Evidence map›Paper›PMID 22139926›Full record

ArticleNucleic acids research2012

The N-terminal domains of TRF1 and TRF2 regulate their ability to condense telomeric DNA.

Anaïs Poulet, Sabrina Pisano, Cendrine Faivre-Moskalenko, Bei Pei, Yannick Tauran, Zofia Haftek-Terreau, Frédéric Brunet, Yann-Vaï Le Bihan, Marie-Hélène Ledu, Fabien Montel and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

52 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  3. Article
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  5. Review
  6. Article
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  12. Article
  13. The evolution of metazoan shelterin.Genes & development · 2021
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Telomere Replication: Solving Multiple End Replication Problems.Frontiers in cell and developmental biology · 2021
    Review
  20. Article
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

16 authors at 1 institution in 1 country.

Anaïs PouletUniversité de Lyon, Laboratoire Joliot-Curie, CNRS USR3010, Ecole Normale Supérieure de Lyon, 46, allée d'Italie, F-69364 Lyon, France.
Sabrina Pisano
Cendrine Faivre-Moskalenko
Bei Pei
Yannick Tauran
Zofia Haftek-Terreau
Frédéric Brunet
Yann-Vaï Le Bihan
Marie-Hélène Ledu
Fabien Montel
Nicolas Hugo
Simon Amiard
Françoise Argoul
Annie Chaboud
Eric Gilson
Marie-Josèphe Giraud-Panis
Université Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRF1 and TRF2 are key proteins in human telomeres, which, despite their similarities, have different behaviors upon DNA binding. Previous work has shown that unlike TRF1, TRF2 condenses telomeric, thus creating consequential negative torsion on the adjacent DNA, a property that is thought to lead to the stimulation of single-strand invasion and was proposed to favor telomeric DNA looping. In this report, we show that these activities, originating from the central TRFH domain of TRF2, are also displayed by the TRFH domain of TRF1 but are repressed in the full-length protein by the presence of an acidic domain at the N-terminus. Strikingly, a similar repression is observed on TRF2 through the binding of a TERRA-like RNA molecule to the N-terminus of TRF2. Phylogenetic and biochemical studies suggest that the N-terminal domains of TRF proteins originate from a gradual extension of the coding sequences of a duplicated ancestral gene with a consequential progressive alteration of the biochemical properties of these proteins. Overall, these data suggest that the N-termini of TRF1 and TRF2 have evolved to finely regulate their ability to condense DNA.

Indexed as

Amino Acid SequenceDNAEvolution, MolecularHumansMolecular Sequence DataProtein Structure, TertiaryRNASequence Homology, Amino AcidTelomereTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2DNARNATelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2TERF2 protein, human

Identifiers

PMID22139926
PMCPMC3315331
OpenAlexW2162471619

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.