Jon W Poulsen's research while affiliated with University of Copenhagen and other places

... Its conventional function is as a covalently bound coenzyme for carboxylases used in leucine catabolism, gluconeogenesis, branched-chain amino acid and odd-chain fatty acid breakdown, and fatty acid synthesis and oxidation [30]. More recently, its noncarboxylic biological functions have also come to light, including those related to cell signaling, epigenetic gene control, chromatin structure, and immunological response [31,32]. New research on biotin's function in the immune system showed that it is associated with inflammation and that a biotin shortage increases the production of pro-inflammatory cytokines [30]. ...

... On the one hand, GuHCl, a chaotropic agent that disturbs the hydrogen bond of protein to unfold the structure, 60 was used for sericin solubilization for the study at an optimum temperature of 60°C. 61 The percentage yield obtained was 5.87 ± 0.40%, which is much lower than 25% of all sericin present in silk, indicating that only a part of the sericin was removed in this process. Three distinct bands at 415, 243, and 40 kDa along with some low-molecular-weight bands were observed in lane 1 (Figure 1, lane 1). ...

... The coalition of genome maintenance factors on RPA-ssDNA is controlled by complex damage-induced posttranslational modifications that include phosphorylation, SUMOylation, acetylation, crotonylation, and ubiquitylation [10,[36][37][38][39][40][41]. For example, DNA damage-induced RPA ubiquitylation by the PRP19 and RFWD3 E3 ubiquitin ligases has been implicated in ATR checkpoint activation and replication fork repair [37][38][39]42,43]. ...

... Previous studies have shown that the proteomes of WT and ubp3Δ differ by 30% (26,27). This makes the study of fluconazole resistance in ubp3Δ particularly challenging, as most of the changes in proteome might indirectly affect the sensitivity of the strains to fluconazole stress. ...

... Despite our determination that GTPases are primarily monoubiquitinated, our proteomic analysis identified multiple ubiquitinated lysines on most ubiquitinated GTPases. This is not entirely surprising, as ubiquitination of a given lysine residue is thought to be governed more by accessibility than amino acid sequence context; E3 ligases are often promiscuous in modifying lysine residues on substrates (Danielsen et al., 2011;Kim et al., 2011;Mattiroli and Sixma, 2014). Through sequence alignment and binning of ubiquitinated residues into different structural regions, we were able to determine that most ubiquitination sites fell within GTPase C-terminal regions after the G4 box, including the conserved G5 box SAK motif lysine that makes contacts with the guanine of GTP, and the hypervariable C-terminal domain (HVD), which contains sequence elements required for lipidation . ...