Evidence map›Paper›PMID 18787688›Full record

ArticlePLoS computational biology2008

Identifying cognate binding pairs among a large set of paralogs: the case of PE/PPE proteins of Mycobacterium tuberculosis.

Robert Riley, Matteo Pellegrini, David Eisenberg

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. PE/PPE Proteome and ESX-5 Substrate Spectrum inInternational journal of molecular sciences · 2024
    Article
  4. Frontiers in immunology · 2023
    Article
  5. Article
  6. The rate and role of pseudogenes of theMicrobial genomics · 2022
    Article
  7. TheInternational journal of molecular sciences · 2022
    Review
  8. Review
  9. Structural basis of the PE-PPE protein interaction inThe Journal of biological chemistry · 2017
    Article
  10. Article
  11. Genomics Study ofEvolutionary bioinformatics online · 2016
    Article
  12. Article
  13. Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. General secretion signal for the mycobacterial type VII secretion pathway.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Article
  19. Article
  20. The TB Structural Genomics Consortium: a decade of progress.Tuberculosis (Edinburgh, Scotland) · 2011
    Review
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 at 3 institutions in 1 country.

Robert RileyDepartment of Human Genetics, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California, United States of America.
Matteo Pellegrini
David Eisenberg
Broad Institute · USHoward Hughes Medical Institute · USUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We consider the problem of how to detect cognate pairs of proteins that bind when each belongs to a large family of paralogs. To illustrate the problem, we have undertaken a genomewide analysis of interactions of members of the PE and PPE protein families of Mycobacterium tuberculosis. Our computational method uses structural information, operon organization, and protein coevolution to infer the interaction of PE and PPE proteins. Some 289 PE/PPE complexes were predicted out of a possible 5,590 PE/PPE pairs genomewide. Thirty-five of these predicted complexes were also found to have correlated mRNA expression, providing additional evidence for these interactions. We show that our method is applicable to other protein families, by analyzing interactions of the Esx family of proteins. Our resulting set of predictions is a starting point for genomewide experimental interaction screens of the PE and PPE families, and our method may be generally useful for detecting interactions of proteins within families having many paralogs.

Indexed as

Models, GeneticBacterial ProteinsBinding SitesComputational BiologyComputer SimulationEscherichia coliEvolution, MolecularGene ExpressionGenome, BacterialMultiprotein ComplexesMycobacterium tuberculosisOperonPhylogenyProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingBacterial ProteinsMultiprotein ComplexesRNA, BacterialRNA, Messenger

Identifiers

PMID18787688
PMCPMC2519833
OpenAlexW2037980409

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.