Evidence map›Paper›PMID 24663061›Full record

ArticlePloS one2014

Fast and accurate multivariate Gaussian modeling of protein families: predicting residue contacts and protein-interaction partners.

Carlo Baldassi, Marco Zamparo, Christoph Feinauer, Andrea Procaccini, Riccardo Zecchina, Martin Weigt, Andrea Pagnani

Abstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

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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

64 citing papers in PubMed.

  1. Article
  2. Article
  3. Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025
    Article
  4. PHACE: Phylogeny-Aware Detection of Molecular Coevolution.Molecular biology and evolution · 2025
    Article
  5. Article
  6. Protein language models learn evolutionary statistics of interacting sequence motifs.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Deep graph learning of inter-protein contacts.Bioinformatics (Oxford, England) · 2022
    Article
  19. Article
  20. Article

4 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

7 authors.

Carlo BaldassiDepartment of Applied Science and Technology and Center for Computational Sciences, Politecnico di Torino, Torino, Italy; Human Genetics Foundation-Torino, Torino, Italy.
Marco ZamparoDepartment of Applied Science and Technology and Center for Computational Sciences, Politecnico di Torino, Torino, Italy; Human Genetics Foundation-Torino, Torino, Italy.
Christoph FeinauerDepartment of Applied Science and Technology and Center for Computational Sciences, Politecnico di Torino, Torino, Italy.
Andrea ProcacciniHuman Genetics Foundation-Torino, Torino, Italy.
Riccardo ZecchinaDepartment of Applied Science and Technology and Center for Computational Sciences, Politecnico di Torino, Torino, Italy; Human Genetics Foundation-Torino, Torino, Italy.
Martin WeigtSorbonne Universités, Université Pierre et Marie Curie Paris 06, UMR 7238, Computational and Quantitative Biology, Paris, France; Centre National de la Recherche Scientifique, UMR 7238, Computational and Quantitative Biology, Paris, France.
Andrea PagnaniDepartment of Applied Science and Technology and Center for Computational Sciences, Politecnico di Torino, Torino, Italy; Human Genetics Foundation-Torino, Torino, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the course of evolution, proteins show a remarkable conservation of their three-dimensional structure and their biological function, leading to strong evolutionary constraints on the sequence variability between homologous proteins. Our method aims at extracting such constraints from rapidly accumulating sequence data, and thereby at inferring protein structure and function from sequence information alone. Recently, global statistical inference methods (e.g. direct-coupling analysis, sparse inverse covariance estimation) have achieved a breakthrough towards this aim, and their predictions have been successfully implemented into tertiary and quaternary protein structure prediction methods. However, due to the discrete nature of the underlying variable (amino-acids), exact inference requires exponential time in the protein length, and efficient approximations are needed for practical applicability. Here we propose a very efficient multivariate Gaussian modeling approach as a variant of direct-coupling analysis: the discrete amino-acid variables are replaced by continuous Gaussian random variables. The resulting statistical inference problem is efficiently and exactly solvable. We show that the quality of inference is comparable or superior to the one achieved by mean-field approximations to inference with discrete variables, as done by direct-coupling analysis. This is true for (i) the prediction of residue-residue contacts in proteins, and (ii) the identification of protein-protein interaction partner in bacterial signal transduction. An implementation of our multivariate Gaussian approach is available at the website http://areeweb.polito.it/ricerca/cmp/code.

Indexed as

Models, MolecularBacteriaMultivariate AnalysisNormal DistributionProtein BindingProtein ConformationProteinsProtein Structure, TertiarySequence AlignmentSignal TransductionTime FactorsProteins

Identifiers

PMID24663061
PMCPMC3963956

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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.