Evidence map›Paper›PMID 36210722›Full record

ArticleProtein science : a publication of the Protein Society2022

Intrinsic protein disorder and conditional folding in AlphaFoldDB.

Damiano Piovesan, Alexander Miguel Monzon, Silvio C E Tosatto

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed, 1 pooled it
–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

99 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. Queue Gaps Among the IQGAPs inInternational journal of molecular sciences · 2026
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  16. Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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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.

Damiano PiovesanDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Alexander Miguel MonzonDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-0362-8218
Silvio C E TosattoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-4525-7793

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered regions (IDRs) defying the traditional protein structure-function paradigm have been difficult to analyze. The availability of accurate structure predictions on a large scale in AlphaFoldDB offers a fresh perspective on IDR prediction. Here, we establish three baselines for IDR prediction from AlphaFoldDB models based on the recent CAID dataset. Surprisingly, AlphaFoldDB is highly competitive for predicting both IDRs and conditionally folded binding regions, demonstrating the plasticity of the disorder to structure continuum.

Indexed as

Intrinsically Disordered ProteinsProtein ConformationProtein FoldingIntrinsically Disordered ProteinsCAIDcritical assessmentintrinsically disordered proteinsmachine learningprotein structurestructural bioinformatics

Identifiers

PMID36210722
PMCPMC9601767

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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.