Evidence map›Paper›PMID 24842992›Full record

ArticleeLife2014

Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information.

Sergey Ovchinnikov, Hetunandan Kamisetty, David Baker

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 379 papers.

0numbers the graph read from it
0cells of the map it votes in
379citing 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

379 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Linear-time prediction of proteome-scale microbial protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Identification of 14-3-3 Proteins as Binding Partners of TRP Channels.Journal of chemical information and modeling · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Stepwise DNA unwinding gates TnpB genome-editing activity.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Predicting Protein-Protein Interactions from Machine-Learned Representations.Advances in experimental medicine and biology · 2026
    Review
  13. Article
  14. Structure and evolution-guided design of minimal RNA-guided nucleases.bioRxiv : the preprint server for biology · 2025
    Article
  15. Review
  16. Review
  17. An AlphaFold guided model for the evolution of the CaMKII interactome.bioRxiv : the preprint server for biology · 2025
    Article
  18. Review
  19. Review
  20. Article

319 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

3 authors.

Sergey OvchinnikovDepartment of Biochemistry, Howard Hughes Medical Institute, University of Washington, Seattle, United States Molecular and Cellular Biology Program, University of Washington, Seattle, United States.
Hetunandan KamisettyDepartment of Biochemistry, Howard Hughes Medical Institute, University of Washington, Seattle, United States Facebook Inc., Seattle, United States.
David BakerDepartment of Biochemistry, Howard Hughes Medical Institute, University of Washington, Seattle, United States dabaker@u.washington.edu.

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
High resolution structure modeling with RosettaR01GM092802 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2010 to 2017
$2.3M
NIGMS NIH HHS 1R01GM092802-04NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM092802NIGMS NIH HHS T32 GM007270
6 · The paper itself

Abstract

Do the amino acid sequence identities of residues that make contact across protein interfaces covary during evolution? If so, such covariance could be used to predict contacts across interfaces and assemble models of biological complexes. We find that residue pairs identified using a pseudo-likelihood-based method to covary across protein-protein interfaces in the 50S ribosomal unit and 28 additional bacterial protein complexes with known structure are almost always in contact in the complex, provided that the number of aligned sequences is greater than the average length of the two proteins. We use this method to make subunit contact predictions for an additional 36 protein complexes with unknown structures, and present models based on these predictions for the tripartite ATP-independent periplasmic (TRAP) transporter, the tripartite efflux system, the pyruvate formate lyase-activating enzyme complex, and the methionine ABC transporter.DOI: http://dx.doi.org/10.7554/eLife.02030.001.

Indexed as

Biological EvolutionModels, MolecularProtein BindingProtein ConformationProteinsProteinsprotein coevolutionprotein complexespseudo-likelihood

Identifiers

PMID24842992
PMCPMC4034769

What OpenQuestion holds

Textmetadata
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.