Evidence map›Paper›PMID 19165315›Full record

ArticlePLoS computational biology2009

Joint evolutionary trees: a large-scale method to predict protein interfaces based on sequence sampling.

Stefan Engelen, Ladislas A Trojan, Sophie Sacquin-Mora, Richard Lavery, Alessandra Carbone

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Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

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42citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

42 citing papers in PubMed.

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  18. A hybrid method for protein-protein interface prediction.Protein science : a publication of the Protein Society · 2016
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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

5 authors.

Stefan EngelenGénomique Analytique, Université Pierre et Marie Curie-Paris 6, UMR S511, Paris, France.
Ladislas A Trojan
Sophie Sacquin-Mora
Richard Lavery
Alessandra Carbone

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Joint Evolutionary Trees (JET) method detects protein interfaces, the core residues involved in the folding process, and residues susceptible to site-directed mutagenesis and relevant to molecular recognition. The approach, based on the Evolutionary Trace (ET) method, introduces a novel way to treat evolutionary information. Families of homologous sequences are analyzed through a Gibbs-like sampling of distance trees to reduce effects of erroneous multiple alignment and impacts of weakly homologous sequences on distance tree construction. The sampling method makes sequence analysis more sensitive to functional and structural importance of individual residues by avoiding effects of the overrepresentation of highly homologous sequences and improves computational efficiency. A carefully designed clustering method is parametrized on the target structure to detect and extend patches on protein surfaces into predicted interaction sites. Clustering takes into account residues' physical-chemical properties as well as conservation. Large-scale application of JET requires the system to be adjustable for different datasets and to guarantee predictions even if the signal is low. Flexibility was achieved by a careful treatment of the number of retrieved sequences, the amino acid distance between sequences, and the selective thresholds for cluster identification. An iterative version of JET (iJET) that guarantees finding the most likely interface residues is proposed as the appropriate tool for large-scale predictions. Tests are carried out on the Huang database of 62 heterodimer, homodimer, and transient complexes and on 265 interfaces belonging to signal transduction proteins, enzymes, inhibitors, antibodies, antigens, and others. A specific set of proteins chosen for their special functional and structural properties illustrate JET behavior on a large variety of interactions covering proteins, ligands, DNA, and RNA. JET is compared at a large scale to ET and to Consurf, Rate4Site, siteFiNDER|3D, and SCORECONS on specific structures. A significant improvement in performance and computational efficiency is shown.

Indexed as

Evolution, MolecularNeural Networks, ComputerBinding SitesCluster AnalysisComputational BiologyConserved SequenceDatabases, ProteinModels, ChemicalModels, MolecularPhylogenyProtein BindingProtein ConformationProtein Interaction MappingProteinsSequence Analysis, ProteinSequence Homology, Amino AcidProteins

Identifiers

PMID19165315
PMCPMC2613531

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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.