Evidence map›Paper›PMID 30857591›Full record

ArticleeLife2019

Learning protein constitutive motifs from sequence data.

Jérôme Tubiana, Simona Cocco, Rémi Monasson

Abstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Article
  2. Constrained evolutionary funnels shape viral immune escape.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
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  6. Constrained Evolutionary Funnels Shape Viral Immune Escape.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
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  13. Machine learning in biological physics: From biomolecular prediction to design.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  15. Review
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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

3 authors.

Jérôme TubianaLaboratory of Physics of the Ecole Normale Supérieure, CNRS UMR 8023 & PSL Research, Paris, France.ORCID 0000-0001-8878-5620
Simona CoccoLaboratory of Physics of the Ecole Normale Supérieure, CNRS UMR 8023 & PSL Research, Paris, France.ORCID 0000-0002-1852-7789
Rémi MonassonLaboratory of Physics of the Ecole Normale Supérieure, CNRS UMR 8023 & PSL Research, Paris, France.ORCID 0000-0002-4459-0204

Funding

Agence Nationale de la Recherche CE30-0021-01 RBMProEcole Normale Supérieure Allocation SpecifiqueÉcole Normale Supérieure Allocation Specifique
6 · The paper itself

Abstract

Statistical analysis of evolutionary-related protein sequences provides information about their structure, function, and history. We show that Restricted Boltzmann Machines (RBM), designed to learn complex high-dimensional data and their statistical features, can efficiently model protein families from sequence information. We here apply RBM to 20 protein families, and present detailed results for two short protein domains (Kunitz and WW), one long chaperone protein (Hsp70), and synthetic lattice proteins for benchmarking. The features inferred by the RBM are biologically interpretable: they are related to structure (residue-residue tertiary contacts, extended secondary motifs (α-helixes and β-sheets) and intrinsically disordered regions), to function (activity and ligand specificity), or to phylogenetic identity. In addition, we use RBM to design new protein sequences with putative properties by composing and 'turning up' or 'turning down' the different modes at will. Our work therefore shows that RBM are versatile and practical tools that can be used to unveil and exploit the genotype-phenotype relationship for protein families.

Indexed as

Amino Acid MotifsAlgorithmsComputational BiologyEscherichia coliEscherichia coli ProteinsGenetic Association StudiesHSP70 Heat-Shock ProteinsHumansLigandsMachine LearningModels, StatisticalMutagenesisNormal DistributionPhylogenyProbabilityProtein BindingdnaK protein, E coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsLigandsProteinscoevolutioncomputational biologymachine learningnonephysics of living systemssequence analysissystems biology

Identifiers

PMID30857591
PMCPMC6436896

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.