<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jiajia H</submitter><funding>the National Natural Science Foundation of China</funding><pagination>567</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10657630</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(1)</volume><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</pubmed_abstract><journal>BMC cardiovascular disorders</journal><pubmed_title>Screening UFMylation-associated genes in heart tissues of Ufm1-transgenic mice.</pubmed_title><pmcid>PMC10657630</pmcid><funding_grant_id>No. 81870196</funding_grant_id><pubmed_authors>Jiaqi Z</pubmed_authors><pubmed_authors>Ziyao Y</pubmed_authors><pubmed_authors>Xiaotao Z</pubmed_authors><pubmed_authors>Yanli C</pubmed_authors><pubmed_authors>Ming S</pubmed_authors><pubmed_authors>Jiajia H</pubmed_authors></additional><is_claimable>false</is_claimable><name>Screening UFMylation-associated genes in heart tissues of Ufm1-transgenic mice.</name><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</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Nov</publication><modification>2025-04-18T13:13:13.2Z</modification><creation>2025-02-19T01:52:16.922Z</creation></dates><accession>S-EPMC10657630</accession><cross_references><pubmed>37980507</pubmed><doi>10.1186/s12872-023-03563-7</doi></cross_references></HashMap>