Evidence map›Paper›PMID 30175546›Full record

ArticleAngewandte Chemie (International ed. in English)2018

XLSY: Extra-Large NMR Spectroscopy.

Yulia Pustovalova, Maxim Mayzel, Vladislav Yu Orekhov

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.Angewandte Chemie (International ed. in English) · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. XLSY: Extra-Large NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2018
    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

3 authors.

Yulia PustovalovaDepartment of Chemistry and Molecular Biology, University of Gothenburg, P.O. Box 465, Gothenburg, 405 30, Sweden.ORCID 0000-0003-3024-1764
Maxim MayzelSwedish NMR Centre, University of Gothenburg, P.O. Box 465, Gothenburg, 405 30, Sweden.
Vladislav Yu OrekhovDepartment of Chemistry and Molecular Biology, University of Gothenburg, P.O. Box 465, Gothenburg, 405 30, Sweden.ORCID 0000-0002-7892-6896

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NMR studies of intrinsically disordered proteins and other complex biomolecular systems require spectra with the highest resolution and dimensionality. An efficient approach, extra-large NMR spectroscopy, is presented for experimental data collection, reconstruction, and handling of very large NMR spectra by a combination of the radial and non-uniform sampling, a new processing algorithm, and rigorous statistical validation. We demonstrate the first high-quality reconstruction of a full seven-dimensional HNCOCACONH and two five-dimensional HACACONH and HN(CA)CONH experiments for a representative intrinsically disordered protein α-synuclein. XLSY will significantly enhance the NMR toolbox in challenging biomolecular studies.

Indexed as

Algorithmsalpha-SynucleinIntrinsically Disordered ProteinsNuclear Magnetic Resonance, BiomolecularProtein Conformationalpha-SynucleinIntrinsically Disordered Proteinsintrinsically disordered proteinNMR spectroscopynon-uniform samplingXLSY

Identifiers

PMID30175546
PMCPMC6585689

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.