{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Saratov GA"],"funding":["Ministry of Science and Higher Education of the Russian Federation"],"pagination":["2091"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9917034"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(3)"],"pubmed_abstract":["Proteasomes exist in mammalian cells in multiple combinatorial variants due to the diverse regulatory particles and exchange of catalytic subunits. Here, using biotin carboxyl carrier domain of transcarboxylase from <i>Propionibacterium shermanii</i> fused with different proteasome subunits of catalytic and regulatory particles, we report comprehensive characterization of highly homogenous one-step purified human constitutive and immune 20S and 26S/30S proteasomes. Hydrolysis of a multiple sclerosis (MS) autoantigen, myelin basic protein (MBP), by engineered human proteasomes with different catalytic phenotypes, revealed that peptides which may be directly loaded on the HLA class I molecules are produced mainly by immunoproteasomes. We detected at least five MBP immunodominant core regions"],"journal":["International journal of molecular sciences"],"pubmed_title":["Myelin Basic Protein Fragmentation by Engineered Human Proteasomes with Different Catalytic Phenotypes Revealed Direct Peptide Ligands of MS-Associated and Protective HLA Class I Molecules."],"pmcid":["PMC9917034"],"funding_grant_id":["075-15-2020-795","RF-190220X0027","13.1902.21.0027"],"pubmed_authors":["Konevega AL","Belogurov AA","Kudriaeva AA","Saratov GA","Chen G","Baymukhametov TN","Ziganshin RH","Vladimirov VI","Novoselov AL"],"additional_accession":[]},"is_claimable":false,"name":"Myelin Basic Protein Fragmentation by Engineered Human Proteasomes with Different Catalytic Phenotypes Revealed Direct Peptide Ligands of MS-Associated and Protective HLA Class I Molecules.","description":"Proteasomes exist in mammalian cells in multiple combinatorial variants due to the diverse regulatory particles and exchange of catalytic subunits. Here, using biotin carboxyl carrier domain of transcarboxylase from <i>Propionibacterium shermanii</i> fused with different proteasome subunits of catalytic and regulatory particles, we report comprehensive characterization of highly homogenous one-step purified human constitutive and immune 20S and 26S/30S proteasomes. Hydrolysis of a multiple sclerosis (MS) autoantigen, myelin basic protein (MBP), by engineered human proteasomes with different catalytic phenotypes, revealed that peptides which may be directly loaded on the HLA class I molecules are produced mainly by immunoproteasomes. We detected at least five MBP immunodominant core regions","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-04-08T13:58:50.196Z","creation":"2025-04-06T00:50:59.472Z"},"accession":"S-EPMC9917034","cross_references":{"pubmed":["36768413"],"doi":["10.3390/ijms24032091"]}}