Evidence map›Paper›PMID 20452955›Full record

ReviewCold Spring Harbor perspectives in biology2010

PML nuclear bodies.

Valérie Lallemand-Breitenbach, Hugues de Thé

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 344 papers.

0numbers the graph read from it
0cells of the map it votes in
344citing papers in PubMed
–field-weighted citation impact
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

344 citing papers in PubMed.

  1. Discovery of novel murine PML isoforms.Nucleus (Austin, Tex.) · 2026
    Article
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  6. Chemical reviews · 2026
    Review
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  17. Biomolecular condensates in immune cell fate.Nature reviews. Immunology · 2025
    Review
  18. Article
  19. Article
  20. Review

284 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

2 authors.

Valérie Lallemand-BreitenbachINSERM/CNRS/Université Paris Diderot/Institut Universitaire Hématologie U944/ UMR7212, Laboratoire associé de la Ligue Nationale contre le Cancer, Hôpital St. Louis, 1, Av. C. Vellefaux 75475 Paris Cedex 10, France.
Hugues de Thé

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PML nuclear bodies are matrix-associated domains that recruit an astonishing variety of seemingly unrelated proteins. Since their discovery in the early 1960s, PML bodies have fascinated cell biologists because of their beauty and their tight association with cellular disorders. The identification of PML, a gene involved in an oncogenic chromosomal translocation, as the key organizer of these domains drew instant interest onto them. The multiple levels of PML body regulation by a specific posttranslational modification, sumoylation, have raised several unsolved issues. Functionally, PML bodies may sequester, modify or degrade partner proteins, but in many ways, PML bodies still constitute an enigma.

Indexed as

Intranuclear Inclusion BodiesAnimalsHumansNuclear ProteinsPromyelocytic Leukemia ProteinProtein Processing, Post-TranslationalTranscription FactorsTranslocation, GeneticTumor Suppressor ProteinsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID20452955
PMCPMC2857171

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.