Evidence map›Paper›PMID 37558241›Full record

ArticleNucleic acids research2023

Identification of G-quadruplex structures in MALAT1 lncRNA that interact with nucleolin and nucleophosmin.

Arpita Ghosh, Satya Prakash Pandey, Dheeraj Chandra Joshi, Priya Rana, Asgar Hussain Ansari, Jennifer Seematti Sundar, Praveen Singh, Yasmeen Khan, Mary Krishna Ekka, Debojyoti Chakraborty and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. 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
9.1field-weighted citation impact, top 2% 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, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. iScience · 2026
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  8. Article
  9. Review
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  11. Article
  12. Article
  13. Article
  14. Review
  15. Regulation of the lncRNANAR molecular medicine · 2025
    Article
  16. Article
  17. Article
  18. Review
  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

11 authors at 1 institution in 1 country.

Arpita GhoshCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Satya Prakash PandeyCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Dheeraj Chandra JoshiCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Priya RanaCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Asgar Hussain AnsariCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Jennifer Seematti SundarCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Praveen SinghCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Yasmeen KhanCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Mary Krishna EkkaCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.
Debojyoti ChakrabortyCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.ORCID 0000-0003-1460-7594
Souvik MaitiCSIR-Institute of Genomics & Integrative Biology, Mathura Road, Delhi 110025, India.ORCID 0000-0001-9897-1419
Institute of Genomics and Integrative Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear-retained long non-coding RNAs (lncRNAs) including MALAT1 have emerged as critical regulators of many molecular processes including transcription, alternative splicing and chromatin organization. Here, we report the presence of three conserved and thermodynamically stable RNA G-quadruplexes (rG4s) located in the 3' region of MALAT1. Using rG4 domain-specific RNA pull-down followed by mass spectrometry and RNA immunoprecipitation, we demonstrated that the MALAT1 rG4 structures are specifically bound by two nucleolar proteins, Nucleolin (NCL) and Nucleophosmin (NPM). Using imaging, we found that the MALAT1 rG4s facilitate the localization of both NCL and NPM to nuclear speckles, and specific G-to-A mutations that disrupt the rG4 structures compromised the localization of both NCL and NPM in speckles. In vitro biophysical studies established that a truncated version of NCL (ΔNCL) binds tightly to all three rG4s. Overall, our study revealed new rG4s within MALAT1, established that they are specifically recognized by NCL and NPM, and showed that disrupting the rG4s abolished localization of these proteins to nuclear speckles.

Indexed as

G-QuadruplexesRNA, Long NoncodingHumansNucleolinNucleophosminPhosphoproteinsMALAT1 long non-coding RNA, humanNucleolinNucleophosminPhosphoproteinsRNA, Long Noncoding

Identifiers

PMID37558241
PMCPMC11314421
OpenAlexW4385691025

What Socratic 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 Socratic graph.