Evidence map›Paper›PMID 41174312›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Computational Identification of Potential Shape-Shifting Proteins from Structures.

Francisco M Pérez-Canales, Enrique Alanís-Domínguez, Ana M Rojas

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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Francisco M Pérez-CanalesCABD-CSIC, Computational Biology and Bioinformatics Group, Seville, Spain.
Enrique Alanís-DomínguezCABD-CSIC, Computational Biology and Bioinformatics Group, Seville, Spain.
Ana M RojasCABD-CSIC, Computational Biology and Bioinformatics Group, Seville, Spain. a.rojas.m@csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The "one structure-one function" paradigm is central to most computational methods for predicting protein function. However, a subset of proteins known as shape-shifters can adopt multiple well-defined structures to perform distinct biological functions. These proteins, along with intrinsically disordered proteins (IDPs) that fold upon binding, challenge conventional views of protein functionality. Despite their biological significance, identifying fold-switching proteins remains difficult due to limited structural data and the limitations of current prediction methods.In this study, we present a computational protocol to identify potential shape-shifting proteins within structural databases. By integrating structural and sequence data, this approach enables the screening of the Protein Data Bank (PDB) for proteins exhibiting significant conformational variability.

Indexed as

Computational BiologyIntrinsically Disordered ProteinsProtein ConformationProteinsAmino Acid SequenceCryoelectron MicroscopyDatabases, ProteinModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein FoldingSequence AlignmentIntrinsically Disordered ProteinsProteinsFold-switchingFunctionShape-shifting proteinsStructural alignment

Identifiers

PMID41174312

What OpenQuestion holds

Textmetadata
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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.