{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Moises JE"],"funding":["Bundesministerium für Digitalisierung und Wirtschaftsstandort","Paris Lodron University of Salzburg"],"pagination":["1341-1353"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10338404"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["40(6)"],"pubmed_abstract":["<h4>Objective</h4>Glycation is a non-enzymatic and spontaneous post-translational modification (PTM) generated by the reaction between reducing sugars and primary amine groups within proteins. Because glycation can alter the properties of proteins, it is a critical quality attribute of therapeutic monoclonal antibodies (mAbs) and should therefore be carefully monitored. The most abundant product of glycation is formed by glucose and lysine side chains resulting in fructoselysine after Amadori rearrangement. In proteomics, which routinely uses a combination of chromatography and mass spectrometry to analyze PTMs, there is no straight-forward way to distinguish between glycation products of a reducing monosaccharide and an additional hexose within a glycan, since both lead to a mass differen"],"journal":["Pharmaceutical research"],"pubmed_title":["Unambiguous Identification of Glucose-Induced Glycation in mAbs and other Proteins by NMR Spectroscopy."],"pmcid":["PMC10338404"],"funding_grant_id":["00000000"],"pubmed_authors":["Hinterholzer A","Moises JE","Regl C","Schubert M","Huber CG"],"additional_accession":[]},"is_claimable":false,"name":"Unambiguous Identification of Glucose-Induced Glycation in mAbs and other Proteins by NMR Spectroscopy.","description":"<h4>Objective</h4>Glycation is a non-enzymatic and spontaneous post-translational modification (PTM) generated by the reaction between reducing sugars and primary amine groups within proteins. Because glycation can alter the properties of proteins, it is a critical quality attribute of therapeutic monoclonal antibodies (mAbs) and should therefore be carefully monitored. The most abundant product of glycation is formed by glucose and lysine side chains resulting in fructoselysine after Amadori rearrangement. In proteomics, which routinely uses a combination of chromatography and mass spectrometry to analyze PTMs, there is no straight-forward way to distinguish between glycation products of a reducing monosaccharide and an additional hexose within a glycan, since both lead to a mass differen","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2025-04-04T13:51:36.921Z","creation":"2025-04-04T13:51:36.921Z"},"accession":"S-EPMC10338404","cross_references":{"pubmed":["36510116"],"doi":["10.1007/s11095-022-03454-0"]}}