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[Preprint]. 2023 Jul 3:2023.07.03.547547. [Version 1] doi: 10.1101/2023.07.03.547547

Fig. 6 |. β-hydroxybutyrate targets display common structural features and are cleared through protein degradation pathways.

Fig. 6 |

a-e, Top 10 significantly enriched protein domains ranked by Q-value from (a) 1/0 mM R-βHB ex vivo upregulated proteins, (b) 5/0 mM R-βHB ex vivo upregulated proteins, (c) BH-BD/control fraction 2 upregulated proteins, (d) BH-BD/control fraction 3 upregulated proteins, and (e) BH-BD/control fraction 4 downregulated proteins. f, Venn diagram of BH-BD/control significantly upregulated proteins from all fractions crossed with upregulated proteins from 1/0 mM R-βHB and 5/0 mM R-βHB ex vivo proteomics groups, the 296 primary protein targets of R-βHB were calculated to have a p-value of 0.000001. g, Dotplot from clusterProfiler KEGG overrepresentation analysis on 296 primary protein targets of R-βHB from Fig. 6f. h, Top 10 significantly enriched protein domains ranked by Q-value from 296 primary protein targets of R-βHB from Fig. 6f.

f, p-value calculated using one-tailed probability test giving a z score = −54.4.