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Browse result for Down-regulation in Glutarylation
※ introduction Post-translational modifications (PTMs) dynamically regulate cellular processes. Lysine undergoes a range of acylations, including malonylation, succinylation (SucK) and glutarylation (GluK). These PTMs increase the size of the lysine side chain and reverse its charge from +1 to ?1 under physiological conditions, probably impacting protein structure and function. To understand the functional roles of these PTMs, homogeneously modified proteins are required for biochemical studies.
Reference
Pubmed: Weyh M, Jokisch ML, Nguyen TA, Fottner M, Lang K. Deciphering functional roles of protein succinylation and glutarylation using genetic code expansion. Nat Chem. 2024 Mar 26. doi: 10.1038/s41557-024-01500-5.
Reference
Pubmed: Weyh M, Jokisch ML, Nguyen TA, Fottner M, Lang K. Deciphering functional roles of protein succinylation and glutarylation using genetic code expansion. Nat Chem. 2024 Mar 26. doi: 10.1038/s41557-024-01500-5.
| PTMD ID | UniProt Accession | Entrez ID | Gene Name | Protein Name | Organism |
|---|---|---|---|---|---|
| PTMD00094 | Q16236 | 4780 | NFE2L2 | Nuclear factor erythroid 2-related factor 2 | Homo sapiens |
| PTMD00990 | P10515 | 1737 | DLAT | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | Homo sapiens |
