Title : N-Terminal Acetylation Affects α-Synuclein Fibril Polymorphism.

Pub. Date : 2019 Sep 3

PMID : 31424918






7 Functional Relationships(s)
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1 Here, we find N-terminally acetylated alphaSyn (Ac-alphaSyn) aggregates more slowly than non-acetylated alphaSyn (NH3-alphaSyn) with significantly reduced sensitivity to thioflavin T (ThT). thioflavin T synuclein alpha Homo sapiens
2 Here, we find N-terminally acetylated alphaSyn (Ac-alphaSyn) aggregates more slowly than non-acetylated alphaSyn (NH3-alphaSyn) with significantly reduced sensitivity to thioflavin T (ThT). thioflavin T synuclein alpha Homo sapiens
3 Here, we find N-terminally acetylated alphaSyn (Ac-alphaSyn) aggregates more slowly than non-acetylated alphaSyn (NH3-alphaSyn) with significantly reduced sensitivity to thioflavin T (ThT). thioflavin T synuclein alpha Homo sapiens
4 Here, we find N-terminally acetylated alphaSyn (Ac-alphaSyn) aggregates more slowly than non-acetylated alphaSyn (NH3-alphaSyn) with significantly reduced sensitivity to thioflavin T (ThT). thioflavin T synuclein alpha Homo sapiens
5 Interestingly, the low-ThT Ac-alphaSyn fibrils seed both acetylated and non-acetylated alphaSyn and faithfully propagate the low-ThT character through several generations, indicating a stable fibril polymorph. thioflavin T synuclein alpha Homo sapiens
6 Interestingly, the low-ThT Ac-alphaSyn fibrils seed both acetylated and non-acetylated alphaSyn and faithfully propagate the low-ThT character through several generations, indicating a stable fibril polymorph. thioflavin T synuclein alpha Homo sapiens
7 Interestingly, the low-ThT Ac-alphaSyn fibrils seed both acetylated and non-acetylated alphaSyn and faithfully propagate the low-ThT character through several generations, indicating a stable fibril polymorph. thioflavin T synuclein alpha Homo sapiens