Evidence map›Paper›PMID 25406362›Full record

ArticleRNA (New York, N.Y.)2015

G quadruplex RNA structures in PSD-95 mRNA: potential regulators of miR-125a seed binding site accessibility.

Snezana Stefanovic, Gary J Bassell, Mihaela Rita Mihailescu

Open 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. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. RNA and DNA G-quadruplexes bind to human dicer and inhibit its activity.Cellular and molecular life sciences : CMLS · 2021
    Article
  9. Article
  10. GRNA biology · 2020
    Article
  11. Article
  12. Article
  13. FUS Recognizes G Quadruplex Structures Within Neuronal mRNAs.Frontiers in molecular biosciences · 2020
    Article
  14. Article
  15. Detecting RNA G-Quadruplexes (rG4s) in the Transcriptome.Cold Spring Harbor perspectives in biology · 2018
    Review
  16. Article
  17. Synaptopathology Involved in Autism Spectrum Disorder.Frontiers in cellular neuroscience · 2018
    Review
  18. Review
  19. Review
  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

3 authors at 2 institutions in 1 country.

Snezana StefanovicDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
Gary J BassellDepartment of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Mihaela Rita MihailescuDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, USA mihailescum@duq.edu.
Duquesne University · USEmory University · US

Funding

Role of microRNAs and RISC in activity regulated translation in neuronsR21DA033478 · NIDA · EMORY UNIVERSITY · PI BASSELL, GARY J · 2013 to 2014
$429k
Fragile X Mental Retardation Protein translation regulator function: interactionsR15HD078017 · NICHD · DUQUESNE UNIVERSITY · PI MIHAILESCU, MIHAELA R · 2013 to 2013
$394k
NICHD NIH HHS 9R15HD078017-03A1NICHD NIH HHS R15 HD078017NIDA NIH HHS R21 DA033478NIDA NIH HHS R21DA033478
6 · The paper itself

Abstract

Fragile X syndrome (FXS) is the most common inherited form of intellectual disability caused by the CGG trinucleotide expansion in the 3'-untranslated region of the FMR1 gene on the X chromosome, that silences the expression of the Fragile X mental retardation protein (FMRP). FMRP has been shown to bind to a G-rich region within the PSD-95 mRNA which encodes for the postsynaptic density protein 95 (PSD-95), and together with the microRNA miR-125a, to play an important role in the reversible inhibition of the PSD-95 mRNA translation in neurons. The loss of FMRP in Fmr1 KO mice disables this translation control in the production of the PSD-95 protein. Interestingly, the miR-125a binding site on PSD-95 mRNA is embedded in the G-rich region bound by FMRP and postulated to adopt one or more G quadruplex structures. In this study, we have used different biophysical techniques to validate and characterize the formation of parallel G quadruplex structures and binding of miR-125a to its complementary sequence located within the 3' UTR of PSD-95 mRNA. Our results indicate that the PSD-95 mRNA G-rich region folds into alternate G quadruplex conformations that coexist in equilibrium. miR-125a forms a stable complex with PSD-95 mRNA, as evident by characteristic Watson-Crick base-pairing that coexists with one of the G quadruplex forms, suggesting a novel mechanism for G quadruplex structures to regulate the access of miR-125a to its binding site.

Indexed as

3' Untranslated RegionsBase PairingBase SequenceBinding SitesDisks Large Homolog 4 ProteinFragile X SyndromeG-QuadruplexesHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicroRNAsMolecular Sequence DataRNA, MessengerThermodynamics3' Untranslated RegionsDisks Large Homolog 4 ProteinDLG4 protein, humanIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicroRNAsMIRN125 microRNA, humanRNA, MessengerFragile XmiR-125aPSD-95 mRNA

Identifiers

PMID25406362
PMCPMC4274637
OpenAlexW2146666683

What OpenQuestion holds

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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.