Evidence map›Paper›PMID 31852734›Full record

ArticleRNA (New York, N.Y.)2020

A multipronged approach to understanding the form and function of hStaufen protein.

Silvia Visentin, Giuseppe Cannone, James Doutch, Gemma Harris, Michael L Gleghorn, Luke Clifton, Brian O Smith, Laura Spagnolo

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

8 authors at 4 institutions in 2 countries.

Silvia VisentinInstitute of Molecular Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, United Kingdom.
Giuseppe CannoneInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JQ, United Kingdom.
James DoutchISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Didcot OX11 OQX, United Kingdom.
Gemma HarrisResearch Complex at Harwell, Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0FA, United Kingdom.
Michael L GleghornSchool of Chemistry and Materials Science, College of Science, Rochester Institute of Technology, Rochester, New York 14623, USA.
Luke CliftonISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Didcot OX11 OQX, United Kingdom.
Brian O SmithInstitute of Molecular Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0000-0003-3363-4168
Laura SpagnoloInstitute of Molecular Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0000-0002-0794-566X
Rutherford Appleton Laboratory · GBUniversity of Glasgow · GBMRC Laboratory of Molecular Biology · GBRochester Institute of Technology · US

Funding

Medical Research Council MC_U105184326
6 · The paper itself

Abstract

Staufen is a dsRNA-binding protein involved in many aspects of RNA regulation, such as mRNA transport, Staufen-mediated mRNA decay and the regulation of mRNA translation. It is a modular protein characterized by the presence of conserved consensus amino acid sequences that fold into double-stranded RNA binding domains (RBDs) as well as degenerated RBDs that are instead involved in protein-protein interactions. The variety of biological processes in which Staufen participates in the cell suggests that this protein associates with many diverse RNA targets, some of which have been identified experimentally. Staufen binding mediates the recruitment of effectors via protein-protein and protein-RNA interactions. The structural determinants of a number of these interactions, as well as the structure of full-length Staufen, remain unknown. Here, we present the first solution structure models for full-length hStaufen1

Indexed as

Protein ConformationAmino Acid SequenceCytoskeletal ProteinsHumansNucleic Acid ConformationProtein BiosynthesisProtein Interaction Domains and MotifsRNA-Binding ProteinsRNA StabilityCytoskeletal ProteinsRNA-Binding ProteinsSTAU1 protein, humandsRNA-binding domainSAXSStaufenstructural biology

Identifiers

PMID31852734
PMCPMC7025507
OpenAlexW2996719451

What OpenQuestion 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 OpenQuestion graph.