Evidence map›Paper›PMID 26412477›Full record

ArticleMolecular bioSystems2015

Fragile X mental retardation protein interactions with a G quadruplex structure in the 3'-untranslated region of NR2B mRNA.

Snezana Stefanovic, Brett A DeMarco, Ayana Underwood, Kathryn R Williams, Gary J Bassell, Mihaela Rita Mihailescu

Abstract read
In one paragraph

Article in Molecular bioSystems, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  8. FUS Recognizes G Quadruplex Structures Within Neuronal mRNAs.Frontiers in molecular biosciences · 2020
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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

6 authors at 2 institutions in 1 country.

Snezana StefanovicDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA. mihailescum@duq.edu.
Brett A DeMarcoDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA. mihailescum@duq.edu.
Ayana UnderwoodDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA. mihailescum@duq.edu.
Kathryn R WilliamsDepartment of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Gary J BassellDepartment of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Mihaela Rita MihailescuDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA. mihailescum@duq.edu.
Duquesne University · USEmory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Role of MicroRNAs in Activity Regulated Synthesis and Insertion of Membrane ProteinsR21NS089080 · NINDS · EMORY UNIVERSITY · PI BASSELL, GARY J · 2015 to 2016
$424k
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 HD078017NIGMS NIH HHS T32 GM008367NINDS NIH HHS 1R21NS089080NINDS NIH HHS R21 NS089080
6 · The paper itself

Abstract

Fragile X syndrome, the most common cause of inherited intellectual disability, is caused by a trinucleotide CGG expansion in the 5'-untranslated region of the FMR1 gene, which leads to the loss of expression of the fragile X mental retardation protein (FMRP). FMRP, an RNA-binding protein that regulates the translation of specific mRNAs, has been shown to bind a subset of its mRNA targets by recognizing G quadruplex structures. It has been suggested that FMRP controls the local protein synthesis of several protein components of the post synaptic density (PSD) in response to specific cellular needs. We have previously shown that the interactions between FMRP and mRNAs of the PSD scaffold proteins PSD-95 and Shank1 are mediated via stable G-quadruplex structures formed within the 3'-untranslated regions of these mRNAs. In this study we used biophysical methods to show that a comparable G quadruplex structure forms in the 3'-untranslated region of the glutamate receptor subunit NR2B mRNA encoding for a subunit of N-methyl-d-aspartate (NMDA) receptors that is recognized specifically by FMRP, suggesting a common theme for FMRP recognition of its dendritic mRNA targets.

Indexed as

3' Untranslated RegionsG-QuadruplexesBase SequenceFragile X Messenger Ribonucleoprotein 1Fragile X SyndromeHumansProtein BindingProton Magnetic Resonance SpectroscopyReceptors, N-Methyl-D-AspartateRNA, MessengerThermodynamics3' Untranslated RegionsFragile X Messenger Ribonucleoprotein 1NR2B NMDA receptorReceptors, N-Methyl-D-AspartateRNA, Messenger

Identifiers

PMID26412477
PMCPMC4643373
OpenAlexW1763130527

What OpenQuestion holds

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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.