Evidence map›Paper›PMID 24096002›Full record

ArticleMethods (San Diego, Calif.)2014

Screening protein--single stranded RNA complexes by NMR spectroscopy for structure determination.

Jaelle N Foot, Mikael Feracci, Cyril Dominguez

Open access · hybridAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
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  8. Intrinsically disordered proteins in the nucleus of human cells.Biochemistry and biophysics reports · 2015
    Article
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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

3 authors at 2 institutions in 1 country.

Jaelle N FootDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, UK.
Mikael FeracciDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, UK.
Cyril DominguezDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, UK. Electronic address: cyril.dominguez@leicester.ac.uk.
University of Leicester · GBInstitute of Structural and Molecular Biology · GB

Funding

Medical Research Council G1000526
6 · The paper itself

Abstract

In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory roles. Associated with that, the number of identified RNA binding proteins (RBPs) has increased considerably and mutations in RNA molecules or RBP have been shown to cause various diseases, such as cancers. It is therefore crucial to understand at the molecular level how these proteins specifically recognise their RNA targets in order to design new generation drug therapies targeting protein-RNA complexes. Nuclear magnetic resonance (NMR) is a particularly well-suited technique to study such protein-RNA complexes at the atomic level and can provide valuable information for new drug discovery programs. In this article, we describe the NMR strategy that we and other laboratories use for screening optimal conditions necessary for structural studies of protein-single stranded RNA complexes, using two proteins, Sam68 and T-STAR, as examples.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAptamers, NucleotideBinding SitesCrystallography, X-RayDNA-Binding ProteinsEscherichia coliGene ExpressionHumansMagnetic Resonance SpectroscopyMolecular Sequence DataProtein BindingProtein Structure, TertiaryRecombinant ProteinsRNA-Binding ProteinsSequence AlignmentAdaptor Proteins, Signal TransducingAptamers, NucleotideDNA-Binding ProteinsKHDRBS1 protein, humanKHDRBS3 protein, humanRecombinant ProteinsRNA-Binding ProteinsNMR spectroscopyProtein–RNA complexSam68STAR proteinsT-STAR

Identifiers

PMID24096002
PMCPMC3959648
OpenAlexW2000954453

What OpenQuestion holds

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LicenceCC BY
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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.