Evidence map›Paper›PMID 38251829›Full record

ArticleJournal of the American Chemical Society2024

Picosecond Dynamics of a Small Molecule in Its Bound State with an Intrinsically Disordered Protein.

Gabriella T Heller, Vaibhav Kumar Shukla, Angelo Miguel Figueiredo, D Flemming Hansen

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Rapid Fragment Screening byAngewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. AcceleratedMagnetic resonance (Gottingen, Germany) · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

4 authors.

Gabriella T HellerDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, U.K.ORCID 0000-0002-5672-0467
Vaibhav Kumar ShuklaDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, U.K.
Angelo Miguel FigueiredoDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, U.K.ORCID 0000-0001-7039-5341
D Flemming HansenDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, U.K.ORCID 0000-0003-0891-220X

Funding

Wellcome Trust
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are highly dynamic biomolecules that rapidly interconvert among many structural conformations. These dynamic biomolecules are involved in cancers, neurodegeneration, cardiovascular illnesses, and viral infections. Despite their enormous therapeutic potential, IDPs have generally been considered undruggable because of their lack of classical long-lived binding pockets for small molecules. Currently, only a few instances are known where small molecules have been observed to interact with IDPs, and this situation is further exacerbated by the limited sensitivity of experimental techniques to detect such binding events. Here, using experimental nuclear magnetic resonance (NMR) spectroscopy

Indexed as

Intrinsically Disordered ProteinsMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein ConformationIntrinsically Disordered Proteins

Identifiers

PMID38251829
PMCPMC10835725

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.