Evidence map›Paper›PMID 19835419›Full record

ArticleBiochemistry2009

Single-molecule analysis of the human telomerase RNA.dyskerin interaction and the effect of dyskeratosis congenita mutations.

Beth Ashbridge, Angel Orte, Justin A Yeoman, Michael Kirwan, Tom Vulliamy, Inderjeet Dokal, David Klenerman, Shankar Balasubramanian

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Single-Run Catalysis and Kinetic Control of Human Telomerase Holoenzyme.Advances in experimental medicine and biology · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Medical genetics and epigenetics of telomerase.Journal of cellular and molecular medicine · 2011
    Review
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

8 authors at 2 institutions in 3 countries.

Beth AshbridgeUniversity Chemical Laboratories, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Angel Orte
Justin A Yeoman
Michael Kirwan
Tom Vulliamy
Inderjeet Dokal
David Klenerman
Shankar Balasubramanian
University of Cambridge · GBQueen Mary University of London · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0400534Wellcome Trust 069399/Z/02
6 · The paper itself

Abstract

It has been proposed that human telomerase RNA (hTR) interacts with dyskerin, prior to assembly of the telomerase holoenzyme. The direct interaction of dyskerin and hTR has not been demonstrated and is an experimentally challenging research problem because of difficulties in expressing and purifying dyskerin in quantities that are useful for biophysical analysis. By orthogonally labeling dyskerin and hTR, we have been able to employ single-molecule two-color coincidence detection (TCCD) to observe directly the formation of a dyskerin.hTR complex. By systematic deletion of hTR subdomains, we have gained insights into the RNA sites required for interaction with dyskerin. We then investigated mutated forms of hTR and dyskerin that are associated with dyskeratosis congenita (DC), on the basis of clinical genetics studies, for their effects on the dyskerin.hTR interaction. Dyskerin mutations associated with X-linked DC resulted in significant impairment of the dyskerin.hTR interaction, whereas mutations in hTR associated with autosomal dominant (AD) DC did not affect the interaction. We propose that disruption of the dyskerin.hTR interaction may contribute to X-linked DC.

Indexed as

Amino Acid SubstitutionBinding SitesCell Cycle ProteinsCell LineDNA Restriction EnzymesDyskeratosis CongenitaHumansMicroscopy, ConfocalMutationNuclear ProteinsPoint MutationProtein BindingRecombinant Fusion ProteinsRNASignal Processing, Computer-AssistedSpectrometry, FluorescenceCell Cycle ProteinsDKC1 protein, humanDNA Restriction EnzymesNuclear ProteinsRecombinant Fusion ProteinsRNATelomerasetelomerase RNA

Identifiers

PMID19835419
PMCPMC2778356
OpenAlexW2051227660

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.