Evidence map›Paper›PMID 34610267›Full record

ReviewOpen biology2021

Intrinsically disordered proteins: modes of binding with emphasis on disordered domains.

Owen Michael Morris, James Hilary Torpey, Rivka Leah Isaacson

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
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

57 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Review
  3. RSC chemical biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. bioRxiv : the preprint server for biology · 2026
    Article
  10. Functions of prolyl hydroxylation in elastin.The Journal of biological chemistry · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025
    Review
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 at 1 institution in 1 country.

Owen Michael MorrisDepartment of Chemistry, Faculty of Natural, Mathematical and Engineering Sciences, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, UK.
James Hilary TorpeyDepartment of Chemistry, Faculty of Natural, Mathematical and Engineering Sciences, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, UK.ORCID 0000-0003-3388-4992
Rivka Leah IsaacsonDepartment of Chemistry, Faculty of Natural, Mathematical and Engineering Sciences, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, UK.ORCID 0000-0002-9978-8904
King's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N006267/1Biotechnology and Biological Sciences Research Council BB/S006877/1
6 · The paper itself

Abstract

Our notions of protein function have long been determined by the protein structure-function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly challenged. Interactions involving intrinsically disordered proteins (IDPs) have indicated a significant degree of disorder present in the bound state, ranging from static disorder to complete disorder, termed 'random fuzziness'. This review assesses the anatomy of an IDP and relates how its intrinsic properties permit promiscuity and allow for the various modes of interaction. Furthermore, a mechanistic overview of the types of disordered domains is detailed, while also relating to a recent example and the kinetic and thermodynamic principles governing its formation.

Indexed as

AnimalsHumansIntrinsically Disordered ProteinsModels, MolecularProtein BindingProtein ConformationProtein DomainsProtein FoldingIntrinsically Disordered Proteinsfuzzy bindingintrinsic disorderprotein folding

Identifiers

PMID34610267
PMCPMC8492171
OpenAlexW3202009088

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.