{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li R"],"funding":["National Natural Science Foundation of China"],"pagination":["1126-1138"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10423328"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(9)"],"pubmed_abstract":["Cryphonectria parasitica, the chestnut blight fungus, and hypoviruses are excellent models for examining fungal pathogenesis and virus-host interactions. Increasing evidence suggests that lysine acetylation plays a regulatory role in cell processes and signalling. To understand protein regulation in C. parasitica by hypoviruses at the level of posttranslational modification, a label-free comparative acetylome analysis was performed in the fungus with or without Cryphonectria hypovirus 1 (CHV1) infection. Using enrichment of acetyl-peptides with a specific anti-acetyl-lysine antibody, followed by high accuracy liquid chromatography-tandem mass spectrometry analysis, 638 lysine acetylation sites were identified on 616 peptides, corresponding to 325 unique proteins. Further analysis revealed "],"journal":["Molecular plant pathology"],"pubmed_title":["Comparative acetylomic analysis reveals differentially acetylated proteins regulating fungal metabolism in hypovirus-infected chestnut blight fungus."],"pmcid":["PMC10423328"],"funding_grant_id":["31760498"],"pubmed_authors":["Zhao L","Li S","Yuan L","Chen F","Tian S","Li R","Chen B"],"additional_accession":[]},"is_claimable":false,"name":"Comparative acetylomic analysis reveals differentially acetylated proteins regulating fungal metabolism in hypovirus-infected chestnut blight fungus.","description":"Cryphonectria parasitica, the chestnut blight fungus, and hypoviruses are excellent models for examining fungal pathogenesis and virus-host interactions. Increasing evidence suggests that lysine acetylation plays a regulatory role in cell processes and signalling. To understand protein regulation in C. parasitica by hypoviruses at the level of posttranslational modification, a label-free comparative acetylome analysis was performed in the fungus with or without Cryphonectria hypovirus 1 (CHV1) infection. Using enrichment of acetyl-peptides with a specific anti-acetyl-lysine antibody, followed by high accuracy liquid chromatography-tandem mass spectrometry analysis, 638 lysine acetylation sites were identified on 616 peptides, corresponding to 325 unique proteins. Further analysis revealed ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2026-06-26T03:20:48.825Z","creation":"2025-04-06T17:44:59.269Z"},"accession":"S-EPMC10423328","cross_references":{"pubmed":["37278715"],"doi":["10.1111/mpp.13358"]}}