Evidence map›Paper›PMID 35562983›Full record

ArticleInternational journal of molecular sciences2022

AlphaFold2: A Role for Disordered Protein/Region Prediction?

Carter J Wilson, Wing-Yiu Choy, Mikko Karttunen

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
13.4field-weighted citation impact, top 1% 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

99 citing papers in PubMed, 168 citations in OpenAlex.

  1. Article
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  9. Generative design of intrinsically disordered protein regions with IDiom.bioRxiv : the preprint server for biology · 2026
    Article
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  11. Article
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  13. ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  14. Article
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  17. Proton-selective conductance and gating of the lysosomal cation channel TMEM175.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  20. Article

39 more citing papers are in PubMed but not listed here.

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.

Carter J WilsonDepartment of Mathematics, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5B7, Canada.ORCID 0000-0002-8992-6269
Wing-Yiu ChoyDepartment of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, Canada.ORCID 0000-0002-2124-7278
Mikko KarttunenCentre for Advanced Materials and Biomaterials Research, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5B7, Canada.ORCID 0000-0002-8626-3033
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of AlphaFold2 marked a paradigm-shift in the structural biology community. Herein, we assess the ability of AlphaFold2 to predict disordered regions against traditional sequence-based disorder predictors. We find that AlphaFold2 performs well at discriminating disordered regions, but also note that the disorder predictor one constructs from an AlphaFold2 structure determines accuracy. In particular, a naïve, but non-trivial assumption that residues assigned to helices, strands, and H-bond stabilized turns are likely ordered and all other residues are disordered results in a dramatic overestimation in disorder; conversely, the predicted local distance difference test (pLDDT) provides an excellent measure of residue-wise disorder. Furthermore, by employing molecular dynamics (MD) simulations, we note an interesting relationship between the pLDDT and secondary structure, that may explain our observations and suggests a broader application of the pLDDT for characterizing the local dynamics of intrinsically disordered proteins and regions (IDPs/IDRs).

Indexed as

Intrinsically Disordered ProteinsMolecular Dynamics SimulationProtein ConformationProtein DomainsProtein Structure, SecondaryIntrinsically Disordered ProteinsAlphaFold2biophysicsdisordered proteinsIDPs/IDRsmachine-learningmolecular dynamicssimulationstructural bioinformatics

Identifiers

PMID35562983
PMCPMC9104326
OpenAlexW4224259818

What OpenQuestion holds

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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.