Evidence map›Paper›PMID 23314728›Full record

ArticleJournal of biomolecular NMR2013

Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins.

Wolfgang Bermel, Marta Bruix, Isabella C Felli, Vasantha Kumar M V, Roberta Pierattelli, Soraya Serrano

Abstract read
PubMed Publisher
In one paragraph

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Journal of biomolecular NMR · 2025
    Article
  2. OptimalNature protocols · 2024
    Review
  3. A call to order: Examining structured domains in biomolecular condensates.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  4. Chemical reviews · 2022
    Review
  5. Article
  6. Journal of biomolecular NMR · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
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.

Wolfgang BermelBruker BioSpin GmbH, 76287 Rheinstetten, Germany.
Marta Bruix
Isabella C Felli
Vasantha Kumar M V
Roberta Pierattelli
Soraya Serrano

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) have recently attracted the attention of the scientific community challenging the well accepted structure-function paradigm. In the characterization of the dynamic features of proteins nuclear magnetic resonance spectroscopy (NMR) is a strategic tool of investigation. However the peculiar properties of IDPs, with the lack of a unique 3D structure and their high flexibility, have a strong impact on NMR observables (low chemical shift dispersion, efficient solvent exchange broadening) and thus on the quality of NMR spectra. Key aspects to be considered in the design of new NMR experiments optimized for the study of IDPs are discussed. A new experiment, based on direct detection of (13)C(α), is proposed.

Indexed as

HumansNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsProteins

Identifiers

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.