{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(52)"],"submitter":["Gagne JP"],"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 "],"journal":["Oncotarget"],"pagination":["85680-85696"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5349866"],"repository":["biostudies-literature"],"pubmed_title":["Different non-synonymous polymorphisms modulate the interaction of the WRN protein to its protein partners and its enzymatic activities."],"pmcid":["PMC5349866"],"pubmed_authors":["Garand C","Caron MC","Poirier GG","Tsofack SP","Coulombe Y","Lebel M","Masson JY","Gagne JP","Lachapelle S"],"additional_accession":[]},"is_claimable":false,"name":"Different non-synonymous polymorphisms modulate the interaction of the WRN protein to its protein partners and its enzymatic activities.","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 ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Dec","modification":"2026-05-05T18:22:56.215Z","creation":"2019-03-27T02:38:37Z"},"accession":"S-EPMC5349866","cross_references":{"pubmed":["27863399"],"doi":["10.18632/oncotarget.13341"]}}