Evidence map›Paper›PMID 25999294›Full record

ArticleScientific reports2015

Intrinsically disordered energy landscapes.

Yassmine Chebaro, Andrew J Ballard, Debayan Chakraborty, David J Wales

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 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. SIRT1 Exon 2-Encoded IDR Gates CREB-Dependent Transcriptional Timing During Fasting.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Article
  3. Review
  4. Intrinsic Disorder as a Biomimetic Design Paradigm.Biomimetics (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Decoding Solubility Signatures from Amyloid Monomer Energy Landscapes.Journal of chemical theory and computation · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Transition Networks Unveil Disorder-to-Order Transformations in AInternational journal of molecular sciences · 2023
    Article
  19. Article
  20. Oligomeric State and Holding Activity of Hsp60.International journal of molecular sciences · 2023
    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.

Yassmine ChebaroDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW.
Andrew J BallardDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW.
Debayan ChakrabortyDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW.
David J WalesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Analysis of an intrinsically disordered protein (IDP) reveals an underlying multifunnel structure for the energy landscape. We suggest that such 'intrinsically disordered' landscapes, with a number of very different competing low-energy structures, are likely to characterise IDPs, and provide a useful way to address their properties. In particular, IDPs are present in many cellular protein interaction networks, and several questions arise regarding how they bind to partners. Are conformations resembling the bound structure selected for binding, or does further folding occur on binding the partner in a induced-fit fashion? We focus on the p53 upregulated modulator of apoptosis (PUMA) protein, which adopts an α-helical conformation when bound to its partner, and is involved in the activation of apoptosis. Recent experimental evidence shows that folding is not necessary for binding, and supports an induced-fit mechanism. Using a variety of computational approaches we deduce the molecular mechanism behind the instability of the PUMA peptide as a helix in isolation. We find significant barriers between partially folded states and the helix. Our results show that the favoured conformations are molten-globule like, stabilised by charged and hydrophobic contacts, with structures resembling the bound state relatively unpopulated in equilibrium.

Indexed as

AnimalsApoptosis Regulatory ProteinsHydrogen BondingMiceMolecular Dynamics SimulationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySolventsThermodynamicsTumor Suppressor ProteinsApoptosis Regulatory ProteinsPUMA protein, mouseSolventsTumor Suppressor Proteins

Identifiers

PMID25999294
PMCPMC4441119

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.