Evidence map›Paper›PMID 28277547›Full record

ArticleNature protocols2017

Backbone assignment of perdeuterated proteins by solid-state NMR using proton detection and ultrafast magic-angle spinning.

Pascal Fricke, Veniamin Chevelkov, Maximilian Zinke, Karin Giller, Stefan Becker, Adam Lange

Abstract read
PubMed Publisher
In one paragraph

Article in Nature protocols, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.8field-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

47 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  4. bioRxiv : the preprint server for biology · 2025
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  7. OPTO: Automated Optimization for Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2025
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  9. Review
  10. Low power supercycled TPPM decoupling.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024
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  11. Homonuclear Simplified Preservation of Equivalent Pathways Spectroscopy.The journal of physical chemistry letters · 2024
    Article
  12. Article
  13. Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024
    Article
  14. Detecting Bound Ions in Ion Channels by Solid-State NMR Experiments onMethods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Journal of biomolecular NMR · 2023
    Article
  16. Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.Journal of the American Chemical Society · 2023
    Article
  17. TapA acts as specific chaperone in TasA filament formation by strand complementation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Review
  19. Article
  20. PHRONESIS: A One-Shot Approach for Sequential Assignment of Protein Resonances by Ultrafast MAS Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    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

6 authors at 2 institutions in 1 country.

Pascal FrickeDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.
Veniamin ChevelkovDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.
Maximilian ZinkeDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.
Karin GillerDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Stefan BeckerDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Adam LangeDepartment of Molecular Biophysics, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solid-state NMR (ssNMR) is a technique that allows the study of protein structure and dynamics at atomic detail. In contrast to X-ray crystallography and cryo-electron microscopy, proteins can be studied under physiological conditions-for example, in a lipid bilayer and at room temperature (0-35 °C). However, ssNMR requires considerable amounts (milligram quantities) of isotopically labeled samples. In recent years,

Indexed as

ProtonsLipid BilayersMagnetic Resonance SpectroscopyProteinsTemperatureTime FactorsLipid BilayersProteinsProtons

Identifiers

PMID28277547
OpenAlexW2594084949

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.