{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Veggiani G"],"funding":["National Institute of General Medical Sciences","Canadian Institutes of Health Research","NIGMS NIH HHS","CIHR"],"pagination":["941-956"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9305627"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(4)"],"pubmed_abstract":["Ubiquitin (Ub)-binding domains embedded in intracellular proteins act as readers of the complex Ub code and contribute to regulation of numerous eukaryotic processes. Ub-interacting motifs (UIMs) are short α-helical modular recognition elements whose role in controlling proteostasis and signal transduction has been poorly investigated. Moreover, impaired or aberrant activity of UIM-containing proteins has been implicated in numerous diseases, but targeting modular recognition elements in proteins remains a major challenge. To overcome this limitation, we developed Ub variants (UbVs) that bind to 42 UIMs in the human proteome with high affinity and specificity. Structural analysis of a UbV:UIM complex revealed the molecular determinants of enhanced affinity and specificity. Furthermore, we "],"journal":["ACS chemical biology"],"pubmed_title":["Panel of Engineered Ubiquitin Variants Targeting the Family of Human Ubiquitin Interacting Motifs."],"pmcid":["PMC9305627"],"funding_grant_id":["MOP-93684","P30 GM124165"],"pubmed_authors":["Manczyk N","Kurinov I","Sidhu SS","Veggiani G","Singer AU","Sicheri F","Martyn GD","Yates BP"],"additional_accession":[]},"is_claimable":false,"name":"Panel of Engineered Ubiquitin Variants Targeting the Family of Human Ubiquitin Interacting Motifs.","description":"Ubiquitin (Ub)-binding domains embedded in intracellular proteins act as readers of the complex Ub code and contribute to regulation of numerous eukaryotic processes. Ub-interacting motifs (UIMs) are short α-helical modular recognition elements whose role in controlling proteostasis and signal transduction has been poorly investigated. Moreover, impaired or aberrant activity of UIM-containing proteins has been implicated in numerous diseases, but targeting modular recognition elements in proteins remains a major challenge. To overcome this limitation, we developed Ub variants (UbVs) that bind to 42 UIMs in the human proteome with high affinity and specificity. Structural analysis of a UbV:UIM complex revealed the molecular determinants of enhanced affinity and specificity. Furthermore, we ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-19T14:17:59.475Z","creation":"2025-02-19T04:46:16.993Z"},"accession":"S-EPMC9305627","cross_references":{"pubmed":["35385646"],"doi":["10.1021/acschembio.2c00089"]}}