{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu JJ"],"funding":["the Research Foundation of Education Bureau of Hunan Province, China","National Natural Science Foundation of China"],"pagination":["5829"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8512392"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(19)"],"pubmed_abstract":["Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (Fe<sup>III</sup>) in rea"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose."],"pmcid":["PMC8512392"],"funding_grant_id":["22007045 and 21977042","19A441"],"pubmed_authors":["You Y","Liu JJ","Chen L","Lin YW","Gao SQ","Tang S","Wen GB"],"additional_accession":[]},"is_claimable":false,"name":"Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose.","description":"Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (Fe<sup>III</sup>) in rea","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2026-04-08T06:51:52.611Z","creation":"2022-02-11T12:12:34.13Z"},"accession":"S-EPMC8512392","cross_references":{"pubmed":["34641382"],"doi":["10.3390/molecules26195829"]}}