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AligNet: alignment of protein-protein interaction networks

BACKGROUND: All molecular functions and biological processes are carried out by groups of proteins that interact with each other. Metaproteomic data continuously generates new proteins whose molecular functions and relations must be discovered. A widely accepted structure to model functional relatio...

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Detalles Bibliográficos
Autores principales: Alcalá, Adrià, Alberich, Ricardo, Llabrés, Mercè, Rosselló, Francesc, Valiente, Gabriel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7672851/
https://www.ncbi.nlm.nih.gov/pubmed/33203353
http://dx.doi.org/10.1186/s12859-020-3502-1
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author Alcalá, Adrià
Alberich, Ricardo
Llabrés, Mercè
Rosselló, Francesc
Valiente, Gabriel
author_facet Alcalá, Adrià
Alberich, Ricardo
Llabrés, Mercè
Rosselló, Francesc
Valiente, Gabriel
author_sort Alcalá, Adrià
collection PubMed
description BACKGROUND: All molecular functions and biological processes are carried out by groups of proteins that interact with each other. Metaproteomic data continuously generates new proteins whose molecular functions and relations must be discovered. A widely accepted structure to model functional relations between proteins are protein-protein interaction networks (PPIN), and their analysis and alignment has become a key ingredient in the study and prediction of protein-protein interactions, protein function, and evolutionary conserved assembly pathways of protein complexes. Several PPIN aligners have been proposed, but attaining the right balance between network topology and biological information is one of the most difficult and key points in the design of any PPIN alignment algorithm. RESULTS: Motivated by the challenge of well-balanced and efficient algorithms, we have designed and implemented AligNet, a parameter-free pairwise PPIN alignment algorithm aimed at bridging the gap between topologically efficient and biologically meaningful matchings. A comparison of the results obtained with AligNet and with the best aligners shows that AligNet achieves indeed a good balance between topological and biological matching. CONCLUSION: In this paper we present AligNet, a new pairwise global PPIN aligner that produces biologically meaningful alignments, by achieving a good balance between structural matching and protein function conservation, and more efficient computations than state-of-the-art tools.
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spelling pubmed-76728512020-11-19 AligNet: alignment of protein-protein interaction networks Alcalá, Adrià Alberich, Ricardo Llabrés, Mercè Rosselló, Francesc Valiente, Gabriel BMC Bioinformatics Research BACKGROUND: All molecular functions and biological processes are carried out by groups of proteins that interact with each other. Metaproteomic data continuously generates new proteins whose molecular functions and relations must be discovered. A widely accepted structure to model functional relations between proteins are protein-protein interaction networks (PPIN), and their analysis and alignment has become a key ingredient in the study and prediction of protein-protein interactions, protein function, and evolutionary conserved assembly pathways of protein complexes. Several PPIN aligners have been proposed, but attaining the right balance between network topology and biological information is one of the most difficult and key points in the design of any PPIN alignment algorithm. RESULTS: Motivated by the challenge of well-balanced and efficient algorithms, we have designed and implemented AligNet, a parameter-free pairwise PPIN alignment algorithm aimed at bridging the gap between topologically efficient and biologically meaningful matchings. A comparison of the results obtained with AligNet and with the best aligners shows that AligNet achieves indeed a good balance between topological and biological matching. CONCLUSION: In this paper we present AligNet, a new pairwise global PPIN aligner that produces biologically meaningful alignments, by achieving a good balance between structural matching and protein function conservation, and more efficient computations than state-of-the-art tools. BioMed Central 2020-11-18 /pmc/articles/PMC7672851/ /pubmed/33203353 http://dx.doi.org/10.1186/s12859-020-3502-1 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Alcalá, Adrià
Alberich, Ricardo
Llabrés, Mercè
Rosselló, Francesc
Valiente, Gabriel
AligNet: alignment of protein-protein interaction networks
title AligNet: alignment of protein-protein interaction networks
title_full AligNet: alignment of protein-protein interaction networks
title_fullStr AligNet: alignment of protein-protein interaction networks
title_full_unstemmed AligNet: alignment of protein-protein interaction networks
title_short AligNet: alignment of protein-protein interaction networks
title_sort alignet: alignment of protein-protein interaction networks
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7672851/
https://www.ncbi.nlm.nih.gov/pubmed/33203353
http://dx.doi.org/10.1186/s12859-020-3502-1
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