Evidence map›Paper›PMID 39446390›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

AlphaFold-Multimer accurately captures interactions and dynamics of intrinsically disordered protein regions.

Alireza Omidi, Mads Harder Møller, Nawar Malhis, Jennifer M Bui, Jörg Gsponer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
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  5. Autosomal recessive MALTA syndrome with compound heterozygousJID innovations : skin science from molecules to population health · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. When can AlphaFold predict the oligomeric states of proteins?Protein science : a publication of the Protein Society · 2026
    Article
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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

5 authors.

Alireza OmidiMichael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.ORCID 0000-0003-3598-9480
Mads Harder MøllerMichael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.ORCID 0009-0004-0318-7058
Nawar MalhisMichael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.ORCID 0000-0002-1317-833X
Jennifer M BuiMichael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.ORCID 0009-0004-4861-3778
Jörg GsponerMichael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.

Funding

Canadian Government | Natural Sciences and Engineering Research Council of Canada (NSERC) AWD-015312
6 · The paper itself

Abstract

Interactions mediated by intrinsically disordered protein regions (IDRs) pose formidable challenges in structural characterization. IDRs are highly versatile, capable of adopting diverse structures and engagement modes. Motivated by recent strides in protein structure prediction, we embarked on exploring the extent to which AlphaFold-Multimer can faithfully reproduce the intricacies of interactions involving IDRs. To this end, we gathered multiple datasets covering the versatile spectrum of IDR binding modes and used them to probe AlphaFold-Multimer's prediction of IDR interactions and their dynamics. Our analyses revealed that AlphaFold-Multimer is not only capable of predicting various types of bound IDR structures with high success rate, but that distinguishing true interactions from decoys, and unreliable predictions from accurate ones is achievable by appropriate use of AlphaFold-Multimer's intrinsic scores. We found that the quality of predictions drops for more heterogeneous, fuzzy interaction types, most likely due to lower interface hydrophobicity and higher coil content. Notably though, certain AlphaFold-Multimer scores, such as the Predicted Aligned Error and residue-ipTM, are highly correlated with structural heterogeneity of the bound IDR, enabling clear distinctions between predictions of fuzzy and more homogeneous binding modes. Finally, our benchmarking revealed that predictions of IDR interactions can also be successful when using full-length proteins, but not as accurate as with cognate IDRs. To facilitate identification of the cognate IDR of a given partner, we established "minD," which pinpoints potential interaction sites in a full-length protein. Our study demonstrates that AlphaFold-Multimer can correctly identify interacting IDRs and predict their mode of engagement with a given partner.

Indexed as

Intrinsically Disordered ProteinsProtein FoldingHydrophobic and Hydrophilic InteractionsModels, MolecularProtein BindingProtein ConformationIntrinsically Disordered ProteinsAlphaFold2fuzzinessinteractionsintrinsically disordered protein

Identifiers

PMID39446390
PMCPMC11536093

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.