Leonard Roth

Abstract Amyloidogenic mutant huntingtin exon-1 (mHTTex1) protein aggregates with pathogenic polyglutamine (polyQ) tracts are the potential root cause of Huntington's disease (HD). Here, we assessed the gain-of-function toxicity of mHTTex1 aggregation in neurons of HD transgenic flies. We show that the rate of mHTTex1 aggregation in neurons and early mortality of HD transgenic flies are correlated.

Data availability statement All data and materials (such as the data extraction form) are available from the corresponding author. References Aspden T. J., Silwal P. R., Marowa M., Ponton R. (2021). Why do pharmacists leave the profession? A mixed-method exploratory study. Pharmacy Practice, 19(2), 2332. https://doi.org/10.18549/PharmPract.2021.2.2332 Babbar S., Adams D. R., Becker-Haimes E. M., Skriner L. C., Kratz H. E., Cliggitt L., Inacker P., Beidas R. S. (2018).

Graphical Abstract Site-directed mutagenesis was used to investigate the α-hydroxy acid activation in the adenylation domains of fungal, iterative non-ribosomal peptide synthetases. The results suggest a stabilization of the substrate's hydroxy group by hydrogen bond formation via backbone carbonyls of two distinct residues. The substitution of a frequently apparent Pro residue adjacent to one of the carbonyls seems mandatory for adenylation.