Evidence map›Paper›PMID 24055314›Full record

ArticleStructure (London, England : 1993)2013

A motif in the vertebrate telomerase N-terminal linker of TERT contributes to RNA binding and telomerase activity and processivity.

Michael Harkisheimer, Mark Mason, Elena Shuvaeva, Emmanuel Skordalakes

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 38 citations in OpenAlex.

  1. 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
  2. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  3. Functional Interactions ofInternational journal of molecular sciences · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020
    Review
  9. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  10. Article
  11. How RNAi machinery enters the world of telomerase.Cell cycle (Georgetown, Tex.) · 2019
    Review
  12. Article
  13. Article
  14. Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Structural conservation in the template/pseudoknot domain of vertebrate telomerase RNA from teleost fish to human.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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 1 institution in 1 country.

Michael HarkisheimerThe Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
Mark Mason
Elena Shuvaeva
Emmanuel Skordalakes
The Wistar Institute · US

Funding

TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
Structural and Biochemical Analysis of Telomerase FunctionR01GM088332 · NIGMS · WISTAR INSTITUTE · PI SKORDALAKES, EMMANUEL · 2010 to 2014
$1.7M
NCI NIH HHS T32 CA009171NIGMS NIH HHS 5 R01 GM088332-03NIGMS NIH HHS R01 GM088332
6 · The paper itself

Abstract

Telomerase is a ribonucleoprotein reverse transcriptase that replicates the ends of chromosomes, thus maintaining genome stability. Telomerase ribonucleoprotein assembly is primarily mediated by the RNA binding domain (TRBD) of the enzyme. Here we present the high-resolution TRBD structure of the vertebrate, Takifugu rubripes (trTRBD). The structure shows that with the exception of the N-terminal linker, the trTRBD is conserved with the Tribolium castaneum and Tetrahymena thermophila TRBDs, suggesting evolutionary conservation across species. The structure provides a view of the structural organization of the vertebrate-specific VSR motif that binds the activation domain (CR4/5) of the RNA component of telomerase. It also reveals a motif (TFLY) that forms part of the T-CP pocket implicated in template boundary element (TBE) binding. Mutant proteins of conserved residues that consist of part of the T and TFLY motifs disrupt trTRBD-TBE binding and telomerase activity and processivity, supporting an essential role of these motifs in telomerase RNP assembly and function.

Indexed as

TakifuguAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionAnimalsBase SequenceBinding SitesCrystallography, X-RayFish ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNucleic Acid ConformationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryFish ProteinsRNATelomerase

Identifiers

PMID24055314
PMCPMC3803134
OpenAlexW2086030580

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.