Evidence map›Paper›PMID 29694866›Full record

ArticleBiophysical journal2018

How Robust Is the Mechanism of Folding-Upon-Binding for an Intrinsically Disordered Protein?

Daniela Bonetti, Francesca Troilo, Maurizio Brunori, Sonia Longhi, Stefano Gianni

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Determinants of Protein Folding Pathways: Lessons from Metamorphic Proteins.International journal of molecular sciences · 2026
    Review
  3. Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Regulation of Age-Related Protein Toxicity.Frontiers in cell and developmental biology · 2021
    Review
  11. Article
  12. Classifying the Binding Modes of Disordered Proteins.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Article
  15. Review
  16. Templated folding of intrinsically disordered proteins.The Journal of biological chemistry · 2020
    Review
  17. Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020
    Review
  18. Article
  19. Review
  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

5 authors.

Daniela BonettiIstituto Pasteur - Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli," Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma, Rome, Italy.
Francesca TroiloIstituto Pasteur - Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli," Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma, Rome, Italy.
Maurizio BrunoriIstituto Pasteur - Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli," Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma, Rome, Italy.
Sonia LonghiArchitecture et Fonction des Macromolécules Biologiques, UMR 7257, National Centre for Scientific Research, Aix-Marseille Université, Marseille, France.
Stefano GianniIstituto Pasteur - Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli," Istituto di Biologia e Patologia Molecolari del CNR, Sapienza Università di Roma, Rome, Italy. Electronic address: stefano.gianni@uniroma1.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism of interaction of an intrinsically disordered protein (IDP) with its physiological partner is characterized by a disorder-to-order transition in which a recognition and a binding step take place. Even if the mechanism is quite complex, IDPs tend to bind their partner in a cooperative manner such that it is generally possible to detect experimentally only the disordered unbound state and the structured complex. The interaction between the disordered C-terminal domain of the measles virus nucleoprotein (N

Indexed as

Protein FoldingIntrinsically Disordered ProteinsModels, MolecularNucleocapsid ProteinsNucleoproteinsPhosphoproteinsProtein BindingProtein DomainsViral ProteinsIntrinsically Disordered ProteinsNucleocapsid Proteinsnucleoprotein, Measles virusNucleoproteinsPhosphoproteinsViral Proteins

Identifiers

PMID29694866
PMCPMC5937165

What OpenQuestion holds

Textmetadata
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.