Evidence map›Paper›PMID 24335084›Full record

ArticleNucleic acids research2014

Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function.

Nak-Kyoon Kim, Qi Zhang, Juli Feigon

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 31 citations in OpenAlex.

  1. Application of NMR to Large RNAs.Journal of molecular biology · 2025
    Review
  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. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020
    Review
  8. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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
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

3 authors at 1 institution in 1 country.

Nak-Kyoon KimDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569, USA, Advanced Analysis Center, Korea Institute of Science and Technology, Seoul, 136-791, Republic of Korea and Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Qi Zhang
Juli Feigon
University of North Carolina at Chapel Hill · US

Funding

STRUCTURE OF TELOMERIC DNA OLIGONUCLEOTIDESR01GM048123 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FEIGON, JULI · 1992 to 2018
$6.4M
NIGMS NIH HHS GM48123NIGMS NIH HHS R01 GM048123
6 · The paper itself

Abstract

Telomerase is a unique reverse transcriptase that maintains the 3' ends of eukaryotic chromosomes by adding tandem telomeric repeats. The RNA subunit (TR) of vertebrate telomerase provides a template for reverse transcription, contained within the conserved template/pseudoknot domain, and a conserved regions 4 and 5 (CR4/5) domain, all essential for catalytic activity. We report the nuclear magnetic resonance (NMR) solution structure of the full-length CR4/5 domain from the teleost fish medaka (Oryzias latipes). Three helices emanate from a structured internal loop, forming a Y-shaped structure, where helix P6 stacks on P5 and helix P6.1 points away from P6. The relative orientations of the three helices are Mg2+ dependent and dynamic. Although the three-way junction is structured and has unexpected base pairs, telomerase activity assays with nucleotide substitutions and deletions in CR4/5 indicate that none of these are essential for activity. The results suggest that the junction is likely to change conformation in complex with telomerase reverse transcriptase and that it provides a flexible scaffold that allows P6 and P6.1 to correctly fold and interact with telomerase reverse transcriptase.

Indexed as

AnimalsMagnesiumModels, MolecularNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationOryziasRNATelomeraseMagnesiumRNATelomerasetelomerase RNA

Identifiers

PMID24335084
PMCPMC3950677
OpenAlexW2050168806

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.