{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jiajia H"],"funding":["the National Natural Science Foundation of China"],"pagination":["567"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10657630"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(1)"],"pubmed_abstract":["UFMylation is a ubiquitination-like modification that is related to endoplasmic reticulum stress and unfolded protein response. A recent study reported that Ufl1, a key enzyme of UFMylation, protects against heart failure, indicating that UFMylation may be associated with heart function regulation. In the present study, we initially constructed a Flag-6×His-tagged Ufm1ΔSC transgenic (Tg-Ufm1) mouse model that enables UFMylation studies in vivo. Tg-Ufm1 mice showed significant activation of UFMylation in hearts. By using this model, we identified 38 potential Ufm1-binding proteins in heart tissues through LC‒MS/MS methods. We found that these proteins were associated with mitochondria, metabolism and chaperone binding. By using transcriptomic screening, we identified Tnfaip2 as a novel UFMy"],"journal":["BMC cardiovascular disorders"],"pubmed_title":["Screening UFMylation-associated genes in heart tissues of Ufm1-transgenic mice."],"pmcid":["PMC10657630"],"funding_grant_id":["No. 81870196"],"pubmed_authors":["Jiaqi Z","Ziyao Y","Xiaotao Z","Yanli C","Ming S","Jiajia H"],"additional_accession":[]},"is_claimable":false,"name":"Screening UFMylation-associated genes in heart tissues of Ufm1-transgenic mice.","description":"UFMylation is a ubiquitination-like modification that is related to endoplasmic reticulum stress and unfolded protein response. A recent study reported that Ufl1, a key enzyme of UFMylation, protects against heart failure, indicating that UFMylation may be associated with heart function regulation. In the present study, we initially constructed a Flag-6×His-tagged Ufm1ΔSC transgenic (Tg-Ufm1) mouse model that enables UFMylation studies in vivo. Tg-Ufm1 mice showed significant activation of UFMylation in hearts. By using this model, we identified 38 potential Ufm1-binding proteins in heart tissues through LC‒MS/MS methods. We found that these proteins were associated with mitochondria, metabolism and chaperone binding. By using transcriptomic screening, we identified Tnfaip2 as a novel UFMy","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2025-04-18T13:13:13.2Z","creation":"2025-02-19T01:52:16.922Z"},"accession":"S-EPMC10657630","cross_references":{"pubmed":["37980507"],"doi":["10.1186/s12872-023-03563-7"]}}