Evidence map›Paper›PMID 31960224›Full record

ArticleJournal of biomolecular NMR2020

Boosting the resolution of low-field

Zuzana Jaseňáková, Vojtěch Zapletal, Petr Padrta, Milan Zachrdla, Nicolas Bolik-Coulon, Thorsten Marquardsen, Jean-Max Tyburn, Lukáš Žídek, Fabien Ferrage, Pavel Kadeřávek

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

10 authors.

Zuzana JaseňákováNational Centre for Biomolecular Research, Faculty of Science and Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.
Vojtěch ZapletalNational Centre for Biomolecular Research, Faculty of Science and Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.
Petr PadrtaCentral European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.
Milan ZachrdlaLaboratoire des Biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.
Nicolas Bolik-CoulonLaboratoire des Biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.
Thorsten MarquardsenBruker BioSpin GmbH, Silberstreifen 4, 76287, Rheinstetten, Germany.
Jean-Max TyburnBruker BioSpin, 34 rue de l'Industrie BP 10002, 67166, Wissembourg Cedex, France.
Lukáš ŽídekNational Centre for Biomolecular Research, Faculty of Science and Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.
Fabien FerrageLaboratoire des Biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France. fabien.ferrage@ens.fr.
Pavel KadeřávekCentral European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic. pavel.kaderavek@mail.muni.cz.ORCID 0000-0002-3561-354X

Funding

Agence Nationale de la Recherche ANR-18-CE29-0003European Cooperation in Science and Technology CA15209Grantová Agentura České Republiky GA18-04197Y
6 · The paper itself

Abstract

Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of relaxation have, so far, only been based on the recording of one- or two-dimensional spectra, which provide insufficient resolution for challenging disordered proteins. Here, we introduce a 3D-HNCO-based two-field NMR experiment for measurements of protein backbone

Indexed as

Nuclear Magnetic Resonance, BiomolecularBacillus subtilisBacterial ProteinsDNA-Directed RNA PolymerasesIntrinsically Disordered ProteinsRecombinant ProteinsBacterial ProteinsDNA-Directed RNA PolymerasesIntrinsically Disordered ProteinsRecombinant ProteinsDynamicsHigh-resolution relaxometryIntrinsically disordered proteinsNon-uniform samplingNuclear magnetic resonanceRelaxation

Identifiers

PMID31960224

What OpenQuestion holds

Textmetadata
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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.