<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-04-29T15:25:25Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/22868" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/22868</identifier><datestamp>2024-11-29T03:42:10Z</datestamp><setSpec>com_20.500.12105_15322</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>col_20.500.12105_16967</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Alcala, Adria</subfield>
      <subfield code="e">author</subfield>
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      <subfield code="a">Alberich, Ricardo</subfield>
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      <subfield code="a">Llabres, Merce</subfield>
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      <subfield code="a">Rossello, Francesc</subfield>
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      <subfield code="a">Valiente, Gabriel</subfield>
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      <subfield code="c">2020-11-18</subfield>
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      <subfield code="a">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.</subfield>
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      <subfield code="a">Alcala A, Alberich R, Llabres M, Rossello F, Valiente G. AligNet: alignment of protein-protein interaction networks. BMC Bioinformatics. 2020 Nov 18;21 Suppl 6:265.</subfield>
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      <subfield code="a">10.1186/s12859-020-3502-1</subfield>
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      <subfield code="a">1471-2105</subfield>
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      <subfield code="a">BMC Bioinformatics</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.13003/15886</subfield>
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      <subfield code="a">33203353</subfield>
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      <subfield code="a">L633454222</subfield>
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      <subfield code="a">2-s2.0-85096148502</subfield>
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      <subfield code="a">https://hdl.handle.net/20.500.12105/22868</subfield>
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      <subfield code="a">Protein-protein interaction network</subfield>
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      <subfield code="a">Global alignment</subfield>
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      <subfield code="a">Network matching</subfield>
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      <subfield code="a">Functional consistency</subfield>
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      <subfield code="a">AligNet: alignment of protein-protein interaction networks</subfield>
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