Evidence map›Paper›PMID 20948311›Full record

ArticleCell cycle (Georgetown, Tex.)2010

Taking apart Rap1: an adaptor protein with telomeric and non-telomeric functions.

Shaheen Kabir, Agnel Sfeir, Titia de Lange

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

24 citing papers in PubMed, 30 citations in OpenAlex.

  1. Deletion ofmSphere · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The evolution of metazoan shelterin.Genes & development · 2021
    Article
  8. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Shaheen KabirLaboratory for Cell Biology and Genetics, The Rockefeller University, New York, NY, USA.
Agnel Sfeir
Titia de Lange
New York Proton Center · USRockefeller University · US

Funding

MECHANISMS OF TELOMERE INDUCED SENESCENCER01AG016642 · NIA · ROCKEFELLER UNIVERSITY · PI Titia de Lange · 1999 to 2026
$11.9M
Molecular Cytology of Human Telomeres: Telomere proteinR37GM049046 · NIGMS · ROCKEFELLER UNIVERSITY · PI DE LANGE, TITIA · 2005 to 2014
$5.0M
TELOMERE LENGTH CONTROL BY TRF1 AND TRF2R01CA076027 · NCI · ROCKEFELLER UNIVERSITY · PI DE LANGE, TITIA · 1998 to 2012
$4.3M
MOLECULAR CYTOLOGY OF HUMAN TELOMERES--TELOMERE PROTEINR01GM049046 · NIGMS · ROCKEFELLER UNIVERSITY · PI DE LANGE, TITIA · 1993 to 2004
$1.8M
Mechanism of the telomeric proliferation limitR56AG016642 · NIA · ROCKEFELLER UNIVERSITY · PI DE LANGE, TITIA · 2019 to 2019
$598k
NCI NIH HHS CA076027NCI NIH HHS R01 CA076027NIA NIH HHS AG016642NIA NIH HHS R01 AG016642NIA NIH HHS R56 AG016642NIGMS NIH HHS GM049046NIGMS NIH HHS R01 GM049046NIGMS NIH HHS R37 GM049046
6 · The paper itself

Abstract

Mammalian Rap1, a TRF2-interacting protein in the telomeric shelterin complex, was recently shown to repress homology-directed repair at chromosome ends. In addition, Rap1 plays a role in transcriptional regulation and NFκB signaling. Rap1 is unique among the components of shelterin in that it is conserved in budding yeast and has non-telomeric functions. Comparison of mammalian Rap1 to the Rap1 proteins of several budding yeasts and fission yeast reveal both striking similarities and notable differences. The protean nature of Rap1 is best understood by viewing it as an adaptor that can mediate a variety of protein-protein and protein-DNA interactions depending on the organism and the complex in which it is functioning.

Indexed as

AnimalsDNA DamageDNA RepairHumansShelterin ComplexTelomereTelomere-Binding ProteinsShelterin ComplexTelomere-Binding ProteinsTERF2IP protein, human

Identifiers

PMID20948311
PMCPMC2995270
OpenAlexW2152598515

What OpenQuestion holds

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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.