{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang D"],"funding":["National Natural Science Fund for Excellent Young Scientists Fund Program","Fundamental Research Funds for the Provincial Universities of Zhejiang","The Start-up funding from Life Sciences Institute, Zhejiang University","MOST | National Natural Science Foundation of China (NSFC)","National Natural Science Fund for Excellent Young Scientists Fund Program (Oversea)","MOST | National Natural Science Foundation of China"],"pagination":["e0175824"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11784292"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["99(1)"],"pubmed_abstract":["Enteroviral 3C protease (3Cpro) is an essential enzyme for viral replication and is responsible for combating the host anti-viral immune response by targeting cellular proteins for cleavage. The identification and characterization of 3Cpro substrates will contribute to our understanding of viral pathogenesis. In this study, we performed a motif search for 3Cpro substrates in the human protein database using FIMO, which refers to a common cleavage sequence of 3Cpro. We identified and characterized NEDD4-binding protein 1 (N4BP1), a key negative regulator of the NF-κB pathway, as a novel 3Cpro substrate. N4BP1 is cleaved at residue Q816 by 3Cpro from several human enteroviruses, resulting in the loss of its ability to regulate tumor necrosis factor alpha-activated NF-κB signaling. In additio"],"journal":["Journal of virology"],"pubmed_title":["Enteroviral 3C protease cleaves N4BP1 to impair the host inflammatory response."],"pmcid":["PMC11784292"],"funding_grant_id":["K20240145","20230QZJH60","82372249"],"pubmed_authors":["Fan W","Zhang D","Xie Y","Cao J","Huang L"],"additional_accession":[]},"is_claimable":false,"name":"Enteroviral 3C protease cleaves N4BP1 to impair the host inflammatory response.","description":"Enteroviral 3C protease (3Cpro) is an essential enzyme for viral replication and is responsible for combating the host anti-viral immune response by targeting cellular proteins for cleavage. The identification and characterization of 3Cpro substrates will contribute to our understanding of viral pathogenesis. In this study, we performed a motif search for 3Cpro substrates in the human protein database using FIMO, which refers to a common cleavage sequence of 3Cpro. We identified and characterized NEDD4-binding protein 1 (N4BP1), a key negative regulator of the NF-κB pathway, as a novel 3Cpro substrate. N4BP1 is cleaved at residue Q816 by 3Cpro from several human enteroviruses, resulting in the loss of its ability to regulate tumor necrosis factor alpha-activated NF-κB signaling. In additio","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-01T21:58:44.943Z","creation":"2025-04-05T23:36:20.153Z"},"accession":"S-EPMC11784292","cross_references":{"pubmed":["39655957"],"doi":["10.1128/jvi.01758-24"]}}