Evidence map›Paper›PMID 28631009›Full record

ReviewCellular and molecular life sciences : CMLS2017

Methods of probing the interactions between small molecules and disordered proteins.

Gabriella T Heller, Francesco A Aprile, Michele Vendruscolo

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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.

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3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Identification of Catechins' Binding Sites in Monomeric AInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. The Knowns and Unknowns in Protein-Metabolite Interactions.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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

3 authors.

Gabriella T HellerDepartment of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Francesco A AprileDepartment of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. mv245@cam.ac.uk.

Funding

HSRD VA IIR 16-003
6 · The paper itself

Abstract

It is generally recognized that a large fraction of the human proteome is made up of proteins that remain disordered in their native states. Despite the fact that such proteins play key biological roles and are involved in many major human diseases, they still represent challenging targets for drug discovery. A major bottleneck for the identification of compounds capable of interacting with these proteins and modulating their disease-promoting behaviour is the development of effective techniques to probe such interactions. The difficulties in carrying out binding measurements have resulted in a poor understanding of the mechanisms underlying these interactions. In order to facilitate further methodological advances, here we review the most commonly used techniques to probe three types of interactions involving small molecules: (1) those that disrupt functional interactions between disordered proteins; (2) those that inhibit the aberrant aggregation of disordered proteins, and (3) those that lead to binding disordered proteins in their monomeric states. In discussing these techniques, we also point out directions for future developments.

Indexed as

Circular DichroismFluorescence PolarizationFluorescence Resonance Energy TransferHumansIntrinsically Disordered ProteinsProtein BindingScattering, Small AngleSmall Molecule LibrariesSurface Plasmon ResonanceTwo-Hybrid System TechniquesIntrinsically Disordered ProteinsSmall Molecule LibrariesBindingDisordered proteinsDrugsMolecular interactionsSmall molecules

Identifiers

PMID28631009
PMCPMC5533867

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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.