<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(52)</volume><submitter>Gagne JP</submitter><pubmed_abstract>Werner syndrome (WS) is characterized by the premature onset of several age-associated pathologies including cancer. The protein defective in WS patients (WRN) is a helicase/exonuclease involved in DNA replication and repair. Here, we present the results of a large-scale proteome analysis that has been undertaken to determine protein partners of different polymorphic WRN proteins found with relatively high prevalence in the human population. We expressed different fluorescently tagged-WRN (eYFP-WRN) variants in human 293 embryonic kidney cells (HEK293) and used a combination of affinity-purification and mass spectrometry to identify different compositions of WRN-associated protein complexes. We found that a WRN variant containing a phenylalanine residue at position 1074 and an arginine at </pubmed_abstract><journal>Oncotarget</journal><pagination>85680-85696</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5349866</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Different non-synonymous polymorphisms modulate the interaction of the WRN protein to its protein partners and its enzymatic activities.</pubmed_title><pmcid>PMC5349866</pmcid><pubmed_authors>Garand C</pubmed_authors><pubmed_authors>Caron MC</pubmed_authors><pubmed_authors>Poirier GG</pubmed_authors><pubmed_authors>Tsofack SP</pubmed_authors><pubmed_authors>Coulombe Y</pubmed_authors><pubmed_authors>Lebel M</pubmed_authors><pubmed_authors>Masson JY</pubmed_authors><pubmed_authors>Gagne JP</pubmed_authors><pubmed_authors>Lachapelle S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Different non-synonymous polymorphisms modulate the interaction of the WRN protein to its protein partners and its enzymatic activities.</name><description>Werner syndrome (WS) is characterized by the premature onset of several age-associated pathologies including cancer. The protein defective in WS patients (WRN) is a helicase/exonuclease involved in DNA replication and repair. Here, we present the results of a large-scale proteome analysis that has been undertaken to determine protein partners of different polymorphic WRN proteins found with relatively high prevalence in the human population. We expressed different fluorescently tagged-WRN (eYFP-WRN) variants in human 293 embryonic kidney cells (HEK293) and used a combination of affinity-purification and mass spectrometry to identify different compositions of WRN-associated protein complexes. We found that a WRN variant containing a phenylalanine residue at position 1074 and an arginine at </description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Dec</publication><modification>2026-05-05T18:22:56.215Z</modification><creation>2019-03-27T02:38:37Z</creation></dates><accession>S-EPMC5349866</accession><cross_references><pubmed>27863399</pubmed><doi>10.18632/oncotarget.13341</doi></cross_references></HashMap>