Evidence map›Paper›PMID 24336223›Full record

ArticleNature structural & molecular biology2014

Staufen1 senses overall transcript secondary structure to regulate translation.

Emiliano P Ricci, Alper Kucukural, Can Cenik, Blandine C Mercier, Guramrit Singh, Erin E Heyer, Ami Ashar-Patel, Lingtao Peng, Melissa J Moore

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed, 1 pooled it
6.0field-weighted citation impact, top 3% 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

95 citing papers in PubMed, 1 synthesis or guideline pooled it, 131 citations in OpenAlex.

  1. Pooled it
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  19. Emerging Roles of RNA-Binding Proteins in Neurodevelopment.Journal of developmental biology · 2022
    Review
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35 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

Emiliano P Ricci1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Alper Kucukural1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Can Cenik1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [4].
Blandine C Mercier1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Guramrit Singh1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Erin E Heyer1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Ami Ashar-Patel1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Lingtao Peng1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
Melissa J Moore1] Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [2] RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA. [3] Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
University of Massachusetts Chan Medical School · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Human Staufen1 (Stau1) is a double-stranded RNA (dsRNA)-binding protein implicated in multiple post-transcriptional gene-regulatory processes. Here we combined RNA immunoprecipitation in tandem (RIPiT) with RNase footprinting, formaldehyde cross-linking, sonication-mediated RNA fragmentation and deep sequencing to map Staufen1-binding sites transcriptome wide. We find that Stau1 binds complex secondary structures containing multiple short helices, many of which are formed by inverted Alu elements in annotated 3' untranslated regions (UTRs) or in 'strongly distal' 3' UTRs. Stau1 also interacts with actively translating ribosomes and with mRNA coding sequences (CDSs) and 3' UTRs in proportion to their GC content and propensity to form internal secondary structure. On mRNAs with high CDS GC content, higher Stau1 levels lead to greater ribosome densities, thus suggesting a general role for Stau1 in modulating translation elongation through structured CDS regions. Our results also indicate that Stau1 regulates translation of transcription-regulatory proteins.

Indexed as

Nucleic Acid ConformationProtein Biosynthesis3' Untranslated RegionsCytoskeletal ProteinsHEK293 CellsHumansRNA-Binding ProteinsRNA, Messenger3' Untranslated RegionsCytoskeletal ProteinsRNA-Binding ProteinsRNA, MessengerSTAU1 protein, human

Identifiers

PMID24336223
PMCPMC4605437
OpenAlexW2065023490

What OpenQuestion holds

Textmetadata
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.