Evidence map›Paper›PMID 25512567›Full record

ArticleRNA (New York, N.Y.)2015

Refined secondary-structure models of the core of yeast and human telomerase RNAs directed by SHAPE.

Rachel O Niederer, David C Zappulla

Erratum issued Registry-linked trialOpen access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. It is linked to trial NCT03300167 (Study of the Vascular Response to Percutaneous Coronary Intervention in Patients With Non-ST-elevation Acute Coronary Syndromes Using Intravascular Blood Sampling), which is not on this map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 17% 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.

NCT03300167 nawithdrawnnot on this mapstarted 2017, after this paper: background citation

Study of the Vascular Response to Percutaneous Coronary Intervention in Patients With Non-ST-elevation Acute Coronary Syndromes Using Intravascular Blood Sampling

TypeinterventionalSponsorSheffield Teaching Hospitals NHS Foundation TrustRan2017 to 2020Enrolled0ConditionsNon ST Segment Elevation Acute Coronary SyndromeArmsThe Liquid Biopsy System
3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Molecular and cellular biology · 2026
    Article
  2. Advances in understanding telomerase assembly.Biochemical Society transactions · 2023
    Review
  3. Article
  4. Inverse-folding design of yeast telomerase RNA increases activitybioRxiv : the preprint server for biology · 2023
    Article
  5. Review
  6. Article
  7. Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017
    Review
  8. Review
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Rachel O NiedererDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.
David C ZappullaDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA zappulla@jhu.edu.ORCID http://orcid.org/0000-0001-8242-3493
Johns Hopkins University · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
Investigating Telomerase Mechanism by Exploring the RNAR00GM080400 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ZAPPULLA, DAVID CLIFFORD · 2008 to 2010
$745k
NIGMS NIH HHS 2T32 GM007231NIGMS NIH HHS R00 GM080400NIGMS NIH HHS R00 GM80400NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

Telomerase catalyzes the addition of nucleotides to the ends of chromosomes to complete genomic DNA replication in eukaryotes and is implicated in multiple diseases, including most cancers. The core enzyme is composed of a reverse transcriptase and an RNA subunit, which provides the template for DNA synthesis. Despite extensive divergence at the sequence level, telomerase RNAs share several structural features within the catalytic core, suggesting a conserved enzyme mechanism. We have investigated the structure of the core of the human and yeast telomerase RNAs using SHAPE, which interrogates flexibility of each nucleotide. We present improved secondary-structure models, refined by addition of five base triples within the yeast pseudoknot and an alternate pairing within the human-specific element J2a.1 in the human pseudoknot, both of which have implications for thermodynamic stability. We also identified a potentially structured CCC region within the template that may facilitate substrate binding and enzyme mechanism. Overall, the SHAPE findings reveal multiple similarities between the Saccharomyces cerevisiae and Homo sapiens telomerase RNA cores.

Indexed as

AcylationBase SequenceHumansInverted Repeat SequencesModels, MolecularMolecular Sequence DataNucleic Acid ConformationRNARNA, FungalSaccharomyces cerevisiaeTelomeraseRNARNA, FungalTelomerasetelomerase RNAchemical probinghTRlncRNAncRNARNARNPSHAPEtelomerasetelomerase RNATLC1

Identifiers

PMID25512567
PMCPMC4338352
OpenAlexW2159539672

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

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.