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However, soluble -synuclein undergoes aggregation and misfolding under various pathological conditions, including compromised membrane-binding capacity, exposure to dopamine oxidation products or metal ions, or impaired autophagy/proteasome degradation system

[DOI] [PubMed] [Google Scholar] 220.Harrop S.J., DeMaere M.Z., Fairlie W.D., Reztsova T., Valenzuela S.M., Mazzanti M., Tonini R., Qiu M.R., Jankova L., Warton K., et al

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Figure 5 In order to determine if the phosphorylation of Ser42, Ser184, and Tyr198 was involved in the effect of GSTP on HMGB1, six GSTP mutants were constructed, including GSTP-S42A (a Ser42 non-phosphorylatable mutant), GSTP-S42D (a Ser42 constant-phosphomimetic mutant), GSTP-S184A (a Ser184 non-phosphorylatable mutant), GSTP-S184D (a Ser184 constant-phosphomimetic mutant), GSTP-Y198F (a Tyr198 non-phosphorylatable mutant), as well as GSTP-Y198D (a Tyr198 constant-phosphomimetic mutant) (Figure S4B in Supplementary Material)