Evidence map›Paper›PMID 26748096›Full record

ArticleNucleic acids research2016

A higher-order entity formed by the flexible assembly of RAP1 with TRF2.

Guillaume Gaullier, Simona Miron, Sabrina Pisano, Rémi Buisson, Yann-Vaï Le Bihan, Carine Tellier-Lebègue, Wala Messaoud, Pierre Roblin, Beatriz G Guimarães, Robert Thai and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. The evolution of metazoan shelterin.Genes & development · 2021
    Article
  8. Review
  9. Article
  10. Characterization of t-loop formation by TRF2.Nucleus (Austin, Tex.) · 2020
    Article
  11. Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

13 authors at 8 institutions in 2 countries.

Guillaume GaullierDepartment of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), CEA, UMR 9198 CNRS, Université Paris-Sud, Batiment 144, CEA Saclay, Gif-sur-Yvette, F-91191, France.
Simona MironDepartment of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), CEA, UMR 9198 CNRS, Université Paris-Sud, Batiment 144, CEA Saclay, Gif-sur-Yvette, F-91191, France.
Sabrina PisanoInstitute for Research on Cancer and Aging, Nice (IRCAN); CNRS UMR7284/INSERM U1081; Faculty of Medicine; Nice, 06107, France.
Rémi BuissonInstitute for Research on Cancer and Aging, Nice (IRCAN); CNRS UMR7284/INSERM U1081; Faculty of Medicine; Nice, 06107, France.
Yann-Vaï Le BihanDepartment of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), CEA, UMR 9198 CNRS, Université Paris-Sud, Batiment 144, CEA Saclay, Gif-sur-Yvette, F-91191, France.
Carine Tellier-LebègueDepartment of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), CEA, UMR 9198 CNRS, Université Paris-Sud, Batiment 144, CEA Saclay, Gif-sur-Yvette, F-91191, France.
Wala MessaoudDepartment of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), CEA, UMR 9198 CNRS, Université Paris-Sud, Batiment 144, CEA Saclay, Gif-sur-Yvette, F-91191, France.
Pierre RoblinSynchrotron SOLEIL, L'Orme des Merisiers, Saint-Aubin BP 48, 91192 GIF-SUR-YVETTE Cedex, France Institut National de la Recherche Agronomique, Unité Biopolymères, Interactions, Assemblages, 44316 Nantes, France.
Beatriz G GuimarãesSynchrotron SOLEIL, L'Orme des Merisiers, Saint-Aubin BP 48, 91192 GIF-SUR-YVETTE Cedex, France.
Robert ThaiCEA, iBiTecS, F-91191 Gif-sur-Yvette, France.
Marie-Josèphe Giraud-PanisInstitute for Research on Cancer and Aging, Nice (IRCAN); CNRS UMR7284/INSERM U1081; Faculty of Medicine; Nice, 06107, France.
Eric GilsonInstitute for Research on Cancer and Aging, Nice (IRCAN); CNRS UMR7284/INSERM U1081; Faculty of Medicine; Nice, 06107, France Department of Genetics, CHU; Nice, 06107, France.
Marie-Hélène Le DuDepartment of Biochemistry, Biophysics and Structural Biology, Institute for Integrative Biology of the Cell (I2BC), CEA, UMR 9198 CNRS, Université Paris-Sud, Batiment 144, CEA Saclay, Gif-sur-Yvette, F-91191, France marie-helene.ledu@cea.fr.
CEA Paris-Saclay · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInserm · FRSynchrotron soleil · FRFaculty (United Kingdom) · GBInstitut de Biologie et Technologies · FRInstitut de Recherche sur le Cancer et le Vieillissement de Nice · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Telomere integrity is essential to maintain genome stability, and telomeric dysfunctions are associated with cancer and aging pathologies. In human, the shelterin complex binds TTAGGG DNA repeats and provides capping to chromosome ends. Within shelterin, RAP1 is recruited through its interaction with TRF2, and TRF2 is required for telomere protection through a network of nucleic acid and protein interactions. RAP1 is one of the most conserved shelterin proteins although one unresolved question is how its interaction may influence TRF2 properties and regulate its capacity to bind multiple proteins. Through a combination of biochemical, biophysical and structural approaches, we unveiled a unique mode of assembly between RAP1 and TRF2. The complete interaction scheme between the full-length proteins involves a complex biphasic interaction of RAP1 that directly affects the binding properties of the assembly. These results reveal how a non-DNA binding protein can influence the properties of a DNA-binding partner by mutual conformational adjustments.

Indexed as

Genomic InstabilityDNA-Binding ProteinsDNA DamageHumansMultiprotein ComplexesProtein BindingShelterin ComplexTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2DNA-Binding ProteinsMultiprotein ComplexesShelterin ComplexTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2TERF2IP protein, humanTERF2 protein, human

Identifiers

PMID26748096
PMCPMC4770236
OpenAlexW2275484867

What OpenQuestion holds

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Registered trials

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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.