015
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  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

6 authors at 4 institutions in 3 countries.

K JanssenInstitute of Molecular Medicine, Heinrich-Heine-University, Düsseldorf, Germany.
T G Hofmann
D A Jans
R T Hay
K Schulze-Osthoff
U Fischer
Heinrich Heine University Düsseldorf · DEDKFZ-ZMBH Alliance · DEMonash University · AUUniversity of Dundee · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apoptin, a protein of the chicken anemia virus (CAV), represents a novel potential anticancer therapeutic, because it induces apoptotic death specifically in tumor but not normal cells. The cellular localization appears to be crucial for apoptin's selective toxicity. In normal cells apoptin remains in the cytoplasm, whereas in transformed cells it migrates into the nucleus and kills the cell. However, the manner by which apoptin is able to distinguish between tumor and normal cells is unknown. Here, we report for the first time that apoptin interacts directly with the promyelocytic leukemia protein (PML) in tumor cells and accumulates in PML nuclear bodies (NBs), which are involved in apoptosis induction and viral replication. We also demonstrate that apoptin is sumoylated and that a sumoylation-deficient apoptin mutant is no longer recruited to PML-NBs, but localizes in the nuclear matrix. This mutant fails to bind PML, but can still induce apoptosis as efficiently as wild-type apoptin. Moreover, apoptin kills also PML-/- cells and promyelocytic leukemia cells with defective PML expression. Our results therefore suggest that apoptin kills tumor cells independently of PML and sumoylation, however, the interaction of apoptin with PML and small ubiquitin-like modifier (SUMO) proteins might be relevant for CAV replication.

Indexed as

Capsid ProteinsCell LineCell Line, TumorCell NucleusFluorescent Antibody TechniqueHumansImmunoprecipitationNeoplasm ProteinsNuclear ProteinsPromyelocytic Leukemia ProteinSUMO-1 ProteinTranscription FactorsTumor Suppressor ProteinsCapsid ProteinsNeoplasm ProteinsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinSUMO-1 ProteinTranscription FactorsTumor Suppressor ProteinsVP3 protein, Chicken anemia virus

Identifiers

PMID16924230
OpenAlexW1972560438

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.