Evidence map›Paper›PMID 23474713›Full record

ArticleNature structural & molecular biology2013

Structure of active dimeric human telomerase.

Anselm Sauerwald, Sara Sandin, Gaël Cristofari, Sjors H W Scheres, Joachim Lingner, Daniela Rhodes

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  10. Review
  11. Article
  12. Single-Run Catalysis and Kinetic Control of Human Telomerase Holoenzyme.Advances in experimental medicine and biology · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Cryo-EM structures tell a tale of two telomerases.Nature structural & molecular biology · 2021
    Article
  20. Article

16 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

6 authors.

Anselm SauerwaldMedical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Sara Sandin
Gaël Cristofari
Sjors H W Scheres
Joachim Lingner
Daniela Rhodes

Funding

European Research Council 232812Medical Research Council MC_U105184333Medical Research Council MC_UP_A025_1013Medical Research Council U10518433333
6 · The paper itself

Abstract

Telomerase contains a large RNA subunit, TER, and a protein catalytic subunit, TERT. Whether telomerase functions as a monomer or dimer has been a matter of debate. Here we report biochemical and labeling data that show that in vivo-assembled human telomerase contains two TERT subunits and binds two telomeric DNA substrates. Notably, catalytic activity requires both TERT active sites to be functional, which demonstrates that human telomerase functions as a dimer. We also present the three-dimensional structure of the active full-length human telomerase dimer, determined by single-particle EM in negative stain. Telomerase has a bilobal architecture with the two monomers linked by a flexible interface. The monomer reconstruction at 23-Å resolution and fitting of the atomic structure of the TERT subunit from beetle Tribolium castaneum into the EM density reveals the spatial relationship between RNA and protein subunits, providing insights into telomerase architecture.

Indexed as

DimerizationHEK293 CellsHumansProtein ConformationSubstrate SpecificityTelomeraseTelomerase

Identifiers

PMID23474713
PMCPMC3785136

What OpenQuestion holds

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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.