Evidence map›Paper›PMID 26217672›Full record

ArticleFrontiers in molecular biosciences2015

Globular and disordered-the non-identical twins in protein-protein interactions.

Kaare Teilum, Johan G Olsen, Birthe B Kragelund

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Comment on "Intrinsic protein disorder uncouples affinity from binding specificity".Protein science : a publication of the Protein Society · 2023
    Article
  7. Reply to "Intrinsic protein disorder uncouples affinity from binding specificity".Protein science : a publication of the Protein Society · 2023
    Article
  8. Protein Binding: A Fuzzy Concept.Life (Basel, Switzerland) · 2023
    Article
  9. Article
  10. Article
  11. Affinity of disordered protein complexes is modulated by entropy-energy reinforcement.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
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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.

Kaare TeilumStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen Copenhagen, Denmark.
Johan G OlsenStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen Copenhagen, Denmark.
Birthe B KragelundStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen Copenhagen, Denmark.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs. The interactions between intrinsically disordered proteins (IDPs) and other proteins rely on changes in flexibility and this is seen as a strong determinant for their function. This has fostered the notion that IDP's bind with low affinity but high specificity. Here we have analyzed available detailed thermodynamic data for protein-protein interactions to put to the test if the thermodynamic profiles of IDP interactions differ from those of other protein-protein interactions. We find that ordered proteins and the disordered ones act as non-identical twins operating by similar principles but where the disordered proteins complexes are on average less stable by 2.5 kcal mol(-1).

Indexed as

enthalpyentropyIDPintrinsically disorderedITCstability

Identifiers

PMID26217672
PMCPMC4496568

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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.