Evidence map›Paper›PMID 26275894›Full record

ArticleBioinformatics (Oxford, England)2015

Protein contact prediction by integrating joint evolutionary coupling analysis and supervised learning.

Jianzhu Ma, Sheng Wang, Zhiyong Wang, Jinbo Xu

Abstract readEvaluation Study
In one paragraph

Article in Bioinformatics (Oxford, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. Article
  3. General features of transmembrane beta barrels from a large database.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Customized chitooligosaccharide production-controlling their lengthFrontiers in bioengineering and biotechnology · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Toward the solution of the protein structure prediction problem.The Journal of biological chemistry · 2021
    Review
  18. Article
  19. Article
  20. Article
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

4 authors.

Jianzhu MaToyota Technological Institute at Chicago, 6045 S. Kenwood Ave. Chicago, Illinois 60637 USA.
Sheng WangToyota Technological Institute at Chicago, 6045 S. Kenwood Ave. Chicago, Illinois 60637 USA.
Zhiyong WangToyota Technological Institute at Chicago, 6045 S. Kenwood Ave. Chicago, Illinois 60637 USA.
Jinbo XuToyota Technological Institute at Chicago, 6045 S. Kenwood Ave. Chicago, Illinois 60637 USA.

Funding

New Computational Methods for Data-driven Protein Structure PredictionR01GM089753 · NIGMS · TOYOTA TECHNOLOGICAL INSTITUTE / CHICAGO · PI XU, JINBO · 2010 to 2023
$3.8M
NIGMS NIH HHS R01 GM089753NIGMS NIH HHS R01GM0897532
6 · The paper itself

Abstract

motivationProtein contact prediction is important for protein structure and functional study. Both evolutionary coupling (EC) analysis and supervised machine learning methods have been developed, making use of different information sources. However, contact prediction is still challenging especially for proteins without a large number of sequence homologs.

resultsThis article presents a group graphical lasso (GGL) method for contact prediction that integrates joint multi-family EC analysis and supervised learning to improve accuracy on proteins without many sequence homologs. Different from existing single-family EC analysis that uses residue coevolution information in only the target protein family, our joint EC analysis uses residue coevolution in both the target family and its related families, which may have divergent sequences but similar folds. To implement this, we model a set of related protein families using Gaussian graphical models and then coestimate their parameters by maximum-likelihood, subject to the constraint that these parameters shall be similar to some degree. Our GGL method can also integrate supervised learning methods to further improve accuracy. Experiments show that our method outperforms existing methods on proteins without thousands of sequence homologs, and that our method performs better on both conserved and family-specific contacts. AVAILABILITY AND IMPLEMENTATION: See http://raptorx.uchicago.edu/ContactMap/ for a web server implementing the method. CONTACT: j3xu@ttic.edu SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Indexed as

Machine LearningSequence Analysis, ProteinAlgorithmsEvolution, MolecularModels, StatisticalProtein ConformationProteinsSequence AlignmentSoftwareProteins

Identifiers

PMID26275894
PMCPMC4838177

What OpenQuestion holds

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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.