. Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions. J Neurosci. 2010 Mar 3;30(9):3184-98. PubMed.

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  1. I'd like to post a correction to a mistake in this article: the difference in amino acid sequence of alpha-synuclein between human and rat/mouse is 7, not 5. These include A53T, S87N, L100M, N103G, A107Y, D121S/G, and N122S. The sequences were from GenBank: human, NP000336.1; rat, NP062042.1; mice, NP033247.1

    View all comments by Junchao Tong
  2. I have never found the concept of mimicking phosphoserine with glutamate convincing. Glutamate lacks an oxygen and cannot have a doubly negative charge, unlike phosphoserine. Aspartate, which is often also used to replace phosphoserine, is even worse, as it is one bond shorter. If the protein or peptide is short enough, it can be synthesized using a phosphorylated amino acid.

    View all comments by Andrew Doig

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