Evidence map›Paper›PMID 30462290›Full record

ArticleNucleic acids research2019

Finely tuned conformational dynamics regulate the protective function of the lncRNA MALAT1 triple helix.

Abeer A Ageeli, Kayleigh R McGovern-Gooch, Magdalena M Kaminska, Nathan J Baird

Abstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. RNA Triple Helices: From Structures and Mechanisms to Therapeutic Targets.International journal of biological sciences · 2026
    Review
  4. Article
  5. Fluorescent Dyes for Differential Scanning Fluorimetry of RNA.Chembiochem : a European journal of chemical biology · 2025
    Article
  6. RNA triple helix assembled by the poly(A) tail enhances retrotransposon mobilization by preventing RNA deadenylation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Small molecule quercetin bindsMolecular therapy. Nucleic acids · 2022
    Article
  19. Article
  20. 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

4 authors.

Abeer A AgeeliDepartment of Chemistry & Biochemistry, University of the Sciences, Philadelphia, PA 19143, USA.
Kayleigh R McGovern-GoochDepartment of Chemistry & Biochemistry, University of the Sciences, Philadelphia, PA 19143, USA.
Magdalena M KaminskaDepartment of Chemistry & Biochemistry, University of the Sciences, Philadelphia, PA 19143, USA.
Nathan J BairdDepartment of Chemistry & Biochemistry, University of the Sciences, Philadelphia, PA 19143, USA.

Funding

Regulating RNA function by modulating RNA folding with exogenous ligandsK22HL121113 · NHLBI · UNIVERSITY OF THE SCIENCES PHILADELPHIA · PI BAIRD, NATHAN · 2015 to 2017
$732k
NHLBI NIH HHS K22 HL121113
6 · The paper itself

Abstract

Nucleic acid triplexes may regulate many important biological processes. Persistent accumulation of the oncogenic 7-kb long noncoding RNA MALAT1 is dependent on an unusually long intramolecular triple helix. This triplex structure is positioned within a conserved ENE (element for nuclear expression) motif at the lncRNA 3' terminus and protects the entire transcript from degradation in a polyA-independent manner. A requisite 3' maturation step leads to triplex formation though the precise mechanism of triplex folding remains unclear. Furthermore, the contributions of several peripheral structural elements to triplex formation and protective function have not been determined. We evaluated the stability, conformational fluctuations, and function of this MALAT1 ENE triple helix (M1TH) protective element using in vitro mutational analyses coupled with biochemical and biophysical characterizations. Using fluorescence and UV melts, FRET, and an exonucleolytic decay assay we define a concerted mechanism for triplex formation and uncover a metastable, dynamic triplex population under near-physiological conditions. Structural elements surrounding the triplex regulate the dynamic M1TH conformational variability, but increased triplex dynamics lead to M1TH degradation. Taken together, we suggest that finely tuned dynamics may be a general mechanism regulating triplex-mediated functions.

Indexed as

Nucleic Acid ConformationBase SequenceDNAHumansRNA, Long NoncodingDNAMALAT1 long non-coding RNA, humanRNA, Long Noncoding

Identifiers

PMID30462290
PMCPMC6379651

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.