Evidence map›Paper›PMID 24699834›Full record

ArticleJournal of biomolecular NMR2014

New 13C-detected experiments for the assignment of intrinsically disordered proteins.

David Pantoja-Uceda, Jorge Santoro

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Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 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. Article
  3. Article
  4. Chemical reviews · 2022
    Review
  5. Article
  6. HACANCOi: a new HJournal of biomolecular NMR · 2020
    Article
  7. Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020
    Review
  8. Dispersion from CJournal of biomolecular NMR · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Quarterly intrinsic disorder digest (April-May-June, 2014).Intrinsically disordered proteins · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

2 authors.

David Pantoja-UcedaInstituto de Química Física Rocasolano, CSIC, Serrano 119, 28006, Madrid, Spain.
Jorge Santoro

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NMR assignment of intrinsically disordered proteins (IDPs) by conventional HN-detected methods is hampered by the small dispersion of the amide protons chemical shifts and exchange broadening of amide proton signals. Therefore several alternative assignment strategies have been proposed in the last years. Attempting to seize that dispersion of (13)C' and (15)N chemical shifts holds even in IDPs, we recently proposed two (13)C-detected experiments to directly correlate the chemical shifts of two consecutive (13)C'-(15)N groups in proteins, i.e. without mediation of other nuclei. Main drawback of these experiments is the interruption of the connection at prolines. Here we present new (13)C-detected experiments to correlate consecutive (13)C'-(15)N groups in IDPs, hacacoNcaNCO and hacaCOncaNCO, that overcome this limitation. Moreover, the experiments provide recognition of glycine residues, thereby facilitating the assignment process.

Indexed as

Nuclear Magnetic Resonance, BiomolecularCarbon IsotopesIntrinsically Disordered ProteinsNitrogen IsotopesCarbon IsotopesIntrinsically Disordered ProteinsNitrogen Isotopes

Identifiers

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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.