Evidence map›Paper›PMID 26158869›Full record

ArticleNature communications2015

Telomeric G-quadruplexes are a substrate and site of localization for human telomerase.

Aaron L Moye, Karina C Porter, Scott B Cohen, Tram Phan, Katherine G Zyner, Natsuki Sasaki, George O Lovrecz, Jennifer L Beck, Tracy M Bryan

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing 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

151 citing papers in PubMed.

  1. Article
  2. G-Quadruplexes: Structural Diversity and Emerging Roles in Biomolecular Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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91 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

9 authors.

Aaron L MoyeChildren's Medical Research Institute, University of Sydney, 214 Hawkesbury Road, Westmead, New South Wales 2145, Australia.
Karina C PorterChildren's Medical Research Institute, University of Sydney, 214 Hawkesbury Road, Westmead, New South Wales 2145, Australia.
Scott B CohenChildren's Medical Research Institute, University of Sydney, 214 Hawkesbury Road, Westmead, New South Wales 2145, Australia.
Tram PhanCommonwealth Scientific and Industrial Research Organisation, Manufacturing Flagship, 343 Royal Parade, Parkville, Victoria 3052, Australia.
Katherine G ZynerChildren's Medical Research Institute, University of Sydney, 214 Hawkesbury Road, Westmead, New South Wales 2145, Australia.
Natsuki SasakiChildren's Medical Research Institute, University of Sydney, 214 Hawkesbury Road, Westmead, New South Wales 2145, Australia.
George O LovreczCommonwealth Scientific and Industrial Research Organisation, Manufacturing Flagship, 343 Royal Parade, Parkville, Victoria 3052, Australia.
Jennifer L BeckSchool of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia.
Tracy M BryanChildren's Medical Research Institute, University of Sydney, 214 Hawkesbury Road, Westmead, New South Wales 2145, Australia.ORCID 0000000279905501

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has been hypothesized that G-quadruplexes can sequester the 3' end of the telomere and prevent it from being extended by telomerase. Here we purify and characterize stable, conformationally homogenous human telomeric G-quadruplexes, and demonstrate that human telomerase is able to extend parallel, intermolecular conformations in vitro. These G-quadruplexes align correctly with the RNA template of telomerase, demonstrating that at least partial G-quadruplex resolution is required. A highly purified preparation of human telomerase retains this extension ability, establishing that the core telomerase enzyme complex is sufficient for partial G-quadruplex resolution and extension. The parallel-specific G-quadruplex ligand N-methyl mesoporphyrin IX (NMM) causes an increase in telomeric G-quadruplexes, and we show that telomerase colocalizes with a subset of telomeric G-quadruplexes in vivo. The ability of telomerase to partially unwind, extend and localize to these structures implies that parallel telomeric G-quadruplexes may play an important biological role.

Indexed as

G-QuadruplexesBlotting, WesternCircular DichroismDNAElectrophoresis, Polyacrylamide GelHEK293 CellsHumansIn Situ Hybridization, FluorescenceMesoporphyrinsSpectrometry, Mass, Electrospray IonizationTelomeraseTelomere HomeostasisDNAMesoporphyrinsN-methylmesoporphyrin IXTelomeraseTERT protein, human

Identifiers

PMID26158869
PMCPMC4510649

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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.