Evidence map›Paper›PMID 20660025›Full record

ReviewCold Spring Harbor perspectives in biology2011

Telomerase: an RNP enzyme synthesizes DNA.

Elizabeth H Blackburn, Kathleen Collins

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 217 papers.

0numbers the graph read from it
0cells of the map it votes in
217citing 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

217 citing papers in PubMed, 330 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Biogenesis and Regulation of Telomerase during Development and Cancer.Cold Spring Harbor perspectives in biology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Spinal muscular atrophy: Biology, pathogenesis, and therapeutic advances.Therapeutic advances in neurological disorders · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. A (Scientific) Lifetime Affair With Nucleic Acids.Journal of molecular biology · 2025
    Review
  19. Article
  20. Article

157 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 2 institutions in 1 country.

Elizabeth H BlackburnUniversity of California-San Francisco, CA 94158-2517, USA. elizabeth.blackburn@ucsf.edu
Kathleen Collins
University of California, Berkeley · USUniversity of California, San Francisco · US

Funding

STRUCTURE AND FUNCTION OF TELOMERASER01GM054198 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 1996 to 2018
$5.4M
Molecular Mechanism of X-linked Dyskeratosis CongenitaR01HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2004 to 2017
$4.1M
NHLBI NIH HHS R01 HL079585NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

Telomerase is a eukaryotic ribonucleoprotein (RNP) whose specialized reverse transcriptase action performs de novo synthesis of one strand of telomeric DNA. The resulting telomerase-mediated elongation of telomeres, which are the protective end-caps for eukaryotic chromosomes, counterbalances the inevitable attrition from incomplete DNA replication and nuclease action. The telomerase strategy to maintain telomeres is deeply conserved among eukaryotes, yet the RNA component of telomerase, which carries the built-in template for telomeric DNA repeat synthesis, has evolutionarily diverse size and sequence. Telomerase shows a distribution of labor between RNA and protein in aspects of the polymerization reaction. This article first describes the underlying conservation of a core set of structural features of telomerase RNAs important for the fundamental polymerase activity of telomerase. These include a pseudoknot-plus-template domain and at least one other RNA structural motif separate from the template-containing domain. The principles driving the diversity of telomerase RNAs are then explored. Much of the diversification of telomerase RNAs has come from apparent gain-of-function elaborations, through inferred evolutionary acquisitions of various RNA motifs used for telomerase RNP biogenesis, cellular trafficking of enzyme components, and regulation of telomerase action at telomeres. Telomerase offers broadly applicable insights into the interplay of protein and RNA functions in the context of an RNP enzyme.

Indexed as

Base SequenceBinding SitesDNADNA ReplicationEvolution, MolecularNucleic Acid ConformationPolymerizationRNATelomeraseTelomereDNARNATelomerase

Identifiers

PMID20660025
PMCPMC3101848
OpenAlexW2152562488

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.