Evidence map›Paper›PMID 26399546›Full record

ArticleScientific reports2015

Protein interaction patterns in different cellular environments are revealed by in-cell NMR.

Letizia Barbieri, Enrico Luchinat, Lucia Banci

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Direct Quantification of Protein-Protein Interactions in Living Bacterial Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. RNA Structure: Past, Future, and Gene Therapy Applications.International journal of molecular sciences · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Ligand-Based Competition Binding by Real-TimeJournal of medicinal chemistry · 2024
    Article
  11. The Knowns and Unknowns in Protein-Metabolite Interactions.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Colloidal stability of the living cell.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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.

Letizia BarbieriMagnetic Resonance Center - CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.
Enrico LuchinatMagnetic Resonance Center - CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.
Lucia BanciMagnetic Resonance Center - CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiological environment. Soluble proteins may interact with the cellular environment in different ways: either specifically, with their functional partners, or non-specifically, with other cellular components. Such behaviour often causes the disappearance of the NMR signals. Here we show that by introducing mutations on the human protein profilin 1, used here as a test case, the in-cell NMR signals can be recovered. In human cells both specific and non-specific interactions are present, while in bacterial cells only the effect of non-specific interactions is observed. By comparing the NMR signal recovery pattern in human and bacterial cells, the relative contribution of each type of interaction can be assessed. This strategy allows detecting solution in-cell NMR spectra of soluble proteins without altering their fold, thus extending the applicability of in-cell NMR to a wider range of proteins.

Indexed as

Magnetic Resonance SpectroscopyProtein Interaction MappingCarrier ProteinsEscherichia coliHEK293 CellsHumansIntracellular SpaceModels, MolecularMutationNuclear Magnetic Resonance, BiomolecularProfilinsProtein BindingProtein ConformationProteinsCarrier ProteinsProfilinsProteins

Identifiers

PMID26399546
PMCPMC4585868

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.