<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>6</volume><submitter>Idrees S</submitter><funding>University International Postgraduate Award to Sobia Idrees</funding><pubmed_abstract>Many important cellular processes involve protein-protein interactions (PPIs) mediated by a Short Linear Motif (SLiM) in one protein interacting with a globular domain in another. Despite their significance, these domain-motif interactions (DMIs) are typically low affinity, which makes them challenging to identify by classical experimental approaches, such as affinity pulldown mass spectrometry (AP-MS) and yeast two-hybrid (Y2H). DMIs are generally underrepresented in PPI networks as a result. A number of computational methods now exist to predict SLiMs and/or DMIs from experimental interaction data but it is yet to be established how effective different PPI detection methods are for capturing these low affinity SLiM-mediated interactions. Here, we introduce a new computational pipeline (S</pubmed_abstract><journal>PeerJ</journal><pagination>e5858</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6215436</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>SLiM-Enrich: computational assessment of protein-protein interaction data as a source of domain-motif interactions.</pubmed_title><pmcid>PMC6215436</pmcid><pubmed_authors>Idrees S</pubmed_authors><pubmed_authors>Perez-Bercoff A</pubmed_authors><pubmed_authors>Edwards RJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>SLiM-Enrich: computational assessment of protein-protein interaction data as a source of domain-motif interactions.</name><description>Many important cellular processes involve protein-protein interactions (PPIs) mediated by a Short Linear Motif (SLiM) in one protein interacting with a globular domain in another. Despite their significance, these domain-motif interactions (DMIs) are typically low affinity, which makes them challenging to identify by classical experimental approaches, such as affinity pulldown mass spectrometry (AP-MS) and yeast two-hybrid (Y2H). DMIs are generally underrepresented in PPI networks as a result. A number of computational methods now exist to predict SLiMs and/or DMIs from experimental interaction data but it is yet to be established how effective different PPI detection methods are for capturing these low affinity SLiM-mediated interactions. Here, we introduce a new computational pipeline (S</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018</publication><modification>2025-04-04T09:14:48.219Z</modification><creation>2019-03-27T00:06:14Z</creation></dates><accession>S-EPMC6215436</accession><cross_references><pubmed>30402352</pubmed><doi>10.7717/peerj.5858</doi></cross_references></HashMap>