Evidence map›Paper›PMID 21514196›Full record

ArticleMolecular cell2011

Human telomerase domain interactions capture DNA for TEN domain-dependent processive elongation.

Aaron R Robart, Kathleen Collins

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

51 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. 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
  3. Review
  4. Article
  5. Article
  6. Flexibility of telomerase in binding the RNA template and DNA telomeric repeat.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  15. Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019
    Review
  16. Article
  17. Telomere DNA G-quadruplex folding within actively extending human telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Aaron R RobartDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3200, USA.
Kathleen Collins
University of California, Berkeley · 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
Biogenesis and Regulation of Human TelomeraseR56HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2008 to 2008
$367k
NHLBI NIH HHS HL079585NHLBI NIH HHS R01 HL079585NHLBI NIH HHS R56 HL079585NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

Eukaryotic chromosome maintenance requires telomeric repeat synthesis by telomerase. It remains uncertain how telomerase domains interact to organize the active RNP and how this architecture establishes the specificity of the catalytic cycle. We combine human telomerase reconstitutions in vivo, affinity purifications, and discriminating activity assays to uncover a network of protein-protein and protein-RNA domain interactions. Notably, we find that complete single-repeat synthesis requires only a telomerase reverse transcriptase (TERT) core. Single-repeat synthesis does not require the TERT N-terminal (TEN) domain, but RNA-dependent positioning of the TEN domain captures substrate and allows repeat synthesis processivity. A TEN domain physically separate from the TERT core can capture even a minimal template-paired DNA substrate, with substrate association enhanced by the presence of a 5' single-stranded extension. Our results provide insights into active enzyme architecture, explain biological variations of the catalytic cycle, and predict altered activities for TERT proteins of some eukaryotes.

Indexed as

Protein Structure, TertiaryBinding SitesBiocatalysisCell LineDNADNA, Single-StrandedHumansImmunoblottingModels, MolecularNucleic Acid ConformationProtein BindingRNATelomeraseTelomereDNADNA, Single-StrandedRNATelomerasetelomerase RNATERT protein, human

Identifiers

PMID21514196
PMCPMC3097130
OpenAlexW2160576740

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.