Evidence map›Paper›PMID 34204764›Full record

ArticleGenes2021

A Deep-Learning Sequence-Based Method to Predict Protein Stability Changes Upon Genetic Variations.

Corrado Pancotti, Silvia Benevenuta, Valeria Repetto, Giovanni Birolo, Emidio Capriotti, Tiziana Sanavia, Piero Fariselli

Abstract read
In one paragraph

Article in Genes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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  8. Mass balance approximation of unfolding boosts potential-based protein stability predictions.Protein science : a publication of the Protein Society · 2025
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  16. Transfer learning to leverage larger datasets for improved prediction of protein stability changes.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

7 authors.

Corrado PancottiDepartment of Medical Science, University of Turin, Via Santena 19, 10126 Torino, Italy.ORCID 0000-0003-2327-1148
Silvia BenevenutaDepartment of Medical Science, University of Turin, Via Santena 19, 10126 Torino, Italy.ORCID 0000-0002-4733-8338
Valeria RepettoDepartment of Medical Science, University of Turin, Via Santena 19, 10126 Torino, Italy.ORCID 0000-0001-8678-3189
Giovanni BiroloDepartment of Medical Science, University of Turin, Via Santena 19, 10126 Torino, Italy.ORCID 0000-0003-0160-9312
Emidio CapriottiDepartment of Pharmacy and Biotechnology (FaBiT), University of Bologna, Via Francesco Selmi 3, 40126 Bologna, Italy.ORCID 0000-0002-2323-0963
Tiziana SanaviaDepartment of Medical Science, University of Turin, Via Santena 19, 10126 Torino, Italy.ORCID 0000-0003-3288-0631
Piero FariselliDepartment of Medical Science, University of Turin, Via Santena 19, 10126 Torino, Italy.ORCID 0000-0003-1811-4762

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several studies have linked disruptions of protein stability and its normal functions to disease. Therefore, during the last few decades, many tools have been developed to predict the free energy changes upon protein residue variations. Most of these methods require both sequence and structure information to obtain reliable predictions. However, the lower number of protein structures available with respect to their sequences, due to experimental issues, drastically limits the application of these tools. In addition, current methodologies ignore the antisymmetric property characterizing the thermodynamics of the protein stability: a variation from wild-type to a mutated form of the protein structure (XW→XM) and its reverse process (XM→XW) must have opposite values of the free energy difference (ΔΔGWM=-ΔΔGMW). Here we propose ACDC-NN-Seq, a deep neural network system that exploits the sequence information and is able to incorporate into its architecture the antisymmetry property. To our knowledge, this is the first convolutional neural network to predict protein stability changes relying solely on the protein sequence. We show that ACDC-NN-Seq compares favorably with the existing sequence-based methods.

Indexed as

Deep LearningGenetic VariationProtein StabilityAmino Acid SubstitutionHumansMolecular Dynamics SimulationSequence Analysis, ProteinACDCantisymmetrydeep learningfree energy changesprotein stabilitysequence

Identifiers

PMID34204764
PMCPMC8231498

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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.