Evidence map›Paper›PMID 22101935›Full record

ArticleNature structural & molecular biology2011

The RNA accordion model for template positioning by telomerase RNA during telomeric DNA synthesis.

Andrea J Berman, Benjamin M Akiyama, Michael D Stone, Thomas R Cech

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

47 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. A (Scientific) Lifetime Affair With Nucleic Acids.Journal of molecular biology · 2025
    Review
  3. Article
  4. Article
  5. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  6. Article
  7. 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
  8. Article
  9. Article
  10. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020
    Review
  13. Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019
    Review
  14. Article
  15. Article
  16. Review
  17. New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018
    Review
  18. Review
  19. Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017
    Review
  20. Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017
    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

4 authors at 3 institutions in 1 country.

Andrea J BermanDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado, USA.
Benjamin M Akiyama
Michael D Stone
Thomas R Cech
University of California, Santa Cruz · USHoward Hughes Medical Institute · USUniversity of Colorado Boulder · US

Funding

Structure and dynamics of the Tetrahymena telomerase ribonucleoproteinR01GM095850 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STONE, MICHAEL D · 2011 to 2023
$4.4M
Training Program/Molecular/Cell/Developmental BiologyT32GM008646 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STROME, SUSAN · 1999 to 2018
$3.7M
NIGMS NIH HHS GM095850NIGMS NIH HHS R01 GM095850NIGMS NIH HHS T32 GM008646NIGMS NIH HHS T32 GM8646
6 · The paper itself

Abstract

Telomerase is a ribonucleoprotein (RNP) enzyme that maintains the ends of linear eukaryotic chromosomes and whose activation is a hallmark of 90% of all cancers. This RNP minimally contains a reverse transcriptase protein subunit (TERT) that catalyzes telomeric DNA synthesis and an RNA subunit (TER) that has templating, architectural and protein-scaffolding roles. Telomerase is unique among polymerases in that it synthesizes multiple copies of the template on the 3' end of a primer following a single binding event, a process known as repeat addition processivity (RAP). Using biochemical assays and single-molecule Förster resonance energy transfer (smFRET) experiments on Tetrahymena thermophila telomerase, we now directly demonstrate that TER contributes to template positioning within the active site and to the template translocation required for RAP. We propose that the single-stranded RNA elements flanking the template act as a molecular accordion, undergoing reciprocal extension and compaction during telomerase translocation.

Indexed as

DNA, ProtozoanFluorescence Resonance Energy TransferNucleic Acid ConformationRNARNA, ProtozoanTelomeraseTelomereTetrahymena thermophilaDNA, ProtozoanRNARNA, ProtozoanTelomerasetelomerase RNA

Identifiers

PMID22101935
PMCPMC3230705
OpenAlexW2059665929

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.