Evidence map›Paper›PMID 24203099›Full record

ArticleJournal of biomolecular NMR2013

High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.

Wolfgang Bermel, Isabella C Felli, Leonardo Gonnelli, Wiktor Koźmiński, Alessandro Piai, Roberta Pierattelli, Anna Zawadzka-Kazimierczuk

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Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. A call to order: Examining structured domains in biomolecular condensates.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  2. Chemical reviews · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Journal of biomolecular NMR · 2018
    Article
  8. Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. 1H, 15N, 13C resonance assignment of human GAP-43.Biomolecular NMR assignments · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

7 authors.

Wolfgang BermelBruker BioSpin GmbH, Silberstreifen, 76287, Rheinstetten, Germany.
Isabella C Felli
Leonardo Gonnelli
Wiktor Koźmiński
Alessandro Piai
Roberta Pierattelli
Anna Zawadzka-Kazimierczuk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present three novel exclusively heteronuclear 5D (13)C direct-detected NMR experiments, namely (H(N-flip)N)CONCACON, (HCA)CONCACON and (H)CACON(CA)CON, designed for easy sequence-specific resonance assignment of intrinsically disordered proteins (IDPs). The experiments proposed have been optimized to overcome the drawbacks which may dramatically complicate the characterization of IDPs by NMR, namely the small dispersion of chemical shifts and the fast exchange of the amide protons with the solvent. A fast and reliable automatic assignment of α-synuclein chemical shifts was obtained with the Tool for SMFT-based Assignment of Resonances (TSAR) program based on the information provided by these experiments.

Indexed as

Carbon IsotopesIntrinsically Disordered ProteinsNuclear Magnetic Resonance, BiomolecularCarbon IsotopesIntrinsically Disordered Proteins

Identifiers

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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.