Evidence map›Paper›PMID 18500353›Full record

ArticleNature structural & molecular biology2008

Triple-helix structure in telomerase RNA contributes to catalysis.

Feng Qiao, Thomas R Cech

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

85 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular and cellular biology · 2026
    Article
  4. RNA Triple Helices: From Structures and Mechanisms to Therapeutic Targets.International journal of biological sciences · 2026
    Review
  5. Article
  6. A degenerate telomerase RNA directs telomeric DNA synthesis in lepidopteran insects.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Inverse-folding design of yeast telomerase RNA increases activitybioRxiv : the preprint server for biology · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. RNAs as Regulators of Cellular Matchmaking.Frontiers in molecular biosciences · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  19. Review
  20. Article

25 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

2 authors at 1 institution in 1 country.

Feng QiaoHoward Hughes Medical Institute, Department of Chemistry and Biochemistry, Campus Box 215, University of Colorado, Boulder, Colorado 80309-0215, USA.
Thomas R Cech
Howard Hughes Medical Institute · US

Funding

Telomerase and Telomeres: Structure, Function/RegulationR01GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS ROBERT · 1985 to 2009
$2.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM028039NIGMS NIH HHS R01 GM28039
6 · The paper itself

Abstract

Telomerase is responsible for replication of the ends of linear chromosomes in most eukaryotes. Its intrinsic RNA subunit provides the template for synthesis of telomeric DNA by the reverse-transcriptase (TERT) subunit and tethers other proteins into the ribonucleoprotein (RNP) complex. We report that a phylogenetically conserved triple helix within a pseudoknot structure of this RNA contributes to telomerase activity but not by binding the TERT protein. Instead, 2'-OH groups protruding from the triple helix participate in both yeast and human telomerase catalysis; they may orient the primer-template relative to the active site in a manner analogous to group I ribozymes. The role of RNA in telomerase catalysis may have been acquired relatively recently or, alternatively, telomerase may be a molecular fossil representing an evolutionary link between RNA enzymes and RNP enzymes.

Indexed as

Binding SitesCatalysisHumansNucleic Acid ConformationPhylogenyRNATelomeraseYeastsRNATelomerasetelomerase RNA

Identifiers

PMID18500353
PMCPMC2562722
OpenAlexW2164449007

What OpenQuestion holds

Textmetadata
LicenceTDM
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.