<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Stacey RG</submitter><funding>Genome Canada</funding><funding>Canadian Institutes of Health Research</funding><pagination>457</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5654062</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>18(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>An organism's protein interactome, or complete network of protein-protein interactions, defines the protein complexes that drive cellular processes. Techniques for studying protein complexes have traditionally applied targeted strategies such as yeast two-hybrid or affinity purification-mass spectrometry to assess protein interactions. However, given the vast number of protein complexes, more scalable methods are necessary to accelerate interaction discovery and to construct whole interactomes. We recently developed a complementary technique based on the use of protein correlation profiling (PCP) and stable isotope labeling in amino acids in cell culture (SILAC) to assess chromatographic co-elution as evidence of interacting proteins. Importantly, PCP-SILAC is also capab</pubmed_abstract><journal>BMC bioinformatics</journal><pubmed_title>A rapid and accurate approach for prediction of interactomes from co-elution data (PrInCE).</pubmed_title><pmcid>PMC5654062</pmcid><funding_grant_id>MOP77688</funding_grant_id><funding_grant_id>214PRO</funding_grant_id><pubmed_authors>Scott NE</pubmed_authors><pubmed_authors>Stacey RG</pubmed_authors><pubmed_authors>Skinnider MA</pubmed_authors><pubmed_authors>Foster LJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>A rapid and accurate approach for prediction of interactomes from co-elution data (PrInCE).</name><description>&lt;h4>Background&lt;/h4>An organism's protein interactome, or complete network of protein-protein interactions, defines the protein complexes that drive cellular processes. Techniques for studying protein complexes have traditionally applied targeted strategies such as yeast two-hybrid or affinity purification-mass spectrometry to assess protein interactions. However, given the vast number of protein complexes, more scalable methods are necessary to accelerate interaction discovery and to construct whole interactomes. We recently developed a complementary technique based on the use of protein correlation profiling (PCP) and stable isotope labeling in amino acids in cell culture (SILAC) to assess chromatographic co-elution as evidence of interacting proteins. Importantly, PCP-SILAC is also capab</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Oct</publication><modification>2026-06-06T22:40:30.632Z</modification><creation>2019-03-27T02:59:45Z</creation></dates><accession>S-EPMC5654062</accession><cross_references><pubmed>29061110</pubmed><doi>10.1186/s12859-017-1865-8</doi></cross_references></HashMap>