Evidence map›Paper›PMID 24516170›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

G-quadruplex formation in telomeres enhances POT1/TPP1 protection against RPA binding.

Sujay Ray, Jigar N Bandaria, Mohammad H Qureshi, Ahmet Yildiz, Hamza Balci

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

83 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
  2. Reusable Microfluidic Chambers for Single-Molecule Microscopy.ACS applied materials & interfaces · 2024
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  15. Article
  16. Dynamic folding and accessibility of telomeric overhang.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Emerging accessibility patterns in long telomeric overhangs.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Review
  20. Article

23 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

5 authors at 2 institutions in 1 country.

Sujay RayDepartments of Physics and Biological Sciences, Kent State University, Kent, OH 44242.
Jigar N Bandaria
Mohammad H Qureshi
Ahmet Yildiz
Hamza Balci
University of California, Berkeley · USKent State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human telomeres terminate with a single-stranded 3' G overhang, which can be recognized as a DNA damage site by replication protein A (RPA). The protection of telomeres (POT1)/POT1-interacting protein 1 (TPP1) heterodimer binds specifically to single-stranded telomeric DNA (ssTEL) and protects G overhangs against RPA binding. The G overhang spontaneously folds into various G-quadruplex (GQ) conformations. It remains unclear whether GQ formation affects the ability of POT1/TPP1 to compete against RPA to access ssTEL. Using single-molecule Förster resonance energy transfer, we showed that POT1 stably loads to a minimal DNA sequence adjacent to a folded GQ. At 150 mM K(+), POT1 loading unfolds the antiparallel GQ, as the parallel conformation remains folded. POT1/TPP1 loading blocks RPA's access to both folded and unfolded telomeres by two orders of magnitude. This protection is not observed at 150 mM Na(+), in which ssTEL forms only a less-stable antiparallel GQ. These results suggest that GQ formation of telomeric overhangs may contribute to suppression of DNA damage signals.

Indexed as

G-QuadruplexesModels, MolecularProtein ConformationEscherichia coliFluorescence Resonance Energy TransferHumansMicroscopy, FluorescenceReplication Protein ASerine ProteasesShelterin ComplexTelomereTelomere-Binding ProteinsACD protein, humanPOT1 protein, humanReplication Protein ASerine ProteasesShelterin ComplexTelomere-Binding ProteinsDNA damage responsesingle molecule imagingtelomere protection

Identifiers

PMID24516170
PMCPMC3939921
OpenAlexW1974384333

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.